UBE2N

UBE2N
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, 4TKP, 5AIT, 5AIU, 4WHV
Identifiers
Aliases	UBE2N, HEL-S-71, UBC13, UBCHBEN; UBC13, UbcH-ben, UbcH13, ubiquitin conjugating enzyme E2 N, UBCHBEN
External IDs	OMIM: 603679 MGI: 1934835 HomoloGene: 128406 GeneCards: UBE2N
Gene location (Human) Chr. Chromosome 12 (human) Band 12q22 Start 93,405,673 bp End 93,441,947 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10|10 C2 Start 95,351,007 bp End 95,381,519 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sperm ganglionic eminence islet of Langerhans right ventricle pons human penis myocardium Brodmann area 46 secondary oocyte body of tongue Top expressed in spermatid spermatocyte esophagus yolk sac superior frontal gyrus morula lip cerebellar cortex medial vestibular nucleus neural tube More reference expression data BioGPS More reference expression data
Gene ontology Molecular function transferase activity nucleotide binding ubiquitin protein ligase activity ubiquitin binding protein binding ATP binding ubiquitin protein ligase binding RNA binding ubiquitin-protein transferase activity ubiquitin conjugating enzyme activity Cellular component cytoplasm cytosol UBC13-UEV1A complex ubiquitin ligase complex nucleoplasm extracellular exosome UBC13-MMS2 complex nucleus fibrillar center protein-containing complex Biological process postreplication repair protein K63-linked ubiquitination regulation of DNA repair DNA double-strand break processing positive regulation of DNA repair stimulatory C-type lectin receptor signaling pathway proteolysis cellular response to DNA damage stimulus Fc-epsilon receptor signaling pathway global genome nucleotide-excision repair positive regulation of histone modification positive regulation of ubiquitin-protein transferase activity protein ubiquitination regulation of histone ubiquitination positive regulation of I-kappaB kinase/NF-kappaB signaling T cell receptor signaling pathway double-strand break repair via nonhomologous end joining nucleotide-binding oligomerization domain containing signaling pathway histone ubiquitination DNA repair double-strand break repair via homologous recombination JNK cascade positive regulation of NF-kappaB transcription factor activity ubiquitin-dependent protein catabolic process interleukin-1-mediated signaling pathway Sources:Amigo / QuickGO
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: 95.35 – 95.38 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Ubiquitin-conjugating enzyme E2 N is a protein that in humans is encoded by the UBE2N gene.

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.

Interactions

UBE2N has been shown to interact with:

• AURKA,
• HLTF,
• TRAF2,
• TRAF6, and
• UBE2V1.

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. S2CID 17117789.
• 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. S2CID 18154645.
• Chan NL, Hill CP (2001). "Defining polyubiquitin chain topology". Nat. Struct. Biol. 8 (8): 650–2. doi:10.1038/90337. PMID 11473244. S2CID 16579945.
• 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. S2CID 23504541.
• 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. S2CID 29442841.
• 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. Bibcode:2004Natur.427..167Z. doi:10.1038/nature02273. PMID 14695475. S2CID 4429582.
• 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.