UBR5

Available structures

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]
Band	8q22.3	End	102,412,759 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 15 (mouse)^[2]

Band	15\|15 B3.1	Start	37,967,572 bp^[2]
Band	15\|15 B3.1	End	38,079,098 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

sural nerve

ganglionic eminence

Achilles tendon

gastric mucosa

skin of abdomen

secondary oocyte

right uterine tube

canal of the cervix

right lung

anterior pituitary

Top expressed in

saccule

spermatocyte

otic placode

spermatid

cumulus cell

testicle

seminiferous tubule

pituitary gland

ankle

superior colliculus

More reference expression data

BioGPS

n/a

Gene ontology
Molecular function	ubiquitin-protein transferase activity ubiquitin-ubiquitin ligase activity ubiquitin binding protein binding RNA binding zinc ion binding metal ion binding transferase activity ubiquitin protein ligase activity
Cellular component	nucleus nucleoplasm membrane cytosol perinuclear region of cytoplasm protein-containing 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 cell population proliferation DNA repair positive regulation of gene expression 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

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

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:

References

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. hdl:1885/64590. 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. S2CID 25909437.
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. Bibcode:2006PNAS..103.5391N. 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.

v t e PDB gallery
1i2t: X-RAY STRUCTURE OF THE HUMAN HYPERPLASTIC DISCS PROTEIN: AN ORTHOLOG OF THE C-TERMINAL DOMAIN OF POLY(A)-BINDING PROTEIN

Function

Interactions

References

Further reading

External links