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Gene Review

UBC13  -  E2 ubiquitin-conjugating protein UBC13

Saccharomyces cerevisiae S288c

Synonyms: Ubiquitin carrier protein 13, Ubiquitin-conjugating enzyme E2 13, Ubiquitin-protein ligase 13, YD6652.04, YDR092W
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High impact information on UBC13

  • The crystal structure of the Mms2/Ubc13 heterodimer shows the active site of Ubc13 at the intersection of two channels that are potential binding sites for the two substrate ubiquitins [1].
  • We show that Mms2p forms a specific heteromeric complex with the UBC13-encoded E2 and is required for the Ubc13p-dependent assembly of polyubiquitin chains linked through lysine 63 [2].
  • Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A [3].
  • RAD5 recruits the UBC13-MMS2 complex to DNA by means of its RING finger domain [4].
  • The ubiquitin conjugating enzyme complex Mms2-Ubc13 plays a key role in post-replicative DNA repair in yeast and the NF-kappaB signal transduction pathway in humans [5].

Biological context of UBC13

  • Surprisingly, UBC13 and MMS2 are largely cytosolic proteins, but DNA damage triggers their redistribution to the nucleus [4].
  • In addition, UV-induced mutagenesis is fully functional in the ubc13 mutant [6].
  • Quantitative analysis of the affinity and kinetics of the UBC13-MMS2 interaction suggests a highly dynamic association model in which compromised mutual interactions result in phenotypic effects only under conditions where protein levels become limiting [7].
  • We showed previously that the products of the UBC13 and MMS2 genes function in error-free post-replicative DNA repair in the yeast Saccharomyces cerevisiae and form a complex that assembles Lys-63-linked polyubiquitin chains in vitro [8].

Associations of UBC13 with chemical compounds

  • In (1)H (15)N HSQC ((1)H (15)N heteronuclear single quantum coherence) NMR experiments, we have mapped the surface determinants of tethered and untethered ubiquitin that interact with Mms2 and Ubc13 in both their monomeric and dimeric forms [9].

Physical interactions of UBC13

  • The RING finger protein RAD5 interacts and cooperates with the UBC13-MMS2 ubiquitin-conjugating enzyme in postreplication DNA damage repair in yeast [7].

Other interactions of UBC13

  • The ubc13 mutant displays up to a 30-fold increase in the spontaneous mutation rate, and this increase is largely REV3 dependent [6].
  • We found that the ubc13 mutation is epistatic to mms2 and rad6, confirming that UBC13 belongs to the PRR-pathway [6].
  • Moreover, the E2s Ubc9 and Ubc13 were linked to the NEF4 repair pathway by genetic criteria [10].
  • Mutations in NEF4 or Ubc13 result in elevated levels of the DNA damage recognition protein Rad4 and an increase in ubiquitylated species of Rad23 [10].
  • They included genes coding for proteins with domains homologous to calcium transporters, casein kinase II, UBC13, AMSH, Vps23p, and Vps27p of Saccharomyces cerevisiae [11].

Analytical, diagnostic and therapeutic context of UBC13


  1. Molecular insights into polyubiquitin chain assembly: crystal structure of the Mms2/Ubc13 heterodimer. VanDemark, A.P., Hofmann, R.M., Tsui, C., Pickart, C.M., Wolberger, C. Cell (2001) [Pubmed]
  2. Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair. Hofmann, R.M., Pickart, C.M. Cell (1999) [Pubmed]
  3. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. Andersen, P.L., Zhou, H., Pastushok, L., Moraes, T., McKenna, S., Ziola, B., Ellison, M.J., Dixit, V.M., Xiao, W. J. Cell Biol. (2005) [Pubmed]
  4. Two RING finger proteins mediate cooperation between ubiquitin-conjugating enzymes in DNA repair. Ulrich, H.D., Jentsch, S. EMBO J. (2000) [Pubmed]
  5. Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13. Moraes, T.F., Edwards, R.A., McKenna, S., Pastushok, L., Xiao, W., Glover, J.N., Ellison, M.J. Nat. Struct. Biol. (2001) [Pubmed]
  6. UBC13, a DNA-damage-inducible gene, is a member of the error-free postreplication repair pathway in Saccharomyces cerevisiae. Brusky, J., Zhu, Y., Xiao, W. Curr. Genet. (2000) [Pubmed]
  7. Protein-protein interactions within an E2-RING finger complex. Implications for ubiquitin-dependent DNA damage repair. Ulrich, H.D. J. Biol. Chem. (2003) [Pubmed]
  8. In vitro assembly and recognition of Lys-63 polyubiquitin chains. Hofmann, R.M., Pickart, C.M. J. Biol. Chem. (2001) [Pubmed]
  9. Noncovalent interaction between ubiquitin and the human DNA repair protein Mms2 is required for Ubc13-mediated polyubiquitination. McKenna, S., Spyracopoulos, L., Moraes, T., Pastushok, L., Ptak, C., Xiao, W., Ellison, M.J. J. Biol. Chem. (2001) [Pubmed]
  10. The NEF4 complex regulates Rad4 levels and utilizes Snf2/Swi2-related ATPase activity for nucleotide excision repair. Ramsey, K.L., Smith, J.J., Dasgupta, A., Maqani, N., Grant, P., Auble, D.T. Mol. Cell. Biol. (2004) [Pubmed]
  11. Isolation of suppressor mutants of phosphatidylinositol 3-phosphate 5-kinase deficient cells in Schizosaccharomyces pombe. Onishi, M., Nakamura, Y., Koga, T., Takegawa, K., Fukui, Y. Biosci. Biotechnol. Biochem. (2003) [Pubmed]
  12. The TRAF6 RING finger domain mediates physical interaction with Ubc13. Wooff, J., Pastushok, L., Hanna, M., Fu, Y., Xiao, W. FEBS Lett. (2004) [Pubmed]
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