UBR2

E3 ubiquitin-protein ligase UBR2 is an enzyme that in humans is encoded by the UBR2 gene.[5]

UBR2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3NY2, 3NY3
Identifiers
Aliases	UBR2, C6orf133, bA49A4.1, dJ242G1.1, dJ392M17.3, ubiquitin protein ligase E3 component n-recognin 2
External IDs	OMIM: 609134 MGI: 1861099 HomoloGene: 26151 GeneCards: UBR2
Gene location (Human) Chr. Chromosome 6 (human)[1] Band 6p21.1 Start 42,564,062 bp[1] End 42,693,504 bp[1]
Gene location (Mouse) Chr. Chromosome 17 (mouse)[2] Band 17|17 C Start 46,928,295 bp[2] End 47,010,556 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding • zinc ion binding • leucine binding • GO:1904264, GO:1904822, GO:0090622, GO:0090302 ubiquitin protein ligase activity • metal ion binding • ubiquitin-protein transferase activity • transferase activity Cellular component • chromatin • cell nucleus • ubiquitin ligase complex • cytoplasm • cytosol Biological process • cellular response to leucine • protein catabolic process • male meiosis I • ubiquitin-dependent protein catabolic process • protein ubiquitination • ubiquitin-dependent protein catabolic process via the N-end rule pathway • negative regulation of TOR signaling • chromatin silencing • histone H2A ubiquitination • protein polyubiquitination • reciprocal meiotic recombination • male meiotic nuclear division • spermatogenesis • negative regulation of transposition Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	23304	224826
Ensembl	ENSG00000024048	ENSMUSG00000023977
UniProt	Q8IWV8	Q6WKZ8
RefSeq (mRNA)	NM_001184801 NM_015255 NM_001363705	NM_001177374 NM_146078
RefSeq (protein)	NP_001171730 NP_056070 NP_001350634	NP_001170845 NP_666190
Location (UCSC)	Chr 6: 42.56 – 42.69 Mb	Chr 17: 46.93 – 47.01 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Proteolysis by the ubiquitin-proteasome system controls the concentration of many regulatory proteins. The selectivity of ubiquitylation is determined by ubiquitin E3 ligases, which recognize the substrate's destabilization signal, or degron. The E3 ligase UBR2 participates in the N-end rule pathway, which targets proteins bearing an N-terminal degron, or N-degron (Kwon et al., 2003).[supplied by OMIM][5]

References

1. GRCh38: Ensembl release 89: ENSG00000024048 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000023977 - 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. "Entrez Gene: UBR2 ubiquitin protein ligase E3 component n-recognin 2".

Further reading

• Nagase T, Ishikawa K, Nakajima D, et al. (1997). "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro". DNA Res. 4 (2): 141–50. doi:10.1093/dnares/4.2.141. PMID 9205841.
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Mungall AJ, Palmer SA, Sims SK, et al. (2003). "The DNA sequence and analysis of human chromosome 6". Nature. 425 (6960): 805–11. Bibcode:2003Natur.425..805M. doi:10.1038/nature02055. PMID 14574404.
• Kwon YT, Xia Z, An JY, et al. (2003). "Female Lethality and Apoptosis of Spermatocytes in Mice Lacking the UBR2 Ubiquitin Ligase of the N-End Rule Pathway". Mol. Cell. Biol. 23 (22): 8255–71. doi:10.1128/MCB.23.22.8255-8271.2003. PMC 262401. PMID 14585983.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Yin J, Kwon YT, Varshavsky A, Wang W (2005). "RECQL4, mutated in the Rothmund-Thomson and RAPADILINO syndromes, interacts with ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway". Hum. Mol. Genet. 13 (20): 2421–30. doi:10.1093/hmg/ddh269. PMID 15317757.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Kwak KS, Zhou X, Solomon V, et al. (2005). "Regulation of protein catabolism by muscle-specific and cytokine-inducible ubiquitin ligase E3alpha-II during cancer cachexia". Cancer Res. 64 (22): 8193–8. doi:10.1158/0008-5472.CAN-04-2102. PMID 15548684.
• Zenker M, Mayerle J, Lerch MM, et al. (2006). "Deficiency of UBR1, a ubiquitin ligase of the N-end rule pathway, causes pancreatic dysfunction, malformations and mental retardation (Johanson-Blizzard syndrome)" (PDF). Nat. Genet. 37 (12): 1345–50. doi:10.1038/ng1681. PMID 16311597. S2CID 23050042.
• Matta-Camacho E, Kozlov G, Li F, Gehring K, et al. (2010). "Structural basis of substrate recognition and specificity in the N-end rule pathway". Nat Struct Mol Biol. 17 (10): 1182–7. doi:10.1038/nsmb.1894. PMID 20835242. S2CID 20961853.

External links

• Overview of all the structural information available in the PDB for UniProt: Q8IWV8 (E3 ubiquitin-protein ligase UBR2) at the PDBe-KB.