Ubiquitin A-52 residue ribosomal protein fusion product 1

UBA52
	Gene ontology
Molecular function	structural constituent of ribosome; protein binding; protein tag; ubiquitin protein ligase binding;
Cellular component	cytoplasm; endocytic vesicle membrane; nucleus; ribosome; extracellular exosome; endosome membrane; lysosomal membrane; extracellular space; nucleoplasm; mitochondrial outer membrane; endoplasmic reticulum; cytosol; plasma membrane; endoplasmic reticulum quality control compartment; vesicle; endoplasmic reticulum membrane; host cell; cytosolic large ribosomal subunit; cytosolic small ribosomal subunit; synapse;
Biological process	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; negative regulation of epidermal growth factor receptor signaling pathway; interstrand cross-link repair; nucleotide-excision repair, DNA damage recognition; positive regulation of canonical Wnt signaling pathway; tumor necrosis factor-mediated signaling pathway; regulation of type I interferon production; TRIF-dependent toll-like receptor signaling pathway; Fc-epsilon receptor signaling pathway; endosomal transport; global genome nucleotide-excision repair; NIK/NF-kappaB signaling; G2/M transition of mitotic cell cycle; stress-activated MAPK cascade; transforming growth factor beta receptor signaling pathway; macroautophagy; negative regulation of canonical Wnt signaling pathway; nucleotide-excision repair, DNA gap filling; viral transcription; error-free translesion synthesis; regulation of tumor necrosis factor-mediated signaling pathway; stimulatory C-type lectin receptor signaling pathway; negative regulation of transforming growth factor beta receptor signaling pathway; SRP-dependent cotranslational protein targeting to membrane; JNK cascade; regulation of transcription from RNA polymerase II promoter in response to hypoxia; nucleotide-excision repair, DNA incision; I-kappaB kinase/NF-kappaB signaling; innate immune response; Notch signaling pathway; regulation of mRNA stability; protein polyubiquitination; negative regulation of apoptotic process; negative regulation of transcription by RNA polymerase II; virion assembly; positive regulation of NF-kappaB transcription factor activity; anaphase-promoting complex-dependent catabolic process; negative regulation of type I interferon production; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; nucleotide-binding oligomerization domain containing signaling pathway; intracellular transport of virus; viral life cycle; MyD88-dependent toll-like receptor signaling pathway; error-prone translesion synthesis; MAPK cascade; fibroblast growth factor receptor signaling pathway; ion transmembrane transport; glycogen biosynthetic process; positive regulation of apoptotic process; translational initiation; positive regulation of I-kappaB kinase/NF-kappaB signaling; translesion synthesis; transcription-coupled nucleotide-excision repair; T cell receptor signaling pathway; MyD88-independent toll-like receptor signaling pathway; positive regulation of transcription by RNA polymerase II; positive regulation of epidermal growth factor receptor signaling pathway; proteasome-mediated ubiquitin-dependent protein catabolic process; regulation of signal transduction by p53 class mediator; Wnt signaling pathway, planar cell polarity pathway; nucleotide-excision repair, DNA incision, 5'-to lesion; protein biosynthesis; nucleotide-excision repair, preincision complex assembly; rRNA processing; Wnt signaling pathway; ERBB2 signaling pathway; nucleotide-excision repair, DNA duplex unwinding; protein folding; negative regulation of G2/M transition of mitotic cell cycle; protein ubiquitination; protein deubiquitination; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; entry of bacterium into host cell; transmembrane transport; regulation of necroptotic process; membrane organization; endoplasmic reticulum mannose trimming; cellular iron ion homeostasis; regulation of hematopoietic stem cell differentiation; protein targeting to peroxisome; cytokine-mediated signaling pathway; modification-dependent protein catabolic process; interleukin-1-mediated signaling pathway; response to insecticide;
	Sources:Amigo / QuickGO

Ensembl


ENSG00000221983


n/a

UniProt


P62987


n/a

RefSeq (mRNA)

NM_001033930 NM_003333 NM_001321017 NM_001321018 NM_001321019
NM_001321020 NM_001321021 NM_001321022


n/a

RefSeq (protein)

NP_001029102 NP_001307946 NP_001307947 NP_001307948 NP_001307949
NP_001307950 NP_001307951 NP_003324


n/a

Location (UCSC)

Chr 19: 18.57 – 18.58 Mb

n/a

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

60S ribosomal protein L40 (RPL40) is a protein that in humans is encoded by the UBA52 gene.^[4]^[5]

Function

processed pseudogenes derived from this gene are present in the genome.^[5]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000221983 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
PMID 8188300
.

^ ^a ^b "Entrez Gene: UBA52 ubiquitin A-52 residue ribosomal protein fusion product 1".

Further reading

Wool IG, Chan YL, Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochem. Cell Biol. 73 (11–12): 933–47.
PMID 8722009
.

Murphey RK, Godenschwege TA (2002). "New roles for ubiquitin in the assembly and function of neuronal circuits". Neuron. 36 (1): 5–8.
S2CID 15764136
.

Baker RT, Board PG (1992). "The human ubiquitin/52-residue ribosomal protein fusion gene subfamily (UbA52) is composed primarily of processed pseudogenes". Genomics. 14 (2): 520–2.
PMID 1330885
.

Baker RT, Board PG (1991). "The human ubiquitin-52 amino acid fusion protein gene shares several structural features with mammalian ribosomal protein genes". Nucleic Acids Res. 19 (5): 1035–40.
PMID 1850507
.

Monia BP, Ecker DJ, Jonnalagadda S, et al. (1989). "Gene synthesis, expression, and processing of human ubiquitin carboxyl extension proteins". J. Biol. Chem. 264 (7): 4093–103.
PMID 2537304
.

Lund PK, Moats-Staats BM, Simmons JG, et al. (1985). "Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor". J. Biol. Chem. 260 (12): 7609–13.
PMID 2581967
.

Salvesen G, Lloyd C, Farley D (1987). "cDNA encoding a human homolog of yeast ubiquitin 1". Nucleic Acids Res. 15 (13): 5485.
PMID 3037496
.

Cross SH, Charlton JA, Nan X, Bird AP (1994). "Purification of CpG islands using a methylated DNA binding column". Nat. Genet. 6 (3): 236–44.
S2CID 12847618
.

Cook WJ, Jeffrey LC, Kasperek E, Pickart CM (1994). "Structure of tetraubiquitin shows how multiubiquitin chains can be formed". J. Mol. Biol. 236 (2): 601–9.
PMID 8107144
.

Vadlamudi RK, Joung I, Strominger JL, Shin J (1996). "p62, a phosphotyrosine-independent ligand of the SH2 domain of p56lck, belongs to a new class of ubiquitin-binding proteins". J. Biol. Chem. 271 (34): 20235–7.
PMID 8702753
.

Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806.
PMID 8889548
.

Kenmochi N, Kawaguchi T, Rozen S, et al. (1998). "A map of 75 human ribosomal protein genes". Genome Res. 8 (5): 509–23.
PMID 9582194
.

Cruz C, Ventura F, Bartrons R, Rosa JL (2001). "HERC3 binding to and regulation by ubiquitin". FEBS Lett. 488 (1–2): 74–80.
S2CID 20091003
.

Lee TA, Tyers M (2002). "Ubiquitin junction, what's your function?". Genome Biol. 2 (10): REPORTS4025.
PMID 11597332
.

Yoshihama M, Uechi T, Asakawa S, et al. (2002). "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes". Genome Res. 12 (3): 379–90.
PMID 11875025
.

Bishop N, Horman A, Woodman P (2002). "Mammalian class E vps proteins recognize ubiquitin and act in the removal of endosomal protein-ubiquitin conjugates". J. Cell Biol. 157 (1): 91–101.
PMID 11916981
.

Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903.
PMID 12477932
.

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PDB gallery

1aar: STRUCTURE OF A DIUBIQUITIN CONJUGATE AND A MODEL FOR INTERACTION WITH UBIQUITIN CONJUGATING ENZYME (E2)

1cmx: STRUCTURAL BASIS FOR THE SPECIFICITY OF UBIQUITIN C-TERMINAL HYDROLASES

1d3z: UBIQUITIN NMR STRUCTURE

1f9j: STRUCTURE OF A NEW CRYSTAL FORM OF TETRAUBIQUITIN

1fxt: STRUCTURE OF A CONJUGATING ENZYME-UBIQUITIN THIOLESTER COMPLEX

1g6j: STRUCTURE OF RECOMBINANT HUMAN UBIQUITIN IN AOT REVERSE MICELLES

1gjz: SOLUTION STRUCTURE OF A DIMERIC N-TERMINAL FRAGMENT OF HUMAN UBIQUITIN

1nbf: Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde

1ogw: SYNTHETIC UBIQUITIN WITH FLUORO-LEU AT 50 AND 67

1otr: Solution Structure of a CUE-Ubiquitin Complex

1p3q: Mechanism of Ubiquitin Recognition by the CUE Domain of VPS9

1q0w: Solution structure of Vps27 amino-terminal UIM-ubiquitin complex

1q5w: Ubiquitin Recognition by Npl4 Zinc-Fingers

1s1q: TSG101(UEV) domain in complex with Ubiquitin

1sif: Crystal structure of a multiple hydrophobic core mutant of ubiquitin

1tbe: STRUCTURE OF TETRAUBIQUITIN SHOWS HOW MULTIUBIQUITIN CHAINS CAN BE FORMED

1ubi: SYNTHETIC STRUCTURAL AND BIOLOGICAL STUDIES OF THE UBIQUITIN SYSTEM. PART 1

1ubq: STRUCTURE OF UBIQUITIN REFINED AT 1.8 ANGSTROMS RESOLUTION

1ud7: SOLUTION STRUCTURE OF THE DESIGNED HYDROPHOBIC CORE MUTANT OF UBIQUITIN, 1D7

1uzx: A COMPLEX OF THE VPS23 UEV WITH UBIQUITIN

1v80: Solution structures of ubiquitin at 30 bar and 3 kbar

1v81: Solution structures of ubiquitin at 30 bar and 3 kbar

1wr1: The complex structure of Dsk2p UBA with ubiquitin

1wr6: Crystal structure of GGA3 GAT domain in complex with ubiquitin

1wrd: Crystal structure of Tom1 GAT domain in complex with ubiquitin

1xd3: Crystal structure of UCHL3-UbVME complex

1xqq: Simultaneous determination of protein structure and dynamics

1yd8: COMPLEX OF HUMAN GGA3 GAT DOMAIN AND UBIQUITIN

1yiw: X-ray Crystal Structure of a Chemically Synthesized Ubiquitin

1yj1: X-ray Crystal Structure of a Chemically Synthesized [D-Gln35]Ubiquitin

1yx5: Solution Structure of S5a UIM-1/Ubiquitin Complex

1yx6: Solution Structure of S5a UIM-2/Ubiquitin Complex

1zgu: Solution structure of the human Mms2-Ubiquitin complex

2ayo: Structure of USP14 bound to ubquitin aldehyde

2bgf: NMR STRUCTURE OF LYS48-LINKED DI-UBIQUITIN USING CHEMICAL SHIFT PERTURBATION DATA TOGETHER WITH RDCS AND 15N-RELAXATION DATA

2c7m: HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN

2c7n: HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN

2d3g: Double sided ubiquitin binding of Hrs-UIM

2den: Solution Structure of the Ubiquitin-Associated Domain of Human BMSC-UbP and its Complex with Ubiquitin

2dx5: The complex structure between the mouse EAP45-GLUE domain and ubiquitin

2fcm: X-ray Crystal Structure of a Chemically Synthesized [D-Gln35]Ubiquitin with a Cubic Space Group

2fcn: X-ray Crystal Structure of a Chemically Synthesized [D-Val35]Ubiquitin with a Cubic Space Group

2fcq: X-ray Crystal Structure of a Chemically Synthesized Ubiquitin with a Cubic Space Group

2fcs: X-ray Crystal Structure of a Chemically Synthesized [L-Gln35]Ubiquitin with a Cubic Space Group

2fid: Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin

2fif: Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin

2fuh: Solution Structure of the UbcH5c/Ub Non-covalent Complex

2g3q: Solution Structure of Ede1 UBA-ubiquitin complex

2g45: Co-crystal structure of znf ubp domain from the deubiquitinating enzyme isopeptidase T (isot) in complex with ubiquitin

2gbj: Crystal Structure of the 9-10 8 Glycine Insertion Mutant of Ubiquitin.

2gbk: Crystal Structure of the 9-10 MoaD Insertion Mutant of Ubiquitin

2gbm: Crystal Structure of the 35-36 8 Glycine Insertion Mutant of Ubiquitin

2gbn: Crystal Structure of the 35-36 8 Glycine Insertion Mutant of Ubiquitin

2gbr: Crystal Structure of the 35-36 MoaD Insertion Mutant of Ubiquitin

2gmi: Mms2/Ubc13~Ubiquitin

2hd5: USP2 in complex with ubiquitin

2hth: Structural basis for ubiquitin recognition by the human EAP45/ESCRT-II GLUE domain

2ibi: Covalent Ubiquitin-USP2 Complex

2j7q: CRYSTAL STRUCTURE OF THE UBIQUITIN-SPECIFIC PROTEASE ENCODED BY MURINE CYTOMEGALOVIRUS TEGUMENT PROTEIN M48 IN COMPLEX WITH A UBQUITIN-BASED SUICIDE SUBSTRATE

2nr2: The MUMO (minimal under-restraining minimal over-restraining) method for the determination of native states ensembles of proteins

2o6v: Crystal structure and solution NMR studies of Lys48-linked tetraubiquitin at neutral pH

2oob: crystal structure of the UBA domain from Cbl-b ubiquitin ligase in complex with ubiquitin

This article on a gene on human chromosome 19 is a stub. You can help Wikipedia by expanding it.
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Retrieved from "https://en.wikipedia.org/w/index.php?title=Ubiquitin_A-52_residue_ribosomal_protein_fusion_product_1&oldid=1187260539"

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000221983 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8188300-4] PMID 8188300
.

[entrez-5] "Entrez Gene: UBA52 ubiquitin A-52 residue ribosomal protein fusion product 1".

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[5]