UBE2N

Ubiquitin-conjugating enzyme E2N
PDB rendering based on 1j7d.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1J7D​, 2C2V​, 3HCT​, 3HCU​, 3VON​, 3W31​, 4DHI​, 4DHJ​, 4DHZ​, 4IP3​, 4NR3​, 4NRG​, 4NRI​, 4ONL​, 4ONM​, 4ONN​, 4ORH​
Identifiers
Symbols	UBE2N ; HEL-S-71; UBC13; UBCHBEN; UBC13; UbcH-ben; UbcH13
External IDs	OMIM: 603679 MGI: 1934835 HomoloGene: 128406 ChEMBL: 6089 GeneCards: UBE2N Gene
EC number	6.3.2.19
Gene ontology Molecular function • ubiquitin-protein transferase activity • protein binding • ATP binding • ligase activity • ubiquitin protein ligase binding • ubiquitin binding • poly(A) RNA binding • ubiquitin protein ligase activity • ubiquitin conjugating enzyme activity Cellular component • ubiquitin ligase complex • nucleus • cytoplasm • cytosol • UBC13-MMS2 complex • UBC13-UEV1A complex • protein complex • extracellular exosome Biological process • double-strand break repair via homologous recombination • DNA double-strand break processing • stimulatory C-type lectin receptor signaling pathway • toll-like receptor signaling pathway • MyD88-dependent toll-like receptor signaling pathway • regulation of DNA repair • postreplication repair • cellular protein modification process • proteolysis • ubiquitin-dependent protein catabolic process • protein ubiquitination • histone ubiquitination • cytokine-mediated signaling pathway • positive regulation of histone modification • regulation of histone ubiquitination • toll-like receptor 2 signaling pathway • toll-like receptor 4 signaling pathway • toll-like receptor 5 signaling pathway • toll-like receptor 9 signaling pathway • toll-like receptor 10 signaling pathway • nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway • Fc-epsilon receptor signaling pathway • toll-like receptor TLR1:TLR2 signaling pathway • toll-like receptor TLR6:TLR2 signaling pathway • positive regulation of I-kappaB kinase/NF-kappaB signaling • innate immune response • positive regulation of DNA repair • T cell receptor signaling pathway • positive regulation of NF-kappaB transcription factor activity • positive regulation of ubiquitin-protein transferase activity • nucleotide-binding oligomerization domain containing signaling pathway • protein K63-linked ubiquitination Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	7334	93765
Ensembl	ENSG00000177889	ENSMUSG00000074781
UniProt	P61088	P61089
RefSeq (mRNA)	NM_003348	NM_080560
RefSeq (protein)	NP_003339	NP_542127
Location (UCSC)	Chr 12: 93.41 – 93.44 Mb	Chr 10: 95.52 – 95.55 Mb
PubMed search

Ubiquitin-conjugating enzyme E2 N is a protein that in humans is encoded by the UBE2N gene.^[1][2]

Function

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.^[2]

Interactions

UBE2N has been shown to interact with:

• AURKA,^[3]
• HLTF,^[4]
• TRAF2,^[5]
• TRAF6,^[5] and
• UBE2V1.^[5]

References

1. Yamaguchi T, Kim NS, Sekine S, Seino H, Osaka F, Yamao F, Kato S (February 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. doi:10.1093/oxfordjournals.jbchem.a021440. PMID 8902611.
2. "Entrez Gene: UBE2N ubiquitin-conjugating enzyme E2N (UBC13 homolog, yeast)".
3. Ewart-Toland A, Briassouli P, de Koning JP, Mao JH, Yuan J, Chan F, MacCarthy-Morrogh L, Ponder BA, Nagase H, Burn J, Ball S, Almeida M, Linardopoulos S, Balmain A (August 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.
4. Unk I, Hajdú I, Fátyol K, Hurwitz J, Yoon JH, Prakash L, Prakash S, Haracska L (March 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.
5. Deng L, Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C, Pickart C, Chen ZJ (October 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. doi:10.1016/s0092-8674(00)00126-4. PMID 11057907.

Further reading

• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• 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.
• Deng L, Wang C, Spencer E, Yang L, Braun A, You J, Slaughter C, Pickart C, Chen ZJ (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. doi:10.1016/S0092-8674(00)00126-4. 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, 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.
• Ashley C, Pastushok L, McKenna S, Ellison MJ, Xiao W (2002). "Roles of mouse UBC13 in DNA postreplication repair and Lys63-linked ubiquitination.". Gene 285 (1-2): 183–91. doi:10.1016/S0378-1119(02)00409-2. PMID 12039045.
• McKenna S, Moraes T, Pastushok L, Ptak C, Xiao W, Spyracopoulos L, Ellison MJ (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, Holness C, Paragas V, Seroogy C, Skrenta H, Hollenhorst M, Fathman CG, Soares L (2003). "GRAIL: an E3 ubiquitin ligase that inhibits cytokine gene transcription is expressed in anergic CD4+ T cells.". Immunity 18 (4): 535–47. doi:10.1016/S1074-7613(03)00084-0. PMID 12705856.
• Ewart-Toland A, Briassouli P, de Koning JP, Mao JH, Yuan J, Chan F, MacCarthy-Morrogh L, Ponder BA, Nagase H, Burn J, Ball S, Almeida M, Linardopoulos S, Balmain A (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, 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.
• Sun L, Deng L, Ea CK, Xia ZP, Chen ZJ (2004). "The TRAF6 ubiquitin ligase and TAK1 kinase mediate IKK activation by BCL10 and MALT1 in T lymphocytes.". Mol. Cell 14 (3): 289–301. doi:10.1016/S1097-2765(04)00236-9. PMID 15125833.
• Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM (2004). "Functional proteomics mapping of a human signaling pathway.". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
• 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, Kim KI, Dao C, Li J, Zhang DE (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.