UBE2V2
Ubiquitin-conjugating enzyme E2 variant 2 is a protein that in humans is encoded by the UBE2V2 gene.[1][2][3]
Function
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.[3]
Interactions
UBE2V2 has been shown to interact with HLTF.[4]
References
- ↑ Sancho E, Vilá MR, Sánchez-Pulido L, Lozano JJ, Paciucci R, Nadal M, Fox M, Harvey C, Bercovich B, Loukili N, Ciechanover A, Lin SL, Sanz F, Estivill X, Valencia A, Thomson TM (Jan 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. doi:10.1128/mcb.18.1.576. PMC 121525. PMID 9418904.
- ↑ Fritsche J, Rehli M, Krause SW, Andreesen R, Kreutz M (Jul 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. doi:10.1006/bbrc.1997.6798. PMID 9199207.
- 1 2 "Entrez Gene: UBE2V2 ubiquitin-conjugating enzyme E2 variant 2".
- ↑ Unk I, Hajdú I, Fátyol K, Hurwitz J, Yoon JH, Prakash L, Prakash S, Haracska L (Mar 2008). "Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination". Proc. Natl. Acad. Sci. U.S.A. 105 (10): 3768–73. doi:10.1073/pnas.0800563105. PMC 2268824. PMID 18316726.
Further reading
- Xiao W, Lin SL, Broomfield S, Chow BL, Wei YF (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. doi:10.1093/nar/26.17.3908. PMC 147796. 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. doi:10.1016/S0092-8674(00)80575-9. 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, Pastushok L, Xiao W, Glover JN, Ellison MJ (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.
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (2003). "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, Scolnick DM, Halazonetis TD (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, Ultsch M, Seshagiri S, Eby M, Xiao W, Dixit VM (2004). "Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO". Nature 427 (6970): 167–71. doi:10.1038/nature02273. PMID 14695475.
- 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, Moraes T, McKenna S, Ziola B, Ellison MJ, Dixit VM, Xiao W (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. PMC 2171356. PMID 16129784.
- Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (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, Wang H, Xiao W (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, Oka H, Murakawa Y, Yamada K, Ikura T, Wang X, Kobayashi M, Yamamoto K, Boulton SJ, Takeda S (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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