UBE2V2
Ubiquitin-conjugating enzyme E2 variant 2 | |||||||||||||
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File:PBB Protein UBE2V2 image.jpg PDB rendering based on 1j74. | |||||||||||||
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Identifiers | |||||||||||||
Symbols | UBE2V2 ; DDVIT1; DDVit-1; EDAF-1; EDPF-1; EDPF1; MMS2; UEV-2; UEV2 | ||||||||||||
External IDs | Template:OMIM5 Template:MGI HomoloGene: 55739 | ||||||||||||
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RNA expression pattern | |||||||||||||
File:PBB GE UBE2V2 209096 at tn.png | |||||||||||||
More reference expression data | |||||||||||||
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 2, also known as UBE2V2, is a human gene.[1]
Ubiquitin-conjugating enzyme E2 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 also shares homology with ubiquitin-conjugating enzyme E2 variant 1 and yeast MMS2 gene product. It may be involved in the differentiation of monocytes and enterocytes.[1]
References
Further reading
- Fritsche J, Rehli M, Krause SW; et al. (1997). "Molecular cloning of a 1alpha,25-dihydroxyvitamin D3-inducible transcript (DDVit 1) in human blood monocytes". Biochem. Biophys. Res. Commun. 235 (2): 407–12. PMID 9199207.
- 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.
- 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.
- 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.
- Chan NL, Hill CP (2001). "Defining polyubiquitin chain topology". Nat. Struct. Biol. 8 (8): 650–2. doi:10.1038/90337. PMID 11473244.
- Moraes TF, Edwards RA, McKenna S; et al. (2001). "Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13". Nat. Struct. Biol. 8 (8): 669–73. doi:10.1038/90373. PMID 11473255.
- 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.
- Gevaert K, Goethals M, Martens L; et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
- Bothos J, Summers MK, Venere M; et al. (2003). "The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form Lys63-linked polyubiquitin chains". Oncogene. 22 (46): 7101–7. doi:10.1038/sj.onc.1206831. PMID 14562038.
- Zhou H, Wertz I, O'Rourke K; et al. (2004). "Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO". Nature. 427 (6970): 167–71. doi:10.1038/nature02273. PMID 14695475.
- 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.
- 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.
- Simpson LJ, Sale JE (2005). "UBE2V2 (MMS2) is not required for effective immunoglobulin gene conversion or DNA damage tolerance in DT40". DNA Repair (Amst.). 4 (4): 503–10. doi:10.1016/j.dnarep.2004.12.002. PMID 15725630.
- Pastushok L, Moraes TF, Ellison MJ, Xiao W (2005). "A single Mms2 "key" residue insertion into a Ubc13 pocket determines the interface specificity of a human Lys63 ubiquitin conjugation complex". J. Biol. Chem. 280 (18): 17891–900. doi:10.1074/jbc.M410469200. PMID 15749714.
- Spyracopoulos L, Lewis MJ, Saltibus LF (2005). "Main chain and side chain dynamics of the ubiquitin conjugating enzyme variant human Mms2 in the free and ubiquitin-bound States". Biochemistry. 44 (24): 8770–81. doi:10.1021/bi050065k. PMID 15952783.
- 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.
- Stelzl U, Worm U, Lalowski M; et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
- Wen R, Newton L, Li G; et al. (2006). "Arabidopsis thaliana UBC13: implication of error-free DNA damage tolerance and Lys63-linked polyubiquitylation in plants". Plant Mol. Biol. 61 (1–2): 241–53. doi:10.1007/s11103-006-0007-x. PMID 16786304.
- Zhao GY, Sonoda E, Barber LJ; et al. (2007). "A critical role for the ubiquitin-conjugating enzyme Ubc13 in initiating homologous recombination". Mol. Cell. 25 (5): 663–75. doi:10.1016/j.molcel.2007.01.029. PMID 17349954.
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