User:ProteinBoxBot/PBB Log Wiki 11-6-2007 Rerun B-3

Log file for Protein Box Bot

Log page index: User:ProteinBoxBot/PBB_Log_Index

Protein Status Quick Log - Date: 23:03, 14 November 2007 (UTC)

Proteins without matches (10)

Proteins with a High Potential Match (11)

Redirected Proteins (4)

Manual Inspection (Page not found) (21)

Updated (4)

Protein Status Grid - Date: 23:03, 14 November 2007 (UTC)

Vebose Log - Date: 23:03, 14 November 2007 (UTC)

AKT2

• INFO: Beginning work on AKT2... {November 14, 2007 2:34:26 PM PST}
• SEARCH REDIRECT: Control Box Found: AKT2 {November 14, 2007 2:35:15 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 2:35:16 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 2:35:16 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 2:35:16 PM PST}
• UPDATED: Updated protein page: AKT2 {November 14, 2007 2:35:23 PM PST}

CANX

• INFO: Beginning work on CANX... {November 14, 2007 2:35:23 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:35:59 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_CANX_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jhn.
 | PDB = {{PDB2|1jhn}}
 | Name = Calnexin
 | HGNCid = 1473
 | Symbol = CANX
 | AltSymbols =; CNX; FLJ26570; IP90; P90
 | OMIM = 114217
 | ECnumber =  
 | Homologene = 1324
 | MGIid = 88261
 | GeneAtlas_image1 = PBB_GE_CANX_208852_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_CANX_208853_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}} {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}} 
 | Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0009306 |text = protein secretion}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 821
    | Hs_Ensembl = ENSG00000127022
    | Hs_RefseqProtein = NP_001019820
    | Hs_RefseqmRNA = NM_001024649
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 179058536
    | Hs_GenLoc_end = 179091243
    | Hs_Uniprot = P27824
    | Mm_EntrezGene = 12330
    | Mm_Ensembl = ENSMUSG00000020368
    | Mm_RefseqmRNA = NM_007597
    | Mm_RefseqProtein = NP_031623
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 50137886
    | Mm_GenLoc_end = 50169014
    | Mm_Uniprot = Q3TXE5
  }}
}}
'''Calnexin''', also known as '''CANX''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene encodes a member of the calnexin family of molecular chaperones. The encoded protein is a calcium-binding, endoplasmic reticulum (ER)-associated protein that interacts transiently with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. It may also play a central role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation. Alternatively spliced transcript variants encoding the same protein have been described.<ref>{{cite web | title = Entrez Gene: CANX calnexin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=821| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Kleizen B, Braakman I |title=Protein folding and quality control in the endoplasmic reticulum. |journal=Curr. Opin. Cell Biol. |volume=16 |issue= 4 |pages= 343-9 |year= 2005 |pmid= 15261665 |doi= 10.1016/j.ceb.2004.06.012 }}
*{{cite journal  | author=Rasmussen HH, van Damme J, Puype M, ''et al.'' |title=Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 960-9 |year= 1993 |pmid= 1286667 |doi=  }}
*{{cite journal  | author=Galvin K, Krishna S, Ponchel F, ''et al.'' |title=The major histocompatibility complex class I antigen-binding protein p88 is the product of the calnexin gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 18 |pages= 8452-6 |year= 1992 |pmid= 1326756 |doi=  }}
*{{cite journal  | author=Pind S, Riordan JR, Williams DB |title=Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator. |journal=J. Biol. Chem. |volume=269 |issue= 17 |pages= 12784-8 |year= 1994 |pmid= 7513695 |doi=  }}
*{{cite journal  | author=Honoré B, Rasmussen HH, Celis A, ''et al.'' |title=The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin exhibit strikingly different levels in quiescent keratinocytes as compared to their proliferating normal and transformed counterparts: cDNA cloning and expression of calnexin. |journal=Electrophoresis |volume=15 |issue= 3-4 |pages= 482-90 |year= 1994 |pmid= 8055875 |doi=  }}
*{{cite journal  | author=Tjoelker LW, Seyfried CE, Eddy RL, ''et al.'' |title=Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5. |journal=Biochemistry |volume=33 |issue= 11 |pages= 3229-36 |year= 1994 |pmid= 8136357 |doi=  }}
*{{cite journal  | author=Lenter M, Vestweber D |title=The integrin chains beta 1 and alpha 6 associate with the chaperone calnexin prior to integrin assembly. |journal=J. Biol. Chem. |volume=269 |issue= 16 |pages= 12263-8 |year= 1994 |pmid= 8163531 |doi=  }}
*{{cite journal  | author=Rajagopalan S, Xu Y, Brenner MB |title=Retention of unassembled components of integral membrane proteins by calnexin. |journal=Science |volume=263 |issue= 5145 |pages= 387-90 |year= 1994 |pmid= 8278814 |doi=  }}
*{{cite journal  | author=David V, Hochstenbach F, Rajagopalan S, Brenner MB |title=Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin). |journal=J. Biol. Chem. |volume=268 |issue= 13 |pages= 9585-92 |year= 1993 |pmid= 8486646 |doi=  }}
*{{cite journal  | author=Bellovino D, Morimoto T, Tosetti F, Gaetani S |title=Retinol binding protein and transthyretin are secreted as a complex formed in the endoplasmic reticulum in HepG2 human hepatocarcinoma cells. |journal=Exp. Cell Res. |volume=222 |issue= 1 |pages= 77-83 |year= 1996 |pmid= 8549676 |doi= 10.1006/excr.1996.0010 }}
*{{cite journal  | author=Otteken A, Moss B |title=Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin. |journal=J. Biol. Chem. |volume=271 |issue= 1 |pages= 97-103 |year= 1996 |pmid= 8550632 |doi=  }}
*{{cite journal  | author=Devergne O, Hummel M, Koeppen H, ''et al.'' |title=A novel interleukin-12 p40-related protein induced by latent Epstein-Barr virus infection in B lymphocytes. |journal=J. Virol. |volume=70 |issue= 2 |pages= 1143-53 |year= 1996 |pmid= 8551575 |doi=  }}
*{{cite journal  | author=Andersson B, Wentland MA, Ricafrente JY, ''et al.'' |title=A "double adaptor" method for improved shotgun library construction. |journal=Anal. Biochem. |volume=236 |issue= 1 |pages= 107-13 |year= 1996 |pmid= 8619474 |doi= 10.1006/abio.1996.0138 }}
*{{cite journal  | author=van Leeuwen JE, Kearse KP |title=Calnexin associates exclusively with individual CD3 delta and T cell antigen receptor (TCR) alpha proteins containing incompletely trimmed glycans that are not assembled into multisubunit TCR complexes. |journal=J. Biol. Chem. |volume=271 |issue= 16 |pages= 9660-5 |year= 1996 |pmid= 8621641 |doi=  }}
*{{cite journal  | author=Oliver JD, Hresko RC, Mueckler M, High S |title=The glut 1 glucose transporter interacts with calnexin and calreticulin. |journal=J. Biol. Chem. |volume=271 |issue= 23 |pages= 13691-6 |year= 1996 |pmid= 8662691 |doi=  }}
*{{cite journal  | author=Li Y, Bergeron JJ, Luo L, ''et al.'' |title=Effects of inefficient cleavage of the signal sequence of HIV-1 gp 120 on its association with calnexin, folding, and intracellular transport. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 18 |pages= 9606-11 |year= 1996 |pmid= 8790377 |doi=  }}
*{{cite journal  | author=Trombetta ES, Simons JF, Helenius A |title=Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27509-16 |year= 1996 |pmid= 8910335 |doi=  }}
*{{cite journal  | author=Tatu U, Helenius A |title=Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. |journal=J. Cell Biol. |volume=136 |issue= 3 |pages= 555-65 |year= 1997 |pmid= 9024687 |doi=  }}
*{{cite journal  | author=Wiest DL, Bhandoola A, Punt J, ''et al.'' |title=Incomplete endoplasmic reticulum (ER) retention in immature thymocytes as revealed by surface expression of "ER-resident" molecular chaperones. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 5 |pages= 1884-9 |year= 1997 |pmid= 9050874 |doi=  }}
*{{cite journal  | author=Yu W, Andersson B, Worley KC, ''et al.'' |title=Large-scale concatenation cDNA sequencing. |journal=Genome Res. |volume=7 |issue= 4 |pages= 353-8 |year= 1997 |pmid= 9110174 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

CCL4

• INFO: Beginning work on CCL4... {November 14, 2007 2:50:51 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:51:44 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_CCL4_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hum.
 | PDB = {{PDB2|1hum}}, {{PDB2|1hun}}, {{PDB2|1je4}}, {{PDB2|2ffk}}, {{PDB2|2fin}}
 | Name = Chemokine (C-C motif) ligand 4
 | HGNCid = 10630
 | Symbol = CCL4
 | AltSymbols =; SCYA2; ACT2; AT744.1; G-26; LAG1; MGC104418; MGC126025; MGC126026; MIP-1-beta; MIP1B; SCYA4
 | OMIM = 182284
 | ECnumber =  
 | Homologene = 48153
 | MGIid = 98261
 | GeneAtlas_image1 = PBB_GE_CCL4_204103_at_tn.png
 | Function = {{GNF_GO|id=GO:0004716 |text = receptor signaling protein tyrosine kinase activity}} {{GNF_GO|id=GO:0008009 |text = chemokine activity}} 
 | Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} 
 | Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007163 |text = establishment and/or maintenance of cell polarity}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0009615 |text = response to virus}} {{GNF_GO|id=GO:0019079 |text = viral genome replication}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6351
    | Hs_Ensembl = ENSG00000129277
    | Hs_RefseqProtein = NP_002975
    | Hs_RefseqmRNA = NM_002984
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 31455333
    | Hs_GenLoc_end = 31457127
    | Hs_Uniprot = P13236
    | Mm_EntrezGene = 20303
    | Mm_Ensembl = ENSMUSG00000018930
    | Mm_RefseqmRNA = NM_013652
    | Mm_RefseqProtein = NP_038680
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 83478782
    | Mm_GenLoc_end = 83480875
    | Mm_Uniprot = Q5QNV9
  }}
}}
'''Chemokine (C-C motif) ligand 4''', also known as '''CCL4''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = 
}}

==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Menten P, Wuyts A, Van Damme J |title=Macrophage inflammatory protein-1. |journal=Cytokine Growth Factor Rev. |volume=13 |issue= 6 |pages= 455-81 |year= 2003 |pmid= 12401480 |doi=  }}
*{{cite journal  | author=Muthumani K, Desai BM, Hwang DS, ''et al.'' |title=HIV-1 Vpr and anti-inflammatory activity. |journal=DNA Cell Biol. |volume=23 |issue= 4 |pages= 239-47 |year= 2004 |pmid= 15142381 |doi= 10.1089/104454904773819824 }}
*{{cite journal  | author=Conti L, Fantuzzi L, Del Cornò M, ''et al.'' |title=Immunomodulatory effects of the HIV-1 gp120 protein on antigen presenting cells: implications for AIDS pathogenesis. |journal=Immunobiology |volume=209 |issue= 1-2 |pages= 99-115 |year= 2005 |pmid= 15481145 |doi=  }}
*{{cite journal  | author=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87-94 |year= 2005 |pmid= 15638726 |doi=  }}
*{{cite journal  | author=Zhao RY, Elder RT |title=Viral infections and cell cycle G2/M regulation. |journal=Cell Res. |volume=15 |issue= 3 |pages= 143-9 |year= 2005 |pmid= 15780175 |doi= 10.1038/sj.cr.7290279 }}
*{{cite journal  | author=Zhao RY, Bukrinsky M, Elder RT |title=HIV-1 viral protein R (Vpr) & host cellular responses. |journal=Indian J. Med. Res. |volume=121 |issue= 4 |pages= 270-86 |year= 2005 |pmid= 15817944 |doi=  }}
*{{cite journal  | author=Li L, Li HS, Pauza CD, ''et al.'' |title=Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions. |journal=Cell Res. |volume=15 |issue= 11-12 |pages= 923-34 |year= 2006 |pmid= 16354571 |doi= 10.1038/sj.cr.7290370 }}
*{{cite journal  | author=King JE, Eugenin EA, Buckner CM, Berman JW |title=HIV tat and neurotoxicity. |journal=Microbes Infect. |volume=8 |issue= 5 |pages= 1347-57 |year= 2006 |pmid= 16697675 |doi= 10.1016/j.micinf.2005.11.014 }}
*{{cite journal  | author=Napolitano M, Modi WS, Cevario SJ, ''et al.'' |title=The gene encoding the Act-2 cytokine. Genomic structure, HTLV-I/Tax responsiveness of 5' upstream sequences, and chromosomal localization. |journal=J. Biol. Chem. |volume=266 |issue= 26 |pages= 17531-6 |year= 1991 |pmid= 1894635 |doi=  }}
*{{cite journal  | author=Irving SG, Zipfel PF, Balke J, ''et al.'' |title=Two inflammatory mediator cytokine genes are closely linked and variably amplified on chromosome 17q. |journal=Nucleic Acids Res. |volume=18 |issue= 11 |pages= 3261-70 |year= 1990 |pmid= 1972563 |doi=  }}
*{{cite journal  | author=Baixeras E, Roman-Roman S, Jitsukawa S, ''et al.'' |title=Cloning and expression of a lymphocyte activation gene (LAG-1). |journal=Mol. Immunol. |volume=27 |issue= 11 |pages= 1091-102 |year= 1991 |pmid= 2247088 |doi=  }}
*{{cite journal  | author=Lipes MA, Napolitano M, Jeang KT, ''et al.'' |title=Identification, cloning, and characterization of an immune activation gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 24 |pages= 9704-8 |year= 1989 |pmid= 2462251 |doi=  }}
*{{cite journal  | author=Brown KD, Zurawski SM, Mosmann TR, Zurawski G |title=A family of small inducible proteins secreted by leukocytes are members of a new superfamily that includes leukocyte and fibroblast-derived inflammatory agents, growth factors, and indicators of various activation processes. |journal=J. Immunol. |volume=142 |issue= 2 |pages= 679-87 |year= 1989 |pmid= 2521353 |doi=  }}
*{{cite journal  | author=Zipfel PF, Balke J, Irving SG, ''et al.'' |title=Mitogenic activation of human T cells induces two closely related genes which share structural similarities with a new family of secreted factors. |journal=J. Immunol. |volume=142 |issue= 5 |pages= 1582-90 |year= 1989 |pmid= 2521882 |doi=  }}
*{{cite journal  | author=Chang HC, Reinherz EL |title=Isolation and characterization of a cDNA encoding a putative cytokine which is induced by stimulation via the CD2 structure on human T lymphocytes. |journal=Eur. J. Immunol. |volume=19 |issue= 6 |pages= 1045-51 |year= 1989 |pmid= 2568930 |doi=  }}
*{{cite journal  | author=Miller MD, Hata S, De Waal Malefyt R, Krangel MS |title=A novel polypeptide secreted by activated human T lymphocytes. |journal=J. Immunol. |volume=143 |issue= 9 |pages= 2907-16 |year= 1989 |pmid= 2809212 |doi=  }}
*{{cite journal  | author=Adams MD, Kerlavage AR, Fleischmann RD, ''et al.'' |title=Initial assessment of human gene diversity and expression patterns based upon 83 million nucleotides of cDNA sequence. |journal=Nature |volume=377 |issue= 6547 Suppl |pages= 3-174 |year= 1995 |pmid= 7566098 |doi=  }}
*{{cite journal  | author=Post TW, Bozic CR, Rothenberg ME, ''et al.'' |title=Molecular characterization of two murine eosinophil beta chemokine receptors. |journal=J. Immunol. |volume=155 |issue= 11 |pages= 5299-305 |year= 1995 |pmid= 7594543 |doi=  }}
*{{cite journal  | author=Combadiere C, Ahuja SK, Murphy PM |title=Cloning and functional expression of a human eosinophil CC chemokine receptor. |journal=J. Biol. Chem. |volume=270 |issue= 28 |pages= 16491-4 |year= 1995 |pmid= 7622448 |doi=  }}
*{{cite journal  | author=Paolini JF, Willard D, Consler T, ''et al.'' |title=The chemokines IL-8, monocyte chemoattractant protein-1, and I-309 are monomers at physiologically relevant concentrations. |journal=J. Immunol. |volume=153 |issue= 6 |pages= 2704-17 |year= 1994 |pmid= 8077676 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

COL4A5

• INFO: Beginning work on COL4A5... {November 14, 2007 2:35:59 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:36:34 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Collagen, type IV, alpha 5 (Alport syndrome)
 | HGNCid = 2207
 | Symbol = COL4A5
 | AltSymbols =; ASLN; ATS; CA54; MGC42377
 | OMIM = 303630
 | ECnumber =  
 | Homologene = 22422
 | MGIid = 88456
 | Function = {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}} 
 | Component = {{GNF_GO|id=GO:0005581 |text = collagen}} {{GNF_GO|id=GO:0005587 |text = collagen type IV}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} 
 | Process = {{GNF_GO|id=GO:0006817 |text = phosphate transport}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1287
    | Hs_Ensembl = ENSG00000188153
    | Hs_RefseqProtein = NP_000486
    | Hs_RefseqmRNA = NM_000495
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = X
    | Hs_GenLoc_start = 107569810
    | Hs_GenLoc_end = 107827431
    | Hs_Uniprot = P29400
    | Mm_EntrezGene = 12830
    | Mm_Ensembl = ENSMUSG00000031274
    | Mm_RefseqmRNA = XM_623033
    | Mm_RefseqProtein = XP_623033
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = X
    | Mm_GenLoc_start = 136721787
    | Mm_GenLoc_end = 136935548
    | Mm_Uniprot =  
  }}
}}
'''Collagen, type IV, alpha 5 (Alport syndrome)''', also known as '''COL4A5''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene encodes one of the six subunits of type IV collagen, the major structural component of basement membranes. Mutations in this gene are associated with X-linked Alport syndrome, also known as hereditary nephritis. Like the other members of the type IV collagen gene family, this gene is organized in a head-to-head conformation with another type IV collagen gene so that each gene pair shares a common promoter. Three transcript variants have been identified for this gene.<ref>{{cite web | title = Entrez Gene: COL4A5 collagen, type IV, alpha 5 (Alport syndrome)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1287| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Lemmink HH, Schröder CH, Monnens LA, Smeets HJ |title=The clinical spectrum of type IV collagen mutations. |journal=Hum. Mutat. |volume=9 |issue= 6 |pages= 477-99 |year= 1997 |pmid= 9195222 |doi= 10.1002/(SICI)1098-1004(1997)9:6<477::AID-HUMU1>3.0.CO;2-# }}
*{{cite journal  | author=Ständer M, Naumann U, Wick W, Weller M |title=Transforming growth factor-beta and p-21: multiple molecular targets of decorin-mediated suppression of neoplastic growth. |journal=Cell Tissue Res. |volume=296 |issue= 2 |pages= 221-7 |year= 1999 |pmid= 10382266 |doi=  }}
*{{cite journal  | author=Kurpakus Wheater M, Kernacki KA, Hazlett LD |title=Corneal cell proteins and ocular surface pathology. |journal=Biotechnic & histochemistry : official publication of the Biological Stain Commission |volume=74 |issue= 3 |pages= 146-59 |year= 1999 |pmid= 10416788 |doi=  }}
*{{cite journal  | author=Zhou J, Hertz JM, Leinonen A, Tryggvason K |title=Complete amino acid sequence of the human alpha 5 (IV) collagen chain and identification of a single-base mutation in exon 23 converting glycine 521 in the collagenous domain to cysteine in an Alport syndrome patient. |journal=J. Biol. Chem. |volume=267 |issue= 18 |pages= 12475-81 |year= 1992 |pmid= 1352287 |doi=  }}
*{{cite journal  | author=Renieri A, Seri M, Myers JC, ''et al.'' |title=De novo mutation in the COL4A5 gene converting glycine 325 to glutamic acid in Alport syndrome. |journal=Hum. Mol. Genet. |volume=1 |issue= 2 |pages= 127-9 |year= 1993 |pmid= 1363780 |doi=  }}
*{{cite journal  | author=Knebelmann B, Deschenes G, Gros F, ''et al.'' |title=Substitution of arginine for glycine 325 in the collagen alpha 5 (IV) chain associated with X-linked Alport syndrome: characterization of the mutation by direct sequencing of PCR-amplified lymphoblast cDNA fragments. |journal=Am. J. Hum. Genet. |volume=51 |issue= 1 |pages= 135-42 |year= 1992 |pmid= 1376965 |doi=  }}
*{{cite journal  | author=Ghebrehiwet B, Peerschke EI, Hong Y, ''et al.'' |title=Short amino acid sequences derived from C1q receptor (C1q-R) show homology with the alpha chains of fibronectin and vitronectin receptors and collagen type IV. |journal=J. Leukoc. Biol. |volume=51 |issue= 6 |pages= 546-56 |year= 1992 |pmid= 1377218 |doi=  }}
*{{cite journal  | author=Zhou J, Barker DF, Hostikka SL, ''et al.'' |title=Single base mutation in alpha 5(IV) collagen chain gene converting a conserved cysteine to serine in Alport syndrome. |journal=Genomics |volume=9 |issue= 1 |pages= 10-8 |year= 1991 |pmid= 1672282 |doi=  }}
*{{cite journal  | author=Hostikka SL, Eddy RL, Byers MG, ''et al.'' |title=Identification of a distinct type IV collagen alpha chain with restricted kidney distribution and assignment of its gene to the locus of X chromosome-linked Alport syndrome. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 4 |pages= 1606-10 |year= 1990 |pmid= 1689491 |doi=  }}
*{{cite journal  | author=Gupta S, Batchu RB, Datta K |title=Purification, partial characterization of rat kidney hyaluronic acid binding protein and its localization on the cell surface. |journal=Eur. J. Cell Biol. |volume=56 |issue= 1 |pages= 58-67 |year= 1992 |pmid= 1724753 |doi=  }}
*{{cite journal  | author=Zhou J, Hostikka SL, Chow LT, Tryggvason K |title=Characterization of the 3' half of the human type IV collagen alpha 5 gene that is affected in the Alport syndrome. |journal=Genomics |volume=9 |issue= 1 |pages= 1-9 |year= 1991 |pmid= 2004755 |doi=  }}
*{{cite journal  | author=Myers JC, Jones TA, Pohjolainen ER, ''et al.'' |title=Molecular cloning of alpha 5(IV) collagen and assignment of the gene to the region of the X chromosome containing the Alport syndrome locus. |journal=Am. J. Hum. Genet. |volume=46 |issue= 6 |pages= 1024-33 |year= 1990 |pmid= 2339699 |doi=  }}
*{{cite journal  | author=Barker DF, Hostikka SL, Zhou J, ''et al.'' |title=Identification of mutations in the COL4A5 collagen gene in Alport syndrome. |journal=Science |volume=248 |issue= 4960 |pages= 1224-7 |year= 1990 |pmid= 2349482 |doi=  }}
*{{cite journal  | author=Pihlajaniemi T, Pohjolainen ER, Myers JC |title=Complete primary structure of the triple-helical region and the carboxyl-terminal domain of a new type IV collagen chain, alpha 5(IV). |journal=J. Biol. Chem. |volume=265 |issue= 23 |pages= 13758-66 |year= 1990 |pmid= 2380186 |doi=  }}
*{{cite journal  | author=Hernandez MR, Igoe F, Neufeld AH |title=Extracellular matrix of the human optic nerve head. |journal=Am. J. Ophthalmol. |volume=102 |issue= 2 |pages= 139-48 |year= 1986 |pmid= 2426947 |doi=  }}
*{{cite journal  | author=Glant TT, Hadházy C, Mikecz K, Sipos A |title=Appearance and persistence of fibronectin in cartilage. Specific interaction of fibronectin with collagen type II. |journal=Histochemistry |volume=82 |issue= 2 |pages= 149-58 |year= 1985 |pmid= 3997552 |doi=  }}
*{{cite journal  | author=Matsubara T, Trüeb B, Fehr K, ''et al.'' |title=The localization and secretion of type IV collagen in synovial capillaries by immunohistochemistry using a monoclonal antibody against human type IV collagen. |journal=Exp. Cell Biol. |volume=52 |issue= 3 |pages= 159-69 |year= 1984 |pmid= 6386565 |doi=  }}
*{{cite journal  | author=Uscanga L, Kennedy RH, Stocker S, ''et al.'' |title=Immunolocalization of collagen types, laminin and fibronectin in the normal human pancreas. |journal=Digestion |volume=30 |issue= 3 |pages= 158-64 |year= 1984 |pmid= 6389236 |doi=  }}
*{{cite journal  | author=Sundarraj N, Willson J |title=Monoclonal antibody to human basement membrane collagen type IV. |journal=Immunology |volume=47 |issue= 1 |pages= 133-40 |year= 1982 |pmid= 6811420 |doi=  }}
*{{cite journal  | author=Hahn E, Wick G, Pencev D, Timpl R |title=Distribution of basement membrane proteins in normal and fibrotic human liver: collagen type IV, laminin, and fibronectin. |journal=Gut |volume=21 |issue= 1 |pages= 63-71 |year= 1980 |pmid= 6988303 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

COL7A1

• INFO: Beginning work on COL7A1... {November 14, 2007 2:36:34 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:37:02 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Collagen, type VII, alpha 1 (epidermolysis bullosa, dystrophic, dominant and recessive)
 | HGNCid = 2214
 | Symbol = COL7A1
 | AltSymbols =; EBD1; EBDCT; EBR1
 | OMIM = 120120
 | ECnumber =  
 | Homologene = 73
 | MGIid = 88462
 | GeneAtlas_image1 = PBB_GE_COL7A1_204136_at_tn.png
 | GeneAtlas_image2 = PBB_GE_COL7A1_217312_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0005590 |text = collagen type VII}} {{GNF_GO|id=GO:0005604 |text = basement membrane}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} 
 | Process = {{GNF_GO|id=GO:0006817 |text = phosphate transport}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0008544 |text = epidermis development}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1294
    | Hs_Ensembl = ENSG00000114270
    | Hs_RefseqProtein = NP_000085
    | Hs_RefseqmRNA = NM_000094
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 48576510
    | Hs_GenLoc_end = 48607704
    | Hs_Uniprot = Q02388
    | Mm_EntrezGene = 12836
    | Mm_Ensembl = ENSMUSG00000025650
    | Mm_RefseqmRNA = NM_007738
    | Mm_RefseqProtein = NP_031764
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 108810682
    | Mm_GenLoc_end = 108841157
    | Mm_Uniprot =  
  }}
}}
'''Collagen, type VII, alpha 1 (epidermolysis bullosa, dystrophic, dominant and recessive)''', also known as '''COL7A1''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene encodes the alpha chain of type VII collagen. The type VII collagen fibril, composed of three identical alpha collagen chains, is restricted to the basement zone beneath stratified squamous epithelia. It functions as an anchoring fibril between the external epithelia and the underlying stroma. Mutations in this gene are associated with all forms of dystrophic epidermolysis bullosa. In the absence of mutations, however, an acquired form of this disease can result from an autoimmune response made to type VII collagen.<ref>{{cite web | title = Entrez Gene: COL7A1 collagen, type VII, alpha 1 (epidermolysis bullosa, dystrophic, dominant and recessive)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1294| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Mecklenbeck S, Hammami-Hauasli N, Höpfner B, ''et al.'' |title=Clustering of COL7A1 mutations in exon 73: implications for mutation analysis in dystrophic epidermolysis bullosa. |journal=J. Invest. Dermatol. |volume=112 |issue= 3 |pages= 398-400 |year= 1999 |pmid= 10084325 |doi= 10.1046/j.1523-1747.1999.00518.x }}
*{{cite journal  | author=Dang N, Klingberg S, Marr P, Murrell DF |title=Review of collagen VII sequence variants found in Australasian patients with dystrophic epidermolysis bullosa reveals nine novel COL7A1 variants. |journal=J. Dermatol. Sci. |volume=46 |issue= 3 |pages= 169-78 |year= 2007 |pmid= 17425959 |doi= 10.1016/j.jdermsci.2007.02.006 }}
*{{cite journal  | author=Christiano AM, Rosenbaum LM, Chung-Honet LC, ''et al.'' |title=The large non-collagenous domain (NC-1) of type VII collagen is amino-terminal and chimeric. Homology to cartilage matrix protein, the type III domains of fibronectin and the A domains of von Willebrand factor. |journal=Hum. Mol. Genet. |volume=1 |issue= 7 |pages= 475-81 |year= 1993 |pmid= 1307247 |doi=  }}
*{{cite journal  | author=Gammon WR, Abernethy ML, Padilla KM, ''et al.'' |title=Noncollagenous (NC1) domain of collagen VII resembles multidomain adhesion proteins involved in tissue-specific organization of extracellular matrix. |journal=J. Invest. Dermatol. |volume=99 |issue= 6 |pages= 691-6 |year= 1993 |pmid= 1469284 |doi=  }}
*{{cite journal  | author=Tanaka T, Takahashi K, Furukawa F, Imamura S |title=Molecular cloning and characterization of type VII collagen cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=183 |issue= 3 |pages= 958-63 |year= 1992 |pmid= 1567409 |doi=  }}
*{{cite journal  | author=Parente MG, Chung LC, Ryynänen J, ''et al.'' |title=Human type VII collagen: cDNA cloning and chromosomal mapping of the gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 16 |pages= 6931-5 |year= 1991 |pmid= 1871109 |doi=  }}
*{{cite journal  | author=Seltzer JL, Eisen AZ, Bauer EA, ''et al.'' |title=Cleavage of type VII collagen by interstitial collagenase and type IV collagenase (gelatinase) derived from human skin. |journal=J. Biol. Chem. |volume=264 |issue= 7 |pages= 3822-6 |year= 1989 |pmid= 2537292 |doi=  }}
*{{cite journal  | author=Fine JD, Johnson L, Wright T |title=Epidermolysis bullosa simplex superficialis. A new variant of epidermolysis bullosa characterized by subcorneal skin cleavage mimicking peeling skin syndrome. |journal=Archives of dermatology |volume=125 |issue= 5 |pages= 633-8 |year= 1989 |pmid= 2653224 |doi=  }}
*{{cite journal  | author=Bart BJ, Gorlin RJ, Anderson VE, Lynch FW |title=Congenital localized absence of skin and associated abnormalities resembling epidermolysis bullosa. A new syndrome. |journal=Archives of dermatology |volume=93 |issue= 3 |pages= 296-304 |year= 1966 |pmid= 5910871 |doi=  }}
*{{cite journal  | author=Tanaka T, Furukawa F, Imamura S |title=Epitope mapping for epidermolysis bullosa acquisita autoantibody by molecularly cloned cDNA for type VII collagen. |journal=J. Invest. Dermatol. |volume=102 |issue= 5 |pages= 706-9 |year= 1994 |pmid= 7513737 |doi=  }}
*{{cite journal  | author=Christiano AM, Morricone A, Paradisi M, ''et al.'' |title=A glycine-to-arginine substitution in the triple-helical domain of type VII collagen in a family with dominant dystrophic epidermolysis bullosa. |journal=J. Invest. Dermatol. |volume=104 |issue= 3 |pages= 438-40 |year= 1995 |pmid= 7861014 |doi=  }}
*{{cite journal  | author=Christiano AM, Suga Y, Greenspan DS, ''et al.'' |title=Premature termination codons on both alleles of the type VII collagen gene (COL7A1) in three brothers with recessive dystrophic epidermolysis bullosa. |journal=J. Clin. Invest. |volume=95 |issue= 3 |pages= 1328-34 |year= 1995 |pmid= 7883979 |doi=  }}
*{{cite journal  | author=Lapiere JC, Chen JD, Iwasaki T, ''et al.'' |title=Type VII collagen specifically binds fibronectin via a unique subdomain within the collagenous triple helix. |journal=J. Invest. Dermatol. |volume=103 |issue= 5 |pages= 637-41 |year= 1994 |pmid= 7963647 |doi=  }}
*{{cite journal  | author=Christiano AM, Greenspan DS, Lee S, Uitto J |title=Cloning of human type VII collagen. Complete primary sequence of the alpha 1(VII) chain and identification of intragenic polymorphisms. |journal=J. Biol. Chem. |volume=269 |issue= 32 |pages= 20256-62 |year= 1994 |pmid= 8051117 |doi=  }}
*{{cite journal  | author=Christiano AM, Hoffman GG, Chung-Honet LC, ''et al.'' |title=Structural organization of the human type VII collagen gene (COL7A1), composed of more exons than any previously characterized gene. |journal=Genomics |volume=21 |issue= 1 |pages= 169-79 |year= 1994 |pmid= 8088784 |doi= 10.1006/geno.1994.1239 }}
*{{cite journal  | author=Christiano AM, Ryynänen M, Uitto J |title=Dominant dystrophic epidermolysis bullosa: identification of a Gly-->Ser substitution in the triple-helical domain of type VII collagen. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 9 |pages= 3549-53 |year= 1994 |pmid= 8170945 |doi=  }}
*{{cite journal  | author=Greenspan DS, Byers MG, Eddy RL, ''et al.'' |title=Localization of the human collagen gene COL7A1 to 3p21.3 by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=62 |issue= 1 |pages= 35-6 |year= 1993 |pmid= 8422754 |doi=  }}
*{{cite journal  | author=Greenspan DS |title=The carboxyl-terminal half of type VII collagen, including the non-collagenous NC-2 domain and intron/exon organization of the corresponding region of the COL7A1 gene. |journal=Hum. Mol. Genet. |volume=2 |issue= 3 |pages= 273-8 |year= 1993 |pmid= 8499916 |doi=  }}
*{{cite journal  | author=Christiano AM, Greenspan DS, Hoffman GG, ''et al.'' |title=A missense mutation in type VII collagen in two affected siblings with recessive dystrophic epidermolysis bullosa. |journal=Nat. Genet. |volume=4 |issue= 1 |pages= 62-6 |year= 1993 |pmid= 8513326 |doi= 10.1038/ng0593-62 }}
*{{cite journal  | author=Christiano AM, Lee JY, Chen WJ, ''et al.'' |title=Pretibial epidermolysis bullosa: genetic linkage to COL7A1 and identification of a glycine-to-cysteine substitution in the triple-helical domain of type VII collagen. |journal=Hum. Mol. Genet. |volume=4 |issue= 9 |pages= 1579-83 |year= 1996 |pmid= 8541842 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

F11

• INFO: Beginning work on F11... {November 14, 2007 2:37:37 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:38:04 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_F11_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1xx9.
 | PDB = {{PDB2|1xx9}}, {{PDB2|1xxd}}, {{PDB2|1xxf}}, {{PDB2|1zhm}}, {{PDB2|1zhp}}, {{PDB2|1zhr}}, {{PDB2|1zjd}}, {{PDB2|1zlr}}, {{PDB2|1zmj}}, {{PDB2|1zml}}, {{PDB2|1zmn}}, {{PDB2|1zom}}, {{PDB2|1zpb}}, {{PDB2|1zpc}}, {{PDB2|1zpz}}, {{PDB2|1zrk}}, {{PDB2|1zsj}}, {{PDB2|1zsk}}, {{PDB2|1zsl}}, {{PDB2|1ztj}}, {{PDB2|1ztk}}, {{PDB2|1ztl}}, {{PDB2|2f83}}, {{PDB2|2fda}}
 | Name = Coagulation factor XI (plasma thromboplastin antecedent)
 | HGNCid = 3529
 | Symbol = F11
 | AltSymbols =; FXI; MGC141891
 | OMIM = 264900
 | ECnumber =  
 | Homologene = 86654
 | MGIid = 99481
 | GeneAtlas_image1 = PBB_GE_F11_206610_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0003803 |text = coagulation factor IXa activity}} {{GNF_GO|id=GO:0003805 |text = coagulation factor XIa activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} {{GNF_GO|id=GO:0008233 |text = peptidase activity}} 
 | Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0016020 |text = membrane}} 
 | Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2160
    | Hs_Ensembl = ENSG00000088926
    | Hs_RefseqProtein = NP_062505
    | Hs_RefseqmRNA = NM_019559
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 4
    | Hs_GenLoc_start = 187424272
    | Hs_GenLoc_end = 187446928
    | Hs_Uniprot = P03951
    | Mm_EntrezGene = 109821
    | Mm_Ensembl = ENSMUSG00000031645
    | Mm_RefseqmRNA = NM_028066
    | Mm_RefseqProtein = NP_082342
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 8
    | Mm_GenLoc_start = 46739987
    | Mm_GenLoc_end = 46760848
    | Mm_Uniprot = Q9DAT3
  }}
}}
'''Coagulation factor XI (plasma thromboplastin antecedent)''', also known as '''F11''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene encodes coagulation factor XI of the blood coagulation cascade. This protein is present in plasma as a zymogen, which is a unique plasma coagulation enzyme because it exists as a homodimer consisting of two identical polypeptide chains linked by disulfide bonds. During activation of the plasma factor XI, an internal peptide bond is cleaved by factor XIIa (or XII) in each of the two chains, resulting in activated factor XIa, a serine protease composed of two heavy and two light chains held together by disulfide bonds. This activated plasma factor XI triggers the middle phase of the intrisic pathway of blood coagulation by activating factor IX. Defects in this factor lead to Rosenthal syndrome, a blood coagulation abnormality.<ref>{{cite web | title = Entrez Gene: F11 coagulation factor XI (plasma thromboplastin antecedent)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2160| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Gailani D, Zivelin A, Sinha D, Walsh PN |title=Do platelets synthesize factor XI? |journal=J. Thromb. Haemost. |volume=2 |issue= 10 |pages= 1709-12 |year= 2005 |pmid= 15456479 |doi= 10.1111/j.1538-7836.2004.00935.x }}
*{{cite journal  | author=Dossenbach-Glaninger A, Hopmeier P |title=Coagulation factor XI: a database of mutations and polymorphisms associated with factor XI deficiency. |journal=Blood Coagul. Fibrinolysis |volume=16 |issue= 4 |pages= 231-8 |year= 2005 |pmid= 15870541 |doi=  }}
*{{cite journal  | author=Seligsohn U |title=Factor XI in haemostasis and thrombosis: past, present and future. |journal=Thromb. Haemost. |volume=98 |issue= 1 |pages= 84-9 |year= 2007 |pmid= 17597996 |doi=  }}
*{{cite journal  | author=Meijers JC, Davie EW, Chung DW |title=Expression of human blood coagulation factor XI: characterization of the defect in factor XI type III deficiency. |journal=Blood |volume=79 |issue= 6 |pages= 1435-40 |year= 1992 |pmid= 1547342 |doi=  }}
*{{cite journal  | author=Gailani D, Broze GJ |title=Factor XI activation in a revised model of blood coagulation. |journal=Science |volume=253 |issue= 5022 |pages= 909-12 |year= 1991 |pmid= 1652157 |doi=  }}
*{{cite journal  | author=Buetow KH, Shiang R, Yang P, ''et al.'' |title=A detailed multipoint map of human chromosome 4 provides evidence for linkage heterogeneity and position-specific recombination rates. |journal=Am. J. Hum. Genet. |volume=48 |issue= 5 |pages= 911-25 |year= 1991 |pmid= 1673289 |doi=  }}
*{{cite journal  | author=Bodfish P, Warne D, Watkins C, ''et al.'' |title=Dinucleotide repeat polymorphism in the human coagulation factor XI gene, intron B (F11), detected using the polymerase chain reaction. |journal=Nucleic Acids Res. |volume=19 |issue= 24 |pages= 6979 |year= 1992 |pmid= 1762944 |doi=  }}
*{{cite journal  | author=Clarkson K, Rosenfeld B, Fair J, ''et al.'' |title=Factor XI deficiency acquired by liver transplantation. |journal=Ann. Intern. Med. |volume=115 |issue= 11 |pages= 877-9 |year= 1991 |pmid= 1952475 |doi=  }}
*{{cite journal  | author=McMullen BA, Fujikawa K, Davie EW |title=Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains. |journal=Biochemistry |volume=30 |issue= 8 |pages= 2056-60 |year= 1991 |pmid= 1998667 |doi=  }}
*{{cite journal  | author=Naito K, Fujikawa K |title=Activation of human blood coagulation factor XI independent of factor XII. Factor XI is activated by thrombin and factor XIa in the presence of negatively charged surfaces. |journal=J. Biol. Chem. |volume=266 |issue= 12 |pages= 7353-8 |year= 1991 |pmid= 2019570 |doi=  }}
*{{cite journal  | author=Asakai R, Chung DW, Davie EW, Seligsohn U |title=Factor XI deficiency in Ashkenazi Jews in Israel. |journal=N. Engl. J. Med. |volume=325 |issue= 3 |pages= 153-8 |year= 1991 |pmid= 2052060 |doi=  }}
*{{cite journal  | author=España F, Berrettini M, Griffin JH |title=Purification and characterization of plasma protein C inhibitor. |journal=Thromb. Res. |volume=55 |issue= 3 |pages= 369-84 |year= 1989 |pmid= 2551064 |doi=  }}
*{{cite journal  | author=Asakai R, Chung DW, Ratnoff OD, Davie EW |title=Factor XI (plasma thromboplastin antecedent) deficiency in Ashkenazi Jews is a bleeding disorder that can result from three types of point mutations. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 20 |pages= 7667-71 |year= 1989 |pmid= 2813350 |doi=  }}
*{{cite journal  | author=Asakai R, Davie EW, Chung DW |title=Organization of the gene for human factor XI. |journal=Biochemistry |volume=26 |issue= 23 |pages= 7221-8 |year= 1988 |pmid= 2827746 |doi=  }}
*{{cite journal  | author=Fujikawa K, Chung DW, Hendrickson LE, Davie EW |title=Amino acid sequence of human factor XI, a blood coagulation factor with four tandem repeats that are highly homologous with plasma prekallikrein. |journal=Biochemistry |volume=25 |issue= 9 |pages= 2417-24 |year= 1986 |pmid= 3636155 |doi=  }}
*{{cite journal  | author=Warn-Cramer BJ, Bajaj SP |title=Stoichiometry of binding of high molecular weight kininogen to factor XI/XIa. |journal=Biochem. Biophys. Res. Commun. |volume=133 |issue= 2 |pages= 417-22 |year= 1986 |pmid= 3936495 |doi=  }}
*{{cite journal  | author=Bouma BN, Vlooswijk RA, Griffin JH |title=Immunologic studies of human coagulation factor XI and its complex with high molecular weight kininogen. |journal=Blood |volume=62 |issue= 5 |pages= 1123-31 |year= 1983 |pmid= 6626744 |doi=  }}
*{{cite journal  | author=Tuszynski GP, Bevacqua SJ, Schmaier AH, ''et al.'' |title=Factor XI antigen and activity in human platelets. |journal=Blood |volume=59 |issue= 6 |pages= 1148-56 |year= 1982 |pmid= 7044446 |doi=  }}
*{{cite journal  | author=Imanaka Y, Lal K, Nishimura T, ''et al.'' |title=Identification of two novel mutations in non-Jewish factor XI deficiency. |journal=Br. J. Haematol. |volume=90 |issue= 4 |pages= 916-20 |year= 1995 |pmid= 7669672 |doi=  }}
*{{cite journal  | author=Pugh RE, McVey JH, Tuddenham EG, Hancock JF |title=Six point mutations that cause factor XI deficiency. |journal=Blood |volume=85 |issue= 6 |pages= 1509-16 |year= 1995 |pmid= 7888672 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

GCG

• INFO: Beginning work on GCG... {November 14, 2007 2:38:04 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:38:39 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_GCG_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1d0r.
 | PDB = {{PDB2|1d0r}}, {{PDB2|1gcn}}, {{PDB2|1kx6}}, {{PDB2|2g49}}
 | Name = Glucagon
 | HGNCid = 4191
 | Symbol = GCG
 | AltSymbols =; GLP1; GLP2; GRPP
 | OMIM = 138030
 | ECnumber =  
 | Homologene = 1553
 | MGIid = 95674
 | GeneAtlas_image1 = PBB_GE_GCG_206422_at_tn.png
 | Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}} 
 | Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}} 
 | Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007631 |text = feeding behavior}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0050796 |text = regulation of insulin secretion}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2641
    | Hs_Ensembl = ENSG00000115263
    | Hs_RefseqProtein = NP_002045
    | Hs_RefseqmRNA = NM_002054
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 162708779
    | Hs_GenLoc_end = 162713934
    | Hs_Uniprot = P01275
    | Mm_EntrezGene = 14526
    | Mm_Ensembl = ENSMUSG00000000394
    | Mm_RefseqmRNA = NM_008100
    | Mm_RefseqProtein = NP_032126
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 62275369
    | Mm_GenLoc_end = 62284489
    | Mm_Uniprot = P55095
  }}
}}
'''Glucagon''', also known as '''GCG''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The protein encoded by this gene is actually a preproprotein that is cleaved into four distinct mature peptides. One of these, glucagon, is a pancreatic hormone that counteracts the glucose-lowering action of insulin by stimulating glycogenolysis and gluconeogenesis. Glucagon is a ligand for a specific G-protein linked receptor whose signalling pathway controls cell proliferation. Two of the other peptides are secreted from gut endocrine cells and promote nutrient absorption through distinct mechanisms. Finally, the fourth peptide is similar to glicentin, an active enteroglucagon.<ref>{{cite web | title = Entrez Gene: GCG glucagon| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2641| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Kieffer TJ, Habener JF |title=The glucagon-like peptides. |journal=Endocr. Rev. |volume=20 |issue= 6 |pages= 876-913 |year= 2000 |pmid= 10605628 |doi=  }}
*{{cite journal  | author=Drucker DJ |title=Glucagon-like peptides: regulators of cell proliferation, differentiation, and apoptosis. |journal=Mol. Endocrinol. |volume=17 |issue= 2 |pages= 161-71 |year= 2003 |pmid= 12554744 |doi=  }}
*{{cite journal  | author=Jeppesen PB |title=Clinical significance of GLP-2 in short-bowel syndrome. |journal=J. Nutr. |volume=133 |issue= 11 |pages= 3721-4 |year= 2004 |pmid= 14608103 |doi=  }}
*{{cite journal  | author=Brubaker PL, Anini Y |title=Direct and indirect mechanisms regulating secretion of glucagon-like peptide-1 and glucagon-like peptide-2. |journal=Can. J. Physiol. Pharmacol. |volume=81 |issue= 11 |pages= 1005-12 |year= 2004 |pmid= 14719035 |doi= 10.1139/y03-107 }}
*{{cite journal  | author=Baggio LL, Drucker DJ |title=Clinical endocrinology and metabolism. Glucagon-like peptide-1 and glucagon-like peptide-2. |journal=Best Pract. Res. Clin. Endocrinol. Metab. |volume=18 |issue= 4 |pages= 531-54 |year= 2005 |pmid= 15533774 |doi= 10.1016/j.beem.2004.08.001 }}
*{{cite journal  | author=Holz GG, Chepurny OG |title=Diabetes outfoxed by GLP-1? |journal=Sci. STKE |volume=2005 |issue= 268 |pages= pe2 |year= 2006 |pmid= 15671479 |doi= 10.1126/stke.2682005pe2 }}
*{{cite journal  | author=Dunning BE, Foley JE, Ahrén B |title=Alpha cell function in health and disease: influence of glucagon-like peptide-1. |journal=Diabetologia |volume=48 |issue= 9 |pages= 1700-13 |year= 2006 |pmid= 16132964 |doi= 10.1007/s00125-005-1878-0 }}
*{{cite journal  | author=Gautier JF, Fetita S, Sobngwi E, Salaün-Martin C |title=Biological actions of the incretins GIP and GLP-1 and therapeutic perspectives in patients with type 2 diabetes. |journal=Diabetes Metab. |volume=31 |issue= 3 Pt 1 |pages= 233-42 |year= 2005 |pmid= 16142014 |doi=  }}
*{{cite journal  | author=De León DD, Crutchlow MF, Ham JY, Stoffers DA |title=Role of glucagon-like peptide-1 in the pathogenesis and treatment of diabetes mellitus. |journal=Int. J. Biochem. Cell Biol. |volume=38 |issue= 5-6 |pages= 845-59 |year= 2006 |pmid= 16202636 |doi= 10.1016/j.biocel.2005.07.011 }}
*{{cite journal  | author=Beglinger C, Degen L |title=Gastrointestinal satiety signals in humans--physiologic roles for GLP-1 and PYY? |journal=Physiol. Behav. |volume=89 |issue= 4 |pages= 460-4 |year= 2007 |pmid= 16828127 |doi= 10.1016/j.physbeh.2006.05.048 }}
*{{cite journal  | author=Stephens JW, Bain SC |title=Safety and adverse effects associated with GLP-1 analogues. |journal=Expert opinion on drug safety |volume=6 |issue= 4 |pages= 417-22 |year= 2007 |pmid= 17688385 |doi= 10.1517/14740338.6.4.417 }}
*{{cite journal  | author=Orskov C, Bersani M, Johnsen AH, ''et al.'' |title=Complete sequences of glucagon-like peptide-1 from human and pig small intestine. |journal=J. Biol. Chem. |volume=264 |issue= 22 |pages= 12826-9 |year= 1989 |pmid= 2753890 |doi=  }}
*{{cite journal  | author=Drucker DJ, Asa S |title=Glucagon gene expression in vertebrate brain. |journal=J. Biol. Chem. |volume=263 |issue= 27 |pages= 13475-8 |year= 1988 |pmid= 2901414 |doi=  }}
*{{cite journal  | author=Novak U, Wilks A, Buell G, McEwen S |title=Identical mRNA for preproglucagon in pancreas and gut. |journal=Eur. J. Biochem. |volume=164 |issue= 3 |pages= 553-8 |year= 1987 |pmid= 3569278 |doi=  }}
*{{cite journal  | author=White JW, Saunders GF |title=Structure of the human glucagon gene. |journal=Nucleic Acids Res. |volume=14 |issue= 12 |pages= 4719-30 |year= 1986 |pmid= 3725587 |doi=  }}
*{{cite journal  | author=Schroeder WT, Lopez LC, Harper ME, Saunders GF |title=Localization of the human glucagon gene (GCG) to chromosome segment 2q36----37. |journal=Cytogenet. Cell Genet. |volume=38 |issue= 1 |pages= 76-9 |year= 1984 |pmid= 6546710 |doi=  }}
*{{cite journal  | author=Bell GI, Sanchez-Pescador R, Laybourn PJ, Najarian RC |title=Exon duplication and divergence in the human preproglucagon gene. |journal=Nature |volume=304 |issue= 5924 |pages= 368-71 |year= 1983 |pmid= 6877358 |doi=  }}
*{{cite journal  | author=Kärgel HJ, Dettmer R, Etzold G, ''et al.'' |title=Action of rat liver cathepsin L on glucagon. |journal=Acta Biol. Med. Ger. |volume=40 |issue= 9 |pages= 1139-43 |year= 1982 |pmid= 7340337 |doi=  }}
*{{cite journal  | author=Wayman GA, Impey S, Wu Z, ''et al.'' |title=Synergistic activation of the type I adenylyl cyclase by Ca2+ and Gs-coupled receptors in vivo. |journal=J. Biol. Chem. |volume=269 |issue= 41 |pages= 25400-5 |year= 1994 |pmid= 7929237 |doi=  }}
*{{cite journal  | author=Unson CG, Macdonald D, Merrifield RB |title=The role of histidine-1 in glucagon action. |journal=Arch. Biochem. Biophys. |volume=300 |issue= 2 |pages= 747-50 |year= 1993 |pmid= 8382034 |doi= 10.1006/abbi.1993.1103 }}
}}
{{refend}}

{{protein-stub}}
 

GCK

• INFO: Beginning work on GCK... {November 14, 2007 2:38:39 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:39:18 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_GCK_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1v4s.
 | PDB = {{PDB2|1v4s}}, {{PDB2|1v4t}}
 | Name = Glucokinase (hexokinase 4, maturity onset diabetes of the young 2)
 | HGNCid = 4195
 | Symbol = GCK
 | AltSymbols =; GK; GLK; HHF3; HK4; HKIV; HXKP; MODY2
 | OMIM = 138079
 | ECnumber =  
 | Homologene = 55440
 | MGIid = 1270854
 | GeneAtlas_image1 = PBB_GE_GCK_211167_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004340 |text = glucokinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0005536 |text = glucose binding}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} 
 | Component = 
 | Process = {{GNF_GO|id=GO:0006006 |text = glucose metabolic process}} {{GNF_GO|id=GO:0006096 |text = glycolysis}} {{GNF_GO|id=GO:0032024 |text = positive regulation of insulin secretion}} {{GNF_GO|id=GO:0042593 |text = glucose homeostasis}} {{GNF_GO|id=GO:0045721 |text = negative regulation of gluconeogenesis}} {{GNF_GO|id=GO:0045725 |text = positive regulation of glycogen biosynthetic process}} {{GNF_GO|id=GO:0051594 |text = detection of glucose}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2645
    | Hs_Ensembl = ENSG00000106633
    | Hs_RefseqProtein = NP_000153
    | Hs_RefseqmRNA = NM_000162
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 44150395
    | Hs_GenLoc_end = 44195563
    | Hs_Uniprot = P35557
    | Mm_EntrezGene = 103988
    | Mm_Ensembl = ENSMUSG00000041798
    | Mm_RefseqmRNA = NM_010292
    | Mm_RefseqProtein = NP_034422
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 5800826
    | Mm_GenLoc_end = 5850084
    | Mm_Uniprot = Q5SVI5
  }}
}}
'''Glucokinase (hexokinase 4, maturity onset diabetes of the young 2)''', also known as '''GCK''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. Alternative splicing of this gene results in three tissue-specific forms of glucokinase, one found in pancreatic islet beta cells and two found in liver. The protein localizes to the outer membrane of mitochondria. In contrast to other forms of hexokinase, this enzyme is not inhibited by its product glucose-6-phosphate but remains active while glucose is abundant. Mutations in this gene have been associated with non-insulin dependent diabetes mellitus (NIDDM), maturity onset diabetes of the young, type 2 (MODY2) and persistent hyperinsulinemic hypoglycemia of infancy (PHHI).<ref>{{cite web | title = Entrez Gene: GCK glucokinase (hexokinase 4, maturity onset diabetes of the young 2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2645| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Permutt MA, Chiu KC, Tanizawa Y |title=Glucokinase and NIDDM. A candidate gene that paid off. |journal=Diabetes |volume=41 |issue= 11 |pages= 1367-72 |year= 1992 |pmid= 1397713 |doi=  }}
*{{cite journal  | author=Gerbitz KD, Gempel K, Brdiczka D |title=Mitochondria and diabetes. Genetic, biochemical, and clinical implications of the cellular energy circuit. |journal=Diabetes |volume=45 |issue= 2 |pages= 113-26 |year= 1996 |pmid= 8549853 |doi=  }}
*{{cite journal  | author=Foster JD, Pederson BA, Nordlie RC |title=Glucose-6-phosphatase structure, regulation, and function: an update. |journal=Proc. Soc. Exp. Biol. Med. |volume=215 |issue= 4 |pages= 314-32 |year= 1997 |pmid= 9270716 |doi=  }}
*{{cite journal  | author=Postic C, Shiota M, Magnuson MA |title=Cell-specific roles of glucokinase in glucose homeostasis. |journal=Recent Prog. Horm. Res. |volume=56 |issue=  |pages= 195-217 |year= 2001 |pmid= 11237213 |doi=  }}
*{{cite journal  | author=Gloyn AL |title=Glucokinase (GCK) mutations in hyper- and hypoglycemia: maturity-onset diabetes of the young, permanent neonatal diabetes, and hyperinsulinemia of infancy. |journal=Hum. Mutat. |volume=22 |issue= 5 |pages= 353-62 |year= 2004 |pmid= 14517946 |doi= 10.1002/humu.10277 }}
*{{cite journal  | author=Stoffel M, Patel P, Lo YM, ''et al.'' |title=Missense glucokinase mutation in maturity-onset diabetes of the young and mutation screening in late-onset diabetes. |journal=Nat. Genet. |volume=2 |issue= 2 |pages= 153-6 |year= 1993 |pmid= 1303265 |doi= 10.1038/ng1092-153 }}
*{{cite journal  | author=Hattersley AT, Turner RC, Permutt MA, ''et al.'' |title=Linkage of type 2 diabetes to the glucokinase gene. |journal=Lancet |volume=339 |issue= 8805 |pages= 1307-10 |year= 1992 |pmid= 1349989 |doi=  }}
*{{cite journal  | author=Tanizawa Y, Matsutani A, Chiu KC, Permutt MA |title=Human glucokinase gene: isolation, structural characterization, and identification of a microsatellite repeat polymorphism. |journal=Mol. Endocrinol. |volume=6 |issue= 7 |pages= 1070-81 |year= 1992 |pmid= 1354840 |doi=  }}
*{{cite journal  | author=Katagiri H, Asano T, Ishihara H, ''et al.'' |title=Nonsense mutation of glucokinase gene in late-onset non-insulin-dependent diabetes mellitus. |journal=Lancet |volume=340 |issue= 8831 |pages= 1316-7 |year= 1992 |pmid= 1360036 |doi=  }}
*{{cite journal  | author=Sakura H, Eto K, Kadowaki H, ''et al.'' |title=Structure of the human glucokinase gene and identification of a missense mutation in a Japanese patient with early-onset non-insulin-dependent diabetes mellitus. |journal=J. Clin. Endocrinol. Metab. |volume=75 |issue= 6 |pages= 1571-3 |year= 1993 |pmid= 1464666 |doi=  }}
*{{cite journal  | author=Stoffel M, Froguel P, Takeda J, ''et al.'' |title=Human glucokinase gene: isolation, characterization, and identification of two missense mutations linked to early-onset non-insulin-dependent (type 2) diabetes mellitus. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 16 |pages= 7698-702 |year= 1992 |pmid= 1502186 |doi=  }}
*{{cite journal  | author=Nishi S, Stoffel M, Xiang K, ''et al.'' |title=Human pancreatic beta-cell glucokinase: cDNA sequence and localization of the polymorphic gene to chromosome 7, band p 13. |journal=Diabetologia |volume=35 |issue= 8 |pages= 743-7 |year= 1992 |pmid= 1511800 |doi=  }}
*{{cite journal  | author=Froguel P, Vaxillaire M, Sun F, ''et al.'' |title=Close linkage of glucokinase locus on chromosome 7p to early-onset non-insulin-dependent diabetes mellitus. |journal=Nature |volume=356 |issue= 6365 |pages= 162-4 |year= 1992 |pmid= 1545870 |doi= 10.1038/356162a0 }}
*{{cite journal  | author=Vionnet N, Stoffel M, Takeda J, ''et al.'' |title=Nonsense mutation in the glucokinase gene causes early-onset non-insulin-dependent diabetes mellitus. |journal=Nature |volume=356 |issue= 6371 |pages= 721-2 |year= 1992 |pmid= 1570017 |doi= 10.1038/356721a0 }}
*{{cite journal  | author=Koranyi LI, Tanizawa Y, Welling CM, ''et al.'' |title=Human islet glucokinase gene. Isolation and sequence analysis of full-length cDNA. |journal=Diabetes |volume=41 |issue= 7 |pages= 807-11 |year= 1992 |pmid= 1612194 |doi=  }}
*{{cite journal  | author=Matsutani A, Janssen R, Donis-Keller H, Permutt MA |title=A polymorphic (CA)n repeat element maps the human glucokinase gene (GCK) to chromosome 7p. |journal=Genomics |volume=12 |issue= 2 |pages= 319-25 |year= 1992 |pmid= 1740341 |doi=  }}
*{{cite journal  | author=Mishra SK, Helms C, Dorsey D, ''et al.'' |title=A 2-cM genetic linkage map of human chromosome 7p that includes 47 loci. |journal=Genomics |volume=12 |issue= 2 |pages= 326-34 |year= 1992 |pmid= 1740342 |doi=  }}
*{{cite journal  | author=Tanizawa Y, Koranyi LI, Welling CM, Permutt MA |title=Human liver glucokinase gene: cloning and sequence determination of two alternatively spliced cDNAs. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 16 |pages= 7294-7 |year= 1991 |pmid= 1871135 |doi=  }}
*{{cite journal  | author=Froguel P, Velho G |title=Non-sense mutation of glucokinase gene. |journal=Lancet |volume=341 |issue= 8841 |pages= 385 |year= 1993 |pmid= 8094163 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

H2AFX

• INFO: Beginning work on H2AFX... {November 14, 2007 2:39:54 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:40:28 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_H2AFX_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aoi.
 | PDB = {{PDB2|1aoi}}, {{PDB2|1eqz}}, {{PDB2|1hio}}, {{PDB2|1hq3}}, {{PDB2|1kx3}}, {{PDB2|1kx4}}, {{PDB2|1kx5}}, {{PDB2|1s32}}, {{PDB2|1tzy}}, {{PDB2|2aro}}, {{PDB2|2cv5}}, {{PDB2|2f8n}}, {{PDB2|2hio}}, {{PDB2|2nzd}}
 | Name = H2A histone family, member X
 | HGNCid = 4739
 | Symbol = H2AFX
 | AltSymbols =; H2A.X; H2A/X; H2AX
 | OMIM = 601772
 | ECnumber =  
 | Homologene = 68227
 | MGIid = 102688
 | GeneAtlas_image1 = PBB_GE_H2AFX_205436_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_H2AFX_212525_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0003684 |text = damaged DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0000786 |text = nucleosome}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005657 |text = replication fork}} {{GNF_GO|id=GO:0005694 |text = chromosome}} 
 | Process = {{GNF_GO|id=GO:0000724 |text = double-strand break repair via homologous recombination}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006310 |text = DNA recombination}} {{GNF_GO|id=GO:0006334 |text = nucleosome assembly}} {{GNF_GO|id=GO:0007001 |text = chromosome organization and biogenesis (sensu Eukaryota)}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007126 |text = meiosis}} {{GNF_GO|id=GO:0007283 |text = spermatogenesis}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3014
    | Hs_Ensembl = ENSG00000188486
    | Hs_RefseqProtein = NP_002096
    | Hs_RefseqmRNA = NM_002105
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 118469799
    | Hs_GenLoc_end = 118471369
    | Hs_Uniprot = P16104
    | Mm_EntrezGene = 15270
    | Mm_Ensembl = ENSMUSG00000049932
    | Mm_RefseqmRNA = NM_010436
    | Mm_RefseqProtein = NP_034566
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 44085689
    | Mm_GenLoc_end = 44087066
    | Mm_Uniprot = P27661
  }}
}}
'''H2A histone family, member X''', also known as '''H2AFX''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene encodes a member of the histone H2A family, and generates two transcripts through the use of the conserved stem-loop termination motif, and the polyA addition motif.<ref>{{cite web | title = Entrez Gene: H2AFX H2A histone family, member X| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3014| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Redon C, Pilch D, Rogakou E, ''et al.'' |title=Histone H2A variants H2AX and H2AZ. |journal=Curr. Opin. Genet. Dev. |volume=12 |issue= 2 |pages= 162-9 |year= 2002 |pmid= 11893489 |doi=  }}
*{{cite journal  | author=Fernandez-Capetillo O, Lee A, Nussenzweig M, Nussenzweig A |title=H2AX: the histone guardian of the genome. |journal=DNA Repair (Amst.) |volume=3 |issue= 8-9 |pages= 959-67 |year= 2005 |pmid= 15279782 |doi= 10.1016/j.dnarep.2004.03.024 }}
*{{cite journal  | author=Mannironi C, Bonner WM, Hatch CL |title=H2A.X. a histone isoprotein with a conserved C-terminal sequence, is encoded by a novel mRNA with both DNA replication type and polyA 3' processing signals. |journal=Nucleic Acids Res. |volume=17 |issue= 22 |pages= 9113-26 |year= 1990 |pmid= 2587254 |doi=  }}
*{{cite journal  | author=Banerjee S, Smallwood A, Hultén M |title=ATP-dependent reorganization of human sperm nuclear chromatin. |journal=J. Cell. Sci. |volume=108 ( Pt 2) |issue=  |pages= 755-65 |year= 1995 |pmid= 7769017 |doi=  }}
*{{cite journal  | author=Ivanova VS, Hatch CL, Bonner WM |title=Characterization of the human histone H2A.X gene. Comparison of its promoter with other H2A gene promoters. |journal=J. Biol. Chem. |volume=269 |issue= 39 |pages= 24189-94 |year= 1994 |pmid= 7929075 |doi=  }}
*{{cite journal  | author=Ivanova VS, Zimonjic D, Popescu N, Bonner WM |title=Chromosomal localization of the human histone H2A.X gene to 11q23.2-q23.3 by fluorescence in situ hybridization. |journal=Hum. Genet. |volume=94 |issue= 3 |pages= 303-6 |year= 1994 |pmid= 8076949 |doi=  }}
*{{cite journal  | author=Rogakou EP, Pilch DR, Orr AH, ''et al.'' |title=DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139. |journal=J. Biol. Chem. |volume=273 |issue= 10 |pages= 5858-68 |year= 1998 |pmid= 9488723 |doi=  }}
*{{cite journal  | author=El Kharroubi A, Piras G, Zensen R, Martin MA |title=Transcriptional activation of the integrated chromatin-associated human immunodeficiency virus type 1 promoter. |journal=Mol. Cell. Biol. |volume=18 |issue= 5 |pages= 2535-44 |year= 1998 |pmid= 9566873 |doi=  }}
*{{cite journal  | author=Rogakou EP, Boon C, Redon C, Bonner WM |title=Megabase chromatin domains involved in DNA double-strand breaks in vivo. |journal=J. Cell Biol. |volume=146 |issue= 5 |pages= 905-16 |year= 1999 |pmid= 10477747 |doi=  }}
*{{cite journal  | author=Rogakou EP, Nieves-Neira W, Boon C, ''et al.'' |title=Initiation of DNA fragmentation during apoptosis induces phosphorylation of H2AX histone at serine 139. |journal=J. Biol. Chem. |volume=275 |issue= 13 |pages= 9390-5 |year= 2000 |pmid= 10734083 |doi=  }}
*{{cite journal  | author=Paull TT, Rogakou EP, Yamazaki V, ''et al.'' |title=A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage. |journal=Curr. Biol. |volume=10 |issue= 15 |pages= 886-95 |year= 2001 |pmid= 10959836 |doi=  }}
*{{cite journal  | author=Deng L, de la Fuente C, Fu P, ''et al.'' |title=Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones. |journal=Virology |volume=277 |issue= 2 |pages= 278-95 |year= 2001 |pmid= 11080476 |doi= 10.1006/viro.2000.0593 }}
*{{cite journal  | author=Chen HT, Bhandoola A, Difilippantonio MJ, ''et al.'' |title=Response to RAG-mediated VDJ cleavage by NBS1 and gamma-H2AX. |journal=Science |volume=290 |issue= 5498 |pages= 1962-5 |year= 2000 |pmid= 11110662 |doi=  }}
*{{cite journal  | author=Chadwick BP, Willard HF |title=Histone H2A variants and the inactive X chromosome: identification of a second macroH2A variant. |journal=Hum. Mol. Genet. |volume=10 |issue= 10 |pages= 1101-13 |year= 2001 |pmid= 11331621 |doi=  }}
*{{cite journal  | author=Burma S, Chen BP, Murphy M, ''et al.'' |title=ATM phosphorylates histone H2AX in response to DNA double-strand breaks. |journal=J. Biol. Chem. |volume=276 |issue= 45 |pages= 42462-7 |year= 2001 |pmid= 11571274 |doi= 10.1074/jbc.C100466200 }}
*{{cite journal  | author=Ward IM, Chen J |title=Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress. |journal=J. Biol. Chem. |volume=276 |issue= 51 |pages= 47759-62 |year= 2002 |pmid= 11673449 |doi= 10.1074/jbc.C100569200 }}
*{{cite journal  | author=Deng L, Wang D, de la Fuente C, ''et al.'' |title=Enhancement of the p300 HAT activity by HIV-1 Tat on chromatin DNA. |journal=Virology |volume=289 |issue= 2 |pages= 312-26 |year= 2001 |pmid= 11689053 |doi= 10.1006/viro.2001.1129 }}
*{{cite journal  | author=Chen A, Kleiman FE, Manley JL, ''et al.'' |title=Autoubiquitination of the BRCA1*BARD1 RING ubiquitin ligase. |journal=J. Biol. Chem. |volume=277 |issue= 24 |pages= 22085-92 |year= 2002 |pmid= 11927591 |doi= 10.1074/jbc.M201252200 }}
*{{cite journal  | author=Zhu H, Hunter TC, Pan S, ''et al.'' |title=Residue-specific mass signatures for the efficient detection of protein modifications by mass spectrometry. |journal=Anal. Chem. |volume=74 |issue= 7 |pages= 1687-94 |year= 2003 |pmid= 12033261 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

HBEGF

• INFO: Beginning work on HBEGF... {November 14, 2007 2:37:02 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:37:37 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_HBEGF_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1xdt.
 | PDB = {{PDB2|1xdt}}
 | Name = Heparin-binding EGF-like growth factor
 | HGNCid = 3059
 | Symbol = HBEGF
 | AltSymbols =; DTR; DTS; DTSF; HEGFL
 | OMIM = 126150
 | ECnumber =  
 | Homologene = 1466
 | MGIid = 96070
 | GeneAtlas_image1 = PBB_GE_HBEGF_38037_at_tn.png
 | GeneAtlas_image2 = PBB_GE_HBEGF_203821_at_tn.png
 | Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005154 |text = epidermal growth factor receptor binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} 
 | Component = {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0009986 |text = cell surface}} {{GNF_GO|id=GO:0016020 |text = membrane}} 
 | Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007173 |text = epidermal growth factor receptor signaling pathway}} {{GNF_GO|id=GO:0007517 |text = muscle development}} {{GNF_GO|id=GO:0008016 |text = regulation of heart contraction}} {{GNF_GO|id=GO:0035313 |text = wound healing, spreading of epidermal cells}} {{GNF_GO|id=GO:0048661 |text = positive regulation of smooth muscle cell proliferation}} {{GNF_GO|id=GO:0051549 |text = positive regulation of keratinocyte migration}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1839
    | Hs_Ensembl = ENSG00000113070
    | Hs_RefseqProtein = NP_001936
    | Hs_RefseqmRNA = NM_001945
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 139692615
    | Hs_GenLoc_end = 139706359
    | Hs_Uniprot = Q99075
    | Mm_EntrezGene = 15200
    | Mm_Ensembl = ENSMUSG00000024486
    | Mm_RefseqmRNA = NM_010415
    | Mm_RefseqProtein = NP_034545
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 18
    | Mm_GenLoc_start = 36630906
    | Mm_GenLoc_end = 36641748
    | Mm_Uniprot = Q5FW64
  }}
}}
'''Heparin-binding EGF-like growth factor''', also known as '''HBEGF''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = 
}}

==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Higashiyama S, Lau K, Besner GE, ''et al.'' |title=Structure of heparin-binding EGF-like growth factor. Multiple forms, primary structure, and glycosylation of the mature protein. |journal=J. Biol. Chem. |volume=267 |issue= 9 |pages= 6205-12 |year= 1992 |pmid= 1556128 |doi=  }}
*{{cite journal  | author=Yoshizumi M, Kourembanas S, Temizer DH, ''et al.'' |title=Tumor necrosis factor increases transcription of the heparin-binding epidermal growth factor-like growth factor gene in vascular endothelial cells. |journal=J. Biol. Chem. |volume=267 |issue= 14 |pages= 9467-9 |year= 1992 |pmid= 1577791 |doi=  }}
*{{cite journal  | author=Higashiyama S, Abraham JA, Miller J, ''et al.'' |title=A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF. |journal=Science |volume=251 |issue= 4996 |pages= 936-9 |year= 1991 |pmid= 1840698 |doi=  }}
*{{cite journal  | author=Iwamoto R, Senoh H, Okada Y, ''et al.'' |title=An antibody that inhibits the binding of diphtheria toxin to cells revealed the association of a 27-kDa membrane protein with the diphtheria toxin receptor. |journal=J. Biol. Chem. |volume=266 |issue= 30 |pages= 20463-9 |year= 1991 |pmid= 1939101 |doi=  }}
*{{cite journal  | author=Hayes H, Kaneda Y, Uchida T, Okada Y |title=Regional assignment of the gene for diphtheria toxin sensitivity using subchromosomal fragments in microcell hybrids. |journal=Chromosoma |volume=96 |issue= 1 |pages= 26-32 |year= 1988 |pmid= 3436221 |doi=  }}
*{{cite journal  | author=Bennett KL, Jackson DG, Simon JC, ''et al.'' |title=CD44 isoforms containing exon V3 are responsible for the presentation of heparin-binding growth factor. |journal=J. Cell Biol. |volume=128 |issue= 4 |pages= 687-98 |year= 1995 |pmid= 7532176 |doi=  }}
*{{cite journal  | author=Pathak BG, Gilbert DJ, Harrison CA, ''et al.'' |title=Mouse chromosomal location of three EGF receptor ligands: amphiregulin (Areg), betacellulin (Btc), and heparin-binding EGF (Hegfl). |journal=Genomics |volume=28 |issue= 1 |pages= 116-8 |year= 1995 |pmid= 7590736 |doi= 10.1006/geno.1995.1116 }}
*{{cite journal  | author=Mitamura T, Higashiyama S, Taniguchi N, ''et al.'' |title=Diphtheria toxin binds to the epidermal growth factor (EGF)-like domain of human heparin-binding EGF-like growth factor/diphtheria toxin receptor and inhibits specifically its mitogenic activity. |journal=J. Biol. Chem. |volume=270 |issue= 3 |pages= 1015-9 |year= 1995 |pmid= 7836353 |doi=  }}
*{{cite journal  | author=Hashimoto K, Higashiyama S, Asada H, ''et al.'' |title=Heparin-binding epidermal growth factor-like growth factor is an autocrine growth factor for human keratinocytes. |journal=J. Biol. Chem. |volume=269 |issue= 31 |pages= 20060-6 |year= 1994 |pmid= 8051092 |doi=  }}
*{{cite journal  | author=Kobrin MS, Funatomi H, Friess H, ''et al.'' |title=Induction and expression of heparin-binding EGF-like growth factor in human pancreatic cancer. |journal=Biochem. Biophys. Res. Commun. |volume=202 |issue= 3 |pages= 1705-9 |year= 1994 |pmid= 8060360 |doi= 10.1006/bbrc.1994.2131 }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi=  }}
*{{cite journal  | author=Thompson SA, Higashiyama S, Wood K, ''et al.'' |title=Characterization of sequences within heparin-binding EGF-like growth factor that mediate interaction with heparin. |journal=J. Biol. Chem. |volume=269 |issue= 4 |pages= 2541-9 |year= 1994 |pmid= 8300582 |doi=  }}
*{{cite journal  | author=Fen Z, Dhadly MS, Yoshizumi M, ''et al.'' |title=Structural organization and chromosomal assignment of the gene encoding the human heparin-binding epidermal growth factor-like growth factor/diphtheria toxin receptor. |journal=Biochemistry |volume=32 |issue= 31 |pages= 7932-8 |year= 1993 |pmid= 8347598 |doi=  }}
*{{cite journal  | author=Elenius K, Paul S, Allison G, ''et al.'' |title=Activation of HER4 by heparin-binding EGF-like growth factor stimulates chemotaxis but not proliferation. |journal=EMBO J. |volume=16 |issue= 6 |pages= 1268-78 |year= 1997 |pmid= 9135143 |doi= 10.1093/emboj/16.6.1268 }}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi=  }}
*{{cite journal  | author=Louie GV, Yang W, Bowman ME, Choe S |title=Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor. |journal=Mol. Cell |volume=1 |issue= 1 |pages= 67-78 |year= 1998 |pmid= 9659904 |doi=  }}
*{{cite journal  | author=Borer JG, Park JM, Atala A, ''et al.'' |title=Heparin-binding EGF-like growth factor expression increases selectively in bladder smooth muscle in response to lower urinary tract obstruction. |journal=Lab. Invest. |volume=79 |issue= 11 |pages= 1335-45 |year= 1999 |pmid= 10576204 |doi=  }}
*{{cite journal  | author=Nakamura K, Mitamura T, Takahashi T, ''et al.'' |title=Importance of the major extracellular domain of CD9 and the epidermal growth factor (EGF)-like domain of heparin-binding EGF-like growth factor for up-regulation of binding and activity. |journal=J. Biol. Chem. |volume=275 |issue= 24 |pages= 18284-90 |year= 2000 |pmid= 10749879 |doi= 10.1074/jbc.M907971199 }}
*{{cite journal  | author=Duque JL, Adam RM, Mullen JS, ''et al.'' |title=Heparin-binding epidermal growth factor-like growth factor is an autocrine mediator of human prostate stromal cell growth in vitro. |journal=J. Urol. |volume=165 |issue= 1 |pages= 284-8 |year= 2001 |pmid= 11125426 |doi= 10.1097/00005392-200101000-00080 }}
*{{cite journal  | author=Lin J, Hutchinson L, Gaston SM, ''et al.'' |title=BAG-1 is a novel cytoplasmic binding partner of the membrane form of heparin-binding EGF-like growth factor: a unique role for proHB-EGF in cell survival regulation. |journal=J. Biol. Chem. |volume=276 |issue= 32 |pages= 30127-32 |year= 2001 |pmid= 11340068 |doi= 10.1074/jbc.M010237200 }}
}}
{{refend}}

{{protein-stub}}
 

IRS2

• INFO: Beginning work on IRS2... {November 14, 2007 2:55:13 PM PST}
• SEARCH REDIRECT: Control Box Found: IRS2 {November 14, 2007 2:55:50 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 2:55:52 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 2:55:52 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 2:55:52 PM PST}
• UPDATED: Updated protein page: IRS2 {November 14, 2007 2:55:59 PM PST}

JAK1

• INFO: Beginning work on JAK1... {November 14, 2007 2:45:14 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:45:53 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Janus kinase 1 (a protein tyrosine kinase)
 | HGNCid = 6190
 | Symbol = JAK1
 | AltSymbols =; JAK1A; JAK1B
 | OMIM = 147795
 | ECnumber =  
 | Homologene = 1678
 | MGIid = 96628
 | GeneAtlas_image1 = PBB_GE_JAK1_201648_at_tn.png
 | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0004718 |text = Janus kinase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} 
 | Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} 
 | Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3716
    | Hs_Ensembl = ENSG00000162434
    | Hs_RefseqProtein = NP_002218
    | Hs_RefseqmRNA = NM_002227
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 65071500
    | Hs_GenLoc_end = 65204775
    | Hs_Uniprot = P23458
    | Mm_EntrezGene = 16451
    | Mm_Ensembl = ENSMUSG00000028530
    | Mm_RefseqmRNA = NM_146145
    | Mm_RefseqProtein = NP_666257
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 100650299
    | Mm_GenLoc_end = 100763214
    | Mm_Uniprot = Q3TI10
  }}
}}
'''Janus kinase 1 (a protein tyrosine kinase)''', also known as '''JAK1''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = Janus kinase 1 (JAK1), is a member of a new class of protein-tyrosine kinases (PTK) characterized by the presence of a second phosphotransferase-related domain immediately N-terminal to the PTK domain. The second phosphotransferase domain bears all the hallmarks of a protein kinase, although its structure differs significantly from that of the PTK and threonine/serine kinase family members. JAK1 is a large, widely expressed membrane-associated phosphoprotein.  JAK1 is involved in the interferon-alpha/beta and -gamma signal transduction pathways. The reciprocal interdependence between JAK1 and TYK2 activities in the interferon-alpha pathway, and between JAK1 and JAK2 in the interferon-gamma pathway, may reflect a requirement for these kinases in the correct assembly of interferon receptor complexes. These kinases couple cytokine ligand binding to tyrosine phosphorylation of various known signaling proteins and of a unique family of transcription factors termed the signal transducers and activators of transcription, or STATs.<ref>{{cite web | title = Entrez Gene: JAK1 Janus kinase 1 (a protein tyrosine kinase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3716| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Donnelly RP, Dickensheets H, Finbloom DS |title=The interleukin-10 signal transduction pathway and regulation of gene expression in mononuclear phagocytes. |journal=J. Interferon Cytokine Res. |volume=19 |issue= 6 |pages= 563-73 |year= 1999 |pmid= 10433356 |doi= 10.1089/107999099313695 }}
*{{cite journal  | author=Carter-Su C, Rui L, Stofega MR |title=SH2-B and SIRP: JAK2 binding proteins that modulate the actions of growth hormone. |journal=Recent Prog. Horm. Res. |volume=55 |issue=  |pages= 293-311 |year= 2000 |pmid= 11036942 |doi=  }}
*{{cite journal  | author=Kostrodymova GM |title=[An experimental study of the possible sensitizing properties of triethanolamine contained in chemical compounds used at home] |journal=Gigiena i sanitariia |volume= |issue= 6 |pages= 10-2 |year= 1976 |pmid= 1213395 |doi=  }}
*{{cite journal  | author=Howard OM, Dean M, Young H, ''et al.'' |title=Characterization of a class 3 tyrosine kinase. |journal=Oncogene |volume=7 |issue= 5 |pages= 895-900 |year= 1992 |pmid= 1373877 |doi=  }}
*{{cite journal  | author=Pritchard MA, Baker E, Callen DF, ''et al.'' |title=Two members of the JAK family of protein tyrosine kinases map to chromosomes 1p31.3 and 9p24. |journal=Mamm. Genome |volume=3 |issue= 1 |pages= 36-8 |year= 1992 |pmid= 1581631 |doi=  }}
*{{cite journal  | author=Wilks AF, Harpur AG, Kurban RR, ''et al.'' |title=Two novel protein-tyrosine kinases, each with a second phosphotransferase-related catalytic domain, define a new class of protein kinase. |journal=Mol. Cell. Biol. |volume=11 |issue= 4 |pages= 2057-65 |year= 1991 |pmid= 1848670 |doi=  }}
*{{cite journal  | author=Johnston JA, Wang LM, Hanson EP, ''et al.'' |title=Interleukins 2, 4, 7, and 15 stimulate tyrosine phosphorylation of insulin receptor substrates 1 and 2 in T cells. Potential role of JAK kinases. |journal=J. Biol. Chem. |volume=270 |issue= 48 |pages= 28527-30 |year= 1996 |pmid= 7499365 |doi=  }}
*{{cite journal  | author=Nicholson SE, Oates AC, Harpur AG, ''et al.'' |title=Tyrosine kinase JAK1 is associated with the granulocyte-colony-stimulating factor receptor and both become tyrosine-phosphorylated after receptor activation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 8 |pages= 2985-8 |year= 1994 |pmid= 7512720 |doi=  }}
*{{cite journal  | author=Domanski P, Yan H, Witte MM, ''et al.'' |title=Homodimerization and intermolecular tyrosine phosphorylation of the Tyk-2 tyrosine kinase. |journal=FEBS Lett. |volume=374 |issue= 3 |pages= 317-22 |year= 1995 |pmid= 7589562 |doi=  }}
*{{cite journal  | author=Modi WS, Farrar WL, Howard OM |title=Confirmed assignment of a novel human tyrosine kinase gene (JAK1A) to 1p32.3-->p31.3 by nonisotopic in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=69 |issue= 3-4 |pages= 232-4 |year= 1995 |pmid= 7698020 |doi=  }}
*{{cite journal  | author=Miyazaki T, Kawahara A, Fujii H, ''et al.'' |title=Functional activation of Jak1 and Jak3 by selective association with IL-2 receptor subunits. |journal=Science |volume=266 |issue= 5187 |pages= 1045-7 |year= 1994 |pmid= 7973659 |doi=  }}
*{{cite journal  | author=Müller M, Briscoe J, Laxton C, ''et al.'' |title=The protein tyrosine kinase JAK1 complements defects in interferon-alpha/beta and -gamma signal transduction. |journal=Nature |volume=366 |issue= 6451 |pages= 129-35 |year= 1993 |pmid= 8232552 |doi= 10.1038/366129a0 }}
*{{cite journal  | author=Lee ST, Strunk KM, Spritz RA |title=A survey of protein tyrosine kinase mRNAs expressed in normal human melanocytes. |journal=Oncogene |volume=8 |issue= 12 |pages= 3403-10 |year= 1993 |pmid= 8247543 |doi=  }}
*{{cite journal  | author=Lütticken C, Wegenka UM, Yuan J, ''et al.'' |title=Association of transcription factor APRF and protein kinase Jak1 with the interleukin-6 signal transducer gp130. |journal=Science |volume=263 |issue= 5143 |pages= 89-92 |year= 1994 |pmid= 8272872 |doi=  }}
*{{cite journal  | author=Giorgetti-Peraldi S, Peyrade F, Baron V, Van Obberghen E |title=Involvement of Janus kinases in the insulin signaling pathway. |journal=Eur. J. Biochem. |volume=234 |issue= 2 |pages= 656-60 |year= 1996 |pmid= 8536716 |doi=  }}
*{{cite journal  | author=Friedmann MC, Migone TS, Russell SM, Leonard WJ |title=Different interleukin 2 receptor beta-chain tyrosines couple to at least two signaling pathways and synergistically mediate interleukin 2-induced proliferation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 5 |pages= 2077-82 |year= 1996 |pmid= 8700888 |doi=  }}
*{{cite journal  | author=Gauzzi MC, Velazquez L, McKendry R, ''et al.'' |title=Interferon-alpha-dependent activation of Tyk2 requires phosphorylation of positive regulatory tyrosines by another kinase. |journal=J. Biol. Chem. |volume=271 |issue= 34 |pages= 20494-500 |year= 1996 |pmid= 8702790 |doi=  }}
*{{cite journal  | author=Demoulin JB, Uyttenhove C, Van Roost E, ''et al.'' |title=A single tyrosine of the interleukin-9 (IL-9) receptor is required for STAT activation, antiapoptotic activity, and growth regulation by IL-9. |journal=Mol. Cell. Biol. |volume=16 |issue= 9 |pages= 4710-6 |year= 1996 |pmid= 8756628 |doi=  }}
*{{cite journal  | author=Yin T, Shen R, Feng GS, Yang YC |title=Molecular characterization of specific interactions between SHP-2 phosphatase and JAK tyrosine kinases. |journal=J. Biol. Chem. |volume=272 |issue= 2 |pages= 1032-7 |year= 1997 |pmid= 8995399 |doi=  }}
*{{cite journal  | author=Bluyssen HA, Levy DE |title=Stat2 is a transcriptional activator that requires sequence-specific contacts provided by stat1 and p48 for stable interaction with DNA. |journal=J. Biol. Chem. |volume=272 |issue= 7 |pages= 4600-5 |year= 1997 |pmid= 9020188 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

KPNA1

• INFO: Beginning work on KPNA1... {November 14, 2007 2:45:53 PM PST}
• SEARCH REDIRECT: Control Box Found: KPNA1 {November 14, 2007 2:46:32 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 2:46:33 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 2:46:33 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 2:46:33 PM PST}
• UPDATED: Updated protein page:
  KPNA1
  {November 14, 2007 2:46:39 PM PST}

MBP

• INFO: Beginning work on MBP... {November 14, 2007 2:48:04 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:48:29 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Myelin basic protein
 | HGNCid = 6925
 | Symbol = MBP
 | AltSymbols =; MGC99675
 | OMIM = 159430
 | ECnumber =  
 | Homologene = 1788
 | MGIid = 96925
 | GeneAtlas_image1 = PBB_GE_MBP_207323_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_MBP_209072_at_tn.png
 | Function = {{GNF_GO|id=GO:0019911 |text = structural constituent of myelin sheath}} 
 | Component = 
 | Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007417 |text = central nervous system development}} {{GNF_GO|id=GO:0042552 |text = myelination}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4155
    | Hs_Ensembl = ENSG00000197971
    | Hs_RefseqProtein = NP_001020252
    | Hs_RefseqmRNA = NM_001025081
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 18
    | Hs_GenLoc_start = 72819778
    | Hs_GenLoc_end = 72973762
    | Hs_Uniprot = P02686
    | Mm_EntrezGene = 17196
    | Mm_Ensembl = ENSMUSG00000041607
    | Mm_RefseqmRNA = NM_001025245
    | Mm_RefseqProtein = NP_001020416
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 18
    | Mm_GenLoc_start = 82609551
    | Mm_GenLoc_end = 82720065
    | Mm_Uniprot = P04370
  }}
}}
'''Myelin basic protein''', also known as '''MBP''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The protein encoded by the classic MBP gene is a major constituent of the myelin sheath of oligodendrocytes and Schwann cells in the nervous system. However, MBP-related transcripts are also present in the bone marrow and the immune system. These mRNAs arise from the long MBP gene (otherwise called &quot;Golli-MBP&quot;) that contains 3 additional exons located upstream of the classic MBP exons. Alternative splicing from the Golli and the MBP transcription start sites gives rise to 2 sets of MBP-related transcripts and gene products. The Golli mRNAs contain 3 exons unique to Golli-MBP, spliced in-frame to 1 or more MBP exons. They encode hybrid proteins that have N-terminal Golli aa sequence linked to MBP aa sequence. The second family of transcripts contain only MBP exons and produce the well characterized myelin basic proteins. This complex gene structure is conserved among species suggesting that the MBP transcription unit is an integral part of the Golli transcription unit and that this arrangement is important for the function and/or regulation of these genes.<ref>{{cite web | title = Entrez Gene: MBP myelin basic protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4155| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Boylan KB, Ayres TM, Popko B, ''et al.'' |title=Repetitive DNA (TGGA)n 5' to the human myelin basic protein gene: a new form of oligonucleotide repetitive sequence showing length polymorphism. |journal=Genomics |volume=6 |issue= 1 |pages= 16-22 |year= 1990 |pmid= 1689270 |doi=  }}
*{{cite journal  | author=Kishimoto A, Nishiyama K, Nakanishi H, ''et al.'' |title=Studies on the phosphorylation of myelin basic protein by protein kinase C and adenosine 3':5'-monophosphate-dependent protein kinase. |journal=J. Biol. Chem. |volume=260 |issue= 23 |pages= 12492-9 |year= 1985 |pmid= 2413024 |doi=  }}
*{{cite journal  | author=Saxe DF, Takahashi N, Hood L, Simon MI |title=Localization of the human myelin basic protein gene (MBP) to region 18q22----qter by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=39 |issue= 4 |pages= 246-9 |year= 1985 |pmid= 2414074 |doi=  }}
*{{cite journal  | author=Kamholz J, de Ferra F, Puckett C, Lazzarini R |title=Identification of three forms of human myelin basic protein by cDNA cloning. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 13 |pages= 4962-6 |year= 1986 |pmid= 2425357 |doi=  }}
*{{cite journal  | author=Scoble HA, Whitaker JN, Biemann K |title=Analysis of the primary sequence of human myelin basic protein peptides 1-44 and 90-170 by fast atom bombardment mass spectrometry. |journal=J. Neurochem. |volume=47 |issue= 2 |pages= 614-6 |year= 1986 |pmid= 2426402 |doi=  }}
*{{cite journal  | author=Roth HJ, Kronquist K, Pretorius PJ, ''et al.'' |title=Isolation and characterization of a cDNA coding for a novel human 17.3K myelin basic protein (MBP) variant. |journal=J. Neurosci. Res. |volume=16 |issue= 1 |pages= 227-38 |year= 1986 |pmid= 2427738 |doi= 10.1002/jnr.490160120 }}
*{{cite journal  | author=Popko B, Puckett C, Lai E, ''et al.'' |title=Myelin deficient mice: expression of myelin basic protein and generation of mice with varying levels of myelin. |journal=Cell |volume=48 |issue= 4 |pages= 713-21 |year= 1987 |pmid= 2434243 |doi=  }}
*{{cite journal  | author=Kamholz J, Spielman R, Gogolin K, ''et al.'' |title=The human myelin-basic-protein gene: chromosomal localization and RFLP analysis. |journal=Am. J. Hum. Genet. |volume=40 |issue= 4 |pages= 365-73 |year= 1987 |pmid= 2437795 |doi=  }}
*{{cite journal  | author=Roth HJ, Kronquist KE, Kerlero de Rosbo N, ''et al.'' |title=Evidence for the expression of four myelin basic protein variants in the developing human spinal cord through cDNA cloning. |journal=J. Neurosci. Res. |volume=17 |issue= 4 |pages= 321-8 |year= 1987 |pmid= 2442403 |doi= 10.1002/jnr.490170402 }}
*{{cite journal  | author=Shoji S, Ohnishi J, Funakoshi T, ''et al.'' |title=Phosphorylation sites of bovine brain myelin basic protein phosphorylated with Ca2+-calmodulin-dependent protein kinase from rat brain. |journal=J. Biochem. |volume=102 |issue= 5 |pages= 1113-20 |year= 1988 |pmid= 2449425 |doi=  }}
*{{cite journal  | author=Wood DD, Moscarello MA |title=The isolation, characterization, and lipid-aggregating properties of a citrulline containing myelin basic protein. |journal=J. Biol. Chem. |volume=264 |issue= 9 |pages= 5121-7 |year= 1989 |pmid= 2466844 |doi=  }}
*{{cite journal  | author=Edwards AM, Ross NW, Ulmer JB, Braun PE |title=Interaction of myelin basic protein and proteolipid protein. |journal=J. Neurosci. Res. |volume=22 |issue= 1 |pages= 97-102 |year= 1989 |pmid= 2467009 |doi= 10.1002/jnr.490220113 }}
*{{cite journal  | author=Streicher R, Stoffel W |title=The organization of the human myelin basic protein gene. Comparison with the mouse gene. |journal=Biol. Chem. Hoppe-Seyler |volume=370 |issue= 5 |pages= 503-10 |year= 1989 |pmid= 2472816 |doi=  }}
*{{cite journal  | author=Lennon VA, Wilks AV, Carnegie PR |title=Immunologic properties of the main encephalitogenic peptide from the basic protein of human myelin. |journal=J. Immunol. |volume=105 |issue= 5 |pages= 1223-30 |year= 1971 |pmid= 4099924 |doi=  }}
*{{cite journal  | author=Carnegie PR |title=Amino acid sequence of the encephalitogenic basic protein from human myelin. |journal=Biochem. J. |volume=123 |issue= 1 |pages= 57-67 |year= 1972 |pmid= 4108501 |doi=  }}
*{{cite journal  | author=Baldwin GS, Carnegie PR |title=Specific enzymic methylation of an arginine in the experimental allergic encephalomyelitis protein from human myelin. |journal=Science |volume=171 |issue= 971 |pages= 579-81 |year= 1971 |pmid= 4924231 |doi=  }}
*{{cite journal  | author=Baldwin GS, Carnegie PR |title=Isolation and partial characterization of methylated arginines from the encephalitogenic basic protein of myelin. |journal=Biochem. J. |volume=123 |issue= 1 |pages= 69-74 |year= 1972 |pmid= 5128665 |doi=  }}
*{{cite journal  | author=Wood DD, Vella GJ, Moscarello MA |title=Interaction between human myelin basic protein and lipophilin. |journal=Neurochem. Res. |volume=9 |issue= 10 |pages= 1523-31 |year= 1985 |pmid= 6083474 |doi=  }}
*{{cite journal  | author=Gibson BW, Gilliom RD, Whitaker JN, Biemann K |title=Amino acid sequence of human myelin basic protein peptide 45-89 as determined by mass spectrometry. |journal=J. Biol. Chem. |volume=259 |issue= 8 |pages= 5028-31 |year= 1984 |pmid= 6201481 |doi=  }}
*{{cite journal  | author=Pribyl TM, Campagnoni CW, Kampf K, ''et al.'' |title=The human myelin basic protein gene is included within a 179-kilobase transcription unit: expression in the immune and central nervous systems. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 22 |pages= 10695-9 |year= 1993 |pmid= 7504278 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

MSH6

• INFO: Beginning work on MSH6... {November 14, 2007 2:39:18 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:39:54 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_MSH6_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 2gfu.
 | PDB = {{PDB2|2gfu}}, {{PDB2|2o8b}}, {{PDB2|2o8c}}, {{PDB2|2o8d}}, {{PDB2|2o8e}}, {{PDB2|2o8f}}
 | Name = MutS homolog 6 (E. coli)
 | HGNCid = 7329
 | Symbol = MSH6
 | AltSymbols =; GTBP; HNPCC5; HSAP
 | OMIM = 600678
 | ECnumber =  
 | Homologene = 149
 | MGIid = 1343961
 | GeneAtlas_image1 = PBB_GE_MSH6_202911_at_tn.png
 | GeneAtlas_image2 = PBB_GE_MSH6_211450_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000400 |text = four-way junction DNA binding}} {{GNF_GO|id=GO:0000701 |text = purine-specific mismatch base pair DNA N-glycosylase activity}} {{GNF_GO|id=GO:0003684 |text = damaged DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0015444 |text = magnesium-importing ATPase activity}} {{GNF_GO|id=GO:0032137 |text = guanine/thymine mispair binding}} {{GNF_GO|id=GO:0032139 |text = dinucleotide insertion or deletion binding}} {{GNF_GO|id=GO:0032142 |text = single guanine insertion binding}} {{GNF_GO|id=GO:0032143 |text = single thymine insertion binding}} {{GNF_GO|id=GO:0032357 |text = oxidized purine DNA binding}} {{GNF_GO|id=GO:0032405 |text = MutLalpha complex binding}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0043531 |text = ADP binding}} {{GNF_GO|id=GO:0045027 |text = DNA end binding}} 
 | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0032301 |text = MutSalpha complex}} 
 | Process = {{GNF_GO|id=GO:0006284 |text = base-excision repair}} {{GNF_GO|id=GO:0006298 |text = mismatch repair}} {{GNF_GO|id=GO:0008340 |text = determination of adult life span}} {{GNF_GO|id=GO:0008629 |text = induction of apoptosis by intracellular signals}} {{GNF_GO|id=GO:0009411 |text = response to UV}} {{GNF_GO|id=GO:0016446 |text = somatic hypermutation of immunoglobulin genes}} {{GNF_GO|id=GO:0016447 |text = somatic recombination of immunoglobulin gene segments}} {{GNF_GO|id=GO:0032026 |text = response to magnesium ion}} {{GNF_GO|id=GO:0045910 |text = negative regulation of DNA recombination}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2956
    | Hs_Ensembl = ENSG00000116062
    | Hs_RefseqProtein = NP_000170
    | Hs_RefseqmRNA = NM_000179
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 47863725
    | Hs_GenLoc_end = 47887588
    | Hs_Uniprot = P52701
    | Mm_EntrezGene = 17688
    | Mm_Ensembl = ENSMUSG00000005370
    | Mm_RefseqmRNA = NM_010830
    | Mm_RefseqProtein = NP_034960
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 87883410
    | Mm_GenLoc_end = 87899389
    | Mm_Uniprot = Q61061
  }}
}}
'''MutS homolog 6 (E. coli)''', also known as '''MSH6''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = 
}}

==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Drummond JT, Li GM, Longley MJ, Modrich P |title=Isolation of an hMSH2-p160 heterodimer that restores DNA mismatch repair to tumor cells. |journal=Science |volume=268 |issue= 5219 |pages= 1909-12 |year= 1995 |pmid= 7604264 |doi=  }}
*{{cite journal  | author=Palombo F, Gallinari P, Iaccarino I, ''et al.'' |title=GTBP, a 160-kilodalton protein essential for mismatch-binding activity in human cells. |journal=Science |volume=268 |issue= 5219 |pages= 1912-4 |year= 1995 |pmid= 7604265 |doi=  }}
*{{cite journal  | author=Papadopoulos N, Nicolaides NC, Liu B, ''et al.'' |title=Mutations of GTBP in genetically unstable cells. |journal=Science |volume=268 |issue= 5219 |pages= 1915-7 |year= 1995 |pmid= 7604266 |doi=  }}
*{{cite journal  | author=Risinger JI, Umar A, Boyd J, ''et al.'' |title=Mutation of MSH3 in endometrial cancer and evidence for its functional role in heteroduplex repair. |journal=Nat. Genet. |volume=14 |issue= 1 |pages= 102-5 |year= 1996 |pmid= 8782829 |doi= 10.1038/ng0996-102 }}
*{{cite journal  | author=Nicolaides NC, Palombo F, Kinzler KW, ''et al.'' |title=Molecular cloning of the N-terminus of GTBP. |journal=Genomics |volume=31 |issue= 3 |pages= 395-7 |year= 1997 |pmid= 8838326 |doi= 10.1006/geno.1996.0067 }}
*{{cite journal  | author=Acharya S, Wilson T, Gradia S, ''et al.'' |title=hMSH2 forms specific mispair-binding complexes with hMSH3 and hMSH6. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 24 |pages= 13629-34 |year= 1997 |pmid= 8942985 |doi=  }}
*{{cite journal  | author=Miyaki M, Konishi M, Tanaka K, ''et al.'' |title=Germline mutation of MSH6 as the cause of hereditary nonpolyposis colorectal cancer. |journal=Nat. Genet. |volume=17 |issue= 3 |pages= 271-2 |year= 1997 |pmid= 9354786 |doi= 10.1038/ng1197-271 }}
*{{cite journal  | author=Yin J, Kong D, Wang S, ''et al.'' |title=Mutation of hMSH3 and hMSH6 mismatch repair genes in genetically unstable human colorectal and gastric carcinomas. |journal=Hum. Mutat. |volume=10 |issue= 6 |pages= 474-8 |year= 1998 |pmid= 9401011 |doi= 10.1002/(SICI)1098-1004(1997)10:6<474::AID-HUMU9>3.0.CO;2-D }}
*{{cite journal  | author=Gradia S, Acharya S, Fishel R |title=The human mismatch recognition complex hMSH2-hMSH6 functions as a novel molecular switch. |journal=Cell |volume=91 |issue= 7 |pages= 995-1005 |year= 1998 |pmid= 9428522 |doi=  }}
*{{cite journal  | author=Shiwaku HO, Wakatsuki S, Mori Y, ''et al.'' |title=Alternative splicing of GTBP in normal human tissues. |journal=DNA Res. |volume=4 |issue= 5 |pages= 359-62 |year= 1998 |pmid= 9455487 |doi=  }}
*{{cite journal  | author=Wei Q, Guan Y, Cheng L, ''et al.'' |title=Expression of five selected human mismatch repair genes simultaneously detected in normal and cancer cell lines by a nonradioactive multiplex reverse transcription-polymerase chain reaction. |journal=Pathobiology |volume=65 |issue= 6 |pages= 293-300 |year= 1998 |pmid= 9491849 |doi=  }}
*{{cite journal  | author=Guerrette S, Wilson T, Gradia S, Fishel R |title=Interactions of human hMSH2 with hMSH3 and hMSH2 with hMSH6: examination of mutations found in hereditary nonpolyposis colorectal cancer. |journal=Mol. Cell. Biol. |volume=18 |issue= 11 |pages= 6616-23 |year= 1998 |pmid= 9774676 |doi=  }}
*{{cite journal  | author=Wang Q, Lasset C, Desseigne F, ''et al.'' |title=Prevalence of germline mutations of hMLH1, hMSH2, hPMS1, hPMS2, and hMSH6 genes in 75 French kindreds with nonpolyposis colorectal cancer. |journal=Hum. Genet. |volume=105 |issue= 1-2 |pages= 79-85 |year= 1999 |pmid= 10480359 |doi=  }}
*{{cite journal  | author=Wijnen J, de Leeuw W, Vasen H, ''et al.'' |title=Familial endometrial cancer in female carriers of MSH6 germline mutations. |journal=Nat. Genet. |volume=23 |issue= 2 |pages= 142-4 |year= 1999 |pmid= 10508506 |doi= 10.1038/13773 }}
*{{cite journal  | author=Wu Y, Berends MJ, Mensink RG, ''et al.'' |title=Association of hereditary nonpolyposis colorectal cancer-related tumors displaying low microsatellite instability with MSH6 germline mutations. |journal=Am. J. Hum. Genet. |volume=65 |issue= 5 |pages= 1291-8 |year= 1999 |pmid= 10521294 |doi=  }}
*{{cite journal  | author=Kolodner RD, Tytell JD, Schmeits JL, ''et al.'' |title=Germ-line msh6 mutations in colorectal cancer families. |journal=Cancer Res. |volume=59 |issue= 20 |pages= 5068-74 |year= 1999 |pmid= 10537275 |doi=  }}
*{{cite journal  | author=Wang Y, Cortez D, Yazdi P, ''et al.'' |title=BASC, a super complex of BRCA1-associated proteins involved in the recognition and repair of aberrant DNA structures. |journal=Genes Dev. |volume=14 |issue= 8 |pages= 927-39 |year= 2000 |pmid= 10783165 |doi=  }}
*{{cite journal  | author=Ceccotti S, Ciotta C, Fronza G, ''et al.'' |title=Multiple mutations and frameshifts are the hallmark of defective hPMS2 in pZ189-transfected human tumor cells. |journal=Nucleic Acids Res. |volume=28 |issue= 13 |pages= 2577-84 |year= 2000 |pmid= 10871409 |doi=  }}
*{{cite journal  | author=Christmann M, Kaina B |title=Nuclear translocation of mismatch repair proteins MSH2 and MSH6 as a response of cells to alkylating agents. |journal=J. Biol. Chem. |volume=275 |issue= 46 |pages= 36256-62 |year= 2000 |pmid= 10954713 |doi= 10.1074/jbc.M005377200 }}
*{{cite journal  | author=Clark AB, Valle F, Drotschmann K, ''et al.'' |title=Functional interaction of proliferating cell nuclear antigen with MSH2-MSH6 and MSH2-MSH3 complexes. |journal=J. Biol. Chem. |volume=275 |issue= 47 |pages= 36498-501 |year= 2001 |pmid= 11005803 |doi= 10.1074/jbc.C000513200 }}
}}
{{refend}}

{{protein-stub}}
 

MYCN

• INFO: Beginning work on MYCN... {November 14, 2007 2:48:29 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:49:05 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = V-myc myelocytomatosis viral related oncogene, neuroblastoma derived (avian)
 | HGNCid = 7559
 | Symbol = MYCN
 | AltSymbols =; MODED; N-myc; NMYC; ODED
 | OMIM = 164840
 | ECnumber =  
 | Homologene = 3922
 | MGIid = 97357
 | GeneAtlas_image1 = PBB_GE_MYCN_209757_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_MYCN_209756_s_at_tn.png
 | GeneAtlas_image3 = PBB_GE_MYCN_211377_x_at_tn.png
 | Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0000785 |text = chromatin}} {{GNF_GO|id=GO:0005634 |text = nucleus}} 
 | Process = {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4613
    | Hs_Ensembl = ENSG00000134323
    | Hs_RefseqProtein = NP_005369
    | Hs_RefseqmRNA = NM_005378
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 15998134
    | Hs_GenLoc_end = 16004579
    | Hs_Uniprot = P04198
    | Mm_EntrezGene = 18109
    | Mm_Ensembl = ENSMUSG00000037169
    | Mm_RefseqmRNA = NM_008709
    | Mm_RefseqProtein = NP_032735
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 12962079
    | Mm_GenLoc_end = 12967694
    | Mm_Uniprot = Q3UII1
  }}
}}
'''V-myc myelocytomatosis viral related oncogene, neuroblastoma derived (avian)''', also known as '''MYCN''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene is a member of the MYC family and encodes a protein with a basic helix-loop-helix (bHLH) domain. This protein is located in the nucleus and must dimerize with another bHLH protein in order to bind DNA. Amplification of this gene is associated with a variety of tumors, most notably neuroblastomas.<ref>{{cite web | title = Entrez Gene: MYCN v-myc myelocytomatosis viral related oncogene, neuroblastoma derived (avian)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4613| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Lüscher B |title=Function and regulation of the transcription factors of the Myc/Max/Mad network. |journal=Gene |volume=277 |issue= 1-2 |pages= 1-14 |year= 2001 |pmid= 11602341 |doi=  }}
*{{cite journal  | author=Armstrong BC, Krystal GW |title=Isolation and characterization of complementary DNA for N-cym, a gene encoded by the DNA strand opposite to N-myc. |journal=Cell Growth Differ. |volume=3 |issue= 6 |pages= 385-90 |year= 1992 |pmid= 1419902 |doi=  }}
*{{cite journal  | author=Hagiwara T, Nakaya K, Nakamura Y, ''et al.'' |title=Specific phosphorylation of the acidic central region of the N-myc protein by casein kinase II. |journal=Eur. J. Biochem. |volume=209 |issue= 3 |pages= 945-50 |year= 1992 |pmid= 1425701 |doi=  }}
*{{cite journal  | author=Fougerousse F, Meloni R, Roudaut C, Beckmann JS |title=Dinucleotide repeat polymorphism at the human hemoglobin alpha-1 pseudo-gene (HBAP1). |journal=Nucleic Acids Res. |volume=20 |issue= 5 |pages= 1165 |year= 1992 |pmid= 1549498 |doi=  }}
*{{cite journal  | author=Krystal GW, Armstrong BC, Battey JF |title=N-myc mRNA forms an RNA-RNA duplex with endogenous antisense transcripts. |journal=Mol. Cell. Biol. |volume=10 |issue= 8 |pages= 4180-91 |year= 1990 |pmid= 1695323 |doi=  }}
*{{cite journal  | author=Blackwood EM, Eisenman RN |title=Max: a helix-loop-helix zipper protein that forms a sequence-specific DNA-binding complex with Myc. |journal=Science |volume=251 |issue= 4998 |pages= 1211-7 |year= 1991 |pmid= 2006410 |doi=  }}
*{{cite journal  | author=Emanuel BS, Balaban G, Boyd JP, ''et al.'' |title=N-myc amplification in multiple homogeneously staining regions in two human neuroblastomas. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 11 |pages= 3736-40 |year= 1985 |pmid= 2582423 |doi=  }}
*{{cite journal  | author=Ibson JM, Rabbitts PH |title=Sequence of a germ-line N-myc gene and amplification as a mechanism of activation. |journal=Oncogene |volume=2 |issue= 4 |pages= 399-402 |year= 1988 |pmid= 2834684 |doi=  }}
*{{cite journal  | author=Stanton LW, Schwab M, Bishop JM |title=Nucleotide sequence of the human N-myc gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=83 |issue= 6 |pages= 1772-6 |year= 1986 |pmid= 2869488 |doi=  }}
*{{cite journal  | author=Michitsch RW, Melera PW |title=Nucleotide sequence of the 3' exon of the human N-myc gene. |journal=Nucleic Acids Res. |volume=13 |issue= 7 |pages= 2545-58 |year= 1985 |pmid= 2987858 |doi=  }}
*{{cite journal  | author=Slamon DJ, Boone TC, Seeger RC, ''et al.'' |title=Identification and characterization of the protein encoded by the human N-myc oncogene. |journal=Science |volume=232 |issue= 4751 |pages= 768-72 |year= 1986 |pmid= 3008339 |doi=  }}
*{{cite journal  | author=Garson JA, van den Berghe JA, Kemshead JT |title=Novel non-isotopic in situ hybridization technique detects small (1 Kb) unique sequences in routinely G-banded human chromosomes: fine mapping of N-myc and beta-NGF genes. |journal=Nucleic Acids Res. |volume=15 |issue= 12 |pages= 4761-70 |year= 1987 |pmid= 3299258 |doi=  }}
*{{cite journal  | author=Stanton LW, Bishop JM |title=Alternative processing of RNA transcribed from NMYC. |journal=Mol. Cell. Biol. |volume=7 |issue= 12 |pages= 4266-72 |year= 1988 |pmid= 3437890 |doi=  }}
*{{cite journal  | author=Kohl NE, Legouy E, DePinho RA, ''et al.'' |title=Human N-myc is closely related in organization and nucleotide sequence to c-myc. |journal=Nature |volume=319 |issue= 6048 |pages= 73-7 |year= 1986 |pmid= 3510398 |doi= 10.1038/319073a0 }}
*{{cite journal  | author=Grady EF, Schwab M, Rosenau W |title=Expression of N-myc and c-src during the development of fetal human brain. |journal=Cancer Res. |volume=47 |issue= 11 |pages= 2931-6 |year= 1987 |pmid= 3552210 |doi=  }}
*{{cite journal  | author=Ramsay G, Stanton L, Schwab M, Bishop JM |title=Human proto-oncogene N-myc encodes nuclear proteins that bind DNA. |journal=Mol. Cell. Biol. |volume=6 |issue= 12 |pages= 4450-7 |year= 1987 |pmid= 3796607 |doi=  }}
*{{cite journal  | author=Brodeur GM, Seeger RC |title=Gene amplification in human neuroblastomas: basic mechanisms and clinical implications. |journal=Cancer Genet. Cytogenet. |volume=19 |issue= 1-2 |pages= 101-11 |year= 1986 |pmid= 3940169 |doi=  }}
*{{cite journal  | author=Kanda N, Schreck R, Alt F, ''et al.'' |title=Isolation of amplified DNA sequences from IMR-32 human neuroblastoma cells: facilitation by fluorescence-activated flow sorting of metaphase chromosomes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 13 |pages= 4069-73 |year= 1983 |pmid= 6575396 |doi=  }}
*{{cite journal  | author=Schwab M, Varmus HE, Bishop JM, ''et al.'' |title=Chromosome localization in normal human cells and neuroblastomas of a gene related to c-myc. |journal=Nature |volume=308 |issue= 5956 |pages= 288-91 |year= 1984 |pmid= 6700732 |doi=  }}
*{{cite journal  | author=Brodeur GM, Seeger RC, Schwab M, ''et al.'' |title=Amplification of N-myc in untreated human neuroblastomas correlates with advanced disease stage. |journal=Science |volume=224 |issue= 4653 |pages= 1121-4 |year= 1984 |pmid= 6719137 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

NCAM1

• INFO: Beginning work on NCAM1... {November 14, 2007 2:49:05 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:50:00 PM PST}

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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_NCAM1_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1epf.
 | PDB = {{PDB2|1epf}}, {{PDB2|1lwr}}, {{PDB2|1qz1}}, {{PDB2|2e3v}}, {{PDB2|2haz}}, {{PDB2|2ncm}}, {{PDB2|3ncm}}
 | Name = Neural cell adhesion molecule 1
 | HGNCid = 7656
 | Symbol = NCAM1
 | AltSymbols =; CD56; MSK39; NCAM
 | OMIM = 116930
 | ECnumber =  
 | Homologene = 40754
 | MGIid = 97281
 | GeneAtlas_image1 = PBB_GE_NCAM1_212843_at_tn.png
 | GeneAtlas_image2 = PBB_GE_NCAM1_209968_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}} 
 | Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4684
    | Hs_Ensembl = ENSG00000149294
    | Hs_RefseqProtein = NP_000606
    | Hs_RefseqmRNA = NM_000615
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 112578307
    | Hs_GenLoc_end = 112653781
    | Hs_Uniprot = P13591
    | Mm_EntrezGene = 17967
    | Mm_Ensembl = ENSMUSG00000039542
    | Mm_RefseqmRNA = NM_001081445
    | Mm_RefseqProtein = NP_001074914
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 49257298
    | Mm_GenLoc_end = 49322170
    | Mm_Uniprot = O08909
  }}
}}
'''Neural cell adhesion molecule 1''', also known as '''NCAM1''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = 
}}

==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Rutishauser U, Acheson A, Hall AK, ''et al.'' |title=The neural cell adhesion molecule (NCAM) as a regulator of cell-cell interactions. |journal=Science |volume=240 |issue= 4848 |pages= 53-7 |year= 1988 |pmid= 3281256 |doi=  }}
*{{cite journal  | author=Rønn LC, Hartz BP, Bock E |title=The neural cell adhesion molecule (NCAM) in development and plasticity of the nervous system. |journal=Exp. Gerontol. |volume=33 |issue= 7-8 |pages= 853-64 |year= 1999 |pmid= 9951628 |doi=  }}
*{{cite journal  | author=Zeromski J, Nyczak E, Dyszkiewicz W |title=Significance of cell adhesion molecules, CD56/NCAM in particular, in human tumor growth and spreading. |journal=Folia Histochem. Cytobiol. |volume=39 Suppl 2 |issue=  |pages= 36-7 |year= 2002 |pmid= 11820619 |doi=  }}
*{{cite journal  | author=Itoh K, Kamiguchi H |title=[Neural cell adhesion molecules in lipid microdomains] |journal=Tanpakushitsu Kakusan Koso |volume=47 |issue= 4 Suppl |pages= 338-43 |year= 2002 |pmid= 11915324 |doi=  }}
*{{cite journal  | author=Sahara N, Takeshita A |title=Prognostic significance of surface markers expressed in multiple myeloma: CD56 and other antigens. |journal=Leuk. Lymphoma |volume=45 |issue= 1 |pages= 61-5 |year= 2004 |pmid= 15061198 |doi=  }}
*{{cite journal  | author=van Duijnhoven HL, Helfrich W, de Leij L, ''et al.'' |title=Splicing of the VASE exon of neural cell adhesion molecule (NCAM) in human small-cell lung carcinoma (SCLC). |journal=Int. J. Cancer |volume=50 |issue= 1 |pages= 118-23 |year= 1992 |pmid= 1339414 |doi=  }}
*{{cite journal  | author=Rossell RJ, Malik A, Helfrich W, ''et al.'' |title=A discordance between the human muscle NCAM sequence and those seen in other NCAM cDNA clones. |journal=Biochim. Biophys. Acta |volume=1130 |issue= 1 |pages= 95-6 |year= 1992 |pmid= 1543753 |doi=  }}
*{{cite journal  | author=Lanier LL, Chang C, Azuma M, ''et al.'' |title=Molecular and functional analysis of human natural killer cell-associated neural cell adhesion molecule (N-CAM/CD56). |journal=J. Immunol. |volume=146 |issue= 12 |pages= 4421-6 |year= 1991 |pmid= 1710251 |doi=  }}
*{{cite journal  | author=Bello MJ, Salagnon N, Rey JA, ''et al.'' |title=Precise in situ localization of NCAM, ETS1, and D11S29 on human meiotic chromosomes. |journal=Cytogenet. Cell Genet. |volume=52 |issue= 1-2 |pages= 7-10 |year= 1990 |pmid= 2612216 |doi=  }}
*{{cite journal  | author=Dickson G, Gower HJ, Barton CH, ''et al.'' |title=Human muscle neural cell adhesion molecule (N-CAM): identification of a muscle-specific sequence in the extracellular domain. |journal=Cell |volume=50 |issue= 7 |pages= 1119-30 |year= 1987 |pmid= 2887295 |doi=  }}
*{{cite journal  | author=Gower HJ, Barton CH, Elsom VL, ''et al.'' |title=Alternative splicing generates a secreted form of N-CAM in muscle and brain. |journal=Cell |volume=55 |issue= 6 |pages= 955-64 |year= 1989 |pmid= 3203385 |doi=  }}
*{{cite journal  | author=Barton CH, Dickson G, Gower HJ, ''et al.'' |title=Complete sequence and in vitro expression of a tissue-specific phosphatidylinositol-linked N-CAM isoform from skeletal muscle. |journal=Development |volume=104 |issue= 1 |pages= 165-73 |year= 1989 |pmid= 3253057 |doi=  }}
*{{cite journal  | author=Cunningham BA, Hemperly JJ, Murray BA, ''et al.'' |title=Neural cell adhesion molecule: structure, immunoglobulin-like domains, cell surface modulation, and alternative RNA splicing. |journal=Science |volume=236 |issue= 4803 |pages= 799-806 |year= 1987 |pmid= 3576199 |doi=  }}
*{{cite journal  | author=Nakayama J, Fukuda MN, Fredette B, ''et al.'' |title=Expression cloning of a human polysialyltransferase that forms the polysialylated neural cell adhesion molecule present in embryonic brain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 15 |pages= 7031-5 |year= 1995 |pmid= 7624364 |doi=  }}
*{{cite journal  | author=Meyer MB, Bastholm L, Nielsen MH, ''et al.'' |title=Localization of NCAM on NCAM-B-expressing cells with inhibited migration in collagen. |journal=APMIS |volume=103 |issue= 3 |pages= 197-208 |year= 1995 |pmid= 7755976 |doi=  }}
*{{cite journal  | author=Eckhardt M, Mühlenhoff M, Bethe A, ''et al.'' |title=Molecular characterization of eukaryotic polysialyltransferase-1. |journal=Nature |volume=373 |issue= 6516 |pages= 715-8 |year= 1995 |pmid= 7854457 |doi= 10.1038/373715a0 }}
*{{cite journal  | author=Saito S, Tanio Y, Tachibana I, ''et al.'' |title=Complementary DNA sequence encoding the major neural cell adhesion molecule isoform in a human small cell lung cancer cell line. |journal=Lung Cancer |volume=10 |issue= 5-6 |pages= 307-18 |year= 1994 |pmid= 8075973 |doi=  }}
*{{cite journal  | author=Horstkorte R, Schachner M, Magyar JP, ''et al.'' |title=The fourth immunoglobulin-like domain of NCAM contains a carbohydrate recognition domain for oligomannosidic glycans implicated in association with L1 and neurite outgrowth. |journal=J. Cell Biol. |volume=121 |issue= 6 |pages= 1409-21 |year= 1993 |pmid= 8509458 |doi=  }}
*{{cite journal  | author=Kojima N, Tachida Y, Yoshida Y, Tsuji S |title=Characterization of mouse ST8Sia II (STX) as a neural cell adhesion molecule-specific polysialic acid synthase. Requirement of core alpha1,6-linked fucose and a polypeptide chain for polysialylation. |journal=J. Biol. Chem. |volume=271 |issue= 32 |pages= 19457-63 |year= 1996 |pmid= 8702635 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

NCL

• INFO: Beginning work on NCL... {November 14, 2007 2:50:00 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:50:51 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_NCL_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 2fc8.
 | PDB = {{PDB2|2fc8}}, {{PDB2|2fc9}}
 | Name = Nucleolin
 | HGNCid = 7667
 | Symbol = NCL
 | AltSymbols =; C23; FLJ45706
 | OMIM = 164035
 | ECnumber =  
 | Homologene = 21821
 | MGIid =  
 | GeneAtlas_image1 = PBB_GE_NCL_200610_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003676 |text = nucleic acid binding}} {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0008022 |text = protein C-terminus binding}} 
 | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005730 |text = nucleolus}} {{GNF_GO|id=GO:0005938 |text = cell cortex}} 
 | Process = {{GNF_GO|id=GO:0001525 |text = angiogenesis}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4691
    | Hs_Ensembl = ENSG00000115053
    | Hs_RefseqProtein = NP_005372
    | Hs_RefseqmRNA = NM_005381
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 232027704
    | Hs_GenLoc_end = 232037449
    | Hs_Uniprot = P19338
    | Mm_EntrezGene =  
    | Mm_Ensembl =  
    | Mm_RefseqmRNA =  
    | Mm_RefseqProtein =  
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr =  
    | Mm_GenLoc_start =  
    | Mm_GenLoc_end =  
    | Mm_Uniprot =  
  }}
}}
'''Nucleolin''', also known as '''NCL''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = Nucleolin (NCL), a eukaryotic nucleolar phosphoprotein, is involved in the synthesis and maturation of ribosomes. It is located mainly in dense fibrillar regions of the nucleolus. Human NCL gene consists of 14 exons with 13 introns and spans approximately 11kb. The intron 11 of the NCL gene encodes a small nucleolar RNA, termed U20.<ref>{{cite web | title = Entrez Gene: NCL nucleolin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4691| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Tuteja R, Tuteja N |title=Nucleolin: a multifunctional major nucleolar phosphoprotein. |journal=Crit. Rev. Biochem. Mol. Biol. |volume=33 |issue= 6 |pages= 407-36 |year= 1999 |pmid= 9918513 |doi=  }}
*{{cite journal  | author=Pasternack MS, Bleier KJ, McInerney TN |title=Granzyme A binding to target cell proteins. Granzyme A binds to and cleaves nucleolin in vitro. |journal=J. Biol. Chem. |volume=266 |issue= 22 |pages= 14703-8 |year= 1991 |pmid= 1860869 |doi=  }}
*{{cite journal  | author=Belenguer P, Caizergues-Ferrer M, Labbé JC, ''et al.'' |title=Mitosis-specific phosphorylation of nucleolin by p34cdc2 protein kinase. |journal=Mol. Cell. Biol. |volume=10 |issue= 7 |pages= 3607-18 |year= 1990 |pmid= 2192260 |doi=  }}
*{{cite journal  | author=Srivastava M, McBride OW, Fleming PJ, ''et al.'' |title=Genomic organization and chromosomal localization of the human nucleolin gene. |journal=J. Biol. Chem. |volume=265 |issue= 25 |pages= 14922-31 |year= 1990 |pmid= 2394707 |doi=  }}
*{{cite journal  | author=Srivastava M, Fleming PJ, Pollard HB, Burns AL |title=Cloning and sequencing of the human nucleolin cDNA. |journal=FEBS Lett. |volume=250 |issue= 1 |pages= 99-105 |year= 1989 |pmid= 2737305 |doi=  }}
*{{cite journal  | author=Erard MS, Belenguer P, Caizergues-Ferrer M, ''et al.'' |title=A major nucleolar protein, nucleolin, induces chromatin decondensation by binding to histone H1. |journal=Eur. J. Biochem. |volume=175 |issue= 3 |pages= 525-30 |year= 1988 |pmid= 3409881 |doi=  }}
*{{cite journal  | author=Tuteja N, Huang NW, Skopac D, ''et al.'' |title=Human DNA helicase IV is nucleolin, an RNA helicase modulated by phosphorylation. |journal=Gene |volume=160 |issue= 2 |pages= 143-8 |year= 1995 |pmid= 7642087 |doi=  }}
*{{cite journal  | author=Jordan P, Heid H, Kinzel V, Kübler D |title=Major cell surface-located protein substrates of an ecto-protein kinase are homologs of known nuclear proteins. |journal=Biochemistry |volume=33 |issue= 49 |pages= 14696-706 |year= 1995 |pmid= 7993898 |doi=  }}
*{{cite journal  | author=Nicoloso M, Caizergues-Ferrer M, Michot B, ''et al.'' |title=U20, a novel small nucleolar RNA, is encoded in an intron of the nucleolin gene in mammals. |journal=Mol. Cell. Biol. |volume=14 |issue= 9 |pages= 5766-76 |year= 1994 |pmid= 8065311 |doi=  }}
*{{cite journal  | author=Ishikawa F, Matunis MJ, Dreyfuss G, Cech TR |title=Nuclear proteins that bind the pre-mRNA 3' splice site sequence r(UUAG/G) and the human telomeric DNA sequence d(TTAGGG)n. |journal=Mol. Cell. Biol. |volume=13 |issue= 7 |pages= 4301-10 |year= 1993 |pmid= 8321232 |doi=  }}
*{{cite journal  | author=Eggert M, Möws CC, Tripier D, ''et al.'' |title=A fraction enriched in a novel glucocorticoid receptor-interacting protein stimulates receptor-dependent transcription in vitro. |journal=J. Biol. Chem. |volume=270 |issue= 51 |pages= 30755-9 |year= 1996 |pmid= 8530516 |doi=  }}
*{{cite journal  | author=Bharti AK, Olson MO, Kufe DW, Rubin EH |title=Identification of a nucleolin binding site in human topoisomerase I. |journal=J. Biol. Chem. |volume=271 |issue= 4 |pages= 1993-7 |year= 1996 |pmid= 8567649 |doi=  }}
*{{cite journal  | author=Li YP, Busch RK, Valdez BC, Busch H |title=C23 interacts with B23, a putative nucleolar-localization-signal-binding protein. |journal=Eur. J. Biochem. |volume=237 |issue= 1 |pages= 153-8 |year= 1996 |pmid= 8620867 |doi=  }}
*{{cite journal  | author=Li D, Dobrowolska G, Krebs EG |title=The physical association of casein kinase 2 with nucleolin. |journal=J. Biol. Chem. |volume=271 |issue= 26 |pages= 15662-8 |year= 1996 |pmid= 8663258 |doi=  }}
*{{cite journal  | author=Zhou G, Seibenhener ML, Wooten MW |title=Nucleolin is a protein kinase C-zeta substrate. Connection between cell surface signaling and nucleus in PC12 cells. |journal=J. Biol. Chem. |volume=272 |issue= 49 |pages= 31130-7 |year= 1998 |pmid= 9388266 |doi=  }}
*{{cite journal  | author=Haluska P, Saleem A, Edwards TK, Rubin EH |title=Interaction between the N-terminus of human topoisomerase I and SV40 large T antigen. |journal=Nucleic Acids Res. |volume=26 |issue= 7 |pages= 1841-7 |year= 1998 |pmid= 9512561 |doi=  }}
*{{cite journal  | author=Borggrefe T, Wabl M, Akhmedov AT, Jessberger R |title=A B-cell-specific DNA recombination complex. |journal=J. Biol. Chem. |volume=273 |issue= 27 |pages= 17025-35 |year= 1998 |pmid= 9642267 |doi=  }}
*{{cite journal  | author=Larrucea S, González-Rubio C, Cambronero R, ''et al.'' |title=Cellular adhesion mediated by factor J, a complement inhibitor. Evidence for nucleolin involvement. |journal=J. Biol. Chem. |volume=273 |issue= 48 |pages= 31718-25 |year= 1998 |pmid= 9822633 |doi=  }}
*{{cite journal  | author=Parada CA, Roeder RG |title=A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription. |journal=EMBO J. |volume=18 |issue= 13 |pages= 3688-701 |year= 1999 |pmid= 10393184 |doi= 10.1093/emboj/18.13.3688 }}
}}
{{refend}}

{{protein-stub}}
 

SFTPA1

• INFO: Beginning work on SFTPA1... {November 14, 2007 2:51:44 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:52:26 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = Surfactant, pulmonary-associated protein A1
 | HGNCid = 10798
 | Symbol = SFTPA1
 | AltSymbols =; PSAP; COLEC4; MGC133365; PSPA; SFTP1; SP-A; SP-A1; SFTPA1
 | OMIM = 178630
 | ECnumber =  
 | Homologene = 88721
 | MGIid =  
 | Function = {{GNF_GO|id=GO:0005319 |text = lipid transporter activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005529 |text = sugar binding}} 
 | Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} 
 | Process = {{GNF_GO|id=GO:0006817 |text = phosphate transport}} {{GNF_GO|id=GO:0007585 |text = respiratory gaseous exchange}} {{GNF_GO|id=GO:0050828 |text = regulation of liquid surface tension}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6435
    | Hs_Ensembl =  
    | Hs_RefseqProtein = NP_005402
    | Hs_RefseqmRNA = NM_005411
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr =  
    | Hs_GenLoc_start =  
    | Hs_GenLoc_end =  
    | Hs_Uniprot =  
    | Mm_EntrezGene =  
    | Mm_Ensembl =  
    | Mm_RefseqmRNA =  
    | Mm_RefseqProtein =  
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr =  
    | Mm_GenLoc_start =  
    | Mm_GenLoc_end =  
    | Mm_Uniprot =  
  }}
}}
'''Surfactant, pulmonary-associated protein A1''', also known as '''SFTPA1''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = 
}}

==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Lu J |title=Collectins: collectors of microorganisms for the innate immune system. |journal=Bioessays |volume=19 |issue= 6 |pages= 509-18 |year= 1997 |pmid= 9204768 |doi= 10.1002/bies.950190610 }}
*{{cite journal  | author=Floros J, Hoover RR |title=Genetics of the hydrophilic surfactant proteins A and D. |journal=Biochim. Biophys. Acta |volume=1408 |issue= 2-3 |pages= 312-22 |year= 1999 |pmid= 9813381 |doi=  }}
*{{cite journal  | author=Khubchandani KR, Snyder JM |title=Surfactant protein A (SP-A): the alveolus and beyond. |journal=FASEB J. |volume=15 |issue= 1 |pages= 59-69 |year= 2001 |pmid= 11149893 |doi= 10.1096/fj.00-0318rev }}
*{{cite journal  | author=Katyal SL, Singh G, Locker J |title=Characterization of a second human pulmonary surfactant-associated protein SP-A gene. |journal=Am. J. Respir. Cell Mol. Biol. |volume=6 |issue= 4 |pages= 446-52 |year= 1992 |pmid= 1372511 |doi=  }}
*{{cite journal  | author=Childs RA, Wright JR, Ross GF, ''et al.'' |title=Specificity of lung surfactant protein SP-A for both the carbohydrate and the lipid moieties of certain neutral glycolipids. |journal=J. Biol. Chem. |volume=267 |issue= 14 |pages= 9972-9 |year= 1992 |pmid= 1577827 |doi=  }}
*{{cite journal  | author=Endo H, Oka T |title=An immunohistochemical study of bronchial cells producing surfactant protein A in the developing human fetal lung. |journal=Early Hum. Dev. |volume=25 |issue= 3 |pages= 149-56 |year= 1991 |pmid= 1935736 |doi=  }}
*{{cite journal  | author=Voss T, Melchers K, Scheirle G, Schäfer KP |title=Structural comparison of recombinant pulmonary surfactant protein SP-A derived from two human coding sequences: implications for the chain composition of natural human SP-A. |journal=Am. J. Respir. Cell Mol. Biol. |volume=4 |issue= 1 |pages= 88-94 |year= 1991 |pmid= 1986781 |doi=  }}
*{{cite journal  | author=Haagsman HP, White RT, Schilling J, ''et al.'' |title=Studies of the structure of lung surfactant protein SP-A. |journal=Am. J. Physiol. |volume=257 |issue= 6 Pt 1 |pages= L421-9 |year= 1990 |pmid= 2610270 |doi=  }}
*{{cite journal  | author=Fisher JH, Kao FT, Jones C, ''et al.'' |title=The coding sequence for the 32,000-dalton pulmonary surfactant-associated protein A is located on chromosome 10 and identifies two separate restriction-fragment-length polymorphisms. |journal=Am. J. Hum. Genet. |volume=40 |issue= 6 |pages= 503-11 |year= 1987 |pmid= 2884868 |doi=  }}
*{{cite journal  | author=White RT, Damm D, Miller J, ''et al.'' |title=Isolation and characterization of the human pulmonary surfactant apoprotein gene. |journal=Nature |volume=317 |issue= 6035 |pages= 361-3 |year= 1985 |pmid= 2995821 |doi=  }}
*{{cite journal  | author=Floros J, Steinbrink R, Jacobs K, ''et al.'' |title=Isolation and characterization of cDNA clones for the 35-kDa pulmonary surfactant-associated protein. |journal=J. Biol. Chem. |volume=261 |issue= 19 |pages= 9029-33 |year= 1986 |pmid= 3755136 |doi=  }}
*{{cite journal  | author=Schaeffer E, Guillou F, Part D, Zakin MM |title=A different combination of transcription factors modulates the expression of the human transferrin promoter in liver and Sertoli cells. |journal=J. Biol. Chem. |volume=268 |issue= 31 |pages= 23399-408 |year= 1993 |pmid= 8226864 |doi=  }}
*{{cite journal  | author=Khoor A, Gray ME, Hull WM, ''et al.'' |title=Developmental expression of SP-A and SP-A mRNA in the proximal and distal respiratory epithelium in the human fetus and newborn. |journal=J. Histochem. Cytochem. |volume=41 |issue= 9 |pages= 1311-9 |year= 1993 |pmid= 8354874 |doi=  }}
*{{cite journal  | author=Strayer DS, Yang S, Jerng HH |title=Surfactant protein A-binding proteins. Characterization and structures. |journal=J. Biol. Chem. |volume=268 |issue= 25 |pages= 18679-84 |year= 1993 |pmid= 8360162 |doi=  }}
*{{cite journal  | author=Kölble K, Lu J, Mole SE, ''et al.'' |title=Assignment of the human pulmonary surfactant protein D gene (SFTP4) to 10q22-q23 close to the surfactant protein A gene cluster. |journal=Genomics |volume=17 |issue= 2 |pages= 294-8 |year= 1993 |pmid= 8406480 |doi= 10.1006/geno.1993.1324 }}
*{{cite journal  | author=deMello DE, Heyman S, Phelps DS, Floros J |title=Immunogold localization of SP-A in lungs of infants dying from respiratory distress syndrome. |journal=Am. J. Pathol. |volume=142 |issue= 5 |pages= 1631-40 |year= 1993 |pmid= 8494055 |doi=  }}
*{{cite journal  | author=Chroneos ZC, Abdolrasulnia R, Whitsett JA, ''et al.'' |title=Purification of a cell-surface receptor for surfactant protein A. |journal=J. Biol. Chem. |volume=271 |issue= 27 |pages= 16375-83 |year= 1996 |pmid= 8663107 |doi=  }}
*{{cite journal  | author=Planer BC, Ning Y, Kumar SA, Ballard PL |title=Transcriptional regulation of surfactant proteins SP-A and SP-B by phorbol ester. |journal=Biochim. Biophys. Acta |volume=1353 |issue= 2 |pages= 171-9 |year= 1997 |pmid= 9294011 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

SMAD7

• INFO: Beginning work on SMAD7... {November 14, 2007 2:46:39 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:48:04 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image =  
 | image_source =  
 | PDB = 
 | Name = SMAD family member 7
 | HGNCid = 6773
 | Symbol = SMAD7
 | AltSymbols =; MADH7; FLJ16482; MADH8
 | OMIM = 602932
 | ECnumber =  
 | Homologene = 4314
 | MGIid = 1100518
 | GeneAtlas_image1 = PBB_GE_SMAD7_204790_at_tn.png
 | Function = {{GNF_GO|id=GO:0005076 |text = receptor signaling protein serine/threonine kinase signaling protein activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0030617 |text = transforming growth factor beta receptor, inhibitory cytoplasmic mediator activity}} 
 | Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} 
 | Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006950 |text = response to stress}} {{GNF_GO|id=GO:0007179 |text = transforming growth factor beta receptor signaling pathway}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4092
    | Hs_Ensembl = ENSG00000101665
    | Hs_RefseqProtein = NP_005895
    | Hs_RefseqmRNA = NM_005904
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 18
    | Hs_GenLoc_start = 44700222
    | Hs_GenLoc_end = 44731079
    | Hs_Uniprot = O15105
    | Mm_EntrezGene = 17131
    | Mm_Ensembl =  
    | Mm_RefseqmRNA = XM_986975
    | Mm_RefseqProtein = XP_992069
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr =  
    | Mm_GenLoc_start =  
    | Mm_GenLoc_end =  
    | Mm_Uniprot =  
  }}
}}
'''SMAD family member 7''', also known as '''SMAD7''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = 
}}

==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Massagué J |title=TGF-beta signal transduction. |journal=Annu. Rev. Biochem. |volume=67 |issue=  |pages= 753-91 |year= 1998 |pmid= 9759503 |doi= 10.1146/annurev.biochem.67.1.753 }}
*{{cite journal  | author=Verschueren K, Huylebroeck D |title=Remarkable versatility of Smad proteins in the nucleus of transforming growth factor-beta activated cells. |journal=Cytokine Growth Factor Rev. |volume=10 |issue= 3-4 |pages= 187-99 |year= 2000 |pmid= 10647776 |doi=  }}
*{{cite journal  | author=Wrana JL, Attisano L |title=The Smad pathway. |journal=Cytokine Growth Factor Rev. |volume=11 |issue= 1-2 |pages= 5-13 |year= 2000 |pmid= 10708948 |doi=  }}
*{{cite journal  | author=Miyazono K |title=TGF-beta signaling by Smad proteins. |journal=Cytokine Growth Factor Rev. |volume=11 |issue= 1-2 |pages= 15-22 |year= 2000 |pmid= 10708949 |doi=  }}
*{{cite journal  | author=Hayashi H, Abdollah S, Qiu Y, ''et al.'' |title=The MAD-related protein Smad7 associates with the TGFbeta receptor and functions as an antagonist of TGFbeta signaling. |journal=Cell |volume=89 |issue= 7 |pages= 1165-73 |year= 1997 |pmid= 9215638 |doi=  }}
*{{cite journal  | author=Topper JN, Cai J, Qiu Y, ''et al.'' |title=Vascular MADs: two novel MAD-related genes selectively inducible by flow in human vascular endothelium. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 17 |pages= 9314-9 |year= 1997 |pmid= 9256479 |doi=  }}
*{{cite journal  | author=Nakao A, Afrakhte M, Morén A, ''et al.'' |title=Identification of Smad7, a TGFbeta-inducible antagonist of TGF-beta signalling. |journal=Nature |volume=389 |issue= 6651 |pages= 631-5 |year= 1997 |pmid= 9335507 |doi= 10.1038/39369 }}
*{{cite journal  | author=Röijer E, Morén A, ten Dijke P, Stenman G |title=Assignment1 of the Smad7 gene (MADH7) to human chromosome 18q21.1 by fluorescence in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=81 |issue= 3-4 |pages= 189-90 |year= 1998 |pmid= 9730599 |doi=  }}
*{{cite journal  | author=Itóh S, Landström M, Hermansson A, ''et al.'' |title=Transforming growth factor beta1 induces nuclear export of inhibitory Smad7. |journal=J. Biol. Chem. |volume=273 |issue= 44 |pages= 29195-201 |year= 1998 |pmid= 9786930 |doi=  }}
*{{cite journal  | author=Datta PK, Moses HL |title=STRAP and Smad7 synergize in the inhibition of transforming growth factor beta signaling. |journal=Mol. Cell. Biol. |volume=20 |issue= 9 |pages= 3157-67 |year= 2000 |pmid= 10757800 |doi=  }}
*{{cite journal  | author=Denissova NG, Pouponnot C, Long J, ''et al.'' |title=Transforming growth factor beta -inducible independent binding of SMAD to the Smad7 promoter. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 12 |pages= 6397-402 |year= 2000 |pmid= 10823886 |doi= 10.1073/pnas.090099297 }}
*{{cite journal  | author=Stopa M, Anhuf D, Terstegen L, ''et al.'' |title=Participation of Smad2, Smad3, and Smad4 in transforming growth factor beta (TGF-beta)-induced activation of Smad7. THE TGF-beta response element of the promoter requires functional Smad binding element and E-box sequences for transcriptional regulation. |journal=J. Biol. Chem. |volume=275 |issue= 38 |pages= 29308-17 |year= 2000 |pmid= 10887185 |doi= 10.1074/jbc.M003282200 }}
*{{cite journal  | author=Kavsak P, Rasmussen RK, Causing CG, ''et al.'' |title=Smad7 binds to Smurf2 to form an E3 ubiquitin ligase that targets the TGF beta receptor for degradation. |journal=Mol. Cell |volume=6 |issue= 6 |pages= 1365-75 |year= 2001 |pmid= 11163210 |doi=  }}
*{{cite journal  | author=Ebisawa T, Fukuchi M, Murakami G, ''et al.'' |title=Smurf1 interacts with transforming growth factor-beta type I receptor through Smad7 and induces receptor degradation. |journal=J. Biol. Chem. |volume=276 |issue= 16 |pages= 12477-80 |year= 2001 |pmid= 11278251 |doi= 10.1074/jbc.C100008200 }}
*{{cite journal  | author=Itoh F, Asao H, Sugamura K, ''et al.'' |title=Promoting bone morphogenetic protein signaling through negative regulation of inhibitory Smads. |journal=EMBO J. |volume=20 |issue= 15 |pages= 4132-42 |year= 2001 |pmid= 11483516 |doi= 10.1093/emboj/20.15.4132 }}
*{{cite journal  | author=Yanagisawa M, Nakashima K, Takeda K, ''et al.'' |title=Inhibition of BMP2-induced, TAK1 kinase-mediated neurite outgrowth by Smad6 and Smad7. |journal=Genes Cells |volume=6 |issue= 12 |pages= 1091-9 |year= 2002 |pmid= 11737269 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

TFPI

• INFO: Beginning work on TFPI... {November 14, 2007 2:52:26 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:52:59 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_TFPI_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1adz.
 | PDB = {{PDB2|1adz}}, {{PDB2|1irh}}, {{PDB2|1tfx}}
 | Name = Tissue factor pathway inhibitor (lipoprotein-associated coagulation inhibitor)
 | HGNCid = 11760
 | Symbol = TFPI
 | AltSymbols =; TFI; EPI; LACI
 | OMIM = 152310
 | ECnumber =  
 | Homologene = 4579
 | MGIid = 1095418
 | GeneAtlas_image1 = PBB_GE_TFPI_209676_at_tn.png
 | GeneAtlas_image2 = PBB_GE_TFPI_210664_s_at_tn.png
 | GeneAtlas_image3 = PBB_GE_TFPI_210665_at_tn.png
 | Function = {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}} {{GNF_GO|id=GO:0030414 |text = protease inhibitor activity}} 
 | Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} 
 | Process = {{GNF_GO|id=GO:0007596 |text = blood coagulation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7035
    | Hs_Ensembl = ENSG00000003436
    | Hs_RefseqProtein = NP_001027452
    | Hs_RefseqmRNA = NM_001032281
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 188039530
    | Hs_GenLoc_end = 188127410
    | Hs_Uniprot = P10646
    | Mm_EntrezGene = 21788
    | Mm_Ensembl = ENSMUSG00000027082
    | Mm_RefseqmRNA = NM_011576
    | Mm_RefseqProtein = NP_035706
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 84233699
    | Mm_GenLoc_end = 84275013
    | Mm_Uniprot = O54819
  }}
}}
'''Tissue factor pathway inhibitor (lipoprotein-associated coagulation inhibitor)''', also known as '''TFPI''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene encodes a protease inhibitor that regulates the tissue factor (TF)-dependent pathway of blood coagulation. The coagulation process initiates with the formation of a factor VIIa-TF complex, which proteolytically activates additional proteases (factors IX and X) and ultimately leads to the formation of a fibrin clot. The product of this gene inhibits the activated factor X and VIIa-TF proteases in an autoregulatory loop. The encoded protein is glycosylated and predominantly found in the vascular endothelium and plasma in both free forms and complexed with plasma lipoproteins. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been confirmed.<ref>{{cite web | title = Entrez Gene: TFPI tissue factor pathway inhibitor (lipoprotein-associated coagulation inhibitor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7035| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Broze GJ, Girard TJ, Novotny WF |title=Regulation of coagulation by a multivalent Kunitz-type inhibitor. |journal=Biochemistry |volume=29 |issue= 33 |pages= 7539-46 |year= 1991 |pmid= 2271516 |doi=  }}
*{{cite journal  | author=McVey JH |title=Tissue factor pathway. |journal=Baillieres Best Pract. Res. Clin. Haematol. |volume=12 |issue= 3 |pages= 361-72 |year= 2000 |pmid= 10856975 |doi=  }}
*{{cite journal  | author=Bajaj MS, Birktoft JJ, Steer SA, Bajaj SP |title=Structure and biology of tissue factor pathway inhibitor. |journal=Thromb. Haemost. |volume=86 |issue= 4 |pages= 959-72 |year= 2002 |pmid= 11686353 |doi=  }}
*{{cite journal  | author=Witt I |title=[Tissue factor pathway inhibitor: biochemistry, molecular biology, physiology and physiopathology] |journal=Hamostaseologie |volume=22 |issue= 2 |pages= 30-5 |year= 2002 |pmid= 12193974 |doi= 10.1267/Hamo02020071 }}
*{{cite journal  | author=Lwaleed BA, Bass PS |title=Tissue factor pathway inhibitor: structure, biology and involvement in disease. |journal=J. Pathol. |volume=208 |issue= 3 |pages= 327-39 |year= 2006 |pmid= 16261634 |doi= 10.1002/path.1871 }}
*{{cite journal  | author=Van der Logt CP, Kluck PM, Wiegant J, ''et al.'' |title=Refined regional assignment of the human tissue factor pathway inhibitor (TFPI) gene to chromosome band 2q32 by non-isotopic in situ hybridization. |journal=Hum. Genet. |volume=89 |issue= 5 |pages= 577-8 |year= 1992 |pmid= 1353057 |doi=  }}
*{{cite journal  | author=Higuchi DA, Wun TC, Likert KM, Broze GJ |title=The effect of leukocyte elastase on tissue factor pathway inhibitor. |journal=Blood |volume=79 |issue= 7 |pages= 1712-9 |year= 1992 |pmid= 1558967 |doi=  }}
*{{cite journal  | author=van der Logt CP, Reitsma PH, Bertina RM |title=Intron-exon organization of the human gene coding for the lipoprotein-associated coagulation inhibitor: the factor Xa dependent inhibitor of the extrinsic pathway of coagulation. |journal=Biochemistry |volume=30 |issue= 6 |pages= 1571-7 |year= 1991 |pmid= 1993173 |doi=  }}
*{{cite journal  | author=Girard TJ, Eddy R, Wesselschmidt RL, ''et al.'' |title=Structure of the human lipoprotein-associated coagulation inhibitor gene. Intro/exon gene organization and localization of the gene to chromosome 2. |journal=J. Biol. Chem. |volume=266 |issue= 8 |pages= 5036-41 |year= 1991 |pmid= 2002045 |doi=  }}
*{{cite journal  | author=Wun TC, Kretzmer KK, Girard TJ, ''et al.'' |title=Cloning and characterization of a cDNA coding for the lipoprotein-associated coagulation inhibitor shows that it consists of three tandem Kunitz-type inhibitory domains. |journal=J. Biol. Chem. |volume=263 |issue= 13 |pages= 6001-4 |year= 1988 |pmid= 2452157 |doi=  }}
*{{cite journal  | author=Novotny WF, Girard TJ, Miletich JP, Broze GJ |title=Purification and characterization of the lipoprotein-associated coagulation inhibitor from human plasma. |journal=J. Biol. Chem. |volume=264 |issue= 31 |pages= 18832-7 |year= 1989 |pmid= 2553722 |doi=  }}
*{{cite journal  | author=Girard TJ, Warren LA, Novotny WF, ''et al.'' |title=Identification of the 1.4 kb and 4.0 kb messages for the lipoprotein associated coagulation inhibitor and expression of the encoded protein. |journal=Thromb. Res. |volume=55 |issue= 1 |pages= 37-50 |year= 1989 |pmid= 2781520 |doi=  }}
*{{cite journal  | author=Girard TJ, Warren LA, Novotny WF, ''et al.'' |title=Functional significance of the Kunitz-type inhibitory domains of lipoprotein-associated coagulation inhibitor. |journal=Nature |volume=338 |issue= 6215 |pages= 518-20 |year= 1989 |pmid= 2927510 |doi= 10.1038/338518a0 }}
*{{cite journal  | author=Broze GJ, Miletich JP |title=Characterization of the inhibition of tissue factor in serum. |journal=Blood |volume=69 |issue= 1 |pages= 150-5 |year= 1987 |pmid= 3024756 |doi=  }}
*{{cite journal  | author=Broze GJ, Warren LA, Novotny WF, ''et al.'' |title=The lipoprotein-associated coagulation inhibitor that inhibits the factor VII-tissue factor complex also inhibits factor Xa: insight into its possible mechanism of action. |journal=Blood |volume=71 |issue= 2 |pages= 335-43 |year= 1988 |pmid= 3422166 |doi=  }}
*{{cite journal  | author=Rao LV, Rapaport SI |title=Studies of a mechanism inhibiting the initiation of the extrinsic pathway of coagulation. |journal=Blood |volume=69 |issue= 2 |pages= 645-51 |year= 1987 |pmid= 3492226 |doi=  }}
*{{cite journal  | author=Stubbs MT, Huber R, Bode W |title=Crystal structures of factor Xa specific inhibitors in complex with trypsin: structural grounds for inhibition of factor Xa and selectivity against thrombin. |journal=FEBS Lett. |volume=375 |issue= 1-2 |pages= 103-7 |year= 1996 |pmid= 7498454 |doi=  }}
*{{cite journal  | author=Warshawsky I, Bu G, Mast A, ''et al.'' |title=The carboxy terminus of tissue factor pathway inhibitor is required for interacting with hepatoma cells in vitro and in vivo. |journal=J. Clin. Invest. |volume=95 |issue= 4 |pages= 1773-81 |year= 1995 |pmid= 7706485 |doi=  }}
*{{cite journal  | author=Broze GJ, Lange GW, Duffin KL, MacPhail L |title=Heterogeneity of plasma tissue factor pathway inhibitor. |journal=Blood Coagul. Fibrinolysis |volume=5 |issue= 4 |pages= 551-9 |year= 1995 |pmid= 7841311 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

TNC

• INFO: Beginning work on TNC... {November 14, 2007 2:40:28 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:45:14 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_TNC_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ten.
 | PDB = {{PDB2|1ten}}
 | Name = Tenascin C (hexabrachion)
 | HGNCid = 5318
 | Symbol = TNC
 | AltSymbols =; HXB; TN
 | OMIM = 187380
 | ECnumber =  
 | Homologene = 55636
 | MGIid = 101922
 | GeneAtlas_image1 = PBB_GE_TNC_201645_at_tn.png
 | Function = {{GNF_GO|id=GO:0005102 |text = receptor binding}} 
 | Component = {{GNF_GO|id=GO:0005604 |text = basement membrane}} 
 | Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007528 |text = neuromuscular junction development}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3371
    | Hs_Ensembl = ENSG00000041982
    | Hs_RefseqProtein = NP_002151
    | Hs_RefseqmRNA = NM_002160
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 116822634
    | Hs_GenLoc_end = 116920260
    | Hs_Uniprot = P24821
    | Mm_EntrezGene = 21923
    | Mm_Ensembl = ENSMUSG00000028364
    | Mm_RefseqmRNA = NM_011607
    | Mm_RefseqProtein = NP_035737
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 63446149
    | Mm_GenLoc_end = 63533177
    | Mm_Uniprot = Q80YX0
  }}
}}
'''Tenascin C (hexabrachion)''', also known as '''TNC''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = 
}}

==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Imanaka-Yoshida K, Hiroe M, Yoshida T |title=Interaction between cell and extracellular matrix in heart disease: multiple roles of tenascin-C in tissue remodeling. |journal=Histol. Histopathol. |volume=19 |issue= 2 |pages= 517-25 |year= 2004 |pmid= 15024713 |doi=  }}
*{{cite journal  | author=Leahy DJ, Hendrickson WA, Aukhil I, Erickson HP |title=Structure of a fibronectin type III domain from tenascin phased by MAD analysis of the selenomethionyl protein. |journal=Science |volume=258 |issue= 5084 |pages= 987-91 |year= 1992 |pmid= 1279805 |doi=  }}
*{{cite journal  | author=White DM, Mikol DD, Espinosa R, ''et al.'' |title=Structure and chromosomal localization of the human gene for a brain form of prostaglandin D2 synthase. |journal=J. Biol. Chem. |volume=267 |issue= 32 |pages= 23202-8 |year= 1992 |pmid= 1385416 |doi=  }}
*{{cite journal  | author=Nies DE, Hemesath TJ, Kim JH, ''et al.'' |title=The complete cDNA sequence of human hexabrachion (Tenascin). A multidomain protein containing unique epidermal growth factor repeats. |journal=J. Biol. Chem. |volume=266 |issue= 5 |pages= 2818-23 |year= 1991 |pmid= 1704365 |doi=  }}
*{{cite journal  | author=Siri A, Carnemolla B, Saginati M, ''et al.'' |title=Human tenascin: primary structure, pre-mRNA splicing patterns and localization of the epitopes recognized by two monoclonal antibodies. |journal=Nucleic Acids Res. |volume=19 |issue= 3 |pages= 525-31 |year= 1991 |pmid= 1707164 |doi=  }}
*{{cite journal  | author=Gulcher JR, Nies DE, Alexakos MJ, ''et al.'' |title=Structure of the human hexabrachion (tenascin) gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 21 |pages= 9438-42 |year= 1991 |pmid= 1719530 |doi=  }}
*{{cite journal  | author=Gulcher JR, Nies DE, Marton LS, Stefansson K |title=An alternatively spliced region of the human hexabrachion contains a repeat of potential N-glycosylation sites. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 5 |pages= 1588-92 |year= 1989 |pmid= 2466295 |doi=  }}
*{{cite journal  | author=Chung CY, Zardi L, Erickson HP |title=Binding of tenascin-C to soluble fibronectin and matrix fibrils. |journal=J. Biol. Chem. |volume=270 |issue= 48 |pages= 29012-7 |year= 1996 |pmid= 7499434 |doi=  }}
*{{cite journal  | author=Yokosaki Y, Palmer EL, Prieto AL, ''et al.'' |title=The integrin alpha 9 beta 1 mediates cell attachment to a non-RGD site in the third fibronectin type III repeat of tenascin. |journal=J. Biol. Chem. |volume=269 |issue= 43 |pages= 26691-6 |year= 1994 |pmid= 7523411 |doi=  }}
*{{cite journal  | author=Glumoff V, Savontaus M, Vehanen J, Vuorio E |title=Analysis of aggrecan and tenascin gene expression in mouse skeletal tissues by northern and in situ hybridization using species specific cDNA probes. |journal=Biochim. Biophys. Acta |volume=1219 |issue= 3 |pages= 613-22 |year= 1994 |pmid= 7524681 |doi=  }}
*{{cite journal  | author=Gherzi R, Carnemolla B, Siri A, ''et al.'' |title=Human tenascin gene. Structure of the 5'-region, identification, and characterization of the transcription regulatory sequences. |journal=J. Biol. Chem. |volume=270 |issue= 7 |pages= 3429-34 |year= 1995 |pmid= 7531707 |doi=  }}
*{{cite journal  | author=Weinacker A, Ferrando R, Elliott M, ''et al.'' |title=Distribution of integrins alpha v beta 6 and alpha 9 beta 1 and their known ligands, fibronectin and tenascin, in human airways. |journal=Am. J. Respir. Cell Mol. Biol. |volume=12 |issue= 5 |pages= 547-56 |year= 1995 |pmid= 7537970 |doi=  }}
*{{cite journal  | author=Schnapp LM, Hatch N, Ramos DM, ''et al.'' |title=The human integrin alpha 8 beta 1 functions as a receptor for tenascin, fibronectin, and vitronectin. |journal=J. Biol. Chem. |volume=270 |issue= 39 |pages= 23196-202 |year= 1995 |pmid= 7559467 |doi=  }}
*{{cite journal  | author=Sriramarao P, Mendler M, Bourdon MA |title=Endothelial cell attachment and spreading on human tenascin is mediated by alpha 2 beta 1 and alpha v beta 3 integrins. |journal=J. Cell. Sci. |volume=105 ( Pt 4) |issue=  |pages= 1001-12 |year= 1993 |pmid= 7693733 |doi=  }}
*{{cite journal  | author=Prieto AL, Edelman GM, Crossin KL |title=Multiple integrins mediate cell attachment to cytotactin/tenascin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 21 |pages= 10154-8 |year= 1993 |pmid= 7694284 |doi=  }}
*{{cite journal  | author=Zagzag D, Friedlander DR, Dosik J, ''et al.'' |title=Tenascin-C expression by angiogenic vessels in human astrocytomas and by human brain endothelial cells in vitro. |journal=Cancer Res. |volume=56 |issue= 1 |pages= 182-9 |year= 1996 |pmid= 8548761 |doi=  }}
*{{cite journal  | author=Yokosaki Y, Monis H, Chen J, Sheppard D |title=Differential effects of the integrins alpha9beta1, alphavbeta3, and alphavbeta6 on cell proliferative responses to tenascin. Roles of the beta subunit extracellular and cytoplasmic domains. |journal=J. Biol. Chem. |volume=271 |issue= 39 |pages= 24144-50 |year= 1996 |pmid= 8798654 |doi=  }}
*{{cite journal  | author=Burg MA, Tillet E, Timpl R, Stallcup WB |title=Binding of the NG2 proteoglycan to type VI collagen and other extracellular matrix molecules. |journal=J. Biol. Chem. |volume=271 |issue= 42 |pages= 26110-6 |year= 1996 |pmid= 8824254 |doi=  }}
*{{cite journal  | author=Jones PL, Crack J, Rabinovitch M |title=Regulation of tenascin-C, a vascular smooth muscle cell survival factor that interacts with the alpha v beta 3 integrin to promote epidermal growth factor receptor phosphorylation and growth. |journal=J. Cell Biol. |volume=139 |issue= 1 |pages= 279-93 |year= 1998 |pmid= 9314546 |doi=  }}
*{{cite journal  | author=Rauch U, Clement A, Retzler C, ''et al.'' |title=Mapping of a defined neurocan binding site to distinct domains of tenascin-C. |journal=J. Biol. Chem. |volume=272 |issue= 43 |pages= 26905-12 |year= 1997 |pmid= 9341124 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

UCP2

• INFO: Beginning work on UCP2... {November 14, 2007 2:52:59 PM PST}
• SEARCH REDIRECT: Control Box Found: UCP2 {November 14, 2007 2:53:40 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 14, 2007 2:53:42 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 14, 2007 2:53:42 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 14, 2007 2:53:42 PM PST}
• UPDATED: Updated protein page: UCP2 {November 14, 2007 2:53:49 PM PST}

VTN

• INFO: Beginning work on VTN... {November 14, 2007 2:53:49 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:54:18 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_VTN_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1oc0.
 | PDB = {{PDB2|1oc0}}, {{PDB2|1s4g}}, {{PDB2|1ssu}}
 | Name = Vitronectin
 | HGNCid = 12724
 | Symbol = VTN
 | AltSymbols =; V75; VN; VNT
 | OMIM = 193190
 | ECnumber =  
 | Homologene = 532
 | MGIid = 98940
 | GeneAtlas_image1 = PBB_GE_VTN_204534_at_tn.png
 | Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008201 |text = heparin binding}} 
 | Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} 
 | Process = {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007160 |text = cell-matrix adhesion}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7448
    | Hs_Ensembl = ENSG00000109072
    | Hs_RefseqProtein = NP_000629
    | Hs_RefseqmRNA = NM_000638
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 23718425
    | Hs_GenLoc_end = 23721844
    | Hs_Uniprot = P04004
    | Mm_EntrezGene = 22370
    | Mm_Ensembl = ENSMUSG00000017344
    | Mm_RefseqmRNA = NM_011707
    | Mm_RefseqProtein = NP_035837
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 78315315
    | Mm_GenLoc_end = 78318518
    | Mm_Uniprot = Q5SYG4
  }}
}}
'''Vitronectin''', also known as '''VTN''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = The protein encoded by this gene is a member of the pexin family. It is found in serum and tissues and promotes cell adhesion and spreading, inhibits the membrane-damaging effect of the terminal cytolytic complement pathway, and binds to several serpin serine protease inhibitors. It is a secreted protein and exists in either a single chain form or a clipped, two chain form held together by a disulfide bond.<ref>{{cite web | title = Entrez Gene: VTN vitronectin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7448| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Schroeck F, Arroyo de Prada N, Sperl S, ''et al.'' |title=Interaction of plasminogen activator inhibitor type-1 (PAI-1) with vitronectin (Vn): mapping the binding sites on PAI-1 and Vn. |journal=Biol. Chem. |volume=383 |issue= 7-8 |pages= 1143-9 |year= 2003 |pmid= 12437099 |doi=  }}
*{{cite journal  | author=Fryklund L, Sievertsson H |title=Primary structure of somatomedin B: a growth hormone-dependent serum factor with protease inhibiting activity. |journal=FEBS Lett. |volume=87 |issue= 1 |pages= 55-60 |year= 1978 |pmid= 631332 |doi=  }}
*{{cite journal  | author=Fink TM, Jenne DE, Lichter P |title=The human vitronectin (complement S-protein) gene maps to the centromeric region of 17q. |journal=Hum. Genet. |volume=88 |issue= 5 |pages= 569-72 |year= 1992 |pmid= 1372588 |doi=  }}
*{{cite journal  | author=Liakka KA, Autio-Harmainen HI |title=Distribution of the extracellular matrix proteins tenascin, fibronectin, and vitronectin in fetal, infant, and adult human spleens. |journal=J. Histochem. Cytochem. |volume=40 |issue= 8 |pages= 1203-10 |year= 1992 |pmid= 1377736 |doi=  }}
*{{cite journal  | author=Smith JW, Vestal DJ, Irwin SV, ''et al.'' |title=Purification and functional characterization of integrin alpha v beta 5. An adhesion receptor for vitronectin. |journal=J. Biol. Chem. |volume=265 |issue= 19 |pages= 11008-13 |year= 1990 |pmid= 1694173 |doi=  }}
*{{cite journal  | author=Chain D, Korc-Grodzicki B, Kreizman T, Shaltiel S |title=The phosphorylation of the two-chain form of vitronectin by protein kinase A is heparin dependent. |journal=FEBS Lett. |volume=269 |issue= 1 |pages= 221-5 |year= 1990 |pmid= 1696913 |doi=  }}
*{{cite journal  | author=Seiffert D, Loskutoff DJ |title=Evidence that type 1 plasminogen activator inhibitor binds to the somatomedin B domain of vitronectin. |journal=J. Biol. Chem. |volume=266 |issue= 5 |pages= 2824-30 |year= 1991 |pmid= 1704366 |doi=  }}
*{{cite journal  | author=Chain D, Korc-Grodzicki B, Kreizman T, Shaltiel S |title=Endogenous cleavage of the Arg-379-Ala-380 bond in vitronectin results in a distinct conformational change which 'buries' Ser-378, its site of phosphorylation by protein kinase A. |journal=Biochem. J. |volume=274 ( Pt 2) |issue=  |pages= 387-94 |year= 1991 |pmid= 1706595 |doi=  }}
*{{cite journal  | author=Yaoi Y, Hashimoto K, Takahara K, Kato I |title=Insulin binds to type V collagen with retention of mitogenic activity. |journal=Exp. Cell Res. |volume=194 |issue= 2 |pages= 180-5 |year= 1991 |pmid= 1709100 |doi=  }}
*{{cite journal  | author=Suzuki S, Oldberg A, Hayman EG, ''et al.'' |title=Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin. |journal=EMBO J. |volume=4 |issue= 10 |pages= 2519-24 |year= 1985 |pmid= 2414098 |doi=  }}
*{{cite journal  | author=Preissner KT, Heimburger N, Anders E, Müller-Berghaus G |title=Physicochemical, immunochemical and functional comparison of human S-protein and vitronectin. Evidence for the identity of both plasma proteins. |journal=Biochem. Biophys. Res. Commun. |volume=134 |issue= 2 |pages= 951-6 |year= 1986 |pmid= 2418831 |doi=  }}
*{{cite journal  | author=Dahlbäck K, Löfberg H, Dahlbäck B |title=Localization of vitronectin (S-protein of complement) in normal human skin. |journal=Acta Derm. Venereol. |volume=66 |issue= 6 |pages= 461-7 |year= 1987 |pmid= 2433863 |doi=  }}
*{{cite journal  | author=Jenne D, Stanley KK |title=Nucleotide sequence and organization of the human S-protein gene: repeating peptide motifs in the "pexin" family and a model for their evolution. |journal=Biochemistry |volume=26 |issue= 21 |pages= 6735-42 |year= 1988 |pmid= 2447940 |doi=  }}
*{{cite journal  | author=McGuire EA, Peacock ME, Inhorn RC, ''et al.'' |title=Phosphorylation of vitronectin by a protein kinase in human plasma. Identification of a unique phosphorylation site in the heparin-binding domain. |journal=J. Biol. Chem. |volume=263 |issue= 4 |pages= 1942-5 |year= 1988 |pmid= 2448300 |doi=  }}
*{{cite journal  | author=Kubota K, Katayama S, Matsuda M, Hayashi M |title=Three types of vitronectin in human blood. |journal=Cell Struct. Funct. |volume=13 |issue= 2 |pages= 123-8 |year= 1988 |pmid= 2454751 |doi=  }}
*{{cite journal  | author=Hildebrand A, Preissner KT, Müller-Berghaus G, Teschemacher H |title=A novel beta-endorphin binding protein. Complement S protein (= vitronectin) exhibits specific non-opioid binding sites for beta-endorphin upon interaction with heparin or surfaces. |journal=J. Biol. Chem. |volume=264 |issue= 26 |pages= 15429-34 |year= 1989 |pmid= 2475499 |doi=  }}
*{{cite journal  | author=Jenne D, Hille A, Stanley KK, Huttner WB |title=Sulfation of two tyrosine-residues in human complement S-protein (vitronectin). |journal=Eur. J. Biochem. |volume=185 |issue= 2 |pages= 391-5 |year= 1990 |pmid= 2479556 |doi=  }}
*{{cite journal  | author=Jenne D, Stanley KK |title=Molecular cloning of S-protein, a link between complement, coagulation and cell-substrate adhesion. |journal=EMBO J. |volume=4 |issue= 12 |pages= 3153-7 |year= 1986 |pmid= 3004934 |doi=  }}
*{{cite journal  | author=Suzuki S, Pierschbacher MD, Hayman EG, ''et al.'' |title=Domain structure of vitronectin. Alignment of active sites. |journal=J. Biol. Chem. |volume=259 |issue= 24 |pages= 15307-14 |year= 1985 |pmid= 6210287 |doi=  }}
*{{cite journal  | author=Castaños-Velez E, Biberfeld P, Patarroyo M |title=Extracellular matrix proteins and integrin receptors in reactive and non-reactive lymph nodes. |journal=Immunology |volume=86 |issue= 2 |pages= 270-8 |year= 1996 |pmid= 7490129 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

YWHAE

• INFO: Beginning work on YWHAE... {November 14, 2007 2:54:18 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 14, 2007 2:55:13 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| require_manual_inspection = no 
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_YWHAE_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 2br9.
 | PDB = {{PDB2|2br9}}
 | Name = Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, epsilon polypeptide
 | HGNCid = 12851
 | Symbol = YWHAE
 | AltSymbols =; MDCR; MDS; KCIP-1; 14-3-3E; FLJ45465
 | OMIM = 605066
 | ECnumber =  
 | Homologene = 38223
 | MGIid = 894689
 | GeneAtlas_image1 = PBB_GE_YWHAE_210317_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_YWHAE_210996_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0019899 |text = enzyme binding}} {{GNF_GO|id=GO:0019904 |text = protein domain specific binding}} 
 | Component = 
 | Process = {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7531
    | Hs_Ensembl = ENSG00000108953
    | Hs_RefseqProtein = XP_001126863
    | Hs_RefseqmRNA = XM_001126863
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 17
    | Hs_GenLoc_start = 1194558
    | Hs_GenLoc_end = 1250231
    | Hs_Uniprot = P62258
    | Mm_EntrezGene = 22627
    | Mm_Ensembl = ENSMUSG00000020849
    | Mm_RefseqmRNA = NM_009536
    | Mm_RefseqProtein = NP_033562
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 11
    | Mm_GenLoc_start = 75549134
    | Mm_GenLoc_end = 75582033
    | Mm_Uniprot = Q3V453
  }}
}}
'''Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, epsilon polypeptide''', also known as '''YWHAE''', is a human [[gene]].

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = This gene product belongs to the 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. This highly conserved protein family is found in both plants and mammals, and this protein is 100% identical to the mouse ortholog. It interacts with CDC25 phosphatases, RAF1 and IRS1 proteins, suggesting its role in diverse biochemical activities related to signal transduction, such as cell division and regulation of insulin sensitivity. It has also been implicated in the pathogenesis of small cell lung cancer.<ref>{{cite web | title = Entrez Gene: YWHAE tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, epsilon polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7531| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Kino T, Pavlakis GN |title=Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1. |journal=DNA Cell Biol. |volume=23 |issue= 4 |pages= 193-205 |year= 2004 |pmid= 15142377 |doi= 10.1089/104454904773819789 }}
*{{cite journal  | author=Kino T, Chrousos GP |title=Human immunodeficiency virus type-1 accessory protein Vpr: a causative agent of the AIDS-related insulin resistance/lipodystrophy syndrome? |journal=Ann. N. Y. Acad. Sci. |volume=1024 |issue=  |pages= 153-67 |year= 2004 |pmid= 15265780 |doi= 10.1196/annals.1321.013 }}
*{{cite journal  | author=Jones DH, Ley S, Aitken A |title=Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteins. |journal=FEBS Lett. |volume=368 |issue= 1 |pages= 55-8 |year= 1995 |pmid= 7615088 |doi=  }}
*{{cite journal  | author=Conklin DS, Galaktionov K, Beach D |title=14-3-3 proteins associate with cdc25 phosphatases. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 17 |pages= 7892-6 |year= 1995 |pmid= 7644510 |doi=  }}
*{{cite journal  | author=Jin DY, Lyu MS, Kozak CA, Jeang KT |title=Function of 14-3-3 proteins. |journal=Nature |volume=382 |issue= 6589 |pages= 308 |year= 1996 |pmid= 8684458 |doi= 10.1038/382308a0 }}
*{{cite journal  | author=Vincenz C, Dixit VM |title=14-3-3 proteins associate with A20 in an isoform-specific manner and function both as chaperone and adapter molecules. |journal=J. Biol. Chem. |volume=271 |issue= 33 |pages= 20029-34 |year= 1996 |pmid= 8702721 |doi=  }}
*{{cite journal  | author=Chong SS, Tanigami A, Roschke AV, Ledbetter DH |title=14-3-3 epsilon has no homology to LIS1 and lies telomeric to it on chromosome 17p13.3 outside the Miller-Dieker syndrome chromosome region. |journal=Genome Res. |volume=6 |issue= 8 |pages= 735-41 |year= 1997 |pmid= 8858348 |doi=  }}
*{{cite journal  | author=Craparo A, Freund R, Gustafson TA |title=14-3-3 (epsilon) interacts with the insulin-like growth factor I receptor and insulin receptor substrate I in a phosphoserine-dependent manner. |journal=J. Biol. Chem. |volume=272 |issue= 17 |pages= 11663-9 |year= 1997 |pmid= 9111084 |doi=  }}
*{{cite journal  | author=Han L, Wong D, Dhaka A, ''et al.'' |title=Protein binding and signaling properties of RIN1 suggest a unique effector function. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 10 |pages= 4954-9 |year= 1997 |pmid= 9144171 |doi=  }}
*{{cite journal  | author=Ogihara T, Isobe T, Ichimura T, ''et al.'' |title=14-3-3 protein binds to insulin receptor substrate-1, one of the binding sites of which is in the phosphotyrosine binding domain. |journal=J. Biol. Chem. |volume=272 |issue= 40 |pages= 25267-74 |year= 1997 |pmid= 9312143 |doi=  }}
*{{cite journal  | author=Hsu SY, Kaipia A, Zhu L, Hsueh AJ |title=Interference of BAD (Bcl-xL/Bcl-2-associated death promoter)-induced apoptosis in mammalian cells by 14-3-3 isoforms and P11. |journal=Mol. Endocrinol. |volume=11 |issue= 12 |pages= 1858-67 |year= 1997 |pmid= 9369453 |doi=  }}
*{{cite journal  | author=Luk SC, Garcia-Barcelo M, Tsui SK, ''et al.'' |title=Assignment of the human 14-3-3 epsilon isoform (YWHAE) to human chromosome 17p13 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=78 |issue= 2 |pages= 105-6 |year= 1997 |pmid= 9371399 |doi=  }}
*{{cite journal  | author=Nagata K, Puls A, Futter C, ''et al.'' |title=The MAP kinase kinase kinase MLK2 co-localizes with activated JNK along microtubules and associates with kinesin superfamily motor KIF3. |journal=EMBO J. |volume=17 |issue= 1 |pages= 149-58 |year= 1998 |pmid= 9427749 |doi= 10.1093/emboj/17.1.149 }}
*{{cite journal  | author=Fanger GR, Widmann C, Porter AC, ''et al.'' |title=14-3-3 proteins interact with specific MEK kinases. |journal=J. Biol. Chem. |volume=273 |issue= 6 |pages= 3476-83 |year= 1998 |pmid= 9452471 |doi=  }}
*{{cite journal  | author=Ku NO, Liao J, Omary MB |title=Phosphorylation of human keratin 18 serine 33 regulates binding to 14-3-3 proteins. |journal=EMBO J. |volume=17 |issue= 7 |pages= 1892-906 |year= 1998 |pmid= 9524113 |doi= 10.1093/emboj/17.7.1892 }}
*{{cite journal  | author=Luk SC, Ngai SM, Tsui SK, ''et al.'' |title=In vivo and in vitro association of 14-3-3 epsilon isoform with calmodulin: implication for signal transduction and cell proliferation. |journal=J. Cell. Biochem. |volume=73 |issue= 1 |pages= 31-5 |year= 1999 |pmid= 10088721 |doi=  }}
*{{cite journal  | author=Ostrerova N, Petrucelli L, Farrer M, ''et al.'' |title=alpha-Synuclein shares physical and functional homology with 14-3-3 proteins. |journal=J. Neurosci. |volume=19 |issue= 14 |pages= 5782-91 |year= 1999 |pmid= 10407019 |doi=  }}
*{{cite journal  | author=Finlin BS, Andres DA |title=Phosphorylation-dependent association of the Ras-related GTP-binding protein Rem with 14-3-3 proteins. |journal=Arch. Biochem. Biophys. |volume=368 |issue= 2 |pages= 401-12 |year= 1999 |pmid= 10441394 |doi= 10.1006/abbi.1999.1316 }}
*{{cite journal  | author=Dorner C, Ullrich A, Häring HU, Lammers R |title=The kinesin-like motor protein KIF1C occurs in intact cells as a dimer and associates with proteins of the 14-3-3 family. |journal=J. Biol. Chem. |volume=274 |issue= 47 |pages= 33654-60 |year= 1999 |pmid= 10559254 |doi=  }}
*{{cite journal  | author=Aoki H, Hayashi J, Moriyama M, ''et al.'' |title=Hepatitis C virus core protein interacts with 14-3-3 protein and activates the kinase Raf-1. |journal=J. Virol. |volume=74 |issue= 4 |pages= 1736-41 |year= 2000 |pmid= 10644344 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

end log.