UBE2V1

Ubiquitin-conjugating enzyme E2 variant 1
File:PBB Protein UBE2V1 image.jpg PDB rendering based on 1j74.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1j74​, 1j7d​, 1zgu​, 2a4d​, 2c2v​, 2hlw​
Identifiers
Symbols	UBE2V1 ; CIR1; CROC-1; CROC1; UBE2V; UEV-1; UEV1; UEV1A
External IDs	Template:OMIM5 Template:MGI HomoloGene: 81888
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Ubiquitin-conjugating enzyme E2 variant 1, also known as UBE2V1, is a human gene.

Ubiquitin-conjugating E2 enzyme variant proteins constitute a distinct subfamily within the E2 protein family. They have sequence similarity to other ubiquitin-conjugating enzymes but lack the conserved cysteine residue that is critical for the catalytic activity of E2s. The protein encoded by this gene is located in the nucleus and can cause transcriptional activation of the human FOS proto-oncogene. It is thought to be involved in the control of differentiation by altering cell cycle behavior. Multiple alternatively spliced transcripts encoding different isoforms have been described for this gene. A pseudogene has been identified which is also located on chromosome 20. Co-transcription of this gene and the neighboring upstream gene generates a rare transcript (Kua-UEV), which encodes a fusion protein comprised of sequence sharing identity with each individual gene product.

Further reading

• Long M (2001). "A new function evolved from gene fusion". Genome Res. 10 (11): 1655–7. PMID 11076848.
• Rothofsky ML, Lin SL (1997). "CROC-1 encodes a protein which mediates transcriptional activation of the human FOS promoter". Gene. 195 (2): 141–9. PMID 9305758.
• Sancho E, Vilá MR, Sánchez-Pulido L; et al. (1998). "Role of UEV-1, an inactive variant of the E2 ubiquitin-conjugating enzymes, in in vitro differentiation and cell cycle behavior of HT-29-M6 intestinal mucosecretory cells". Mol. Cell. Biol. 18 (1): 576–89. PMID 9418904.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Thomson TM, Khalid H, Lozano JJ; et al. (1998). "Role of UEV-1A, a homologue of the tumor suppressor protein TSG101, in protection from DNA damage". FEBS Lett. 423 (1): 49–52. PMID 9580084.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Xiao W, Lin SL, Broomfield S; et al. (1998). "The products of the yeast MMS2 and two human homologs (hMMS2 and CROC-1) define a structurally and functionally conserved Ubc-like protein family". Nucleic Acids Res. 26 (17): 3908–14. PMID 9705497.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ma L, Broomfield S, Lavery C; et al. (1998). "Up-regulation of CIR1/CROC1 expression upon cell immortalization and in tumor-derived human cell lines". Oncogene. 17 (10): 1321–6. doi:10.1038/sj.onc.1202058. PMID 9771976.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Hofmann RM, Pickart CM (1999). "Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair". Cell. 96 (5): 645–53. PMID 10089880.
• Deng L, Wang C, Spencer E; et al. (2000). "Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain". Cell. 103 (2): 351–61. PMID 11057907.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Thomson TM, Lozano JJ, Loukili N; et al. (2001). "Fusion of the human gene for the polyubiquitination coeffector UEV1 with Kua, a newly identified gene". Genome Res. 10 (11): 1743–56. PMID 11076860.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ito M, Shichijo S, Tsuda N; et al. (2001). "Molecular basis of T cell-mediated recognition of pancreatic cancer cells". Cancer Res. 61 (5): 2038–46. PMID 11280764.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Deloukas P, Matthews LH, Ashurst J; et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20". Nature. 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 15489334.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Andersen PL, Zhou H, Pastushok L; et al. (2005). "Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A". J. Cell Biol. 170 (5): 745–55. doi:10.1083/jcb.200502113. PMID 16129784.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Hau DD, Lewis MJ, Saltibus LF; et al. (2006). "Structure and interactions of the ubiquitin-conjugating enzyme variant human Uev1a: implications for enzymatic synthesis of polyubiquitin chains". Biochemistry. 45 (32): 9866–77. doi:10.1021/bi060631r. PMID 16893187.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Syed NA, Andersen PL, Warrington RC, Xiao W (2007). "Uev1A, a ubiquitin conjugating enzyme variant, inhibits stress-induced apoptosis through NF-kappaB activation". Apoptosis. 11 (12): 2147–57. doi:10.1007/s10495-006-0197-3. PMID 17041755.CS1 maint: Multiple names: authors list (link)
• Petroski MD, Zhou X, Dong G; et al. (2007). "Substrate modification with lysine 63-linked ubiquitin chains through the UBC13-UEV1A ubiquitin-conjugating enzyme". J. Biol. Chem. 282 (41): 29936–45. doi:10.1074/jbc.M703911200. PMID 17709375.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)