User:ProteinBoxBot/PBB Log Wiki 11-7-2007-A2-3

Log file for Protein Box Bot

Log page index: User:ProteinBoxBot/PBB_Log_Index

Protein Status Quick Log - Date: 03:48, 16 November 2007 (UTC)

Proteins without matches (11)

Proteins with a High Potential Match (9)

Redirected Proteins (5)

Manual Inspection (Page not found) (20)

Updated (5)

Protein Status Grid - Date: 03:48, 16 November 2007 (UTC)

Vebose Log - Date: 03:48, 16 November 2007 (UTC)

ADRA2A

• INFO: Beginning work on ADRA2A... {November 15, 2007 7:26:59 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:27:28 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_ADRA2A_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hll.
 | PDB = {{PDB2|1hll}}, {{PDB2|1ho9}}, {{PDB2|1hod}}, {{PDB2|1hof}}
 | Name = Adrenergic, alpha-2A-, receptor
 | HGNCid = 281
 | Symbol = ADRA2A
 | AltSymbols =; ADRA2; ADRA2R; ADRAR; ALPHA2AAR; ZNF32
 | OMIM = 104210
 | ECnumber =  
 | Homologene = 47944
 | MGIid = 87934
 | GeneAtlas_image1 = PBB_GE_ADRA2A_209869_at_tn.png
 | Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004935 |text = adrenoceptor activity}} {{GNF_GO|id=GO:0004938 |text = alpha2-adrenergic receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015459 |text = potassium channel regulator activity}} 
 | Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} 
 | Process = {{GNF_GO|id=GO:0000187 |text = activation of MAPK activity}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{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:0007194 |text = negative regulation of adenylate cyclase activity}} {{GNF_GO|id=GO:0007266 |text = Rho protein signal transduction}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0030036 |text = actin cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0042596 |text = fear response}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 150
    | Hs_Ensembl = ENSG00000150594
    | Hs_RefseqProtein = NP_000672
    | Hs_RefseqmRNA = NM_000681
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 112826911
    | Hs_GenLoc_end = 112830655
    | Hs_Uniprot = P08913
    | Mm_EntrezGene = 11551
    | Mm_Ensembl = ENSMUSG00000033717
    | Mm_RefseqmRNA = XM_974141
    | Mm_RefseqProtein = XP_979235
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 54098574
    | Mm_GenLoc_end = 54102292
    | Mm_Uniprot = Q1HL33
  }}
}}
'''Adrenergic, alpha-2A-, receptor''', also known as '''ADRA2A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ADRA2A adrenergic, alpha-2A-, receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=150| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = Alpha-2-adrenergic receptors are members of the G protein-coupled receptor superfamily. They include 3 highly homologous subtypes: alpha2A, alpha2B, and alpha2C. These receptors have a critical role in regulating neurotransmitter release from sympathetic nerves and from adrenergic neurons in the central nervous system. Studies in mouse revealed that both the alpha2A and alpha2C subtypes were required for normal presynaptic control of transmitter release from sympathetic nerves in the heart and from central noradrenergic neurons; the alpha2A subtype inhibited transmitter release at high stimulation frequencies, whereas the alpha2C subtype modulated neurotransmission at lower levels of nerve activity. This gene encodes alpha2A subtype and it contains no introns in either its coding or untranslated sequences.<ref name="entrez">{{cite web | title = Entrez Gene: ADRA2A adrenergic, alpha-2A-, receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=150| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Perälä M, Hirvonen H, Kalimo H, ''et al.'' |title=Differential expression of two alpha 2-adrenergic receptor subtype mRNAs in human tissues. |journal=Brain Res. Mol. Brain Res. |volume=16 |issue= 1-2 |pages= 57-63 |year= 1993 |pmid= 1334200 |doi=  }}
*{{cite journal  | author=Surprenant A, Horstman DA, Akbarali H, Limbird LE |title=A point mutation of the alpha 2-adrenoceptor that blocks coupling to potassium but not calcium currents. |journal=Science |volume=257 |issue= 5072 |pages= 977-80 |year= 1992 |pmid= 1354394 |doi=  }}
*{{cite journal  | author=Handy DE, Gavras H |title=Promoter region of the human alpha 2A adrenergic receptor gene. |journal=J. Biol. Chem. |volume=267 |issue= 33 |pages= 24017-22 |year= 1992 |pmid= 1385431 |doi=  }}
*{{cite journal  | author=Suryanarayana S, Daunt DA, Von Zastrow M, Kobilka BK |title=A point mutation in the seventh hydrophobic domain of the alpha 2 adrenergic receptor increases its affinity for a family of beta receptor antagonists. |journal=J. Biol. Chem. |volume=266 |issue= 23 |pages= 15488-92 |year= 1991 |pmid= 1678390 |doi=  }}
*{{cite journal  | author=Wang CD, Buck MA, Fraser CM |title=Site-directed mutagenesis of alpha 2A-adrenergic receptors: identification of amino acids involved in ligand binding and receptor activation by agonists. |journal=Mol. Pharmacol. |volume=40 |issue= 2 |pages= 168-79 |year= 1991 |pmid= 1678850 |doi=  }}
*{{cite journal  | author=Chhajlani V, Rangel N, Uhlén S, Wikberg JE |title=Identification of an additional gene belonging to the alpha 2 adrenergic receptor family in the human genome by PCR. |journal=FEBS Lett. |volume=280 |issue= 2 |pages= 241-4 |year= 1991 |pmid= 1849485 |doi=  }}
*{{cite journal  | author=Guyer CA, Horstman DA, Wilson AL, ''et al.'' |title=Cloning, sequencing, and expression of the gene encoding the porcine alpha 2-adrenergic receptor. Allosteric modulation by Na+, H+, and amiloride analogs. |journal=J. Biol. Chem. |volume=265 |issue= 28 |pages= 17307-17 |year= 1990 |pmid= 2170371 |doi=  }}
*{{cite journal  | author=Fraser CM, Arakawa S, McCombie WR, Venter JC |title=Cloning, sequence analysis, and permanent expression of a human alpha 2-adrenergic receptor in Chinese hamster ovary cells. Evidence for independent pathways of receptor coupling to adenylate cyclase attenuation and activation. |journal=J. Biol. Chem. |volume=264 |issue= 20 |pages= 11754-61 |year= 1989 |pmid= 2568356 |doi=  }}
*{{cite journal  | author=Kobilka BK, Matsui H, Kobilka TS, ''et al.'' |title=Cloning, sequencing, and expression of the gene coding for the human platelet alpha 2-adrenergic receptor. |journal=Science |volume=238 |issue= 4827 |pages= 650-6 |year= 1987 |pmid= 2823383 |doi=  }}
*{{cite journal  | author=Lynch CJ, Steer ML |title=Evidence for high and low affinity alpha 2-receptors. Comparison of [3H]norepinephrine and [3H]phentolamine binding to human platelet membranes. |journal=J. Biol. Chem. |volume=256 |issue= 7 |pages= 3298-303 |year= 1981 |pmid= 6259160 |doi=  }}
*{{cite journal  | author=Eason MG, Moreira SP, Liggett SB |title=Four consecutive serines in the third intracellular loop are the sites for beta-adrenergic receptor kinase-mediated phosphorylation and desensitization of the alpha 2A-adrenergic receptor. |journal=J. Biol. Chem. |volume=270 |issue= 9 |pages= 4681-8 |year= 1995 |pmid= 7876239 |doi=  }}
*{{cite journal  | author=Grassie MA, Milligan G |title=Analysis of the relative interactions between the alpha 2C10 adrenoceptor and the guanine-nucleotide-binding proteins G(o)1 alpha and Gi 2 alpha following co-expression of these polypeptides in rat 1 fibroblasts. |journal=Biochem. J. |volume=306 ( Pt 2) |issue=  |pages= 525-30 |year= 1995 |pmid= 7887906 |doi=  }}
*{{cite journal  | author=Shilo L, Sakaue M, Thomas JM, ''et al.'' |title=Enhanced transcription of the human alpha 2A-adrenergic receptor gene by cAMP: evidence for multiple cAMP responsive sequences in the promoter region of this gene. |journal=Cell. Signal. |volume=6 |issue= 1 |pages= 73-82 |year= 1994 |pmid= 8011430 |doi=  }}
*{{cite journal  | author=Valet P, Senard JM, Devedjian JC, ''et al.'' |title=Characterization and distribution of alpha 2-adrenergic receptors in the human intestinal mucosa. |journal=J. Clin. Invest. |volume=91 |issue= 5 |pages= 2049-57 |year= 1993 |pmid= 8098045 |doi=  }}
*{{cite journal  | author=Alblas J, van Corven EJ, Hordijk PL, ''et al.'' |title=Gi-mediated activation of the p21ras-mitogen-activated protein kinase pathway by alpha 2-adrenergic receptors expressed in fibroblasts. |journal=J. Biol. Chem. |volume=268 |issue= 30 |pages= 22235-8 |year= 1993 |pmid= 8226727 |doi=  }}
*{{cite journal  | author=Klein U, Ramirez MT, Kobilka BK, von Zastrow M |title=A novel interaction between adrenergic receptors and the alpha-subunit of eukaryotic initiation factor 2B. |journal=J. Biol. Chem. |volume=272 |issue= 31 |pages= 19099-102 |year= 1997 |pmid= 9235896 |doi=  }}
*{{cite journal  | author=Bétuing S, Daviaud D, Pagès C, ''et al.'' |title=Gbeta gamma-independent coupling of alpha2-adrenergic receptor to p21(rhoA) in preadipocytes. |journal=J. Biol. Chem. |volume=273 |issue= 25 |pages= 15804-10 |year= 1998 |pmid= 9624180 |doi=  }}
*{{cite journal  | author=Prezeau L, Richman JG, Edwards SW, Limbird LE |title=The zeta isoform of 14-3-3 proteins interacts with the third intracellular loop of different alpha2-adrenergic receptor subtypes. |journal=J. Biol. Chem. |volume=274 |issue= 19 |pages= 13462-9 |year= 1999 |pmid= 10224112 |doi=  }}
*{{cite journal  | author=Hein L, Altman JD, Kobilka BK |title=Two functionally distinct alpha2-adrenergic receptors regulate sympathetic neurotransmission. |journal=Nature |volume=402 |issue= 6758 |pages= 181-4 |year= 2000 |pmid= 10647009 |doi= 10.1038/46040 }}
*{{cite journal  | author=Schaak S, Cussac D, Cayla C, ''et al.'' |title=Alpha(2) adrenoceptors regulate proliferation of human intestinal epithelial cells. |journal=Gut |volume=47 |issue= 2 |pages= 242-50 |year= 2000 |pmid= 10896916 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

AICDA

• INFO: Beginning work on AICDA... {November 15, 2007 7:40:59 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:41:30 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 = Activation-induced cytidine deaminase
 | HGNCid = 13203
 | Symbol = AICDA
 | AltSymbols =; ARP2; AID; CDA2; HIGM2
 | OMIM = 605257
 | ECnumber =  
 | Homologene = 7623
 | MGIid = 1342279
 | GeneAtlas_image1 = PBB_GE_AICDA_219841_at_tn.png
 | Function = {{GNF_GO|id=GO:0004126 |text = cytidine deaminase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} 
 | Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} 
 | Process = {{GNF_GO|id=GO:0006397 |text = mRNA processing}} {{GNF_GO|id=GO:0030183 |text = B cell differentiation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 57379
    | Hs_Ensembl = ENSG00000111732
    | Hs_RefseqProtein = NP_065712
    | Hs_RefseqmRNA = NM_020661
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 8648147
    | Hs_GenLoc_end = 8650880
    | Hs_Uniprot = Q9GZX7
    | Mm_EntrezGene = 11628
    | Mm_Ensembl = ENSMUSG00000040627
    | Mm_RefseqmRNA = NM_009645
    | Mm_RefseqProtein = NP_033775
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 122519432
    | Mm_GenLoc_end = 122529799
    | Mm_Uniprot = Q546Y8
  }}
}}
'''Activation-induced cytidine deaminase''', also known as '''AICDA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: AICDA activation-induced cytidine deaminase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=57379| accessdate = }}</ref>

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

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Wedekind JE, Dance GS, Sowden MP, Smith HC |title=Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business. |journal=Trends Genet. |volume=19 |issue= 4 |pages= 207-16 |year= 2003 |pmid= 12683974 |doi=  }}
*{{cite journal  | author=Bransteitter R, Sneeden JL, Allen S, ''et al.'' |title=First AID (activation-induced cytidine deaminase) is needed to produce high affinity isotype-switched antibodies. |journal=J. Biol. Chem. |volume=281 |issue= 25 |pages= 16833-6 |year= 2006 |pmid= 16624806 |doi= 10.1074/jbc.R600006200 }}
*{{cite journal  | author=Muto T, Muramatsu M, Taniwaki M, ''et al.'' |title=Isolation, tissue distribution, and chromosomal localization of the human activation-induced cytidine deaminase (AID) gene. |journal=Genomics |volume=68 |issue= 1 |pages= 85-8 |year= 2001 |pmid= 10950930 |doi= 10.1006/geno.2000.6268 }}
*{{cite journal  | author=Revy P, Muto T, Levy Y, ''et al.'' |title=Activation-induced cytidine deaminase (AID) deficiency causes the autosomal recessive form of the Hyper-IgM syndrome (HIGM2). |journal=Cell |volume=102 |issue= 5 |pages= 565-75 |year= 2000 |pmid= 11007475 |doi=  }}
*{{cite journal  | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi=  }}
*{{cite journal  | author=Minegishi Y, Lavoie A, Cunningham-Rundles C, ''et al.'' |title=Mutations in activation-induced cytidine deaminase in patients with hyper IgM syndrome. |journal=Clin. Immunol. |volume=97 |issue= 3 |pages= 203-10 |year= 2001 |pmid= 11112359 |doi= 10.1006/clim.2000.4956 }}
*{{cite journal  | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
*{{cite journal  | author=Noguchi E, Shibasaki M, Inudou M, ''et al.'' |title=Association between a new polymorphism in the activation-induced cytidine deaminase gene and atopic asthma and the regulation of total serum IgE levels. |journal=J. Allergy Clin. Immunol. |volume=108 |issue= 3 |pages= 382-6 |year= 2001 |pmid= 11544457 |doi= 10.1067/mai.2001.117456 }}
*{{cite journal  | author=Martin A, Bardwell PD, Woo CJ, ''et al.'' |title=Activation-induced cytidine deaminase turns on somatic hypermutation in hybridomas. |journal=Nature |volume=415 |issue= 6873 |pages= 802-6 |year= 2002 |pmid= 11823785 |doi= 10.1038/nature714 }}
*{{cite journal  | author=Rada C, Jarvis JM, Milstein C |title=AID-GFP chimeric protein increases hypermutation of Ig genes with no evidence of nuclear localization. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 10 |pages= 7003-8 |year= 2002 |pmid= 12011459 |doi= 10.1073/pnas.092160999 }}
*{{cite journal  | author=Petersen-Mahrt SK, Harris RS, Neuberger MS |title=AID mutates E. coli suggesting a DNA deamination mechanism for antibody diversification. |journal=Nature |volume=418 |issue= 6893 |pages= 99-103 |year= 2002 |pmid= 12097915 |doi= 10.1038/nature00862 }}
*{{cite journal  | author=Dudley DD, Manis JP, Zarrin AA, ''et al.'' |title=Internal IgH class switch region deletions are position-independent and enhanced by AID expression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 15 |pages= 9984-9 |year= 2002 |pmid= 12114543 |doi= 10.1073/pnas.152333499 }}
*{{cite journal  | author=Martin A, Scharff MD |title=Somatic hypermutation of the AID transgene in B and non-B cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 19 |pages= 12304-8 |year= 2002 |pmid= 12202747 |doi= 10.1073/pnas.192442899 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Greeve J, Philipsen A, Krause K, ''et al.'' |title=Expression of activation-induced cytidine deaminase in human B-cell non-Hodgkin lymphomas. |journal=Blood |volume=101 |issue= 9 |pages= 3574-80 |year= 2003 |pmid= 12511417 |doi= 10.1182/blood-2002-08-2424 }}
*{{cite journal  | author=Oppezzo P, Vuillier F, Vasconcelos Y, ''et al.'' |title=Chronic lymphocytic leukemia B cells expressing AID display dissociation between class switch recombination and somatic hypermutation. |journal=Blood |volume=101 |issue= 10 |pages= 4029-32 |year= 2003 |pmid= 12521993 |doi= 10.1182/blood-2002-10-3175 }}
*{{cite journal  | author=Bransteitter R, Pham P, Scharff MD, Goodman MF |title=Activation-induced cytidine deaminase deaminates deoxycytidine on single-stranded DNA but requires the action of RNase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 7 |pages= 4102-7 |year= 2003 |pmid= 12651944 |doi= 10.1073/pnas.0730835100 }}
*{{cite journal  | author=Zhu Y, Nonoyama S, Morio T, ''et al.'' |title=Type two hyper-IgM syndrome caused by mutation in activation-induced cytidine deaminase. |journal=J. Med. Dent. Sci. |volume=50 |issue= 1 |pages= 41-6 |year= 2003 |pmid= 12715918 |doi=  }}
*{{cite journal  | author=Sohail A, Klapacz J, Samaranayake M, ''et al.'' |title=Human activation-induced cytidine deaminase causes transcription-dependent, strand-biased C to U deaminations. |journal=Nucleic Acids Res. |volume=31 |issue= 12 |pages= 2990-4 |year= 2003 |pmid= 12799424 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

C4A

• INFO: Beginning work on C4A... {November 15, 2007 7:27:28 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:28:37 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_C4A_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1hzf.
 | PDB = {{PDB2|1hzf}}
 | Name = Complement component 4A (Rodgers blood group)
 | HGNCid = 1323
 | Symbol = C4A
 | AltSymbols =; C4; C4A2; C4A3; C4A4; C4A6; C4B; C4S; CO4; CPAMD2; RG; C4A; C4A13; C4A91; C4B1; C4B12; C4B2; C4B3; C4B5; C4F; CH; CPAMD3
 | OMIM = 120810
 | ECnumber =  
 | Homologene = 36030
 | MGIid = 88228
 | GeneAtlas_image1 = PBB_GE_C4A_208451_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_C4A_214428_x_at_tn.png
 | Function = {{GNF_GO|id=GO:0004866 |text = endopeptidase inhibitor activity}} 
 | Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} 
 | Process = {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006956 |text = complement activation}} {{GNF_GO|id=GO:0006958 |text = complement activation, classical pathway}} {{GNF_GO|id=GO:0045087 |text = innate immune response}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 720
    | Hs_Ensembl = ENSG00000204319
    | Hs_RefseqProtein = NP_009224
    | Hs_RefseqmRNA = NM_007293
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 32090517
    | Hs_GenLoc_end = 32111174
    | Hs_Uniprot = P0C0L4
    | Mm_EntrezGene = 12268
    | Mm_Ensembl =  
    | Mm_RefseqmRNA = XM_001002697
    | Mm_RefseqProtein = XP_001002697
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr =  
    | Mm_GenLoc_start =  
    | Mm_GenLoc_end =  
    | Mm_Uniprot =  
  }}
}}
'''Complement component 4A (Rodgers blood group)''', also known as '''C4A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: C4A complement component 4A (Rodgers blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=720| accessdate = }}</ref>

<!-- 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 acidic form of complement factor 4, part of the classical activation pathway. The protein is expressed as a single chain precursor which is proteolytically cleaved into a trimer of alpha, beta, and gamma chains prior to secretion. The trimer provides a surface for interaction between the antigen-antibody complex and other complement components. The alpha chain may be cleaved to release C4 anaphylatoxin, a mediator of local inflammation. Deficiency of this protein is associated with systemic lupus erythematosus and type I diabetes mellitus. This gene localizes to the major histocompatibility complex (MHC) class III region on chromosome 6. Varying haplotypes of this gene cluster exist, such that individuals may have 1, 2, or 3 copies of this gene.<ref name="entrez">{{cite web | title = Entrez Gene: C4A complement component 4A (Rodgers blood group)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=720| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Hugli TE |title=Biochemistry and biology of anaphylatoxins. |journal=Complement |volume=3 |issue= 3 |pages= 111-27 |year= 1987 |pmid= 3542363 |doi=  }}
*{{cite journal  | author=Yu CY |title=Molecular genetics of the human MHC complement gene cluster. |journal=Exp. Clin. Immunogenet. |volume=15 |issue= 4 |pages= 213-30 |year= 1999 |pmid= 10072631 |doi=  }}
*{{cite journal  | author=Anderson MJ, Milner CM, Cotton RG, Campbell RD |title=The coding sequence of the hemolytically inactive C4A6 allotype of human complement component C4 reveals that a single arginine to tryptophan substitution at beta-chain residue 458 is the likely cause of the defect. |journal=J. Immunol. |volume=148 |issue= 9 |pages= 2795-802 |year= 1992 |pmid= 1573268 |doi=  }}
*{{cite journal  | author=Hessing M, van 't Veer C, Hackeng TM, ''et al.'' |title=Importance of the alpha 3-fragment of complement C4 for the binding with C4b-binding protein. |journal=FEBS Lett. |volume=271 |issue= 1-2 |pages= 131-6 |year= 1990 |pmid= 1699796 |doi=  }}
*{{cite journal  | author=Yu CY |title=The complete exon-intron structure of a human complement component C4A gene. DNA sequences, polymorphism, and linkage to the 21-hydroxylase gene. |journal=J. Immunol. |volume=146 |issue= 3 |pages= 1057-66 |year= 1991 |pmid= 1988494 |doi=  }}
*{{cite journal  | author=Ghiso J, Saball E, Leoni J, ''et al.'' |title=Binding of cystatin C to C4: the importance of sense-antisense peptides in their interaction. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 4 |pages= 1288-91 |year= 1990 |pmid= 2304899 |doi=  }}
*{{cite journal  | author=Yu CY, Belt KT, Giles CM, ''et al.'' |title=Structural basis of the polymorphism of human complement components C4A and C4B: gene size, reactivity and antigenicity. |journal=EMBO J. |volume=5 |issue= 11 |pages= 2873-81 |year= 1987 |pmid= 2431902 |doi=  }}
*{{cite journal  | author=Speiser PW, White PC |title=Structure of the human RD gene: a highly conserved gene in the class III region of the major histocompatibility complex. |journal=DNA |volume=8 |issue= 10 |pages= 745-51 |year= 1990 |pmid= 2612324 |doi=  }}
*{{cite journal  | author=Palsdottir A, Fossdal R, Arnason A, ''et al.'' |title=Heterogeneity of human C4 gene size. A large intron (6.5 kb) is present in all C4A genes and some C4B genes. |journal=Immunogenetics |volume=25 |issue= 5 |pages= 299-304 |year= 1987 |pmid= 2883116 |doi=  }}
*{{cite journal  | author=Kishore N, Shah D, Skanes VM, Levine RP |title=The fluid-phase binding of human C4 and its genetic variants, C4A3 and C4B1, to immunoglobulins. |journal=Mol. Immunol. |volume=25 |issue= 9 |pages= 811-9 |year= 1989 |pmid= 3264881 |doi=  }}
*{{cite journal  | author=Chakravarti DN, Campbell RD, Porter RR |title=The chemical structure of the C4d fragment of the human complement component C4. |journal=Mol. Immunol. |volume=24 |issue= 11 |pages= 1187-97 |year= 1988 |pmid= 3696167 |doi=  }}
*{{cite journal  | author=Belt KT, Yu CY, Carroll MC, Porter RR |title=Polymorphism of human complement component C4. |journal=Immunogenetics |volume=21 |issue= 2 |pages= 173-80 |year= 1985 |pmid= 3838531 |doi=  }}
*{{cite journal  | author=Hortin G, Sims H, Strauss AW |title=Identification of the site of sulfation of the fourth component of human complement. |journal=J. Biol. Chem. |volume=261 |issue= 4 |pages= 1786-93 |year= 1986 |pmid= 3944109 |doi=  }}
*{{cite journal  | author=Moon KE, Gorski JP, Hugli TE |title=Complete primary structure of human C4a anaphylatoxin. |journal=J. Biol. Chem. |volume=256 |issue= 16 |pages= 8685-92 |year= 1981 |pmid= 6167582 |doi=  }}
*{{cite journal  | author=Palsdottir A, Cross SJ, Edwards JH, Carroll MC |title=Correlation between a DNA restriction fragment length polymorphism and C4A6 protein. |journal=Nature |volume=306 |issue= 5943 |pages= 615-6 |year= 1984 |pmid= 6316164 |doi=  }}
*{{cite journal  | author=Belt KT, Carroll MC, Porter RR |title=The structural basis of the multiple forms of human complement component C4. |journal=Cell |volume=36 |issue= 4 |pages= 907-14 |year= 1984 |pmid= 6546707 |doi=  }}
*{{cite journal  | author=Carroll MC, Campbell RD, Bentley DR, Porter RR |title=A molecular map of the human major histocompatibility complex class III region linking complement genes C4, C2 and factor B. |journal=Nature |volume=307 |issue= 5948 |pages= 237-41 |year= 1984 |pmid= 6559257 |doi=  }}
*{{cite journal  | author=Carroll MC, Porter RR |title=Cloning of a human complement component C4 gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 1 |pages= 264-7 |year= 1983 |pmid= 6572000 |doi=  }}
*{{cite journal  | author=Whitehead AS, Goldberger G, Woods DE, ''et al.'' |title=Use of a cDNA clone for the fourth component of human complement (C4) for analysis of a genetic deficiency of C4 in guinea pig. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=80 |issue= 17 |pages= 5387-91 |year= 1983 |pmid= 6577433 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

CAPN1

• INFO: Beginning work on CAPN1... {November 15, 2007 7:28:37 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:29:03 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_CAPN1_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1zcm.
 | PDB = {{PDB2|1zcm}}, {{PDB2|2ary}}
 | Name = Calpain 1, (mu/I) large subunit
 | HGNCid = 1476
 | Symbol = CAPN1
 | AltSymbols =; CANP; CANPL1; muCANP; muCL
 | OMIM = 114220
 | ECnumber =  
 | Homologene = 3800
 | MGIid = 88263
 | GeneAtlas_image1 = PBB_GE_CAPN1_200752_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0004198 |text = calpain activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} 
 | Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} 
 | Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 823
    | Hs_Ensembl = ENSG00000014216
    | Hs_RefseqProtein = NP_005177
    | Hs_RefseqmRNA = NM_005186
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 64705792
    | Hs_GenLoc_end = 64736048
    | Hs_Uniprot = P07384
    | Mm_EntrezGene = 12333
    | Mm_Ensembl = ENSMUSG00000024942
    | Mm_RefseqmRNA = NM_007600
    | Mm_RefseqProtein = NP_031626
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 5988546
    | Mm_GenLoc_end = 6015163
    | Mm_Uniprot = Q3TB79
  }}
}}
'''Calpain 1, (mu/I) large subunit''', also known as '''CAPN1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CAPN1 calpain 1, (mu/I) large subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=823| accessdate = }}</ref>

<!-- 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 calpains, calcium-activated neutral proteases, are nonlysosomal, intracellular cysteine proteases. The mammalian calpains include ubiquitous, stomach-specific, and muscle-specific proteins. The ubiquitous enzymes consist of heterodimers with distinct large, catalytic subunits associated with a common small, regulatory subunit. This gene encodes the large subunit of the ubiquitous enzyme, calpain 1.<ref name="entrez">{{cite web | title = Entrez Gene: CAPN1 calpain 1, (mu/I) large subunit| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=823| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Suzuki K, Sorimachi H, Yoshizawa T, ''et al.'' |title=Calpain: novel family members, activation, and physiologic function. |journal=Biol. Chem. Hoppe-Seyler |volume=376 |issue= 9 |pages= 523-9 |year= 1996 |pmid= 8561910 |doi=  }}
*{{cite journal  | author=Huang Y, Wang KK |title=The calpain family and human disease. |journal=Trends in molecular medicine |volume=7 |issue= 8 |pages= 355-62 |year= 2001 |pmid= 11516996 |doi=  }}
*{{cite journal  | author=Goll DE, Thompson VF, Li H, ''et al.'' |title=The calpain system. |journal=Physiol. Rev. |volume=83 |issue= 3 |pages= 731-801 |year= 2003 |pmid= 12843408 |doi= 10.1152/physrev.00029.2002 }}
*{{cite journal  | author=Banik NL, DeVries GH, Neuberger T, ''et al.'' |title=Calcium-activated neutral proteinase (CANP; calpain) activity in Schwann cells: immunofluorescence localization and compartmentation of mu- and mCANP. |journal=J. Neurosci. Res. |volume=29 |issue= 3 |pages= 346-54 |year= 1991 |pmid= 1656060 |doi= 10.1002/jnr.490290310 }}
*{{cite journal  | author=Ohno S, Minoshima S, Kudoh J, ''et al.'' |title=Four genes for the calpain family locate on four distinct human chromosomes. |journal=Cytogenet. Cell Genet. |volume=53 |issue= 4 |pages= 225-9 |year= 1990 |pmid= 2209092 |doi=  }}
*{{cite journal  | author=Sorimachi H, Ohmi S, Emori Y, ''et al.'' |title=A novel member of the calcium-dependent cysteine protease family. |journal=Biol. Chem. Hoppe-Seyler |volume=371 Suppl |issue=  |pages= 171-6 |year= 1990 |pmid= 2400579 |doi=  }}
*{{cite journal  | author=Harris AS, Croall DE, Morrow JS |title=The calmodulin-binding site in alpha-fodrin is near the calcium-dependent protease-I cleavage site. |journal=J. Biol. Chem. |volume=263 |issue= 30 |pages= 15754-61 |year= 1988 |pmid= 2844821 |doi=  }}
*{{cite journal  | author=Aoki K, Imajoh S, Ohno S, ''et al.'' |title=Complete amino acid sequence of the large subunit of the low-Ca2+-requiring form of human Ca2+-activated neutral protease (muCANP) deduced from its cDNA sequence. |journal=FEBS Lett. |volume=205 |issue= 2 |pages= 313-7 |year= 1986 |pmid= 3017764 |doi=  }}
*{{cite journal  | author=Ishiguro H, Higashiyama S, Namikawa C, ''et al.'' |title=Interaction of human calpains I and II with high molecular weight and low molecular weight kininogens and their heavy chain: mechanism of interaction and the role of divalent cations. |journal=Biochemistry |volume=26 |issue= 10 |pages= 2863-70 |year= 1987 |pmid= 3038169 |doi=  }}
*{{cite journal  | author=Morishita R, Nakayama H, Isobe T, ''et al.'' |title=Primary structure of a gamma subunit of G protein, gamma 12, and its phosphorylation by protein kinase C. |journal=J. Biol. Chem. |volume=270 |issue= 49 |pages= 29469-75 |year= 1996 |pmid= 7493986 |doi=  }}
*{{cite journal  | author=Kavita U, Mizel SB |title=Differential sensitivity of interleukin-1 alpha and -beta precursor proteins to cleavage by calpain, a calcium-dependent protease. |journal=J. Biol. Chem. |volume=270 |issue= 46 |pages= 27758-65 |year= 1996 |pmid= 7499244 |doi=  }}
*{{cite journal  | author=Du X, Saido TC, Tsubuki S, ''et al.'' |title=Calpain cleavage of the cytoplasmic domain of the integrin beta 3 subunit. |journal=J. Biol. Chem. |volume=270 |issue= 44 |pages= 26146-51 |year= 1995 |pmid= 7592818 |doi=  }}
*{{cite journal  | author=Bradford HN, Jameson BA, Adam AA, ''et al.'' |title=Contiguous binding and inhibitory sites on kininogens required for the inhibition of platelet calpain. |journal=J. Biol. Chem. |volume=268 |issue= 35 |pages= 26546-51 |year= 1994 |pmid= 8253784 |doi=  }}
*{{cite journal  | author=Oda A, Ozaki K, Druker BJ, ''et al.'' |title=p120c-cbl is present in human blood platelets and is differentially involved in signaling by thrombopoietin and thrombin. |journal=Blood |volume=88 |issue= 4 |pages= 1330-8 |year= 1996 |pmid= 8695851 |doi=  }}
*{{cite journal  | author=Zhang W, Lane RD, Mellgren RL |title=The major calpain isozymes are long-lived proteins. Design of an antisense strategy for calpain depletion in cultured cells. |journal=J. Biol. Chem. |volume=271 |issue= 31 |pages= 18825-30 |year= 1996 |pmid= 8702541 |doi=  }}
*{{cite journal  | author=Courseaux A, Grosgeorge J, Gaudray P, ''et al.'' |title=Definition of the minimal MEN1 candidate area based on a 5-Mb integrated map of proximal 11q13. The European Consortium on Men1, (GENEM 1; Groupe d'Etude des Néoplasies Endocriniennes Multiples de type 1). |journal=Genomics |volume=37 |issue= 3 |pages= 354-65 |year= 1997 |pmid= 8938448 |doi=  }}
*{{cite journal  | author=Corasaniti MT, Navarra M, Catani MV, ''et al.'' |title=NMDA and HIV-1 coat protein, GP120, produce necrotic but not apoptotic cell death in human CHP100 neuroblastoma cultures via a mechanism involving calpain. |journal=Biochem. Biophys. Res. Commun. |volume=229 |issue= 1 |pages= 299-304 |year= 1997 |pmid= 8954122 |doi= 10.1006/bbrc.1996.1796 }}
*{{cite journal  | author=Stabach PR, Cianci CD, Glantz SB, ''et al.'' |title=Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its mu-calpain susceptibility. |journal=Biochemistry |volume=36 |issue= 1 |pages= 57-65 |year= 1997 |pmid= 8993318 |doi= 10.1021/bi962034i }}
*{{cite journal  | author=Norris FA, Atkins RC, Majerus PW |title=Inositol polyphosphate 4-phosphatase is inactivated by calpain-mediated proteolysis in stimulated human platelets. |journal=J. Biol. Chem. |volume=272 |issue= 17 |pages= 10987-9 |year= 1997 |pmid= 9110986 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

CAV3

• INFO: Beginning work on CAV3... {November 15, 2007 7:29:03 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:29:41 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 = Caveolin 3
 | HGNCid = 1529
 | Symbol = CAV3
 | AltSymbols =; VIP21; LGMD1C; MGC126100; MGC126101; MGC126129; VIP-21
 | OMIM = 601253
 | ECnumber =  
 | Homologene = 7255
 | MGIid = 107570
 | GeneAtlas_image1 = PBB_GE_CAV3_208204_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0016010 |text = dystrophin-associated glycoprotein complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0016599 |text = caveolar membrane}} 
 | Process = {{GNF_GO|id=GO:0007517 |text = muscle development}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 859
    | Hs_Ensembl = ENSG00000182533
    | Hs_RefseqProtein = NP_001225
    | Hs_RefseqmRNA = NM_001234
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 8750253
    | Hs_GenLoc_end = 8763451
    | Hs_Uniprot = P56539
    | Mm_EntrezGene = 12391
    | Mm_Ensembl = ENSMUSG00000062694
    | Mm_RefseqmRNA = XM_973503
    | Mm_RefseqProtein = XP_978597
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 112425278
    | Mm_GenLoc_end = 112438649
    | Mm_Uniprot = Q9EPR3
  }}
}}
'''Caveolin 3''', also known as '''CAV3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CAV3 caveolin 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=859| accessdate = }}</ref>

<!-- 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 caveolin family member, which functions as a component of the caveolae plasma membranes found in most cell types. Caveolin proteins are proposed to be scaffolding proteins for organizing and concentrating certain caveolin-interacting molecules. Mutations identified in this gene lead to interference with protein oligomerization or intra-cellular routing, disrupting caveolae formation and resulting in Limb-Girdle muscular dystrophy type-1C (LGMD-1C), hyperCKemia or rippling muscle disease (RMD). Alternative splicing has been identified for this locus, with inclusion or exclusion of a differentially spliced intron. In addition, transcripts utilize multiple polyA sites and contain two potential translation initiation sites.<ref name="entrez">{{cite web | title = Entrez Gene: CAV3 caveolin 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=859| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Figarella-Branger D, Pouget J, Bernard R, ''et al.'' |title=Limb-girdle muscular dystrophy in a 71-year-old woman with an R27Q mutation in the CAV3 gene. |journal=Neurology |volume=61 |issue= 4 |pages= 562-4 |year= 2004 |pmid= 12939441 |doi=  }}
*{{cite journal  | author=Woodman SE, Sotgia F, Galbiati F, ''et al.'' |title=Caveolinopathies: mutations in caveolin-3 cause four distinct autosomal dominant muscle diseases. |journal=Neurology |volume=62 |issue= 4 |pages= 538-43 |year= 2005 |pmid= 14981167 |doi=  }}
*{{cite journal  | author=Li S, Okamoto T, Chun M, ''et al.'' |title=Evidence for a regulated interaction between heterotrimeric G proteins and caveolin. |journal=J. Biol. Chem. |volume=270 |issue= 26 |pages= 15693-701 |year= 1995 |pmid= 7797570 |doi=  }}
*{{cite journal  | author=Tang Z, Scherer PE, Okamoto T, ''et al.'' |title=Molecular cloning of caveolin-3, a novel member of the caveolin gene family expressed predominantly in muscle. |journal=J. Biol. Chem. |volume=271 |issue= 4 |pages= 2255-61 |year= 1996 |pmid= 8567687 |doi=  }}
*{{cite journal  | author=Scherer PE, Lisanti MP |title=Association of phosphofructokinase-M with caveolin-3 in differentiated skeletal myotubes. Dynamic regulation by extracellular glucose and intracellular metabolites. |journal=J. Biol. Chem. |volume=272 |issue= 33 |pages= 20698-705 |year= 1997 |pmid= 9252390 |doi=  }}
*{{cite journal  | author=Venema VJ, Ju H, Zou R, Venema RC |title=Interaction of neuronal nitric-oxide synthase with caveolin-3 in skeletal muscle. Identification of a novel caveolin scaffolding/inhibitory domain. |journal=J. Biol. Chem. |volume=272 |issue= 45 |pages= 28187-90 |year= 1997 |pmid= 9353265 |doi=  }}
*{{cite journal  | author=Couet J, Sargiacomo M, Lisanti MP |title=Interaction of a receptor tyrosine kinase, EGF-R, with caveolins. Caveolin binding negatively regulates tyrosine and serine/threonine kinase activities. |journal=J. Biol. Chem. |volume=272 |issue= 48 |pages= 30429-38 |year= 1997 |pmid= 9374534 |doi=  }}
*{{cite journal  | author=McNally EM, de Sá Moreira E, Duggan DJ, ''et al.'' |title=Caveolin-3 in muscular dystrophy. |journal=Hum. Mol. Genet. |volume=7 |issue= 5 |pages= 871-7 |year= 1998 |pmid= 9536092 |doi=  }}
*{{cite journal  | author=Minetti C, Sotgia F, Bruno C, ''et al.'' |title=Mutations in the caveolin-3 gene cause autosomal dominant limb-girdle muscular dystrophy. |journal=Nat. Genet. |volume=18 |issue= 4 |pages= 365-8 |year= 1998 |pmid= 9537420 |doi= 10.1038/ng0498-365 }}
*{{cite journal  | author=Biederer C, Ries S, Drobnik W, Schmitz G |title=Molecular cloning of human caveolin 3. |journal=Biochim. Biophys. Acta |volume=1406 |issue= 1 |pages= 5-9 |year= 1998 |pmid= 9545514 |doi=  }}
*{{cite journal  | author=Yamamoto M, Toya Y, Schwencke C, ''et al.'' |title=Caveolin is an activator of insulin receptor signaling. |journal=J. Biol. Chem. |volume=273 |issue= 41 |pages= 26962-8 |year= 1998 |pmid= 9756945 |doi=  }}
*{{cite journal  | author=Sotgia F, Minetti C, Lisanti MP |title=Localization of the human caveolin-3 gene to the D3S18/D3S4163/D3S4539 locus (3p25), in close proximity to the human oxytocin receptor gene. Identification of the caveolin-3 gene as a candidate for deletion in 3p-syndrome. |journal=FEBS Lett. |volume=452 |issue= 3 |pages= 177-80 |year= 1999 |pmid= 10386585 |doi=  }}
*{{cite journal  | author=Carbone I, Bruno C, Sotgia F, ''et al.'' |title=Mutation in the CAV3 gene causes partial caveolin-3 deficiency and hyperCKemia. |journal=Neurology |volume=54 |issue= 6 |pages= 1373-6 |year= 2000 |pmid= 10746614 |doi=  }}
*{{cite journal  | author=Biederer CH, Ries SJ, Moser M, ''et al.'' |title=The basic helix-loop-helix transcription factors myogenin and Id2 mediate specific induction of caveolin-3 gene expression during embryonic development. |journal=J. Biol. Chem. |volume=275 |issue= 34 |pages= 26245-51 |year= 2000 |pmid= 10835421 |doi= 10.1074/jbc.M001430200 }}
*{{cite journal  | author=Sotgia F, Lee JK, Das K, ''et al.'' |title=Caveolin-3 directly interacts with the C-terminal tail of beta -dystroglycan. Identification of a central WW-like domain within caveolin family members. |journal=J. Biol. Chem. |volume=275 |issue= 48 |pages= 38048-58 |year= 2001 |pmid= 10988290 |doi= 10.1074/jbc.M005321200 }}
*{{cite journal  | author=Herrmann R, Straub V, Blank M, ''et al.'' |title=Dissociation of the dystroglycan complex in caveolin-3-deficient limb girdle muscular dystrophy. |journal=Hum. Mol. Genet. |volume=9 |issue= 15 |pages= 2335-40 |year= 2001 |pmid= 11001938 |doi=  }}
*{{cite journal  | author=Hagiwara Y, Sasaoka T, Araishi K, ''et al.'' |title=Caveolin-3 deficiency causes muscle degeneration in mice. |journal=Hum. Mol. Genet. |volume=9 |issue= 20 |pages= 3047-54 |year= 2001 |pmid= 11115849 |doi=  }}
*{{cite journal  | author=de Paula F, Vainzof M, Bernardino AL, ''et al.'' |title=Mutations in the caveolin-3 gene: When are they pathogenic? |journal=Am. J. Med. Genet. |volume=99 |issue= 4 |pages= 303-7 |year= 2001 |pmid= 11251997 |doi=  }}
*{{cite journal  | author=Betz RC, Schoser BG, Kasper D, ''et al.'' |title=Mutations in CAV3 cause mechanical hyperirritability of skeletal muscle in rippling muscle disease. |journal=Nat. Genet. |volume=28 |issue= 3 |pages= 218-9 |year= 2001 |pmid= 11431690 |doi= 10.1038/90050 }}
*{{cite journal  | author=Matsuda C, Hayashi YK, Ogawa M, ''et al.'' |title=The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle. |journal=Hum. Mol. Genet. |volume=10 |issue= 17 |pages= 1761-6 |year= 2002 |pmid= 11532985 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

CCNH

• INFO: Beginning work on CCNH... {November 15, 2007 7:30:18 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:30:43 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_CCNH_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jkw.
 | PDB = {{PDB2|1jkw}}, {{PDB2|1kxu}}
 | Name = Cyclin H
 | HGNCid = 1594
 | Symbol = CCNH
 | AltSymbols =; CAK; p34; p37
 | OMIM = 601953
 | ECnumber =  
 | Homologene = 946
 | MGIid = 1913921
 | GeneAtlas_image1 = PBB_GE_CCNH_204093_at_tn.png
 | Function = {{GNF_GO|id=GO:0016301 |text = kinase activity}} 
 | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} 
 | Process = {{GNF_GO|id=GO:0000079 |text = regulation of cyclin-dependent protein kinase activity}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 902
    | Hs_Ensembl = ENSG00000134480
    | Hs_RefseqProtein = NP_001230
    | Hs_RefseqmRNA = NM_001239
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 86725838
    | Hs_GenLoc_end = 86744592
    | Hs_Uniprot = P51946
    | Mm_EntrezGene = 66671
    | Mm_Ensembl =  
    | Mm_RefseqmRNA = NM_023243
    | Mm_RefseqProtein = NP_075732
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr =  
    | Mm_GenLoc_start =  
    | Mm_GenLoc_end =  
    | Mm_Uniprot =  
  }}
}}
'''Cyclin H''', also known as '''CCNH''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CCNH cyclin H| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=902| accessdate = }}</ref>

<!-- 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 belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. This cyclin forms a complex with CDK7 kinase and ring finger protein MAT1. The kinase complex is able to phosphorylate CDK2 and CDC2 kinases, thus functions as a CDK-activating kinase (CAK). This cyclin and its kinase partner are components of TFIIH, as well as RNA polymerase II protein complexes. They participate in two different transcriptional regulation processes, suggesting an important link between basal transcription control and the cell cycle machinery.<ref name="entrez">{{cite web | title = Entrez Gene: CCNH cyclin H| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=902| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Jeang KT |title=Tat, Tat-associated kinase, and transcription. |journal=J. Biomed. Sci. |volume=5 |issue= 1 |pages= 24-7 |year= 1998 |pmid= 9570510 |doi=  }}
*{{cite journal  | author=Yankulov K, Bentley D |title=Transcriptional control: Tat cofactors and transcriptional elongation. |journal=Curr. Biol. |volume=8 |issue= 13 |pages= R447-9 |year= 1998 |pmid= 9651670 |doi=  }}
*{{cite journal  | author=Shiekhattar R, Mermelstein F, Fisher RP, ''et al.'' |title=Cdk-activating kinase complex is a component of human transcription factor TFIIH. |journal=Nature |volume=374 |issue= 6519 |pages= 283-7 |year= 1995 |pmid= 7533895 |doi= 10.1038/374283a0 }}
*{{cite journal  | author=Darbon JM, Devault A, Taviaux S, ''et al.'' |title=Cloning, expression and subcellular localization of the human homolog of p40MO15 catalytic subunit of cdk-activating kinase. |journal=Oncogene |volume=9 |issue= 11 |pages= 3127-38 |year= 1994 |pmid= 7936635 |doi=  }}
*{{cite journal  | author=Feaver WJ, Svejstrup JQ, Henry NL, Kornberg RD |title=Relationship of CDK-activating kinase and RNA polymerase II CTD kinase TFIIH/TFIIK. |journal=Cell |volume=79 |issue= 6 |pages= 1103-9 |year= 1995 |pmid= 8001136 |doi=  }}
*{{cite journal  | author=Fisher RP, Morgan DO |title=A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase. |journal=Cell |volume=78 |issue= 4 |pages= 713-24 |year= 1994 |pmid= 8069918 |doi=  }}
*{{cite journal  | author=Mäkelä TP, Tassan JP, Nigg EA, ''et al.'' |title=A cyclin associated with the CDK-activating kinase MO15. |journal=Nature |volume=371 |issue= 6494 |pages= 254-7 |year= 1994 |pmid= 8078587 |doi= 10.1038/371254a0 }}
*{{cite journal  | author=Perez JL, Shen X, Finkernagel S, ''et al.'' |title=Identification and chromosomal mapping of a receptor tyrosine kinase with a putative phospholipid binding sequence in its ectodomain. |journal=Oncogene |volume=9 |issue= 1 |pages= 211-9 |year= 1994 |pmid= 8302582 |doi=  }}
*{{cite journal  | author=Tassan JP, Jaquenoud M, Fry AM, ''et al.'' |title=In vitro assembly of a functional human CDK7-cyclin H complex requires MAT1, a novel 36 kDa RING finger protein. |journal=EMBO J. |volume=14 |issue= 22 |pages= 5608-17 |year= 1996 |pmid= 8521818 |doi=  }}
*{{cite journal  | author=Adamczewski JP, Rossignol M, Tassan JP, ''et al.'' |title=MAT1, cdk7 and cyclin H form a kinase complex which is UV light-sensitive upon association with TFIIH. |journal=EMBO J. |volume=15 |issue= 8 |pages= 1877-84 |year= 1996 |pmid= 8617234 |doi=  }}
*{{cite journal  | author=Blau J, Xiao H, McCracken S, ''et al.'' |title=Three functional classes of transcriptional activation domain. |journal=Mol. Cell. Biol. |volume=16 |issue= 5 |pages= 2044-55 |year= 1996 |pmid= 8628270 |doi=  }}
*{{cite journal  | author=Reardon JT, Ge H, Gibbs E, ''et al.'' |title=Isolation and characterization of two human transcription factor IIH (TFIIH)-related complexes: ERCC2/CAK and TFIIH. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 13 |pages= 6482-7 |year= 1996 |pmid= 8692841 |doi=  }}
*{{cite journal  | author=Drapkin R, Le Roy G, Cho H, ''et al.'' |title=Human cyclin-dependent kinase-activating kinase exists in three distinct complexes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 13 |pages= 6488-93 |year= 1996 |pmid= 8692842 |doi=  }}
*{{cite journal  | author=Kim KK, Chamberlin HM, Morgan DO, Kim SH |title=Three-dimensional structure of human cyclin H, a positive regulator of the CDK-activating kinase. |journal=Nat. Struct. Biol. |volume=3 |issue= 10 |pages= 849-55 |year= 1996 |pmid= 8836101 |doi=  }}
*{{cite journal  | author=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. |journal=Science |volume=274 |issue= 5287 |pages= 605-10 |year= 1996 |pmid= 8849451 |doi=  }}
*{{cite journal  | author=Parada CA, Roeder RG |title=Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain. |journal=Nature |volume=384 |issue= 6607 |pages= 375-8 |year= 1996 |pmid= 8934526 |doi= 10.1038/384375a0 }}
*{{cite journal  | author=García-Martínez LF, Ivanov D, Gaynor RB |title=Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 6951-8 |year= 1997 |pmid= 9054383 |doi=  }}
*{{cite journal  | author=Poterszman A, Andersen G, Busso D, ''et al.'' |title=Expression in Escherichia coli: purification and characterization of cyclin H, a subunit of the human general transcription/DNA repair factor TFIIH. |journal=Protein Expr. Purif. |volume=9 |issue= 2 |pages= 153-8 |year= 1997 |pmid= 9056480 |doi= 10.1006/prep.1996.0693 }}
*{{cite journal  | author=Marinoni JC, Roy R, Vermeulen W, ''et al.'' |title=Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH. |journal=EMBO J. |volume=16 |issue= 5 |pages= 1093-102 |year= 1997 |pmid= 9118947 |doi= 10.1093/emboj/16.5.1093 }}
*{{cite journal  | author=Andersen G, Busso D, Poterszman A, ''et al.'' |title=The structure of cyclin H: common mode of kinase activation and specific features. |journal=EMBO J. |volume=16 |issue= 5 |pages= 958-67 |year= 1997 |pmid= 9118957 |doi= 10.1093/emboj/16.5.958 }}
}}
{{refend}}

{{protein-stub}}
 

CDH5

• INFO: Beginning work on CDH5... {November 15, 2007 7:30:43 PM PST}
• SEARCH REDIRECT: Control Box Found: CDH5 {November 15, 2007 7:31:03 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 7:31:05 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 7:31:05 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 7:31:05 PM PST}
• UPDATED: Updated protein page:
  CDH5
  {November 15, 2007 7:31:12 PM PST}

CX3CR1

• INFO: Beginning work on CX3CR1... {November 15, 2007 7:31:12 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:31:39 PM PST}

 <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes 
| 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 = Chemokine (C-X3-C motif) receptor 1
 | HGNCid = 2558
 | Symbol = CX3CR1
 | AltSymbols =; CCRL1; CMKBRL1; CMKDR1; GPR13; GPRV28; V28
 | OMIM = 601470
 | ECnumber =  
 | Homologene = 20350
 | MGIid = 1333815
 | GeneAtlas_image1 = PBB_GE_CX3CR1_205898_at_tn.png
 | Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015026 |text = coreceptor activity}} {{GNF_GO|id=GO:0016494 |text = C-X-C chemokine receptor activity}} 
 | Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} 
 | Process = {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{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:0009611 |text = response to wounding}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1524
    | Hs_Ensembl = ENSG00000168329
    | Hs_RefseqProtein = NP_001328
    | Hs_RefseqmRNA = NM_001337
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 39279989
    | Hs_GenLoc_end = 39298190
    | Hs_Uniprot = P49238
    | Mm_EntrezGene = 13051
    | Mm_Ensembl = ENSMUSG00000052336
    | Mm_RefseqmRNA = XM_983192
    | Mm_RefseqProtein = XP_988286
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 119750314
    | Mm_GenLoc_end = 119916981
    | Mm_Uniprot = Q543X3
  }}
}}
'''Chemokine (C-X3-C motif) receptor 1''', also known as '''CX3CR1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CX3CR1 chemokine (C-X3-C motif) receptor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1524| accessdate = }}</ref>

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

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Robertson MJ |title=Role of chemokines in the biology of natural killer cells. |journal=J. Leukoc. Biol. |volume=71 |issue= 2 |pages= 173-83 |year= 2002 |pmid= 11818437 |doi=  }}
*{{cite journal  | author=Raport CJ, Schweickart VL, Eddy RL, ''et al.'' |title=The orphan G-protein-coupled receptor-encoding gene V28 is closely related to genes for chemokine receptors and is expressed in lymphoid and neural tissues. |journal=Gene |volume=163 |issue= 2 |pages= 295-9 |year= 1995 |pmid= 7590284 |doi=  }}
*{{cite journal  | author=Combadiere C, Ahuja SK, Murphy PM |title=Cloning, chromosomal localization, and RNA expression of a human beta chemokine receptor-like gene. |journal=DNA Cell Biol. |volume=14 |issue= 8 |pages= 673-80 |year= 1995 |pmid= 7646814 |doi=  }}
*{{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=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=Imai T, Hieshima K, Haskell C, ''et al.'' |title=Identification and molecular characterization of fractalkine receptor CX3CR1, which mediates both leukocyte migration and adhesion. |journal=Cell |volume=91 |issue= 4 |pages= 521-30 |year= 1997 |pmid= 9390561 |doi=  }}
*{{cite journal  | author=Combadiere C, Salzwedel K, Smith ED, ''et al.'' |title=Identification of CX3CR1. A chemotactic receptor for the human CX3C chemokine fractalkine and a fusion coreceptor for HIV-1. |journal=J. Biol. Chem. |volume=273 |issue= 37 |pages= 23799-804 |year= 1998 |pmid= 9726990 |doi=  }}
*{{cite journal  | author=Mizoue LS, Bazan JF, Johnson EC, Handel TM |title=Solution structure and dynamics of the CX3C chemokine domain of fractalkine and its interaction with an N-terminal fragment of CX3CR1. |journal=Biochemistry |volume=38 |issue= 5 |pages= 1402-14 |year= 1999 |pmid= 9931005 |doi= 10.1021/bi9820614 }}
*{{cite journal  | author=Maho A, Bensimon A, Vassart G, Parmentier M |title=Mapping of the CCXCR1, CX3CR1, CCBP2 and CCR9 genes to the CCR cluster within the 3p21.3 region of the human genome. |journal=Cytogenet. Cell Genet. |volume=87 |issue= 3-4 |pages= 265-8 |year= 2000 |pmid= 10702689 |doi=  }}
*{{cite journal  | author=Faure S, Meyer L, Costagliola D, ''et al.'' |title=Rapid progression to AIDS in HIV+ individuals with a structural variant of the chemokine receptor CX3CR1. |journal=Science |volume=287 |issue= 5461 |pages= 2274-7 |year= 2000 |pmid= 10731151 |doi=  }}
*{{cite journal  | author=Yoneda O, Imai T, Goda S, ''et al.'' |title=Fractalkine-mediated endothelial cell injury by NK cells. |journal=J. Immunol. |volume=164 |issue= 8 |pages= 4055-62 |year= 2000 |pmid= 10754298 |doi=  }}
*{{cite journal  | author=Meucci O, Fatatis A, Simen AA, Miller RJ |title=Expression of CX3CR1 chemokine receptors on neurons and their role in neuronal survival. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 14 |pages= 8075-80 |year= 2000 |pmid= 10869418 |doi= 10.1073/pnas.090017497 }}
*{{cite journal  | author=Papadopoulos EJ, Fitzhugh DJ, Tkaczyk C, ''et al.'' |title=Mast cells migrate, but do not degranulate, in response to fractalkine, a membrane-bound chemokine expressed constitutively in diverse cells of the skin. |journal=Eur. J. Immunol. |volume=30 |issue= 8 |pages= 2355-61 |year= 2000 |pmid= 10940926 |doi=  }}
*{{cite journal  | author=Moatti D, Faure S, Fumeron F, ''et al.'' |title=Polymorphism in the fractalkine receptor CX3CR1 as a genetic risk factor for coronary artery disease. |journal=Blood |volume=97 |issue= 7 |pages= 1925-8 |year= 2001 |pmid= 11264153 |doi=  }}
*{{cite journal  | author=Foussat A, Bouchet-Delbos L, Berrebi D, ''et al.'' |title=Deregulation of the expression of the fractalkine/fractalkine receptor complex in HIV-1-infected patients. |journal=Blood |volume=98 |issue= 6 |pages= 1678-86 |year= 2001 |pmid= 11535497 |doi=  }}
*{{cite journal  | author=Dichmann S, Herouy Y, Purlis D, ''et al.'' |title=Fractalkine induces chemotaxis and actin polymerization in human dendritic cells. |journal=Inflamm. Res. |volume=50 |issue= 11 |pages= 529-33 |year= 2002 |pmid= 11766992 |doi=  }}
*{{cite journal  | author=Brand S, Sakaguchi T, Gu X, ''et al.'' |title=Fractalkine-mediated signals regulate cell-survival and immune-modulatory responses in intestinal epithelial cells. |journal=Gastroenterology |volume=122 |issue= 1 |pages= 166-77 |year= 2002 |pmid= 11781291 |doi=  }}
*{{cite journal  | author=Utaipat U, Duerr A, Rudolph DL, ''et al.'' |title=Coreceptor utilization of HIV type 1 subtype E viral isolates from Thai men with HIV type 1-infected and uninfected wives. |journal=AIDS Res. Hum. Retroviruses |volume=18 |issue= 1 |pages= 1-11 |year= 2002 |pmid= 11804551 |doi= 10.1089/088922202753394664 }}
*{{cite journal  | author=Fong AM, Alam SM, Imai T, ''et al.'' |title=CX3CR1 tyrosine sulfation enhances fractalkine-induced cell adhesion. |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 19418-23 |year= 2002 |pmid= 11909868 |doi= 10.1074/jbc.M201396200 }}
}}
{{refend}}

{{protein-stub}}
 

EIF2S1

• INFO: Beginning work on EIF2S1... {November 15, 2007 7:31:39 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:32:12 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_EIF2S1_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1kl9.
 | PDB = {{PDB2|1kl9}}, {{PDB2|1q8k}}
 | Name = Eukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa
 | HGNCid = 3265
 | Symbol = EIF2S1
 | AltSymbols =; EIF-2; EIF-2A; EIF-2alpha; EIF2; EIF2A
 | OMIM = 603907
 | ECnumber =  
 | Homologene = 3020
 | MGIid = 95299
 | GeneAtlas_image1 = PBB_GE_EIF2S1_201142_at_tn.png
 | GeneAtlas_image2 = PBB_GE_EIF2S1_201143_s_at_tn.png
 | GeneAtlas_image3 = PBB_GE_EIF2S1_201144_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0003743 |text = translation initiation factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005844 |text = polysome}} {{GNF_GO|id=GO:0005850 |text = eukaryotic translation initiation factor 2 complex}} {{GNF_GO|id=GO:0005851 |text = eukaryotic translation initiation factor 2B complex}} 
 | Process = {{GNF_GO|id=GO:0006417 |text = regulation of translation}} {{GNF_GO|id=GO:0043558 |text = regulation of translation initiation in response to stress}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1965
    | Hs_Ensembl = ENSG00000134001
    | Hs_RefseqProtein = NP_004085
    | Hs_RefseqmRNA = NM_004094
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 14
    | Hs_GenLoc_start = 66896787
    | Hs_GenLoc_end = 66922986
    | Hs_Uniprot = P05198
    | Mm_EntrezGene = 13665
    | Mm_Ensembl =  
    | Mm_RefseqmRNA = NM_026114
    | Mm_RefseqProtein = NP_080390
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr =  
    | Mm_GenLoc_start =  
    | Mm_GenLoc_end =  
    | Mm_Uniprot =  
  }}
}}
'''Eukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa''', also known as '''EIF2S1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: EIF2S1 eukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1965| accessdate = }}</ref>

<!-- 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 translation initiation factor eIF2 catalyzes the first regulated step of protein synthesis initiation, promoting the binding of the initiator tRNA to 40S ribosomal subunits. Binding occurs as a ternary complex of methionyl-tRNA, eIF2, and GTP. eIF2 is composed of 3 nonidentical subunits, alpha (36 kD), beta (38 kD, MIM 603908), and gamma (52 kD, MIM 300161). The rate of formation of the ternary complex is modulated by the phosphorylation state of eIF2-alpha (Ernst et al., 1987).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: EIF2S1 eukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1965| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Hershey JW |title=Translational control in mammalian cells. |journal=Annu. Rev. Biochem. |volume=60 |issue=  |pages= 717-55 |year= 1991 |pmid= 1883206 |doi= 10.1146/annurev.bi.60.070191.003441 }}
*{{cite journal  | author=Mao X, Green JM, Safer B, ''et al.'' |title=Regulation of translation initiation factor gene expression during human T cell activation. |journal=J. Biol. Chem. |volume=267 |issue= 28 |pages= 20444-50 |year= 1992 |pmid= 1400363 |doi=  }}
*{{cite journal  | author=Mellor H, Proud CG |title=A synthetic peptide substrate for initiation factor-2 kinases. |journal=Biochem. Biophys. Res. Commun. |volume=178 |issue= 2 |pages= 430-7 |year= 1991 |pmid= 1677563 |doi=  }}
*{{cite journal  | author=Green SR, Spalding A, Ashford T, ''et al.'' |title=Synthesis of human initiation factor-2 alpha in Saccharomyces cerevisiae. |journal=Gene |volume=108 |issue= 2 |pages= 253-8 |year= 1992 |pmid= 1748310 |doi=  }}
*{{cite journal  | author=Kramer G |title=Two phosphorylation sites on eIF-2 alpha. |journal=FEBS Lett. |volume=267 |issue= 2 |pages= 181-2 |year= 1990 |pmid= 2116318 |doi=  }}
*{{cite journal  | author=Ernst H, Duncan RF, Hershey JW |title=Cloning and sequencing of complementary DNAs encoding the alpha-subunit of translational initiation factor eIF-2. Characterization of the protein and its messenger RNA. |journal=J. Biol. Chem. |volume=262 |issue= 3 |pages= 1206-12 |year= 1987 |pmid= 2948954 |doi=  }}
*{{cite journal  | author=Kato S, Sekine S, Oh SW, ''et al.'' |title=Construction of a human full-length cDNA bank. |journal=Gene |volume=150 |issue= 2 |pages= 243-50 |year= 1995 |pmid= 7821789 |doi=  }}
*{{cite journal  | author=Ray MK, Chakraborty A, Datta B, ''et al.'' |title=Characteristics of the eukaryotic initiation factor 2 associated 67-kDa polypeptide. |journal=Biochemistry |volume=32 |issue= 19 |pages= 5151-9 |year= 1993 |pmid= 8098621 |doi=  }}
*{{cite journal  | author=Dever TE, Chen JJ, Barber GN, ''et al.'' |title=Mammalian eukaryotic initiation factor 2 alpha kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeast. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 10 |pages= 4616-20 |year= 1993 |pmid= 8099443 |doi=  }}
*{{cite journal  | author=Barber GN, Wambach M, Wong ML, ''et al.'' |title=Translational regulation by the interferon-induced double-stranded-RNA-activated 68-kDa protein kinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 10 |pages= 4621-5 |year= 1993 |pmid= 8099444 |doi=  }}
*{{cite journal  | author=Miyamoto S, Chiorini JA, Urcelay E, Safer B |title=Regulation of gene expression for translation initiation factor eIF-2 alpha: importance of the 3' untranslated region. |journal=Biochem. J. |volume=315 ( Pt 3) |issue=  |pages= 791-8 |year= 1996 |pmid= 8645159 |doi=  }}
*{{cite journal  | author=Yang W, Hinnebusch AG |title=Identification of a regulatory subcomplex in the guanine nucleotide exchange factor eIF2B that mediates inhibition by phosphorylated eIF2. |journal=Mol. Cell. Biol. |volume=16 |issue= 11 |pages= 6603-16 |year= 1996 |pmid= 8887689 |doi=  }}
*{{cite journal  | author=Brand SR, Kobayashi R, Mathews MB |title=The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8388-95 |year= 1997 |pmid= 9079663 |doi=  }}
*{{cite journal  | author=Ting NS, Kao PN, Chan DW, ''et al.'' |title=DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45. |journal=J. Biol. Chem. |volume=273 |issue= 4 |pages= 2136-45 |year= 1998 |pmid= 9442054 |doi=  }}
*{{cite journal  | author=Kimball SR, Heinzinger NK, Horetsky RL, Jefferson LS |title=Identification of interprotein interactions between the subunits of eukaryotic initiation factors eIF2 and eIF2B. |journal=J. Biol. Chem. |volume=273 |issue= 5 |pages= 3039-44 |year= 1998 |pmid= 9446619 |doi=  }}
*{{cite journal  | author=Shi Y, Vattem KM, Sood R, ''et al.'' |title=Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control. |journal=Mol. Cell. Biol. |volume=18 |issue= 12 |pages= 7499-509 |year= 1998 |pmid= 9819435 |doi=  }}
*{{cite journal  | author=Satoh S, Hijikata M, Handa H, Shimotohno K |title=Caspase-mediated cleavage of eukaryotic translation initiation factor subunit 2alpha. |journal=Biochem. J. |volume=342 ( Pt 1) |issue=  |pages= 65-70 |year= 1999 |pmid= 10432301 |doi=  }}
*{{cite journal  | author=Berlanga JJ, Santoyo J, De Haro C |title=Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2alpha kinase. |journal=Eur. J. Biochem. |volume=265 |issue= 2 |pages= 754-62 |year= 1999 |pmid= 10504407 |doi=  }}
*{{cite journal  | author=Lu J, O'Hara EB, Trieselmann BA, ''et al.'' |title=The interferon-induced double-stranded RNA-activated protein kinase PKR will phosphorylate serine, threonine, or tyrosine at residue 51 in eukaryotic initiation factor 2alpha. |journal=J. Biol. Chem. |volume=274 |issue= 45 |pages= 32198-203 |year= 1999 |pmid= 10542257 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

FCGR3A

• INFO: Beginning work on FCGR3A... {November 15, 2007 7:32:12 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:32:38 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_FCGR3A_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1e4j.
 | PDB = {{PDB2|1e4j}}, {{PDB2|1e4k}}, {{PDB2|1fnl}}, {{PDB2|1iis}}, {{PDB2|1iix}}, {{PDB2|1t83}}, {{PDB2|1t89}}
 | Name = Fc fragment of IgG, low affinity IIIa, receptor (CD16a)
 | HGNCid = 3619
 | Symbol = FCGR3A
 | AltSymbols =; CD16; CD16a; FCG3; FCGR3; IGFR3
 | OMIM = 146740
 | ECnumber =  
 | Homologene = 477
 | MGIid = 2179523
 | Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0019864 |text = IgG binding}} 
 | Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = {{GNF_GO|id=GO:0006955 |text = immune response}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 2214
    | Hs_Ensembl =  
    | Hs_RefseqProtein = XP_001133750
    | Hs_RefseqmRNA = XM_001133750
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr =  
    | Hs_GenLoc_start =  
    | Hs_GenLoc_end =  
    | Hs_Uniprot =  
    | Mm_EntrezGene = 246256
    | Mm_Ensembl = ENSMUSG00000059089
    | Mm_RefseqmRNA = NM_144559
    | Mm_RefseqProtein = NP_653142
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 1
    | Mm_GenLoc_start = 172855601
    | Mm_GenLoc_end = 172866436
    | Mm_Uniprot =  
  }}
}}
'''Fc fragment of IgG, low affinity IIIa, receptor (CD16a)''', also known as '''FCGR3A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FCGR3A Fc fragment of IgG, low affinity IIIa, receptor (CD16a)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2214| accessdate = }}</ref>

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

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Anderson P, Caligiuri M, O'Brien C, ''et al.'' |title=Fc gamma receptor type III (CD16) is included in the zeta NK receptor complex expressed by human natural killer cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 6 |pages= 2274-8 |year= 1990 |pmid= 2138330 |doi=  }}
*{{cite journal  | author=Qiu WQ, de Bruin D, Brownstein BH, ''et al.'' |title=Organization of the human and mouse low-affinity Fc gamma R genes: duplication and recombination. |journal=Science |volume=248 |issue= 4956 |pages= 732-5 |year= 1990 |pmid= 2139735 |doi=  }}
*{{cite journal  | author=Le Coniat M, Kinet JP, Berger R |title=The human genes for the alpha and gamma subunits of the mast cell receptor for immunoglobulin E are located on human chromosome band 1q23. |journal=Immunogenetics |volume=32 |issue= 3 |pages= 183-6 |year= 1990 |pmid= 2146219 |doi=  }}
*{{cite journal  | author=Ory PA, Clark MR, Kwoh EE, ''et al.'' |title=Sequences of complementary DNAs that encode the NA1 and NA2 forms of Fc receptor III on human neutrophils. |journal=J. Clin. Invest. |volume=84 |issue= 5 |pages= 1688-91 |year= 1989 |pmid= 2478590 |doi=  }}
*{{cite journal  | author=Peltz GA, Grundy HO, Lebo RV, ''et al.'' |title=Human Fc gamma RIII: cloning, expression, and identification of the chromosomal locus of two Fc receptors for IgG. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 3 |pages= 1013-7 |year= 1989 |pmid= 2521732 |doi=  }}
*{{cite journal  | author=Scallon BJ, Scigliano E, Freedman VH, ''et al.'' |title=A human immunoglobulin G receptor exists in both polypeptide-anchored and phosphatidylinositol-glycan-anchored forms. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 13 |pages= 5079-83 |year= 1989 |pmid= 2525780 |doi=  }}
*{{cite journal  | author=Ravetch JV, Perussia B |title=Alternative membrane forms of Fc gamma RIII(CD16) on human natural killer cells and neutrophils. Cell type-specific expression of two genes that differ in single nucleotide substitutions. |journal=J. Exp. Med. |volume=170 |issue= 2 |pages= 481-97 |year= 1989 |pmid= 2526846 |doi=  }}
*{{cite journal  | author=Simmons D, Seed B |title=The Fc gamma receptor of natural killer cells is a phospholipid-linked membrane protein. |journal=Nature |volume=333 |issue= 6173 |pages= 568-70 |year= 1988 |pmid= 2967436 |doi= 10.1038/333568a0 }}
*{{cite journal  | author=Indik ZK, Hunter S, Huang MM, ''et al.'' |title=The high affinity Fc gamma receptor (CD64) induces phagocytosis in the absence of its cytoplasmic domain: the gamma subunit of Fc gamma RIIIA imparts phagocytic function to Fc gamma RI. |journal=Exp. Hematol. |volume=22 |issue= 7 |pages= 599-606 |year= 1994 |pmid= 7516890 |doi=  }}
*{{cite journal  | author=Detmers PA, Zhou D, Powell D, ''et al.'' |title=Endotoxin receptors (CD14) are found with CD16 (Fc gamma RIII) in an intracellular compartment of neutrophils that contains alkaline phosphatase. |journal=J. Immunol. |volume=155 |issue= 4 |pages= 2085-95 |year= 1995 |pmid= 7543538 |doi=  }}
*{{cite journal  | author=Morcos M, Hänsch GM, Schönermark M, ''et al.'' |title=Human glomerular mesangial cells express CD16 and may be stimulated via this receptor. |journal=Kidney Int. |volume=46 |issue= 6 |pages= 1627-34 |year= 1995 |pmid= 7700021 |doi=  }}
*{{cite journal  | author=Schumann G, Dasgupta JD |title=Specificity of signal transduction through CD16, TCR-CD3 and BCR receptor chains containing the tyrosine-associated activation motif. |journal=Int. Immunol. |volume=6 |issue= 9 |pages= 1383-92 |year= 1995 |pmid= 7819147 |doi=  }}
*{{cite journal  | author=Gessner JE, Grussenmeyer T, Kolanus W, Schmidt RE |title=The human low affinity immunoglobulin G Fc receptor III-A and III-B genes. Molecular characterization of the promoter regions. |journal=J. Biol. Chem. |volume=270 |issue= 3 |pages= 1350-61 |year= 1995 |pmid= 7836402 |doi=  }}
*{{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=Altin JG, Pagler EB, Kinnear BF, Warren HS |title=Molecular associations involving CD16, CD45 and zeta and gamma chains on human natural killer cells. |journal=Immunol. Cell Biol. |volume=72 |issue= 1 |pages= 87-96 |year= 1994 |pmid= 8157290 |doi=  }}
*{{cite journal  | author=Pignata C, Prasad KV, Robertson MJ, ''et al.'' |title=Fc gamma RIIIA-mediated signaling involves src-family lck in human natural killer cells. |journal=J. Immunol. |volume=151 |issue= 12 |pages= 6794-800 |year= 1994 |pmid= 8258691 |doi=  }}
*{{cite journal  | author=Cone JC, Lu Y, Trevillyan JM, ''et al.'' |title=Association of the p56lck protein tyrosine kinase with the Fc gamma RIIIA/CD16 complex in human natural killer cells. |journal=Eur. J. Immunol. |volume=23 |issue= 10 |pages= 2488-97 |year= 1993 |pmid= 8405050 |doi=  }}
*{{cite journal  | author=de Haas M, Koene HR, Kleijer M, ''et al.'' |title=A triallelic Fc gamma receptor type IIIA polymorphism influences the binding of human IgG by NK cell Fc gamma RIIIa. |journal=J. Immunol. |volume=156 |issue= 8 |pages= 3948-55 |year= 1996 |pmid= 8609432 |doi=  }}
*{{cite journal  | author=Gessner JE, Grussenmeyer T, Dumbsky M, Schmidt RE |title=Separate promoters from proximal and medial control regions contribute to the natural killer cell-specific transcription of the human FcgammaRIII-A (CD16-A) receptor gene. |journal=J. Biol. Chem. |volume=271 |issue= 48 |pages= 30755-64 |year= 1997 |pmid= 8940055 |doi=  }}
*{{cite journal  | author=Koene HR, Kleijer M, Algra J, ''et al.'' |title=Fc gammaRIIIa-158V/F polymorphism influences the binding of IgG by natural killer cell Fc gammaRIIIa, independently of the Fc gammaRIIIa-48L/R/H phenotype. |journal=Blood |volume=90 |issue= 3 |pages= 1109-14 |year= 1997 |pmid= 9242542 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

GLB1

• INFO: Beginning work on GLB1... {November 15, 2007 7:32:38 PM PST}
• SEARCH REDIRECT: Control Box Found: GLB1 {November 15, 2007 7:32:58 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 7:33:00 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 7:33:00 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 7:33:00 PM PST}
• UPDATED: Updated protein page: GLB1 {November 15, 2007 7:33:08 PM PST}

HMGA2

• INFO: Beginning work on HMGA2... {November 15, 2007 7:39:19 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:39:45 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 = High mobility group AT-hook 2
 | HGNCid = 5009
 | Symbol = HMGA2
 | AltSymbols =; BABL; HMGI-C; HMGIC; LIPO
 | OMIM = 600698
 | ECnumber =  
 | Homologene = 2602
 | MGIid = 101761
 | Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003680 |text = AT DNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0000785 |text = chromatin}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005694 |text = chromosome}} 
 | Process = {{GNF_GO|id=GO:0006325 |text = establishment and/or maintenance of chromatin architecture}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007001 |text = chromosome organization and biogenesis (sensu Eukaryota)}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8091
    | Hs_Ensembl = ENSG00000149948
    | Hs_RefseqProtein = NP_003474
    | Hs_RefseqmRNA = NM_003483
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 64504507
    | Hs_GenLoc_end = 64595566
    | Hs_Uniprot =  
    | Mm_EntrezGene = 15364
    | Mm_Ensembl = ENSMUSG00000056758
    | Mm_RefseqmRNA = NM_010441
    | Mm_RefseqProtein = NP_034571
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 119865724
    | Mm_GenLoc_end = 119879123
    | Mm_Uniprot = Q6NSP9
  }}
}}
'''High mobility group AT-hook 2''', also known as '''HMGA2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HMGA2 high mobility group AT-hook 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8091| accessdate = }}</ref>

<!-- 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 protein that belongs to the non-histone chromosomal high mobility group (HMG) protein family. HMG proteins function as architectural factors and are essential components of the enhancesome. This protein contains structural DNA-binding domains and may act as a transcriptional regulating factor. Identification of the deletion, amplification, and rearrangement of this gene that are associated with myxoid liposarcoma suggests a role in adipogenesis and mesenchymal differentiation. A gene knock out study of the mouse counterpart demonstrated that this gene is involved in diet-induced obesity. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref name="entrez">{{cite web | title = Entrez Gene: HMGA2 high mobility group AT-hook 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8091| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Pedeutour F, Ligon AH, Morton CC |title=[Genetics of uterine leiomyomata] |journal=Bulletin du cancer |volume=86 |issue= 11 |pages= 920-8 |year= 1999 |pmid= 10586108 |doi=  }}
*{{cite journal  | author=Reeves R, Beckerbauer L |title=HMGI/Y proteins: flexible regulators of transcription and chromatin structure. |journal=Biochim. Biophys. Acta |volume=1519 |issue= 1-2 |pages= 13-29 |year= 2001 |pmid= 11406267 |doi=  }}
*{{cite journal  | author=Manfioletti G, Giancotti V, Bandiera A, ''et al.'' |title=cDNA cloning of the HMGI-C phosphoprotein, a nuclear protein associated with neoplastic and undifferentiated phenotypes. |journal=Nucleic Acids Res. |volume=19 |issue= 24 |pages= 6793-7 |year= 1992 |pmid= 1762909 |doi=  }}
*{{cite journal  | author=Chau KY, Patel UA, Lee KL, ''et al.'' |title=The gene for the human architectural transcription factor HMGI-C consists of five exons each coding for a distinct functional element. |journal=Nucleic Acids Res. |volume=23 |issue= 21 |pages= 4262-6 |year= 1996 |pmid= 7501444 |doi=  }}
*{{cite journal  | author=Schoenmakers EF, Mols R, Wanschura S, ''et al.'' |title=Identification, molecular cloning, and characterization of the chromosome 12 breakpoint cluster region of uterine leiomyomas. |journal=Genes Chromosomes Cancer |volume=11 |issue= 2 |pages= 106-18 |year= 1995 |pmid= 7529547 |doi=  }}
*{{cite journal  | author=Ashar HR, Fejzo MS, Tkachenko A, ''et al.'' |title=Disruption of the architectural factor HMGI-C: DNA-binding AT hook motifs fused in lipomas to distinct transcriptional regulatory domains. |journal=Cell |volume=82 |issue= 1 |pages= 57-65 |year= 1995 |pmid= 7606786 |doi=  }}
*{{cite journal  | author=Schoenmakers EF, Wanschura S, Mols R, ''et al.'' |title=Recurrent rearrangements in the high mobility group protein gene, HMGI-C, in benign mesenchymal tumours. |journal=Nat. Genet. |volume=10 |issue= 4 |pages= 436-44 |year= 1995 |pmid= 7670494 |doi= 10.1038/ng0895-436 }}
*{{cite journal  | author=Patel UA, Bandiera A, Manfioletti G, ''et al.'' |title=Expression and cDNA cloning of human HMGI-C phosphoprotein. |journal=Biochem. Biophys. Res. Commun. |volume=201 |issue= 1 |pages= 63-70 |year= 1994 |pmid= 8198613 |doi=  }}
*{{cite journal  | author=Ashar HR, Cherath L, Przybysz KM, Chada K |title=Genomic characterization of human HMGIC, a member of the accessory transcription factor family found at translocation breakpoints in lipomas. |journal=Genomics |volume=31 |issue= 2 |pages= 207-14 |year= 1997 |pmid= 8824803 |doi= 10.1006/geno.1996.0033 }}
*{{cite journal  | author=Ishwad CS, Shriver MD, Lassige DM, Ferrell RE |title=The high mobility group I-C gene (HMGI-C): polymorphism and genetic localization. |journal=Hum. Genet. |volume=99 |issue= 1 |pages= 103-5 |year= 1997 |pmid= 9003504 |doi=  }}
*{{cite journal  | author=Petit MM, Swarts S, Bridge JA, Van de Ven WJ |title=Expression of reciprocal fusion transcripts of the HMGIC and LPP genes in parosteal lipoma. |journal=Cancer Genet. Cytogenet. |volume=106 |issue= 1 |pages= 18-23 |year= 1998 |pmid= 9772904 |doi=  }}
*{{cite journal  | author=Schoenmakers EF, Huysmans C, Van de Ven WJ |title=Allelic knockout of novel splice variants of human recombination repair gene RAD51B in t(12;14) uterine leiomyomas. |journal=Cancer Res. |volume=59 |issue= 1 |pages= 19-23 |year= 1999 |pmid= 9892177 |doi=  }}
*{{cite journal  | author=Gattas GJ, Quade BJ, Nowak RA, Morton CC |title=HMGIC expression in human adult and fetal tissues and in uterine leiomyomata. |journal=Genes Chromosomes Cancer |volume=25 |issue= 4 |pages= 316-22 |year= 1999 |pmid= 10398424 |doi=  }}
*{{cite journal  | author=Schwanbeck R, Manfioletti G, Wiśniewski JR |title=Architecture of high mobility group protein I-C.DNA complex and its perturbation upon phosphorylation by Cdc2 kinase. |journal=J. Biol. Chem. |volume=275 |issue= 3 |pages= 1793-801 |year= 2000 |pmid= 10636877 |doi=  }}
*{{cite journal  | author=Piekielko A, Drung A, Rogalla P, ''et al.'' |title=Distinct organization of DNA complexes of various HMGI/Y family proteins and their modulation upon mitotic phosphorylation. |journal=J. Biol. Chem. |volume=276 |issue= 3 |pages= 1984-92 |year= 2001 |pmid= 11034995 |doi= 10.1074/jbc.M004065200 }}
*{{cite journal  | author=Rogalla P, Lemke I, Kazmierczak B, Bullerdiek J |title=An identical HMGIC-LPP fusion transcript is consistently expressed in pulmonary chondroid hamartomas with t(3;12)(q27-28;q14-15). |journal=Genes Chromosomes Cancer |volume=29 |issue= 4 |pages= 363-6 |year= 2001 |pmid= 11066083 |doi=  }}
*{{cite journal  | author=Zentner MD, Lin HH, Deng HT, ''et al.'' |title=Requirement for high mobility group protein HMGI-C interaction with STAT3 inhibitor PIAS3 in repression of alpha-subunit of epithelial Na+ channel (alpha-ENaC) transcription by Ras activation in salivary epithelial cells. |journal=J. Biol. Chem. |volume=276 |issue= 32 |pages= 29805-14 |year= 2001 |pmid= 11390395 |doi= 10.1074/jbc.M103153200 }}
*{{cite journal  | author=Röijer E, Nordkvist A, Ström AK, ''et al.'' |title=Translocation, deletion/amplification, and expression of HMGIC and MDM2 in a carcinoma ex pleomorphic adenoma. |journal=Am. J. Pathol. |volume=160 |issue= 2 |pages= 433-40 |year= 2002 |pmid= 11839563 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

KLRK1

• INFO: Beginning work on KLRK1... {November 15, 2007 7:40:26 PM PST}
• SEARCH REDIRECT: Control Box Found: KLRK1 {November 15, 2007 7:40:53 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 7:40:54 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 7:40:54 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 7:40:54 PM PST}
• UPDATED: Updated protein page:
  KLRK1
  {November 15, 2007 7:40:59 PM PST}

NR1I2

• INFO: Beginning work on NR1I2... {November 15, 2007 7:39:45 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:40:26 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
}}

<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
 | image = PBB_Protein_NR1I2_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ilg.
 | PDB = {{PDB2|1ilg}}, {{PDB2|1ilh}}, {{PDB2|1m13}}, {{PDB2|1nrl}}, {{PDB2|1skx}}, {{PDB2|2o9i}}
 | Name = Nuclear receptor subfamily 1, group I, member 2
 | HGNCid = 7968
 | Symbol = NR1I2
 | AltSymbols =; SAR; PAR1; PAR2; PRR; BXR; ONR1; PAR; PARq; PXR; SXR
 | OMIM = 603065
 | ECnumber =  
 | Homologene = 40757
 | MGIid = 1337040
 | GeneAtlas_image1 = PBB_GE_NR1I2_207202_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_NR1I2_207203_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003707 |text = steroid hormone receptor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} 
 | Component = {{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:0006805 |text = xenobiotic metabolic process}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008202 |text = steroid metabolic process}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 8856
    | Hs_Ensembl = ENSG00000144852
    | Hs_RefseqProtein = NP_003880
    | Hs_RefseqmRNA = NM_003889
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 3
    | Hs_GenLoc_start = 120984236
    | Hs_GenLoc_end = 121020021
    | Hs_Uniprot = O75469
    | Mm_EntrezGene = 18171
    | Mm_Ensembl = ENSMUSG00000022809
    | Mm_RefseqmRNA = NM_010936
    | Mm_RefseqProtein = NP_035066
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 16
    | Mm_GenLoc_start = 38167590
    | Mm_GenLoc_end = 38214062
    | Mm_Uniprot = Q0P525
  }}
}}
'''Nuclear receptor subfamily 1, group I, member 2''', also known as '''NR1I2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NR1I2 nuclear receptor subfamily 1, group I, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8856| accessdate = }}</ref>

<!-- 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 nuclear receptor superfamily, members of which are transcription factors characterized by a ligand-binding domain and a DNA-binding domain. The encoded protein is a transcriptional regulator of the cytochrome P450 gene CYP3A4, binding to the response element of the CYP3A4 promoter as a heterodimer with the 9-cis retinoic acid receptor RXR. It is activated by a range of compounds that induce CYP3A4, including dexamethasone and rifampicin. Several alternatively spliced transcripts encoding different isoforms, some of which use non-AUG (CUG) translation initiation codon, have been described for this gene. Additional transcript variants exist, however, they have not been fully characterized.<ref name="entrez">{{cite web | title = Entrez Gene: NR1I2 nuclear receptor subfamily 1, group I, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8856| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Watkins RE, Noble SM, Redinbo MR |title=Structural insights into the promiscuity and function of the human pregnane X receptor. |journal=Current opinion in drug discovery & development |volume=5 |issue= 1 |pages= 150-8 |year= 2002 |pmid= 11865669 |doi=  }}
*{{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=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=Kliewer SA, Moore JT, Wade L, ''et al.'' |title=An orphan nuclear receptor activated by pregnanes defines a novel steroid signaling pathway. |journal=Cell |volume=92 |issue= 1 |pages= 73-82 |year= 1998 |pmid= 9489701 |doi=  }}
*{{cite journal  | author=Lehmann JM, McKee DD, Watson MA, ''et al.'' |title=The human orphan nuclear receptor PXR is activated by compounds that regulate CYP3A4 gene expression and cause drug interactions. |journal=J. Clin. Invest. |volume=102 |issue= 5 |pages= 1016-23 |year= 1998 |pmid= 9727070 |doi=  }}
*{{cite journal  | author=Bertilsson G, Heidrich J, Svensson K, ''et al.'' |title=Identification of a human nuclear receptor defines a new signaling pathway for CYP3A induction. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 21 |pages= 12208-13 |year= 1998 |pmid= 9770465 |doi=  }}
*{{cite journal  | author=Blumberg B, Sabbagh W, Juguilon H, ''et al.'' |title=SXR, a novel steroid and xenobiotic-sensing nuclear receptor. |journal=Genes Dev. |volume=12 |issue= 20 |pages= 3195-205 |year= 1998 |pmid= 9784494 |doi=  }}
*{{cite journal  | author=Dotzlaw H, Leygue E, Watson P, Murphy LC |title=The human orphan receptor PXR messenger RNA is expressed in both normal and neoplastic breast tissue. |journal=Clin. Cancer Res. |volume=5 |issue= 8 |pages= 2103-7 |year= 1999 |pmid= 10473093 |doi=  }}
*{{cite journal  | author=Geick A, Eichelbaum M, Burk O |title=Nuclear receptor response elements mediate induction of intestinal MDR1 by rifampin. |journal=J. Biol. Chem. |volume=276 |issue= 18 |pages= 14581-7 |year= 2001 |pmid= 11297522 |doi= 10.1074/jbc.M010173200 }}
*{{cite journal  | author=Watkins RE, Wisely GB, Moore LB, ''et al.'' |title=The human nuclear xenobiotic receptor PXR: structural determinants of directed promiscuity. |journal=Science |volume=292 |issue= 5525 |pages= 2329-33 |year= 2001 |pmid= 11408620 |doi= 10.1126/science.1060762 }}
*{{cite journal  | author=Zhang J, Kuehl P, Green ED, ''et al.'' |title=The human pregnane X receptor: genomic structure and identification and functional characterization of natural allelic variants. |journal=Pharmacogenetics |volume=11 |issue= 7 |pages= 555-72 |year= 2001 |pmid= 11668216 |doi=  }}
*{{cite journal  | author=Gonzalez MM, Carlberg C |title=Cross-repression, a functional consequence of the physical interaction of non-liganded nuclear receptors and POU domain transcription factors. |journal=J. Biol. Chem. |volume=277 |issue= 21 |pages= 18501-9 |year= 2002 |pmid= 11891224 |doi= 10.1074/jbc.M200205200 }}
*{{cite journal  | author=Takeshita A, Taguchi M, Koibuchi N, Ozawa Y |title=Putative role of the orphan nuclear receptor SXR (steroid and xenobiotic receptor) in the mechanism of CYP3A4 inhibition by xenobiotics. |journal=J. Biol. Chem. |volume=277 |issue= 36 |pages= 32453-8 |year= 2002 |pmid= 12072427 |doi= 10.1074/jbc.M111245200 }}
*{{cite journal  | author=Frungieri MB, Weidinger S, Meineke V, ''et al.'' |title=Proliferative action of mast-cell tryptase is mediated by PAR2, COX2, prostaglandins, and PPARgamma : Possible relevance to human fibrotic disorders. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 23 |pages= 15072-7 |year= 2003 |pmid= 12397176 |doi= 10.1073/pnas.232422999 }}
*{{cite journal  | author=Fukuen S, Fukuda T, Matsuda H, ''et al.'' |title=Identification of the novel splicing variants for the hPXR in human livers. |journal=Biochem. Biophys. Res. Commun. |volume=298 |issue= 3 |pages= 433-8 |year= 2002 |pmid= 12413960 |doi=  }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Chang TK, Bandiera SM, Chen J |title=Constitutive androstane receptor and pregnane X receptor gene expression in human liver: interindividual variability and correlation with CYP2B6 mRNA levels. |journal=Drug Metab. Dispos. |volume=31 |issue= 1 |pages= 7-10 |year= 2003 |pmid= 12485946 |doi=  }}
*{{cite journal  | author=Dussault I, Yoo HD, Lin M, ''et al.'' |title=Identification of an endogenous ligand that activates pregnane X receptor-mediated sterol clearance. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 3 |pages= 833-8 |year= 2003 |pmid= 12569201 |doi= 10.1073/pnas.0336235100 }}
*{{cite journal  | author=Kawana K, Ikuta T, Kobayashi Y, ''et al.'' |title=Molecular mechanism of nuclear translocation of an orphan nuclear receptor, SXR. |journal=Mol. Pharmacol. |volume=63 |issue= 3 |pages= 524-31 |year= 2003 |pmid= 12606758 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

NUP98

• INFO: Beginning work on NUP98... {November 15, 2007 7:33:08 PM PST}
• SEARCH REDIRECT: Control Box Found: NUP98 {November 15, 2007 7:33:41 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 7:33:42 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 7:33:42 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 7:33:42 PM PST}
• UPDATED: Updated protein page: NUP98 {November 15, 2007 7:33:48 PM PST}

PSMB8

• INFO: Beginning work on PSMB8... {November 15, 2007 7:33:48 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:34:15 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 = Proteasome (prosome, macropain) subunit, beta type, 8 (large multifunctional peptidase 7)
 | HGNCid = 9545
 | Symbol = PSMB8
 | AltSymbols =; D6S216; D6S216E; LMP7; MGC1491; RING10
 | OMIM = 177046
 | ECnumber =  
 | Homologene = 56499
 | MGIid = 1346527
 | GeneAtlas_image1 = PBB_GE_PSMB8_209040_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0004298 |text = threonine endopeptidase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} 
 | Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005839 |text = proteasome core complex (sensu Eukaryota)}} 
 | Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006511 |text = ubiquitin-dependent protein catabolic process}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0019882 |text = antigen processing and presentation}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5696
    | Hs_Ensembl = ENSG00000204264
    | Hs_RefseqProtein = NP_004150
    | Hs_RefseqmRNA = NM_004159
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 32916471
    | Hs_GenLoc_end = 32920690
    | Hs_Uniprot = P28062
    | Mm_EntrezGene = 16913
    | Mm_Ensembl = ENSMUSG00000024338
    | Mm_RefseqmRNA = NM_010724
    | Mm_RefseqProtein = NP_034854
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 17
    | Mm_GenLoc_start = 33808583
    | Mm_GenLoc_end = 33811657
    | Mm_Uniprot = P28063
  }}
}}
'''Proteasome (prosome, macropain) subunit, beta type, 8 (large multifunctional peptidase 7)''', also known as '''PSMB8''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PSMB8 proteasome (prosome, macropain) subunit, beta type, 8 (large multifunctional peptidase 7)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5696| accessdate = }}</ref>

<!-- 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 proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 20S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the proteasome B-type family, also known as the T1B family, that is a 20S core beta subunit. This gene is located in the class II region of the MHC (major histocompatibility complex). Expression of this gene is induced by gamma interferon and this gene product replaces catalytic subunit 3 (proteasome beta 5 subunit) in the immunoproteasome. Proteolytic processing is required to generate a mature subunit. Two alternative transcripts encoding two isoforms have been identified; both isoforms are processed to yield the same mature subunit.<ref name="entrez">{{cite web | title = Entrez Gene: PSMB8 proteasome (prosome, macropain) subunit, beta type, 8 (large multifunctional peptidase 7)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5696| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Coux O, Tanaka K, Goldberg AL |title=Structure and functions of the 20S and 26S proteasomes. |journal=Annu. Rev. Biochem. |volume=65 |issue=  |pages= 801-47 |year= 1996 |pmid= 8811196 |doi= 10.1146/annurev.bi.65.070196.004101 }}
*{{cite journal  | author=Goff SP |title=Death by deamination: a novel host restriction system for HIV-1. |journal=Cell |volume=114 |issue= 3 |pages= 281-3 |year= 2003 |pmid= 12914693 |doi=  }}
*{{cite journal  | author=Früh K, Yang Y, Arnold D, ''et al.'' |title=Alternative exon usage and processing of the major histocompatibility complex-encoded proteasome subunits. |journal=J. Biol. Chem. |volume=267 |issue= 31 |pages= 22131-40 |year= 1992 |pmid= 1429565 |doi=  }}
*{{cite journal  | author=Beck S, Kelly A, Radley E, ''et al.'' |title=DNA sequence analysis of 66 kb of the human MHC class II region encoding a cluster of genes for antigen processing. |journal=J. Mol. Biol. |volume=228 |issue= 2 |pages= 433-41 |year= 1992 |pmid= 1453454 |doi=  }}
*{{cite journal  | author=Bodmer JG, Marsh SG, Albert ED, ''et al.'' |title=Nomenclature for factors of the HLA system, 1991. WHO Nomenclature Committee for factors of the HLA system. |journal=Tissue Antigens |volume=39 |issue= 4 |pages= 161-73 |year= 1992 |pmid= 1529427 |doi=  }}
*{{cite journal  | author=Glynne R, Powis SH, Beck S, ''et al.'' |title=A proteasome-related gene between the two ABC transporter loci in the class II region of the human MHC. |journal=Nature |volume=353 |issue= 6342 |pages= 357-60 |year= 1991 |pmid= 1922342 |doi= 10.1038/353357a0 }}
*{{cite journal  | author=Ustrell V, Realini C, Pratt G, Rechsteiner M |title=Human lymphoblast and erythrocyte multicatalytic proteases: differential peptidase activities and responses to the 11S regulator. |journal=FEBS Lett. |volume=376 |issue= 3 |pages= 155-8 |year= 1996 |pmid= 7498531 |doi=  }}
*{{cite journal  | author=Kristensen P, Johnsen AH, Uerkvitz W, ''et al.'' |title=Human proteasome subunits from 2-dimensional gels identified by partial sequencing. |journal=Biochem. Biophys. Res. Commun. |volume=205 |issue= 3 |pages= 1785-9 |year= 1995 |pmid= 7811265 |doi=  }}
*{{cite journal  | author=Meinhardt T, Gräf U, Hämmerling GJ |title=Different genomic structure of mouse and human Lmp7 genes: characterization of MHC-encoded proteasome genes. |journal=Immunogenetics |volume=38 |issue= 5 |pages= 373-9 |year= 1993 |pmid= 8344725 |doi=  }}
*{{cite journal  | author=Glynne R, Kerr LA, Mockridge I, ''et al.'' |title=The major histocompatibility complex-encoded proteasome component LMP7: alternative first exons and post-translational processing. |journal=Eur. J. Immunol. |volume=23 |issue= 4 |pages= 860-6 |year= 1993 |pmid= 8458375 |doi=  }}
*{{cite journal  | author=Roby KF, Yang Y, Gershon D, Hunt JS |title=Cellular distribution of proteasome subunit Lmp7 mRNA and protein in human placentas. |journal=Immunology |volume=86 |issue= 3 |pages= 469-74 |year= 1996 |pmid= 8550087 |doi=  }}
*{{cite journal  | author=Beck S, Abdulla S, Alderton RP, ''et al.'' |title=Evolutionary dynamics of non-coding sequences within the class II region of the human MHC. |journal=J. Mol. Biol. |volume=255 |issue= 1 |pages= 1-13 |year= 1996 |pmid= 8568858 |doi= 10.1006/jmbi.1996.0001 }}
*{{cite journal  | author=Hisamatsu H, Shimbara N, Saito Y, ''et al.'' |title=Newly identified pair of proteasomal subunits regulated reciprocally by interferon gamma. |journal=J. Exp. Med. |volume=183 |issue= 4 |pages= 1807-16 |year= 1996 |pmid= 8666937 |doi=  }}
*{{cite journal  | author=Seeger M, Ferrell K, Frank R, Dubiel W |title=HIV-1 tat inhibits the 20 S proteasome and its 11 S regulator-mediated activation. |journal=J. Biol. Chem. |volume=272 |issue= 13 |pages= 8145-8 |year= 1997 |pmid= 9079628 |doi=  }}
*{{cite journal  | author=Kim TG, Lee YH, Choi HB, Han H |title=Two newly discovered alleles of major histocompatibility complex-encoded LMP7 in Korean populations. |journal=Hum. Immunol. |volume=46 |issue= 1 |pages= 61-4 |year= 1997 |pmid= 9157092 |doi=  }}
*{{cite journal  | author=Vives-Pi M, Vargas F, James RF, ''et al.'' |title=Proteasome subunits, low-molecular-mass polypeptides 2 and 7 are hyperexpressed by target cells in autoimmune thyroid disease but not in insulin-dependent diabetes mellitus: implications for autoimmunity. |journal=Tissue Antigens |volume=50 |issue= 2 |pages= 153-63 |year= 1997 |pmid= 9271825 |doi=  }}
*{{cite journal  | author=Madani N, Kabat D |title=An endogenous inhibitor of human immunodeficiency virus in human lymphocytes is overcome by the viral Vif protein. |journal=J. Virol. |volume=72 |issue= 12 |pages= 10251-5 |year= 1998 |pmid= 9811770 |doi=  }}
*{{cite journal  | author=Simon JH, Gaddis NC, Fouchier RA, Malim MH |title=Evidence for a newly discovered cellular anti-HIV-1 phenotype. |journal=Nat. Med. |volume=4 |issue= 12 |pages= 1397-400 |year= 1998 |pmid= 9846577 |doi= 10.1038/3987 }}
*{{cite journal  | author=Sewell AK, Price DA, Teisserenc H, ''et al.'' |title=IFN-gamma exposes a cryptic cytotoxic T lymphocyte epitope in HIV-1 reverse transcriptase. |journal=J. Immunol. |volume=162 |issue= 12 |pages= 7075-9 |year= 1999 |pmid= 10358150 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

RHCE

• INFO: Beginning work on RHCE... {November 15, 2007 7:34:15 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:35:31 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 = Rh blood group, CcEe antigens
 | HGNCid = 10008
 | Symbol = RHCE
 | AltSymbols =; RHC; CD240CE; MGC103977; RH; RH30A; RHE; RHIXB; RHPI; Rh4; RhIVb(J); RhVI; RhVIII; CD240D; DIIIc; RH30; RHCED; RHDVA(TT); RHDel; RHPII; RHXIII; RhDCw; RhII; RhK562-II; RhPI
 | OMIM = 111700
 | ECnumber =  
 | Homologene = 7918
 | MGIid = 1202882
 | GeneAtlas_image1 = PBB_GE_RHCE_215819_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_RHCE_216317_x_at_tn.png
 | GeneAtlas_image3 = PBB_GE_RHCE_210429_at_tn.png
 | Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0003674 |text = molecular_function}} 
 | Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0008150 |text = biological_process}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6006
    | Hs_Ensembl = ENSG00000188672
    | Hs_RefseqProtein = XP_001130486
    | Hs_RefseqmRNA = XM_001130486
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 25561328
    | Hs_GenLoc_end = 25629270
    | Hs_Uniprot = P18577
    | Mm_EntrezGene = 19746
    | Mm_Ensembl = ENSMUSG00000028825
    | Mm_RefseqmRNA = NM_011270
    | Mm_RefseqProtein = NP_035400
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 134136660
    | Mm_GenLoc_end = 134168248
    | Mm_Uniprot =  
  }}
}}
'''Rh blood group, CcEe antigens''', also known as '''RHCE''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RHCE Rh blood group, CcEe antigens| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6006| accessdate = }}</ref>

<!-- 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 Rh blood group system is the second most clinically significant of the blood groups, second only to ABO. It is also the most polymorphic of the blood groups, with variations due to deletions, gene conversions, and missense mutations. The Rh blood group includes this gene which encodes both the RhC and RhE antigens on a single polypeptide and a second gene which encodes the RhD protein. The classification of Rh-positive and Rh-negative individuals is determined by the presence or absence of the highly immunogenic RhD protein on the surface of erythrocytes. Alternative splicing of this gene results in four transcript variants encoding four different isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: RHCE Rh blood group, CcEe antigens| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6006| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Agre P, Cartron JP |title=Molecular biology of the Rh antigens. |journal=Blood |volume=78 |issue= 3 |pages= 551-63 |year= 1991 |pmid= 1907207 |doi=  }}
*{{cite journal  | author=Avent ND, Reid ME |title=The Rh blood group system: a review. |journal=Blood |volume=95 |issue= 2 |pages= 375-87 |year= 2000 |pmid= 10627438 |doi=  }}
*{{cite journal  | author=Flegel WA, Wagner FF |title=Molecular genetics of RH. |journal=Vox Sang. |volume=78 Suppl 2 |issue=  |pages= 109-15 |year= 2000 |pmid= 10938938 |doi=  }}
*{{cite journal  | author=Wagner FF, Flegel WA |title=Review: the molecular basis of the Rh blood group phenotypes. |journal=Immunohematology / American Red Cross |volume=20 |issue= 1 |pages= 23-36 |year= 2004 |pmid= 15373666 |doi=  }}
*{{cite journal  | author=Callebaut I, Dulin F, Bertrand O, ''et al.'' |title=Hydrophobic cluster analysis and modeling of the human Rh protein three-dimensional structures. |journal=Transfusion clinique et biologique : journal de la Société française de transfusion sanguine |volume=13 |issue= 1-2 |pages= 70-84 |year= 2006 |pmid= 16584906 |doi= 10.1016/j.tracli.2006.02.001 }}
*{{cite journal  | author=Le Van Kim C, Chérif-Zahar B, Raynal V, ''et al.'' |title=Multiple Rh messenger RNA isoforms are produced by alternative splicing. |journal=Blood |volume=80 |issue= 4 |pages= 1074-8 |year= 1992 |pmid= 1379850 |doi=  }}
*{{cite journal  | author=Le van Kim C, Mouro I, Chérif-Zahar B, ''et al.'' |title=Molecular cloning and primary structure of the human blood group RhD polypeptide. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 22 |pages= 10925-9 |year= 1992 |pmid= 1438298 |doi=  }}
*{{cite journal  | author=Chérif-Zahar B, Bloy C, Le Van Kim C, ''et al.'' |title=Molecular cloning and protein structure of a human blood group Rh polypeptide. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 16 |pages= 6243-7 |year= 1990 |pmid= 1696722 |doi=  }}
*{{cite journal  | author=Suyama K, Goldstein J, Aebersold R, Kent S |title=Regarding the size of Rh proteins. |journal=Blood |volume=77 |issue= 2 |pages= 411 |year= 1991 |pmid= 1898705 |doi=  }}
*{{cite journal  | author=Chérif-Zahar B, Mattéi MG, Le Van Kim C, ''et al.'' |title=Localization of the human Rh blood group gene structure to chromosome region 1p34.3-1p36.1 by in situ hybridization. |journal=Hum. Genet. |volume=86 |issue= 4 |pages= 398-400 |year= 1991 |pmid= 1900257 |doi=  }}
*{{cite journal  | author=Sawamura D, Li KH, Nomura K, ''et al.'' |title=Bullous pemphigoid antigen: cDNA cloning, cellular expression, and evidence for polymorphism of the human gene. |journal=J. Invest. Dermatol. |volume=96 |issue= 6 |pages= 908-15 |year= 1991 |pmid= 2045679 |doi=  }}
*{{cite journal  | author=Avent ND, Ridgwell K, Tanner MJ, Anstee DJ |title=cDNA cloning of a 30 kDa erythrocyte membrane protein associated with Rh (Rhesus)-blood-group-antigen expression. |journal=Biochem. J. |volume=271 |issue= 3 |pages= 821-5 |year= 1990 |pmid= 2123099 |doi=  }}
*{{cite journal  | author=Bloy C, Blanchard D, Dahr W, ''et al.'' |title=Determination of the N-terminal sequence of human red cell Rh(D) polypeptide and demonstration that the Rh(D), (c), and (E) antigens are carried by distinct polypeptide chains. |journal=Blood |volume=72 |issue= 2 |pages= 661-6 |year= 1988 |pmid= 3135863 |doi=  }}
*{{cite journal  | author=Avent ND, Ridgwell K, Mawby WJ, ''et al.'' |title=Protein-sequence studies on Rh-related polypeptides suggest the presence of at least two groups of proteins which associate in the human red-cell membrane. |journal=Biochem. J. |volume=256 |issue= 3 |pages= 1043-6 |year= 1989 |pmid= 3146980 |doi=  }}
*{{cite journal  | author=Kajii E, Umenishi F, Iwamoto S, Ikemoto S |title=Isolation of a new cDNA clone encoding an Rh polypeptide associated with the Rh blood group system. |journal=Hum. Genet. |volume=91 |issue= 2 |pages= 157-62 |year= 1993 |pmid= 7916743 |doi=  }}
*{{cite journal  | author=Chérif-Zahar B, Le Van Kim C, Rouillac C, ''et al.'' |title=Organization of the gene (RHCE) encoding the human blood group RhCcEe antigens and characterization of the promoter region. |journal=Genomics |volume=19 |issue= 1 |pages= 68-74 |year= 1994 |pmid= 8188244 |doi= 10.1006/geno.1994.1014 }}
*{{cite journal  | author=Mouro I, Colin Y, Chérif-Zahar B, ''et al.'' |title=Molecular genetic basis of the human Rhesus blood group system. |journal=Nat. Genet. |volume=5 |issue= 1 |pages= 62-5 |year= 1993 |pmid= 8220426 |doi= 10.1038/ng0993-62 }}
*{{cite journal  | author=Huang CH, Chen Y, Reid M, Ghosh S |title=Genetic recombination at the human RH locus: a family study of the red-cell Evans phenotype reveals a transfer of exons 2-6 from the RHD to the RHCE gene. |journal=Am. J. Hum. Genet. |volume=59 |issue= 4 |pages= 825-33 |year= 1996 |pmid= 8808597 |doi=  }}
*{{cite journal  | author=Huang CH |title=Alteration of RH gene structure and expression in human dCCee and DCW-red blood cells: phenotypic homozygosity versus genotypic heterozygosity. |journal=Blood |volume=88 |issue= 6 |pages= 2326-33 |year= 1996 |pmid= 8822955 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

RUNX1T1

• INFO: Beginning work on RUNX1T1... {November 15, 2007 7:29:41 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:30:18 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_RUNX1T1_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1wq6.
 | PDB = {{PDB2|1wq6}}, {{PDB2|2dj8}}, {{PDB2|2h7b}}
 | Name = Runt-related transcription factor 1; translocated to, 1 (cyclin D-related)
 | HGNCid = 1535
 | Symbol = RUNX1T1
 | AltSymbols =; AML1T1; CBFA2T1; CDR; ETO; MGC2796; MTG8; MTG8b; ZMYND2
 | OMIM = 133435
 | ECnumber =  
 | Homologene = 3801
 | MGIid = 104793
 | GeneAtlas_image1 = PBB_GE_RUNX1T1_205529_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_RUNX1T1_205528_s_at_tn.png
 | GeneAtlas_image3 = PBB_GE_RUNX1T1_216831_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016564 |text = transcription repressor activity}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} 
 | Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} 
 | Process = {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0045444 |text = fat cell differentiation}} {{GNF_GO|id=GO:0051101 |text = regulation of DNA binding}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 862
    | Hs_Ensembl = ENSG00000079102
    | Hs_RefseqProtein = NP_004340
    | Hs_RefseqmRNA = NM_004349
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 8
    | Hs_GenLoc_start = 93040328
    | Hs_GenLoc_end = 93176619
    | Hs_Uniprot = Q06455
    | Mm_EntrezGene = 12395
    | Mm_Ensembl = ENSMUSG00000006586
    | Mm_RefseqmRNA = XM_975417
    | Mm_RefseqProtein = XP_980511
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 13670583
    | Mm_GenLoc_end = 13818712
    | Mm_Uniprot = Q61909
  }}
}}
'''Runt-related transcription factor 1; translocated to, 1 (cyclin D-related)''', also known as '''RUNX1T1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RUNX1T1 runt-related transcription factor 1; translocated to, 1 (cyclin D-related)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=862| accessdate = }}</ref>

<!-- 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 putative zinc finger transcription factor and oncoprotein. In acute myeloid leukemia, especially in the M2 subtype, the t(8;21)(q22;q22) translocation is one of the most frequent karyotypic abnormalities. The translocation produces a chimeric gene made up of the 5'-region of the RUNX1 gene fused to the 3'-region of this gene. The chimeric protein is thought to associate with the nuclear corepressor/histone deacetylase complex to block hematopoietic differentiation. Several transcript variants encoding multiple isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: RUNX1T1 runt-related transcription factor 1; translocated to, 1 (cyclin D-related)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=862| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Ferrara F, Del Vecchio L |title=Acute myeloid leukemia with t(8;21)/AML1/ETO: a distinct biological and clinical entity. |journal=Haematologica |volume=87 |issue= 3 |pages= 306-19 |year= 2002 |pmid= 11869944 |doi=  }}
*{{cite journal  | author=Erickson P, Gao J, Chang KS, ''et al.'' |title=Identification of breakpoints in t(8;21) acute myelogenous leukemia and isolation of a fusion transcript, AML1/ETO, with similarity to Drosophila segmentation gene, runt. |journal=Blood |volume=80 |issue= 7 |pages= 1825-31 |year= 1992 |pmid= 1391946 |doi=  }}
*{{cite journal  | author=Nisson PE, Watkins PC, Sacchi N |title=Transcriptionally active chimeric gene derived from the fusion of the AML1 gene and a novel gene on chromosome 8 in t(8;21) leukemic cells. |journal=Cancer Genet. Cytogenet. |volume=63 |issue= 2 |pages= 81-8 |year= 1992 |pmid= 1423235 |doi=  }}
*{{cite journal  | author=Era T, Asou N, Kunisada T, ''et al.'' |title=Identification of two transcripts of AML1/ETO-fused gene in t(8;21) leukemic cells and expression of wild-type ETO gene in hematopoietic cells. |journal=Genes Chromosomes Cancer |volume=13 |issue= 1 |pages= 25-33 |year= 1995 |pmid= 7541640 |doi=  }}
*{{cite journal  | author=Tighe JE, Calabi F |title=Alternative, out-of-frame runt/MTG8 transcripts are encoded by the derivative (8) chromosome in the t(8;21) of acute myeloid leukemia M2. |journal=Blood |volume=84 |issue= 7 |pages= 2115-21 |year= 1994 |pmid= 7919324 |doi=  }}
*{{cite journal  | author=Erickson PF, Robinson M, Owens G, Drabkin HA |title=The ETO portion of acute myeloid leukemia t(8;21) fusion transcript encodes a highly evolutionarily conserved, putative transcription factor. |journal=Cancer Res. |volume=54 |issue= 7 |pages= 1782-6 |year= 1994 |pmid= 8137293 |doi=  }}
*{{cite journal  | author=Miyoshi H, Kozu T, Shimizu K, ''et al.'' |title=The t(8;21) translocation in acute myeloid leukemia results in production of an AML1-MTG8 fusion transcript. |journal=EMBO J. |volume=12 |issue= 7 |pages= 2715-21 |year= 1993 |pmid= 8334990 |doi=  }}
*{{cite journal  | author=Kozu T, Miyoshi H, Shimizu K, ''et al.'' |title=Junctions of the AML1/MTG8(ETO) fusion are constant in t(8;21) acute myeloid leukemia detected by reverse transcription polymerase chain reaction. |journal=Blood |volume=82 |issue= 4 |pages= 1270-6 |year= 1993 |pmid= 8353289 |doi=  }}
*{{cite journal  | author=Niwa-Kawakita M, Miyoshi H, Gotoh O, ''et al.'' |title=Cloning and gene mapping of the mouse homologue of the CBFA2T1 gene associated with human acute myeloid leukemia. |journal=Genomics |volume=29 |issue= 3 |pages= 755-9 |year= 1996 |pmid= 8575770 |doi= 10.1006/geno.1995.9941 }}
*{{cite journal  | author=Erickson PF, Dessev G, Lasher RS, ''et al.'' |title=ETO and AML1 phosphoproteins are expressed in CD34+ hematopoietic progenitors: implications for t(8;21) leukemogenesis and monitoring residual disease. |journal=Blood |volume=88 |issue= 5 |pages= 1813-23 |year= 1996 |pmid= 8781439 |doi=  }}
*{{cite journal  | author=Wolford JK, Bogardus C, Prochazka M |title=Polymorphism in the 3' untranslated region of MTG8 is associated with obesity in Pima Indian males. |journal=Biochem. Biophys. Res. Commun. |volume=246 |issue= 3 |pages= 624-6 |year= 1998 |pmid= 9618262 |doi= 10.1006/bbrc.1998.8683 }}
*{{cite journal  | author=Sacchi N, Tamanini F, Willemsen R, ''et al.'' |title=Subcellular localization of the oncoprotein MTG8 (CDR/ETO) in neural cells. |journal=Oncogene |volume=16 |issue= 20 |pages= 2609-15 |year= 1998 |pmid= 9632137 |doi= 10.1038/sj.onc.1201824 }}
*{{cite journal  | author=Wolford JK, Prochazka M |title=Structure and expression of the human MTG8/ETO gene. |journal=Gene |volume=212 |issue= 1 |pages= 103-9 |year= 1998 |pmid= 9661669 |doi=  }}
*{{cite journal  | author=Calabi F, Cilli V |title=CBFA2T1, a gene rearranged in human leukemia, is a member of a multigene family. |journal=Genomics |volume=52 |issue= 3 |pages= 332-41 |year= 1998 |pmid= 9790752 |doi= 10.1006/geno.1998.5429 }}
*{{cite journal  | author=Komori A, Sueoka E, Fujiki H, ''et al.'' |title=Association of MTG8 (ETO/CDR), a leukemia-related protein, with serine/threonine protein kinases and heat shock protein HSP90 in human hematopoietic cell lines. |journal=Jpn. J. Cancer Res. |volume=90 |issue= 1 |pages= 60-8 |year= 1999 |pmid= 10076566 |doi=  }}
*{{cite journal  | author=Morohoshi F, Mitani S, Mitsuhashi N, ''et al.'' |title=Structure and expression pattern of a human MTG8/ETO family gene, MTGR1. |journal=Gene |volume=241 |issue= 2 |pages= 287-95 |year= 2000 |pmid= 10675041 |doi=  }}
*{{cite journal  | author=Melnick AM, Westendorf JJ, Polinger A, ''et al.'' |title=The ETO protein disrupted in t(8;21)-associated acute myeloid leukemia is a corepressor for the promyelocytic leukemia zinc finger protein. |journal=Mol. Cell. Biol. |volume=20 |issue= 6 |pages= 2075-86 |year= 2000 |pmid= 10688654 |doi=  }}
*{{cite journal  | author=Miyamoto T, Weissman IL, Akashi K |title=AML1/ETO-expressing nonleukemic stem cells in acute myelogenous leukemia with 8;21 chromosomal translocation. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 13 |pages= 7521-6 |year= 2000 |pmid= 10861016 |doi=  }}
*{{cite journal  | author=Odaka Y, Mally A, Elliott LT, Meyers S |title=Nuclear import and subnuclear localization of the proto-oncoprotein ETO (MTG8). |journal=Oncogene |volume=19 |issue= 32 |pages= 3584-97 |year= 2000 |pmid= 10951564 |doi= 10.1038/sj.onc.1203689 }}
*{{cite journal  | author=Wood JD, Nucifora FC, Duan K, ''et al.'' |title=Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene product, interacts with ETO/MTG8 in the nuclear matrix and represses transcription. |journal=J. Cell Biol. |volume=150 |issue= 5 |pages= 939-48 |year= 2000 |pmid= 10973986 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

SPTAN1

• INFO: Beginning work on SPTAN1... {November 15, 2007 7:35:31 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:35:55 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_SPTAN1_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aey.
 | PDB = {{PDB2|1aey}}, {{PDB2|1aj3}}, {{PDB2|1bk2}}, {{PDB2|1cun}}, {{PDB2|1e6g}}, {{PDB2|1e6h}}, {{PDB2|1e7o}}, {{PDB2|1h8k}}, {{PDB2|1hd3}}, {{PDB2|1m8m}}, {{PDB2|1pwt}}, {{PDB2|1qkw}}, {{PDB2|1qkx}}, {{PDB2|1shg}}, {{PDB2|1u06}}, {{PDB2|1u4q}}, {{PDB2|1u5p}}, {{PDB2|1uue}}, {{PDB2|2cdt}}, {{PDB2|2f2v}}, {{PDB2|2f2w}}, {{PDB2|2f2x}}, {{PDB2|2fot}}, {{PDB2|2jm8}}, {{PDB2|2jm9}}, {{PDB2|2jma}}, {{PDB2|2nuz}}
 | Name = Spectrin, alpha, non-erythrocytic 1 (alpha-fodrin)
 | HGNCid = 11273
 | Symbol = SPTAN1
 | AltSymbols =; (ALPHA)II-SPECTRIN; FLJ44613
 | OMIM = 182810
 | ECnumber =  
 | Homologene = 2353
 | MGIid = 98386
 | GeneAtlas_image1 = PBB_GE_SPTAN1_208611_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_SPTAN1_215235_at_tn.png
 | Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} 
 | Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0008091 |text = spectrin}} {{GNF_GO|id=GO:0016020 |text = membrane}} 
 | Process = {{GNF_GO|id=GO:0051016 |text = barbed-end actin filament capping}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6709
    | Hs_Ensembl = ENSG00000197694
    | Hs_RefseqProtein = NP_003118
    | Hs_RefseqmRNA = NM_003127
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 9
    | Hs_GenLoc_start = 130354690
    | Hs_GenLoc_end = 130435762
    | Hs_Uniprot = Q13813
    | Mm_EntrezGene = 20740
    | Mm_Ensembl = ENSMUSG00000057738
    | Mm_RefseqmRNA = XM_001000210
    | Mm_RefseqProtein = XP_001000210
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 29787686
    | Mm_GenLoc_end = 29853457
    | Mm_Uniprot = Q3URW8
  }}
}}
'''Spectrin, alpha, non-erythrocytic 1 (alpha-fodrin)''', also known as '''SPTAN1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SPTAN1 spectrin, alpha, non-erythrocytic 1 (alpha-fodrin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6709| accessdate = }}</ref>

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

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Chow CW |title=Regulation and intracellular localization of the epithelial isoforms of the Na+/H+ exchangers NHE2 and NHE3. |journal=Clinical and investigative medicine. Médecine clinique et experimentale |volume=22 |issue= 5 |pages= 195-206 |year= 1999 |pmid= 10579058 |doi=  }}
*{{cite journal  | author=Hayashi Y, Arakaki R, Ishimaru N |title=The role of caspase cascade on the development of primary Sjögren's syndrome. |journal=J. Med. Invest. |volume=50 |issue= 1-2 |pages= 32-8 |year= 2003 |pmid= 12630566 |doi=  }}
*{{cite journal  | author=Bennett V |title=Immunoreactive forms of human erythrocyte ankyrin are present in diverse cells and tissues. |journal=Nature |volume=281 |issue= 5732 |pages= 597-9 |year= 1979 |pmid= 492324 |doi=  }}
*{{cite journal  | author=Frappier T, Stetzkowski-Marden F, Pradel LA |title=Interaction domains of neurofilament light chain and brain spectrin. |journal=Biochem. J. |volume=275 ( Pt 2) |issue=  |pages= 521-7 |year= 1991 |pmid= 1902666 |doi=  }}
*{{cite journal  | author=Bennett AF, Hayes NV, Baines AJ |title=Site specificity in the interactions of synapsin 1 with tubulin. |journal=Biochem. J. |volume=276 ( Pt 3) |issue=  |pages= 793-9 |year= 1991 |pmid= 1905928 |doi=  }}
*{{cite journal  | author=Davis LH, Bennett V |title=Mapping the binding sites of human erythrocyte ankyrin for the anion exchanger and spectrin. |journal=J. Biol. Chem. |volume=265 |issue= 18 |pages= 10589-96 |year= 1990 |pmid= 2141335 |doi=  }}
*{{cite journal  | author=Moon RT, McMahon AP |title=Generation of diversity in nonerythroid spectrins. Multiple polypeptides are predicted by sequence analysis of cDNAs encompassing the coding region of human nonerythroid alpha-spectrin. |journal=J. Biol. Chem. |volume=265 |issue= 8 |pages= 4427-33 |year= 1990 |pmid= 2307671 |doi=  }}
*{{cite journal  | author=Langley RC, Cohen CM |title=Association of spectrin with desmin intermediate filaments. |journal=J. Cell. Biochem. |volume=30 |issue= 2 |pages= 101-9 |year= 1986 |pmid= 2939097 |doi= 10.1002/jcb.240300202 }}
*{{cite journal  | author=Cianci CD, Giorgi M, Morrow JS |title=Phosphorylation of ankyrin down-regulates its cooperative interaction with spectrin and protein 3. |journal=J. Cell. Biochem. |volume=37 |issue= 3 |pages= 301-15 |year= 1988 |pmid= 2970468 |doi= 10.1002/jcb.240370305 }}
*{{cite journal  | author=Steiner JP, Bennett V |title=Ankyrin-independent membrane protein-binding sites for brain and erythrocyte spectrin. |journal=J. Biol. Chem. |volume=263 |issue= 28 |pages= 14417-25 |year= 1988 |pmid= 2971657 |doi=  }}
*{{cite journal  | author=Herrmann H, Wiche G |title=Plectin and IFAP-300K are homologous proteins binding to microtubule-associated proteins 1 and 2 and to the 240-kilodalton subunit of spectrin. |journal=J. Biol. Chem. |volume=262 |issue= 3 |pages= 1320-5 |year= 1987 |pmid= 3027087 |doi=  }}
*{{cite journal  | author=McMahon AP, Giebelhaus DH, Champion JE, ''et al.'' |title=cDNA cloning, sequencing and chromosome mapping of a non-erythroid spectrin, human alpha-fodrin. |journal=Differentiation |volume=34 |issue= 1 |pages= 68-78 |year= 1987 |pmid= 3038643 |doi=  }}
*{{cite journal  | author=Frappier T, Regnouf F, Pradel LA |title=Binding of brain spectrin to the 70-kDa neurofilament subunit protein. |journal=Eur. J. Biochem. |volume=169 |issue= 3 |pages= 651-7 |year= 1988 |pmid= 3121319 |doi=  }}
*{{cite journal  | author=Leto TL, Fortugno-Erikson D, Barton D, ''et al.'' |title=Comparison of nonerythroid alpha-spectrin genes reveals strict homology among diverse species. |journal=Mol. Cell. Biol. |volume=8 |issue= 1 |pages= 1-9 |year= 1988 |pmid= 3336352 |doi=  }}
*{{cite journal  | author=McMahon AP, Moon RT |title=Structure and evolution of a non-erythroid spectrin, human alpha-fodrin. |journal=Biochem. Soc. Trans. |volume=15 |issue= 5 |pages= 804-7 |year= 1988 |pmid= 3691949 |doi=  }}
*{{cite journal  | author=Lundberg S, Björk J, Löfvenberg L, Backman L |title=Cloning, expression and characterization of two putative calcium-binding sites in human non-erythroid alpha-spectrin. |journal=Eur. J. Biochem. |volume=230 |issue= 2 |pages= 658-65 |year= 1995 |pmid= 7607240 |doi=  }}
*{{cite journal  | author=Hughes CA, Bennett V |title=Adducin: a physical model with implications for function in assembly of spectrin-actin complexes. |journal=J. Biol. Chem. |volume=270 |issue= 32 |pages= 18990-6 |year= 1995 |pmid= 7642559 |doi=  }}
*{{cite journal  | author=Gregorio CC, Repasky EA, Fowler VM, Black JD |title=Dynamic properties of ankyrin in T lymphocytes: colocalization with spectrin and protein kinase C beta. |journal=J. Cell Biol. |volume=125 |issue= 2 |pages= 345-58 |year= 1994 |pmid= 8163551 |doi=  }}
*{{cite journal  | author=Li X, Bennett V |title=Identification of the spectrin subunit and domains required for formation of spectrin/adducin/actin complexes. |journal=J. Biol. Chem. |volume=271 |issue= 26 |pages= 15695-702 |year= 1996 |pmid= 8663089 |doi=  }}
*{{cite journal  | author=Stabach PR, Cianci CD, Glantz SB, ''et al.'' |title=Site-directed mutagenesis of alpha II spectrin at codon 1175 modulates its mu-calpain susceptibility. |journal=Biochemistry |volume=36 |issue= 1 |pages= 57-65 |year= 1997 |pmid= 8993318 |doi= 10.1021/bi962034i }}
}}
{{refend}}

{{protein-stub}}
 

TACR1

• INFO: Beginning work on TACR1... {November 15, 2007 7:35:55 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:36:20 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 = Tachykinin receptor 1
 | HGNCid = 11526
 | Symbol = TACR1
 | AltSymbols =; SPR; NK1R; NKIR; TAC1R
 | OMIM = 162323
 | ECnumber =  
 | Homologene = 20288
 | MGIid = 98475
 | GeneAtlas_image1 = PBB_GE_TACR1_208049_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_TACR1_210637_at_tn.png
 | Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0004995 |text = tachykinin receptor activity}} 
 | Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} 
 | Process = {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{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:0007200 |text = G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)}} {{GNF_GO|id=GO:0007217 |text = tachykinin signaling pathway}} {{GNF_GO|id=GO:0007638 |text = mechanosensory behavior}} {{GNF_GO|id=GO:0009582 |text = detection of abiotic stimulus}} {{GNF_GO|id=GO:0048265 |text = response to pain}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6869
    | Hs_Ensembl = ENSG00000115353
    | Hs_RefseqProtein = NP_001049
    | Hs_RefseqmRNA = NM_001058
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 75129738
    | Hs_GenLoc_end = 75279781
    | Hs_Uniprot = P25103
    | Mm_EntrezGene = 21336
    | Mm_Ensembl = ENSMUSG00000030043
    | Mm_RefseqmRNA = NM_009313
    | Mm_RefseqProtein = NP_033339
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 82368133
    | Mm_GenLoc_end = 82525757
    | Mm_Uniprot = Q3V353
  }}
}}
'''Tachykinin receptor 1''', also known as '''TACR1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TACR1 tachykinin receptor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6869| accessdate = }}</ref>

<!-- 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 belongs to a family of genes that function as receptors for tachykinins.  Receptor affinities are specified by variations in the 5'-end of the sequence.  The receptors belonging to this family are characterized by interactions with G proteins and 7 hydrophobic transmembrane regions.  This gene encodes the receptor for the tachykinin substance P, also referred to as neurokinin 1.  This receptor is also involved in the mediation of phosphatidylinositol metabolism of substance P.<ref name="entrez">{{cite web | title = Entrez Gene: TACR1 tachykinin receptor 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6869| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Burcher E |title=The study of tachykinin receptors. |journal=Clin. Exp. Pharmacol. Physiol. |volume=16 |issue= 6 |pages= 539-43 |year= 1989 |pmid= 2548782 |doi=  }}
*{{cite journal  | author=Kowall NW, Quigley BJ, Krause JE, ''et al.'' |title=Substance P and substance P receptor histochemistry in human neurodegenerative diseases. |journal=Regul. Pept. |volume=46 |issue= 1-2 |pages= 174-85 |year= 1993 |pmid= 7692486 |doi=  }}
*{{cite journal  | author=Patacchini R, Maggi CA |title=Peripheral tachykinin receptors as targets for new drugs. |journal=Eur. J. Pharmacol. |volume=429 |issue= 1-3 |pages= 13-21 |year= 2002 |pmid= 11698023 |doi=  }}
*{{cite journal  | author=Saito R, Takano Y, Kamiya HO |title=Roles of substance P and NK(1) receptor in the brainstem in the development of emesis. |journal=J. Pharmacol. Sci. |volume=91 |issue= 2 |pages= 87-94 |year= 2003 |pmid= 12686752 |doi=  }}
*{{cite journal  | author=Fong TM, Yu H, Huang RR, Strader CD |title=The extracellular domain of the neurokinin-1 receptor is required for high-affinity binding of peptides. |journal=Biochemistry |volume=31 |issue= 47 |pages= 11806-11 |year= 1992 |pmid= 1280161 |doi=  }}
*{{cite journal  | author=Fong TM, Huang RR, Strader CD |title=Localization of agonist and antagonist binding domains of the human neurokinin-1 receptor. |journal=J. Biol. Chem. |volume=267 |issue= 36 |pages= 25664-7 |year= 1993 |pmid= 1281469 |doi=  }}
*{{cite journal  | author=Fong TM, Anderson SA, Yu H, ''et al.'' |title=Differential activation of intracellular effector by two isoforms of human neurokinin-1 receptor. |journal=Mol. Pharmacol. |volume=41 |issue= 1 |pages= 24-30 |year= 1992 |pmid= 1310144 |doi=  }}
*{{cite journal  | author=Takahashi K, Tanaka A, Hara M, Nakanishi S |title=The primary structure and gene organization of human substance P and neuromedin K receptors. |journal=Eur. J. Biochem. |volume=204 |issue= 3 |pages= 1025-33 |year= 1992 |pmid= 1312928 |doi=  }}
*{{cite journal  | author=Walsh DA, Mapp PI, Wharton J, ''et al.'' |title=Localisation and characterisation of substance P binding to human synovial tissue in rheumatoid arthritis. |journal=Ann. Rheum. Dis. |volume=51 |issue= 3 |pages= 313-7 |year= 1992 |pmid= 1374227 |doi=  }}
*{{cite journal  | author=Gerard NP, Garraway LA, Eddy RL, ''et al.'' |title=Human substance P receptor (NK-1): organization of the gene, chromosome localization, and functional expression of cDNA clones. |journal=Biochemistry |volume=30 |issue= 44 |pages= 10640-6 |year= 1991 |pmid= 1657150 |doi=  }}
*{{cite journal  | author=Hopkins B, Powell SJ, Danks P, ''et al.'' |title=Isolation and characterisation of the human lung NK-1 receptor cDNA. |journal=Biochem. Biophys. Res. Commun. |volume=180 |issue= 2 |pages= 1110-7 |year= 1991 |pmid= 1659396 |doi=  }}
*{{cite journal  | author=Takeda Y, Chou KB, Takeda J, ''et al.'' |title=Molecular cloning, structural characterization and functional expression of the human substance P receptor. |journal=Biochem. Biophys. Res. Commun. |volume=179 |issue= 3 |pages= 1232-40 |year= 1991 |pmid= 1718267 |doi=  }}
*{{cite journal  | author=Giuliani S, Barbanti G, Turini D, ''et al.'' |title=NK2 tachykinin receptors and contraction of circular muscle of the human colon: characterization of the NK2 receptor subtype. |journal=Eur. J. Pharmacol. |volume=203 |issue= 3 |pages= 365-70 |year= 1992 |pmid= 1723045 |doi=  }}
*{{cite journal  | author=Ichinose H, Katoh S, Sueoka T, ''et al.'' |title=Cloning and sequencing of cDNA encoding human sepiapterin reductase--an enzyme involved in tetrahydrobiopterin biosynthesis. |journal=Biochem. Biophys. Res. Commun. |volume=179 |issue= 1 |pages= 183-9 |year= 1991 |pmid= 1883349 |doi=  }}
*{{cite journal  | author=Thöny B, Heizmann CW, Mattei MG |title=Human GTP-cyclohydrolase I gene and sepiapterin reductase gene map to region 14q21-q22 and 2p14-p12, respectively, by in situ hybridization. |journal=Genomics |volume=26 |issue= 1 |pages= 168-70 |year= 1995 |pmid= 7782081 |doi=  }}
*{{cite journal  | author=Fong TM, Cascieri MA, Yu H, ''et al.'' |title=Amino-aromatic interaction between histidine 197 of the neurokinin-1 receptor and CP 96345. |journal=Nature |volume=362 |issue= 6418 |pages= 350-3 |year= 1993 |pmid= 8384323 |doi= 10.1038/362350a0 }}
*{{cite journal  | author=Derocq JM, Ségui M, Blazy C, ''et al.'' |title=Effect of substance P on cytokine production by human astrocytic cells and blood mononuclear cells: characterization of novel tachykinin receptor antagonists. |journal=FEBS Lett. |volume=399 |issue= 3 |pages= 321-5 |year= 1997 |pmid= 8985172 |doi=  }}
*{{cite journal  | author=De Felipe C, Herrero JF, O'Brien JA, ''et al.'' |title=Altered nociception, analgesia and aggression in mice lacking the receptor for substance P. |journal=Nature |volume=392 |issue= 6674 |pages= 394-7 |year= 1998 |pmid= 9537323 |doi= 10.1038/32904 }}
}}
{{refend}}

{{protein-stub}}
 

TFAP2A

• INFO: Beginning work on TFAP2A... {November 15, 2007 7:36:20 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:36:56 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 = Transcription factor AP-2 alpha (activating enhancer binding protein 2 alpha)
 | HGNCid = 11742
 | Symbol = TFAP2A
 | AltSymbols =; AP-2; AP-2alpha; AP2TF; TFAP2
 | OMIM = 107580
 | ECnumber =  
 | Homologene = 2421
 | MGIid = 104671
 | GeneAtlas_image1 = PBB_GE_TFAP2A_204653_at_tn.png
 | GeneAtlas_image2 = PBB_GE_TFAP2A_204654_s_at_tn.png
 | GeneAtlas_image3 = PBB_GE_TFAP2A_210669_at_tn.png
 | Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003705 |text = RNA polymerase II transcription factor activity, enhancer binding}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0046983 |text = protein dimerization activity}} 
 | Component = {{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:0006357 |text = regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007398 |text = ectoderm development}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7020
    | Hs_Ensembl = ENSG00000137203
    | Hs_RefseqProtein = NP_001027451
    | Hs_RefseqmRNA = NM_001032280
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 10504906
    | Hs_GenLoc_end = 10527824
    | Hs_Uniprot = P05549
    | Mm_EntrezGene = 21418
    | Mm_Ensembl = ENSMUSG00000021359
    | Mm_RefseqmRNA = NM_011547
    | Mm_RefseqProtein = NP_035677
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 40726649
    | Mm_GenLoc_end = 40745894
    | Mm_Uniprot = Q3UL09
  }}
}}
'''Transcription factor AP-2 alpha (activating enhancer binding protein 2 alpha)''', also known as '''TFAP2A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TFAP2A transcription factor AP-2 alpha (activating enhancer binding protein 2 alpha)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7020| accessdate = }}</ref>

<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title = 
| summary_text = AP2-alpha is a 52-kD retinoic acid-inducible and developmentally regulated activator of transcription that binds to a consensus DNA-binding sequence CCCCAGGC in the SV40 and metallothionein (MIM 156350) promoters.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: TFAP2A transcription factor AP-2 alpha (activating enhancer binding protein 2 alpha)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7020| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Murphy JE, Keen JH |title=Recognition sites for clathrin-associated proteins AP-2 and AP-3 on clathrin triskelia. |journal=J. Biol. Chem. |volume=267 |issue= 15 |pages= 10850-5 |year= 1992 |pmid= 1587861 |doi=  }}
*{{cite journal  | author=Gaynor RB, Muchardt C, Xia YR, ''et al.'' |title=Localization of the gene for the DNA-binding protein AP-2 to human chromosome 6p22.3-pter. |journal=Genomics |volume=10 |issue= 4 |pages= 1100-2 |year= 1991 |pmid= 1916817 |doi=  }}
*{{cite journal  | author=Williams T, Tjian R |title=Characterization of a dimerization motif in AP-2 and its function in heterologous DNA-binding proteins. |journal=Science |volume=251 |issue= 4997 |pages= 1067-71 |year= 1991 |pmid= 1998122 |doi=  }}
*{{cite journal  | author=Williams T, Tjian R |title=Analysis of the DNA-binding and activation properties of the human transcription factor AP-2. |journal=Genes Dev. |volume=5 |issue= 4 |pages= 670-82 |year= 1991 |pmid= 2010091 |doi=  }}
*{{cite journal  | author=Williams T, Admon A, Lüscher B, Tjian R |title=Cloning and expression of AP-2, a cell-type-specific transcription factor that activates inducible enhancer elements. |journal=Genes Dev. |volume=2 |issue= 12A |pages= 1557-69 |year= 1989 |pmid= 3063603 |doi=  }}
*{{cite journal  | author=Bauer R, Imhof A, Pscherer A, ''et al.'' |title=The genomic structure of the human AP-2 transcription factor. |journal=Nucleic Acids Res. |volume=22 |issue= 8 |pages= 1413-20 |year= 1994 |pmid= 8190633 |doi=  }}
*{{cite journal  | author=Buettner R, Kannan P, Imhof A, ''et al.'' |title=An alternatively spliced mRNA from the AP-2 gene encodes a negative regulator of transcriptional activation by AP-2. |journal=Mol. Cell. Biol. |volume=13 |issue= 7 |pages= 4174-85 |year= 1993 |pmid= 8321221 |doi=  }}
*{{cite journal  | author=Williamson JA, Bosher JM, Skinner A, ''et al.'' |title=Chromosomal mapping of the human and mouse homologues of two new members of the AP-2 family of transcription factors. |journal=Genomics |volume=35 |issue= 1 |pages= 262-4 |year= 1996 |pmid= 8661133 |doi= 10.1006/geno.1996.0351 }}
*{{cite journal  | author=Pirozzi G, McConnell SJ, Uveges AJ, ''et al.'' |title=Identification of novel human WW domain-containing proteins by cloning of ligand targets. |journal=J. Biol. Chem. |volume=272 |issue= 23 |pages= 14611-6 |year= 1997 |pmid= 9169421 |doi=  }}
*{{cite journal  | author=Batsché E, Muchardt C, Behrens J, ''et al.'' |title=RB and c-Myc activate expression of the E-cadherin gene in epithelial cells through interaction with transcription factor AP-2. |journal=Mol. Cell. Biol. |volume=18 |issue= 7 |pages= 3647-58 |year= 1998 |pmid= 9632747 |doi=  }}
*{{cite journal  | author=Mertens PR, Alfonso-Jaume MA, Steinmann K, Lovett DH |title=A synergistic interaction of transcription factors AP2 and YB-1 regulates gelatinase A enhancer-dependent transcription. |journal=J. Biol. Chem. |volume=273 |issue= 49 |pages= 32957-65 |year= 1999 |pmid= 9830047 |doi=  }}
*{{cite journal  | author=García MA, Campillos M, Marina A, ''et al.'' |title=Transcription factor AP-2 activity is modulated by protein kinase A-mediated phosphorylation. |journal=FEBS Lett. |volume=444 |issue= 1 |pages= 27-31 |year= 1999 |pmid= 10037142 |doi=  }}
*{{cite journal  | author=Rosenthal JA, Chen H, Slepnev VI, ''et al.'' |title=The epsins define a family of proteins that interact with components of the clathrin coat and contain a new protein module. |journal=J. Biol. Chem. |volume=274 |issue= 48 |pages= 33959-65 |year= 1999 |pmid= 10567358 |doi=  }}
*{{cite journal  | author=Heicklen-Klein A, Ginzburg I |title=Tau promoter confers neuronal specificity and binds Sp1 and AP-2. |journal=J. Neurochem. |volume=75 |issue= 4 |pages= 1408-18 |year= 2000 |pmid= 10987820 |doi=  }}
*{{cite journal  | author=Nyormoi O, Wang Z, Doan D, ''et al.'' |title=Transcription factor AP-2alpha is preferentially cleaved by caspase 6 and degraded by proteasome during tumor necrosis factor alpha-induced apoptosis in breast cancer cells. |journal=Mol. Cell. Biol. |volume=21 |issue= 15 |pages= 4856-67 |year= 2001 |pmid= 11438643 |doi= 10.1128/MCB.21.15.4856-4867.2001 }}
*{{cite journal  | author=Rao DS, Chang JC, Kumar PD, ''et al.'' |title=Huntingtin interacting protein 1 Is a clathrin coat binding protein required for differentiation of late spermatogenic progenitors. |journal=Mol. Cell. Biol. |volume=21 |issue= 22 |pages= 7796-806 |year= 2001 |pmid= 11604514 |doi= 10.1128/MCB.21.22.7796-7806.2001 }}
*{{cite journal  | author=Bragança J, Swingler T, Marques FI, ''et al.'' |title=Human CREB-binding protein/p300-interacting transactivator with ED-rich tail (CITED) 4, a new member of the CITED family, functions as a co-activator for transcription factor AP-2. |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 8559-65 |year= 2002 |pmid= 11744733 |doi= 10.1074/jbc.M110850200 }}
*{{cite journal  | author=Mertens PR, Steinmann K, Alfonso-Jaume MA, ''et al.'' |title=Combinatorial interactions of p53, activating protein-2, and YB-1 with a single enhancer element regulate gelatinase A expression in neoplastic cells. |journal=J. Biol. Chem. |volume=277 |issue= 28 |pages= 24875-82 |year= 2002 |pmid= 11973333 |doi= 10.1074/jbc.M200445200 }}
*{{cite journal  | author=Eloranta JJ, Hurst HC |title=Transcription factor AP-2 interacts with the SUMO-conjugating enzyme UBC9 and is sumolated in vivo. |journal=J. Biol. Chem. |volume=277 |issue= 34 |pages= 30798-804 |year= 2002 |pmid= 12072434 |doi= 10.1074/jbc.M202780200 }}
*{{cite journal  | author=Ben-Zimra M, Koler M, Orly J |title=Transcription of cholesterol side-chain cleavage cytochrome P450 in the placenta: activating protein-2 assumes the role of steroidogenic factor-1 by binding to an overlapping promoter element. |journal=Mol. Endocrinol. |volume=16 |issue= 8 |pages= 1864-80 |year= 2003 |pmid= 12145340 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

TPM1

• INFO: Beginning work on TPM1... {November 15, 2007 7:36:56 PM PST}
• SEARCH REDIRECT: Control Box Found: TPM1 {November 15, 2007 7:37:35 PM PST}
• UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 15, 2007 7:37:36 PM PST}
• UPDATE SUMMARY: Updating Summary, No Errors. {November 15, 2007 7:37:36 PM PST}
• UPDATE CITATIONS: Updating Citations, No Errors. {November 15, 2007 7:37:36 PM PST}
• UPDATED: Updated protein page: TPM1 {November 15, 2007 7:37:43 PM PST}

TPM3

• INFO: Beginning work on TPM3... {November 15, 2007 7:37:43 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:38:36 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_TPM3_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 1mv4.
 | PDB = {{PDB2|1mv4}}, {{PDB2|2g9j}}, {{PDB2|2tma}}
 | Name = Tropomyosin 3
 | HGNCid = 12012
 | Symbol = TPM3
 | AltSymbols =; NEM1; TRK; FLJ41118; MGC14582; MGC3261; MGC72094; OK/SW-cl.5; TM-5; TM3; TM30; TM30nm; TPMsk3; hscp30
 | OMIM = 191030
 | ECnumber =  
 | Homologene = 77475
 | MGIid =  
 | Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0003779 |text = actin binding}} 
 | Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005862 |text = muscle thin filament tropomyosin}} 
 | Process = {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0006937 |text = regulation of muscle contraction}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7170
    | Hs_Ensembl = ENSG00000143549
    | Hs_RefseqProtein = NP_001036816
    | Hs_RefseqmRNA = NM_001043351
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 152395457
    | Hs_GenLoc_end = 152431233
    | Hs_Uniprot = P06753
    | Mm_EntrezGene =  
    | Mm_Ensembl =  
    | Mm_RefseqmRNA =  
    | Mm_RefseqProtein =  
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr =  
    | Mm_GenLoc_start =  
    | Mm_GenLoc_end =  
    | Mm_Uniprot =  
  }}
}}
'''Tropomyosin 3''', also known as '''TPM3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TPM3 tropomyosin 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7170| accessdate = }}</ref>

<!-- 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 tropomyosin family of actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosins are dimers of coiled-coil proteins that polymerize end-to-end along the major groove in most actin filaments. They provide stability to the filaments and regulate access of other actin-binding proteins. In muscle cells, they regulate muscle contraction by controlling the binding of myosin heads to the actin filament. Mutations in this gene result in autosomal dominant nemaline myopathy, and oncogenes formed by chromosomal translocations involving this locus are associated with cancer. Multiple transcript variants encoding different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: TPM3 tropomyosin 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7170| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Lees-Miller JP, Helfman DM |title=The molecular basis for tropomyosin isoform diversity. |journal=Bioessays |volume=13 |issue= 9 |pages= 429-37 |year= 1992 |pmid= 1796905 |doi= 10.1002/bies.950130902 }}
*{{cite journal  | author=Pittenger MF, Kazzaz JA, Helfman DM |title=Functional properties of non-muscle tropomyosin isoforms. |journal=Curr. Opin. Cell Biol. |volume=6 |issue= 1 |pages= 96-104 |year= 1994 |pmid= 8167032 |doi=  }}
*{{cite journal  | author=Gunning P, Weinberger R, Jeffrey P |title=Actin and tropomyosin isoforms in morphogenesis. |journal=Anat. Embryol. |volume=195 |issue= 4 |pages= 311-5 |year= 1997 |pmid= 9108196 |doi=  }}
*{{cite journal  | author=Gunning PW, Schevzov G, Kee AJ, Hardeman EC |title=Tropomyosin isoforms: divining rods for actin cytoskeleton function. |journal=Trends Cell Biol. |volume=15 |issue= 6 |pages= 333-41 |year= 2006 |pmid= 15953552 |doi= 10.1016/j.tcb.2005.04.007 }}
*{{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=Höner B, Shoeman RL, Traub P |title=Degradation of cytoskeletal proteins by the human immunodeficiency virus type 1 protease. |journal=Cell Biol. Int. Rep. |volume=16 |issue= 7 |pages= 603-12 |year= 1992 |pmid= 1516138 |doi=  }}
*{{cite journal  | author=Morris CM, Hao QL, Heisterkamp N, ''et al.'' |title=Localization of the TRK proto-oncogene to human chromosome bands 1q23-1q24. |journal=Oncogene |volume=6 |issue= 6 |pages= 1093-5 |year= 1991 |pmid= 1829807 |doi=  }}
*{{cite journal  | author=Winder SJ, Walsh MP |title=Smooth muscle calponin. Inhibition of actomyosin MgATPase and regulation by phosphorylation. |journal=J. Biol. Chem. |volume=265 |issue= 17 |pages= 10148-55 |year= 1990 |pmid= 2161834 |doi=  }}
*{{cite journal  | author=Takahashi K, Hiwada K, Kokubu T |title=Vascular smooth muscle calponin. A novel troponin T-like protein. |journal=Hypertension |volume=11 |issue= 6 Pt 2 |pages= 620-6 |year= 1988 |pmid= 2455687 |doi=  }}
*{{cite journal  | author=Coulier F, Martin-Zanca D, Ernst M, Barbacid M |title=Mechanism of activation of the human trk oncogene. |journal=Mol. Cell. Biol. |volume=9 |issue= 1 |pages= 15-23 |year= 1989 |pmid= 2538716 |doi=  }}
*{{cite journal  | author=Martin-Zanca D, Hughes SH, Barbacid M |title=A human oncogene formed by the fusion of truncated tropomyosin and protein tyrosine kinase sequences. |journal=Nature |volume=319 |issue= 6056 |pages= 743-8 |year= 1986 |pmid= 2869410 |doi= 10.1038/319743a0 }}
*{{cite journal  | author=Reinach FC, MacLeod AR |title=Tissue-specific expression of the human tropomyosin gene involved in the generation of the trk oncogene. |journal=Nature |volume=322 |issue= 6080 |pages= 648-50 |year= 1986 |pmid= 3018581 |doi= 10.1038/322648a0 }}
*{{cite journal  | author=MacLeod AR, Houlker C, Reinach FC, Talbot K |title=The mRNA and RNA-copy pseudogenes encoding TM30nm, a human cytoskeletal tropomyosin. |journal=Nucleic Acids Res. |volume=14 |issue= 21 |pages= 8413-26 |year= 1987 |pmid= 3024106 |doi=  }}
*{{cite journal  | author=Clayton L, Reinach FC, Chumbley GM, MacLeod AR |title=Organization of the hTMnm gene. Implications for the evolution of muscle and non-muscle tropomyosins. |journal=J. Mol. Biol. |volume=201 |issue= 3 |pages= 507-15 |year= 1988 |pmid= 3418707 |doi=  }}
*{{cite journal  | author=MacLeod AR, Houlker C, Reinach FC, ''et al.'' |title=A muscle-type tropomyosin in human fibroblasts: evidence for expression by an alternative RNA splicing mechanism. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 23 |pages= 7835-9 |year= 1986 |pmid= 3865200 |doi=  }}
*{{cite journal  | author=Butti MG, Bongarzone I, Ferraresi G, ''et al.'' |title=A sequence analysis of the genomic regions involved in the rearrangements between TPM3 and NTRK1 genes producing TRK oncogenes in papillary thyroid carcinomas. |journal=Genomics |volume=28 |issue= 1 |pages= 15-24 |year= 1995 |pmid= 7590742 |doi= 10.1006/geno.1995.1100 }}
*{{cite journal  | author=Laing NG, Wilton SD, Akkari PA, ''et al.'' |title=A mutation in the alpha tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy NEM1. |journal=Nat. Genet. |volume=10 |issue= 2 |pages= 249 |year= 1995 |pmid= 7663526 |doi= 10.1038/ng0695-249 }}
*{{cite journal  | author=Laing NG, Wilton SD, Akkari PA, ''et al.'' |title=A mutation in the alpha tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy. |journal=Nat. Genet. |volume=9 |issue= 1 |pages= 75-9 |year= 1995 |pmid= 7704029 |doi= 10.1038/ng0195-75 }}
*{{cite journal  | author=Wilton SD, Eyre H, Akkari PA, ''et al.'' |title=Assignment of the human a-tropomyosin gene TPM3 to 1q22-->q23 by fluorescence in situ hybridisation. |journal=Cytogenet. Cell Genet. |volume=68 |issue= 1-2 |pages= 122-4 |year= 1994 |pmid= 7956350 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

TPO

• INFO: Beginning work on TPO... {November 15, 2007 7:38:36 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:38:56 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 = Thyroid peroxidase
 | HGNCid = 12015
 | Symbol = TPO
 | AltSymbols =; MSA; TPX
 | OMIM = 606765
 | ECnumber =  
 | Homologene = 461
 | MGIid = 98813
 | GeneAtlas_image1 = PBB_GE_TPO_210342_s_at_tn.png
 | Function = {{GNF_GO|id=GO:0004447 |text = iodide peroxidase activity}} {{GNF_GO|id=GO:0004601 |text = peroxidase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} 
 | Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} 
 | Process = {{GNF_GO|id=GO:0006590 |text = thyroid hormone generation}} {{GNF_GO|id=GO:0006979 |text = response to oxidative stress}} {{GNF_GO|id=GO:0042446 |text = hormone biosynthetic process}} {{GNF_GO|id=GO:0042744 |text = hydrogen peroxide catabolic process}} 
 | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7173
    | Hs_Ensembl = ENSG00000115705
    | Hs_RefseqProtein = NP_000538
    | Hs_RefseqmRNA = NM_000547
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 2
    | Hs_GenLoc_start = 1396240
    | Hs_GenLoc_end = 1525506
    | Hs_Uniprot = P07202
    | Mm_EntrezGene = 22018
    | Mm_Ensembl = ENSMUSG00000020673
    | Mm_RefseqmRNA = XM_975183
    | Mm_RefseqProtein = XP_980277
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 12
    | Mm_GenLoc_start = 30640711
    | Mm_GenLoc_end = 30718661
    | Mm_Uniprot = Q4FZJ9
  }}
}}
'''Thyroid peroxidase''', also known as '''TPO''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TPO thyroid peroxidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7173| accessdate = }}</ref>

<!-- 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 membrane-bound glycoprotein. The encoded protein acts as an enzyme and plays a central role in thyroid gland function. The protein functions in the iodination of tyrosine residues in thyroglobulin and phenoxy-ester formation between pairs of iodinated tyrosines to generate the thyroid hormones, thyroxine and triiodothyronine. Mutations in this gene are associated with several disorders of thyroid hormonogenesis, including congenital hypothyroidism, congenital goiter, and thyroid hormone organification defect IIA. Multiple transcript variants encoding distinct isoforms have been identified for this gene. Additional splice variants have been described but their biological natures have not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: TPO thyroid peroxidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7173| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Asakawa H |title=[Thyroid peroxidase (TPO) gene and pathogenic TPO mutation] |journal=Nippon Rinsho |volume=52 |issue= 4 |pages= 864-8 |year= 1994 |pmid= 8196171 |doi=  }}
*{{cite journal  | author=Abramowicz MJ, Targovnik HM, Varela V, ''et al.'' |title=Identification of a mutation in the coding sequence of the human thyroid peroxidase gene causing congenital goiter. |journal=J. Clin. Invest. |volume=90 |issue= 4 |pages= 1200-4 |year= 1992 |pmid= 1401057 |doi=  }}
*{{cite journal  | author=Barnett PS, Banga JP, Watkins J, ''et al.'' |title=Nucleotide sequence of the alternatively spliced human thyroid peroxidase cDNA, TPO-2. |journal=Nucleic Acids Res. |volume=18 |issue= 3 |pages= 670 |year= 1990 |pmid= 2308857 |doi=  }}
*{{cite journal  | author=Zanelli E, Henry M, Charvet B, Malthièry Y |title=Evidence for an alternate splicing in the thyroperoxidase messenger from patients with Graves' disease. |journal=Biochem. Biophys. Res. Commun. |volume=170 |issue= 2 |pages= 735-41 |year= 1990 |pmid= 2383265 |doi=  }}
*{{cite journal  | author=Kimura S, Hong YS, Kotani T, ''et al.'' |title=Structure of the human thyroid peroxidase gene: comparison and relationship to the human myeloperoxidase gene. |journal=Biochemistry |volume=28 |issue= 10 |pages= 4481-9 |year= 1989 |pmid= 2548579 |doi=  }}
*{{cite journal  | author=Magnusson RP, Chazenbalk GD, Gestautas J, ''et al.'' |title=Molecular cloning of the complementary deoxyribonucleic acid for human thyroid peroxidase. |journal=Mol. Endocrinol. |volume=1 |issue= 11 |pages= 856-61 |year= 1990 |pmid= 3153466 |doi=  }}
*{{cite journal  | author=Libert F, Ruel J, Ludgate M, ''et al.'' |title=Complete nucleotide sequence of the human thyroperoxidase-microsomal antigen cDNA. |journal=Nucleic Acids Res. |volume=15 |issue= 16 |pages= 6735 |year= 1987 |pmid= 3453124 |doi=  }}
*{{cite journal  | author=Kimura S, Kotani T, McBride OW, ''et al.'' |title=Human thyroid peroxidase: complete cDNA and protein sequence, chromosome mapping, and identification of two alternately spliced mRNAs. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 16 |pages= 5555-9 |year= 1987 |pmid= 3475693 |doi=  }}
*{{cite journal  | author=Seto P, Hirayu H, Magnusson RP, ''et al.'' |title=Isolation of a complementary DNA clone for thyroid microsomal antigen. Homology with the gene for thyroid peroxidase. |journal=J. Clin. Invest. |volume=80 |issue= 4 |pages= 1205-8 |year= 1987 |pmid= 3654979 |doi=  }}
*{{cite journal  | author=Bikker H, Vulsma T, Baas F, de Vijlder JJ |title=Identification of five novel inactivating mutations in the human thyroid peroxidase gene by denaturing gradient gel electrophoresis. |journal=Hum. Mutat. |volume=6 |issue= 1 |pages= 9-16 |year= 1995 |pmid= 7550241 |doi= 10.1002/humu.1380060104 }}
*{{cite journal  | author=Endo Y, Onogi S, Umeki K, ''et al.'' |title=Regional localization of the gene for thyroid peroxidase to human chromosome 2p25 and mouse chromosome 12C. |journal=Genomics |volume=25 |issue= 3 |pages= 760-1 |year= 1995 |pmid= 7759120 |doi=  }}
*{{cite journal  | author=Bikker H, den Hartog MT, Baas F, ''et al.'' |title=A 20-basepair duplication in the human thyroid peroxidase gene results in a total iodide organification defect and congenital hypothyroidism. |journal=J. Clin. Endocrinol. Metab. |volume=79 |issue= 1 |pages= 248-52 |year= 1994 |pmid= 8027236 |doi=  }}
*{{cite journal  | author=Bikker H, Waelkens JJ, Bravenboer B, de Vijlder JJ |title=Congenital hypothyroidism caused by a premature termination signal in exon 10 of the human thyroid peroxidase gene. |journal=J. Clin. Endocrinol. Metab. |volume=81 |issue= 6 |pages= 2076-9 |year= 1996 |pmid= 8964831 |doi=  }}
*{{cite journal  | author=Bikker H, Baas F, De Vijlder JJ |title=Molecular analysis of mutated thyroid peroxidase detected in patients with total iodide organification defects. |journal=J. Clin. Endocrinol. Metab. |volume=82 |issue= 2 |pages= 649-53 |year= 1997 |pmid= 9024270 |doi=  }}
*{{cite journal  | author=Medeiros-Neto G, Gil-Da-Costa MJ, Santos CL, ''et al.'' |title=Metastatic thyroid carcinoma arising from congenital goiter due to mutation in the thyroperoxidase gene. |journal=J. Clin. Endocrinol. Metab. |volume=83 |issue= 11 |pages= 4162-6 |year= 1998 |pmid= 9814507 |doi=  }}
*{{cite journal  | author=Kotani T, Umeki K, Yamamoto I, ''et al.'' |title=A novel mutation in the human thyroid peroxidase gene resulting in a total iodide organification defect. |journal=J. Endocrinol. |volume=160 |issue= 2 |pages= 267-73 |year= 1999 |pmid= 9924196 |doi=  }}
*{{cite journal  | author=Pannain S, Weiss RE, Jackson CE, ''et al.'' |title=Two different mutations in the thyroid peroxidase gene of a large inbred Amish kindred: power and limits of homozygosity mapping. |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 3 |pages= 1061-71 |year= 1999 |pmid= 10084596 |doi=  }}
*{{cite journal  | author=Santos CL, Bikker H, Rego KG, ''et al.'' |title=A novel mutation in the TPO gene in goitrous hypothyroid patients with iodide organification defect. |journal=Clin. Endocrinol. (Oxf) |volume=51 |issue= 2 |pages= 165-72 |year= 2000 |pmid= 10468986 |doi=  }}
*{{cite journal  | author=Lazar V, Bidart JM, Caillou B, ''et al.'' |title=Expression of the Na+/I- symporter gene in human thyroid tumors: a comparison study with other thyroid-specific genes. |journal=J. Clin. Endocrinol. Metab. |volume=84 |issue= 9 |pages= 3228-34 |year= 1999 |pmid= 10487692 |doi=  }}
}}
{{refend}}

{{protein-stub}}
 

YES1

• INFO: Beginning work on YES1... {November 15, 2007 7:38:56 PM PST}
• AMBIGUITY: Did not locate an acceptable page to update. {November 15, 2007 7:39:19 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_YES1_image.jpg
 | image_source = [[Protein_Data_Bank|PDB]] rendering based on 2hda.
 | PDB = {{PDB2|2hda}}, {{PDB2|2hwo}}, {{PDB2|2hwp}}, {{PDB2|2oiq}}
 | Name = V-yes-1 Yamaguchi sarcoma viral oncogene homolog 1
 | HGNCid = 12841
 | Symbol = YES1
 | AltSymbols =; HsT441; P61-YES; Yes; c-yes
 | OMIM = 164880
 | ECnumber =  
 | Homologene = 55900
 | MGIid = 99147
 | GeneAtlas_image1 = PBB_GE_YES1_202933_s_at_tn.png
 | GeneAtlas_image2 = PBB_GE_YES1_202932_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:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} 
 | Component = 
 | 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 = 7525
    | Hs_Ensembl = ENSG00000176105
    | Hs_RefseqProtein = NP_005424
    | Hs_RefseqmRNA = NM_005433
    | Hs_GenLoc_db =  
    | Hs_GenLoc_chr = 18
    | Hs_GenLoc_start = 711747
    | Hs_GenLoc_end = 802547
    | Hs_Uniprot = P07947
    | Mm_EntrezGene = 22612
    | Mm_Ensembl = ENSMUSG00000014932
    | Mm_RefseqmRNA = NM_009535
    | Mm_RefseqProtein = NP_033561
    | Mm_GenLoc_db =  
    | Mm_GenLoc_chr = 5
    | Mm_GenLoc_start = 32887814
    | Mm_GenLoc_end = 32963638
    | Mm_Uniprot = Q3TJI7
  }}
}}
'''V-yes-1 Yamaguchi sarcoma viral oncogene homolog 1''', also known as '''YES1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: YES1 v-yes-1 Yamaguchi sarcoma viral oncogene homolog 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7525| accessdate = }}</ref>

<!-- 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 the cellular homolog of the Yamaguchi sarcoma virus oncogene. The encoded protein has tyrosine kinase activity and belongs to the src family of proteins. This gene lies in close proximity to thymidylate synthase gene on chromosome 18, and a corresponding pseudogene has been found on chromosome 22.<ref name="entrez">{{cite web | title = Entrez Gene: YES1 v-yes-1 Yamaguchi sarcoma viral oncogene homolog 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7525| accessdate = }}</ref>
}}

==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Brickell PM |title=The p60c-src family of protein-tyrosine kinases: structure, regulation, and function. |journal=Critical reviews in oncogenesis |volume=3 |issue= 4 |pages= 401-46 |year= 1992 |pmid= 1384720 |doi=  }}
*{{cite journal  | author=Toyoshima K, Semba K, Nishizawa M, ''et al.'' |title=Nakahara memorial lecture. Non-receptor type protein-tyrosine kinases closely related to src and yes compose a multigene family. |journal=Int. Symp. Princess Takamatsu Cancer Res. Fund |volume=17 |issue=  |pages= 11-20 |year= 1988 |pmid= 3332005 |doi=  }}
*{{cite journal  | author=Sudol M, Chen HI, Bougeret C, ''et al.'' |title=Characterization of a novel protein-binding module--the WW domain. |journal=FEBS Lett. |volume=369 |issue= 1 |pages= 67-71 |year= 1995 |pmid= 7641887 |doi=  }}
*{{cite journal  | author=Summy JM, Sudol M, Eck MJ, ''et al.'' |title=Specificity in signaling by c-Yes. |journal=Front. Biosci. |volume=8 |issue=  |pages= s185-205 |year= 2004 |pmid= 12456296 |doi=  }}
*{{cite journal  | author=Cichowski K, McCormick F, Brugge JS |title=p21rasGAP association with Fyn, Lyn, and Yes in thrombin-activated platelets. |journal=J. Biol. Chem. |volume=267 |issue= 8 |pages= 5025-8 |year= 1992 |pmid= 1544885 |doi=  }}
*{{cite journal  | author=Huang MM, Bolen JB, Barnwell JW, ''et al.'' |title=Membrane glycoprotein IV (CD36) is physically associated with the Fyn, Lyn, and Yes protein-tyrosine kinases in human platelets. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 17 |pages= 7844-8 |year= 1991 |pmid= 1715582 |doi=  }}
*{{cite journal  | author=Holtrich U, Bräuninger A, Strebhardt K, Rübsamen-Waigmann H |title=Two additional protein-tyrosine kinases expressed in human lung: fourth member of the fibroblast growth factor receptor family and an intracellular protein-tyrosine kinase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 23 |pages= 10411-5 |year= 1992 |pmid= 1720539 |doi=  }}
*{{cite journal  | author=Krueger J, Zhao YH, Murphy D, Sudol M |title=Differential expression of p62c-yes in normal, hyperplastic and neoplastic human epidermis. |journal=Oncogene |volume=6 |issue= 6 |pages= 933-40 |year= 1991 |pmid= 2067846 |doi=  }}
*{{cite journal  | author=Zhao YH, Krueger JG, Sudol M |title=Expression of cellular-yes protein in mammalian tissues. |journal=Oncogene |volume=5 |issue= 11 |pages= 1629-35 |year= 1991 |pmid= 2267131 |doi=  }}
*{{cite journal  | author=Sukegawa J, Semba K, Yamanashi Y, ''et al.'' |title=Characterization of cDNA clones for the human c-yes gene. |journal=Mol. Cell. Biol. |volume=7 |issue= 1 |pages= 41-7 |year= 1987 |pmid= 2436037 |doi=  }}
*{{cite journal  | author=Semba K, Yamanashi Y, Nishizawa M, ''et al.'' |title=Location of the c-yes gene on the human chromosome and its expression in various tissues. |journal=Science |volume=227 |issue= 4690 |pages= 1038-40 |year= 1985 |pmid= 2983418 |doi=  }}
*{{cite journal  | author=Bull HA, Brickell PM, Dowd PM |title=Src-related protein tyrosine kinases are physically associated with the surface antigen CD36 in human dermal microvascular endothelial cells. |journal=FEBS Lett. |volume=351 |issue= 1 |pages= 41-4 |year= 1994 |pmid= 7521304 |doi=  }}
*{{cite journal  | author=Toshima J, Ohashi K, Iwashita S, Mizuno K |title=Autophosphorylation activity and association with Src family kinase of Sky receptor tyrosine kinase. |journal=Biochem. Biophys. Res. Commun. |volume=209 |issue= 2 |pages= 656-63 |year= 1995 |pmid= 7537495 |doi= 10.1006/bbrc.1995.1549 }}
*{{cite journal  | author=Courtneidge SA, Dhand R, Pilat D, ''et al.'' |title=Activation of Src family kinases by colony stimulating factor-1, and their association with its receptor. |journal=EMBO J. |volume=12 |issue= 3 |pages= 943-50 |year= 1993 |pmid= 7681396 |doi=  }}
*{{cite journal  | author=Mori S, Rönnstrand L, Yokote K, ''et al.'' |title=Identification of two juxtamembrane autophosphorylation sites in the PDGF beta-receptor; involvement in the interaction with Src family tyrosine kinases. |journal=EMBO J. |volume=12 |issue= 6 |pages= 2257-64 |year= 1993 |pmid= 7685273 |doi=  }}
*{{cite journal  | author=Waltenberger J, Claesson-Welsh L, Siegbahn A, ''et al.'' |title=Different signal transduction properties of KDR and Flt1, two receptors for vascular endothelial growth factor. |journal=J. Biol. Chem. |volume=269 |issue= 43 |pages= 26988-95 |year= 1994 |pmid= 7929439 |doi=  }}
*{{cite journal  | author=Silverman GA, Kuo WL, Taillon-Miller P, Gray JW |title=Chromosomal reassignment: YACs containing both YES1 and thymidylate synthase map to the short arm of chromosome 18. |journal=Genomics |volume=15 |issue= 2 |pages= 442-5 |year= 1993 |pmid= 8449516 |doi= 10.1006/geno.1993.1086 }}
}}
{{refend}}

{{protein-stub}}
 

end log.