UBE2N

From Wikipedia, the free encyclopedia

Ubiquitin-conjugating enzyme E2N (UBC13 homolog, yeast)

PDB rendering based on 1j7d.

Available structures: 1j7d, 2c2v

Identifiers

Symbol(s)

UBE2N; MGC131857; MGC8489; UBC13; UbcH-ben

External IDs

OMIM: 603679 MGI: 1934835 HomoloGene: 2512

Gene ontology
Molecular Function:	• ubiquitin-protein ligase activity • protein binding • ligase activity • ubiquitin binding
Cellular Component:	• nucleus • cytoplasm • UBC13-MMS2 complex
Biological Process:	• proteolysis • protein ubiquitination • positive regulation of I-kappaB kinase/NF-kappaB cascade • positive regulation of DNA repair • T cell receptor signaling pathway • activation of NF-kappaB transcription factor

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_003348 (mRNA)
NP_003339 (protein)

NM_080560 (mRNA)
NP_542127 (protein)

Location

Chr 12: 92.33 - 92.36 Mb

n/a

Pubmed search

[1]

[2]

Ubiquitin-conjugating enzyme E2N (UBC13 homolog, yeast), also known as UBE2N, is a human gene.^[1]

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: ubiquitin-activating enzymes, or E1s, ubiquitin-conjugating enzymes, or E2s, and ubiquitin-protein ligases, or E3s. This gene encodes a member of the E2 ubiquitin-conjugating enzyme family. Studies in mouse suggest that this protein plays a role in DNA postreplication repair.^[1]

[edit] References

^ ^a ^b Entrez Gene: UBE2N ubiquitin-conjugating enzyme E2N (UBC13 homolog, yeast).

[edit] Further reading

Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
Yamaguchi T, Kim NS, Sekine S, et al. (1997). "Cloning and expression of cDNA encoding a human ubiquitin-conjugating enzyme similar to the Drosophila bendless gene product.". J. Biochem. 120 (3): 494–97. PMID 8902611.
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.
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.
Ashley C, Pastushok L, McKenna S, et al. (2002). "Roles of mouse UBC13 in DNA postreplication repair and Lys63-linked ubiquitination.". Gene 285 (1-2): 183–91. PMID 12039045.
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.
McKenna S, Moraes T, Pastushok L, et al. (2003). "An NMR-based model of the ubiquitin-bound human ubiquitin conjugation complex Mms2.Ubc13. The structural basis for lysine 63 chain catalysis.". J. Biol. Chem. 278 (15): 13151–8. doi:10.1074/jbc.M212353200. PMID 12569095.
Anandasabapathy N, Ford GS, Bloom D, et al. (2003). "GRAIL: an E3 ubiquitin ligase that inhibits cytokine gene transcription is expressed in anergic CD4+ T cells.". Immunity 18 (4): 535–47. PMID 12705856.
Ewart-Toland A, Briassouli P, de Koning JP, et al. (2003). "Identification of Stk6/STK15 as a candidate low-penetrance tumor-susceptibility gene in mouse and human.". Nat. Genet. 34 (4): 403–12. doi:10.1038/ng1220. PMID 12881723.
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.
Sun L, Deng L, Ea CK, et al. (2004). "The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes.". Mol. Cell 14 (3): 289–301. PMID 15125833.
Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway.". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMID 15231748.
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.
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.
Takeuchi T, Yokosawa H (2005). "ISG15 modification of Ubc13 suppresses its ubiquitin-conjugating activity.". Biochem. Biophys. Res. Commun. 336 (1): 9–13. doi:10.1016/j.bbrc.2005.08.034. PMID 16112642.
Zou W, Papov V, Malakhova O, et al. (2005). "ISG15 modification of ubiquitin E2 Ubc13 disrupts its ability to form thioester bond with ubiquitin.". Biochem. Biophys. Res. Commun. 336 (1): 61–8. doi:10.1016/j.bbrc.2005.08.038. PMID 16122702.