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 et al. (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. 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.
- ↑ 3.0 3.1 "Entrez Gene: UBE2V2 ubiquitin-conjugating enzyme E2 variant 2".
- ↑ Unk I, Hajdú I, Fátyol K, Hurwitz J, Yoon JH, Prakash L et al. (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 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.
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR et al. (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 et al. (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 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. PMC 2171356. PMID 16129784.
- Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H 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, 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 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.
PDB gallery |
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| | 1j74: Crystal Structure of Mms2 |
| 1j7d: Crystal Structure of hMms2-hUbc13 |
| 1zgu: Solution structure of the human Mms2-Ubiquitin complex |
| 2a4d: Structure of the human ubiquitin-conjugating enzyme E2 variant 1 (UEV-1) |
| 2c2v: CRYSTAL STRUCTURE OF THE CHIP-UBC13-UEV1A COMPLEX |
| 2hlw: Solution Structure of the Human Ubiquitin-conjugating Enzyme Variant Uev1a |
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| Index of genetics |
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| | Description |
- Gene expression
- DNA
- replication
- cycle
- recombination
- repair
- binding proteins
- Transcription
- factors
- regulators
- nucleic acids
- RNA
- RNA binding proteins
- ribonucleoproteins
- repeated sequence
- modification
- Translation
- ribosome
- modification
- nexins
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- Structure
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- quaternary
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| | Disease |
- Replication and repair
- Transcription factor
- Transcription
- Translation
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