UBR5

E3 ubiquitin-protein ligase UBR5 is an enzyme that in humans is encoded by the UBR5 gene.[5][6][7]

UBR5
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1I2T, 2QHO, 3PT3
Identifiers
Aliases	UBR5, DD5, EDD, EDD1, HYD, ubiquitin protein ligase E3 component n-recognin 5
External IDs	OMIM: 608413 MGI: 1918040 HomoloGene: 9295 GeneCards: UBR5
Gene location (Human) Chr. Chromosome 8 (human)[1] Band 8q22.3 Start 102,252,273 bp[1] End 102,412,759 bp[1]
Gene location (Mouse) Chr. Chromosome 15 (mouse)[2] Band 15|15 B3.1 Start 37,967,328 bp[2] End 38,078,854 bp[2]
Gene ontology Molecular function • ubiquitin-protein transferase activity • ubiquitin-ubiquitin ligase activity • ubiquitin binding • GO:0001948 protein binding • RNA binding • zinc ion binding • metal ion binding • transferase activity • GO:1904264, GO:1904822, GO:0090622, GO:0090302 ubiquitin protein ligase activity Cellular component • cell nucleus • nucleoplasm • membrane • cytosol • perinuclear region of cytoplasm • macromolecular complex Biological process • negative regulation of double-strand break repair • negative regulation of histone H2A K63-linked ubiquitination • protein polyubiquitination • progesterone receptor signaling pathway • cellular response to DNA damage stimulus • ubiquitin-dependent protein catabolic process • positive regulation of canonical Wnt signaling pathway • protein ubiquitination • cellular proliferation • DNA repair • positive regulation of gene expression • GO:0022415 viral process • protein K48-linked ubiquitination • positive regulation of protein import into nucleus Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	51366	70790
Ensembl	ENSG00000104517	ENSMUSG00000037487
UniProt	O95071	Q80TP3
RefSeq (mRNA)	NM_001282873 NM_015902	NM_001081359 NM_001112721 NM_027553
RefSeq (protein)	NP_001269802 NP_056986	NP_001074828 NP_001106192
Location (UCSC)	Chr 8: 102.25 – 102.41 Mb	Chr 15: 37.97 – 38.08 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

This gene encodes a progestin-induced protein, which belongs to the HECT (homology to E6-AP carboxyl terminus) family. The HECT family proteins function as E3 ubiquitin-protein ligases, targeting specific proteins for ubiquitin-mediated proteolysis. This gene is localized to chromosome 8q22 which is disrupted in a variety of cancers. This gene potentially has a role in regulation of cell proliferation or differentiation.[7]

Interactions

UBR5 has been shown to interact with:

• CIB1,[8]
• Karyopherin alpha 1,[8]
• MAPK1,[9] and
• TOPBP1.[10]

References

1. GRCh38: Ensembl release 89: ENSG00000104517 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000037487 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Callaghan MJ, Russell AJ, Woollatt E, Sutherland GR, Sutherland RL, Watts CK (Mar 1999). "Identification of a human HECT family protein with homology to the Drosophila tumor suppressor gene hyperplastic discs". Oncogene. 17 (26): 3479–91. doi:10.1038/sj.onc.1202249. PMID 10030672.
6. Tasaki T, Mulder LC, Iwamatsu A, Lee MJ, Davydov IV, Varshavsky A, Muesing M, Kwon YT (Aug 2005). "A Family of Mammalian E3 Ubiquitin Ligases That Contain the UBR Box Motif and Recognize N-Degrons". Mol Cell Biol. 25 (16): 7120–36. doi:10.1128/MCB.25.16.7120-7136.2005. PMC 1190250. PMID 16055722.
7. "Entrez Gene: EDD1 E3 ubiquitin protein ligase, HECT domain containing, 1".
8. Henderson MJ, Russell AJ, Hird S, Muñoz M, Clancy JL, Lehrbach GM, Calanni ST, Jans DA, Sutherland RL, Watts CK (Jul 2002). "EDD, the human hyperplastic discs protein, has a role in progesterone receptor coactivation and potential involvement in DNA damage response". J. Biol. Chem. 277 (29): 26468–78. doi:10.1074/jbc.M203527200. PMID 12011095.
9. Eblen ST, Kumar NV, Shah K, Henderson MJ, Watts CK, Shokat KM, Weber MJ (Apr 2003). "Identification of novel ERK2 substrates through use of an engineered kinase and ATP analogs". J. Biol. Chem. 278 (17): 14926–35. doi:10.1074/jbc.M300485200. PMID 12594221.
10. Honda Y, Tojo M, Matsuzaki K, Anan T, Matsumoto M, Ando M, Saya H, Nakao M (Feb 2002). "Cooperation of HECT-domain ubiquitin ligase hHYD and DNA topoisomerase II-binding protein for DNA damage response". J. Biol. Chem. 277 (5): 3599–605. doi:10.1074/jbc.M104347200. PMID 11714696.

Further reading

• Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T (2003). "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones". DNA Res. 9 (3): 99–106. doi:10.1093/dnares/9.3.99. PMID 12168954.
• Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O (1999). "Prediction of the coding sequences of unidentified human genes. XII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro". DNA Res. 5 (6): 355–64. doi:10.1093/dnares/5.6.355. PMID 10048485.
• Deo RC, Sonenberg N, Burley SK (2001). "X-ray structure of the human hyperplastic discs protein: An ortholog of the C-terminal domain of poly(A)-binding protein". Proc. Natl. Acad. Sci. U.S.A. 98 (8): 4414–9. doi:10.1073/pnas.071552198. PMC 31849. PMID 11287654.
• Honda Y, Tojo M, Matsuzaki K, Anan T, Matsumoto M, Ando M, Saya H, Nakao M (2002). "Cooperation of HECT-domain ubiquitin ligase hHYD and DNA topoisomerase II-binding protein for DNA damage response". J. Biol. Chem. 277 (5): 3599–605. doi:10.1074/jbc.M104347200. PMID 11714696.
• Henderson MJ, Russell AJ, Hird S, Muñoz M, Clancy JL, Lehrbach GM, Calanni ST, Jans DA, Sutherland RL, Watts CK (2002). "EDD, the human hyperplastic discs protein, has a role in progesterone receptor coactivation and potential involvement in DNA damage response". J. Biol. Chem. 277 (29): 26468–78. doi:10.1074/jbc.M203527200. PMID 12011095.
• Eblen ST, Kumar NV, Shah K, Henderson MJ, Watts CK, Shokat KM, Weber MJ (2003). "Identification of novel ERK2 substrates through use of an engineered kinase and ATP analogs". J. Biol. Chem. 278 (17): 14926–35. doi:10.1074/jbc.M300485200. PMID 12594221.
• Zhang C, Dowd DR, Staal A, Gu C, Lian JB, van Wijnen AJ, Stein GS, MacDonald PN (2003). "Nuclear coactivator-62 kDa/Ski-interacting protein is a nuclear matrix-associated coactivator that may couple vitamin D receptor-mediated transcription and RNA splicing". J. Biol. Chem. 278 (37): 35325–36. doi:10.1074/jbc.M305191200. PMID 12840015.
• Clancy JL, Henderson MJ, Russell AJ, Anderson DW, Bova RJ, Campbell IG, Choong DY, Macdonald GA, Mann GJ, Nolan T, Brady G, Olopade OI, Woollatt E, Davies MJ, Segara D, Hacker NF, Henshall SM, Sutherland RL, Watts CK (2003). "EDD, the human orthologue of the hyperplastic discs tumour suppressor gene, is amplified and overexpressed in cancer". Oncogene. 22 (32): 5070–81. doi:10.1038/sj.onc.1206775. PMID 12902990.
• Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (2004). "Functional Proteomics Mapping of a Human Signaling Pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
• Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455. S2CID 7200157.
• Kim JE, Tannenbaum SR, White FM (2005). "Global phosphoproteome of HT-29 human colon adenocarcinoma cells". J. Proteome Res. 4 (4): 1339–46. doi:10.1021/pr050048h. PMID 16083285.
• Nousiainen M, Silljé HH, Sauer G, Nigg EA, Körner R (2006). "Phosphoproteome analysis of the human mitotic spindle". Proc. Natl. Acad. Sci. U.S.A. 103 (14): 5391–6. doi:10.1073/pnas.0507066103. PMC 1459365. PMID 16565220.
• Henderson MJ, Munoz MA, Saunders DN, Clancy JL, Russell AJ, Williams B, Pappin D, Khanna KK, Jackson SP, Sutherland RL, Watts CK (2007). "EDD mediates DNA damage-induced activation of CHK2" (PDF). J. Biol. Chem. 281 (52): 39990–40000. doi:10.1074/jbc.M602818200. PMID 17074762. S2CID 25298222.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

External links

• Ubr5 : Protein Overview : UCSD-Nature Molecule Pages
• Overview of all the structural information available in the PDB for UniProt: O95071 (E3 ubiquitin-protein ligase UBR5) at the PDBe-KB.