World Library  
Flag as Inappropriate
Email this Article


Article Id: WHEBN0014763613
Reproduction Date:

Title: Ube2n  
Author: World Heritage Encyclopedia
Language: English
Subject: UBE2V1, Ubiquitin-conjugating enzyme, Shigella flexneri, DNAJC13, DNAJB4
Publisher: World Heritage Encyclopedia


Ubiquitin-conjugating enzyme E2N

PDB rendering based on 1j7d.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols  ; HEL-S-71; UBC13; UbcH-ben; UbcH13
External IDs ChEMBL: GeneCards:
EC number
RNA expression pattern
Species Human Mouse
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

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


UBE2N has been shown to interact with Aurora A kinase,[3] TRAF2,[4] TRAF6,[4] HLTF[5] and UBE2V1.[4]


  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.  
  2. ^ a b "Entrez Gene: UBE2N ubiquitin-conjugating enzyme E2N (UBC13 homolog, yeast)". 
  3. ^ Ewart-Toland, Amanda; Briassouli Paraskevi, de Koning John P, Mao Jian-Hua, Yuan Jinwei, Chan Florence, MacCarthy-Morrogh Lucy, Ponder Bruce A J, Nagase Hiroki, Burn John, Ball Sarah, Almeida Maria, Linardopoulos Spiros, Balmain Allan (August 2003). "Identification of Stk6/STK15 as a candidate low-penetrance tumor-susceptibility gene in mouse and human". Nat. Genet. (United States) 34 (4): 403–12.  
  4. ^ a b c Deng, L; Wang C; Spencer E; Yang L; Braun A; You J; Slaughter C; Pickart C; Chen Z J (October 2000). "Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain". Cell (UNITED STATES) 103 (2): 351–61.  
  5. ^ Unk, Ildiko; Hajdú Ildikó; Fátyol Károly; Hurwitz Jerard; Yoon Jung-Hoon; Prakash Louise; Prakash Satya; Haracska Lajos (March 2008). "Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination".  

Further reading

  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806.  
  • 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.  
  • 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.  
  • Chan NL, Hill CP (2001). "Defining polyubiquitin chain topology.". Nat. Struct. Biol. 8 (8): 650–2.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway.". Genome Res. 14 (7): 1324–32.  
  • 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.  
  • 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.  
  • Takeuchi T, Yokosawa H (2005). "ISG15 modification of Ubc13 suppresses its ubiquitin-conjugating activity.". Biochem. Biophys. Res. Commun. 336 (1): 9–13.  
  • 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.  

This article was sourced from Creative Commons Attribution-ShareAlike License; additional terms may apply. World Heritage Encyclopedia content is assembled from numerous content providers, Open Access Publishing, and in compliance with The Fair Access to Science and Technology Research Act (FASTR), Wikimedia Foundation, Inc., Public Library of Science, The Encyclopedia of Life, Open Book Publishers (OBP), PubMed, U.S. National Library of Medicine, National Center for Biotechnology Information, U.S. National Library of Medicine, National Institutes of Health (NIH), U.S. Department of Health & Human Services, and, which sources content from all federal, state, local, tribal, and territorial government publication portals (.gov, .mil, .edu). Funding for and content contributors is made possible from the U.S. Congress, E-Government Act of 2002.
Crowd sourced content that is contributed to World Heritage Encyclopedia is peer reviewed and edited by our editorial staff to ensure quality scholarly research articles.
By using this site, you agree to the Terms of Use and Privacy Policy. World Heritage Encyclopedia™ is a registered trademark of the World Public Library Association, a non-profit organization.

Copyright © World Library Foundation. All rights reserved. eBooks from Hawaii eBook Library are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.