The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

UBE2N  -  ubiquitin-conjugating enzyme E2N

Homo sapiens

Synonyms: BLU, Bendless-like ubiquitin-conjugating enzyme, HEL-S-71, MGC8489, UBC13, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of UBE2N

  • Frequent epigenetic inactivation of RASSF1A and BLU genes located within the critical 3p21.3 region in gliomas [1].

High impact information on UBE2N

  • The E2 ubiquitin-conjugating enzyme UBE2N was a preferential binding partner of the 'weak' STK15 Phe31 variant form in yeast two-hybrid screens and in human cells [2].
  • We find that TRAF6, a RING domain protein, functions together with Ubc13/Uev1A to catalyze the synthesis of unique polyubiquitin chains linked through lysine-63 (K63) of ubiquitin [3].
  • The Ubc13 E2 ubiquitin-conjugating enzyme is key in the process of 'tagging' target proteins with lysine 63-linked polyubiquitin chains, which are essential for the transmission of immune receptor signals culminating in activation of the transcription factor NF-kappaB [4].
  • Here we demonstrate that conditional ablation of Ubc13 resulted in defective B cell development and in impaired B cell and macrophage activation [4].
  • In response to all tested stimuli except tumor necrosis factor, Ubc13-deficient cells showed almost normal NF-kappaB activation but considerably impaired activation of mitogen-activated protein kinase [4].

Biological context of UBE2N

  • This interaction results in colocalization of UBE2N with STK15 at the centrosomes during mitosis [2].
  • A heterodimer composed of the catalytically active ubiquitin-conjugating enzyme hUbc13 and its catalytically inactive paralogue, hMms2, forms the catalytic core for the synthesis of an alternative type of multiubiquitin chain where ubiquitin molecules are tandemly linked to one another through a Lys-63 isopeptide bond [5].
  • Although the ubiquitin ligase activity of CHIP requires its dimerization through the U box domain, the crystal structure of the CHIP-E2 complex reveals that the protomers in the CHIP homodimer adopt distinct conformations such that only one U box of CHIP interacts with Ubc13 [6].
  • In response to DNA damage, Ubc13 is no longer capable of facilitating p53 monomerization, in part due to a decrease in its own levels which is p53 dependent [7].
  • In addition, PMA/ionophore-mediated ubiquitination of NF-kappaB essential modulator (NEMO)/IkappaB kinase gamma (IKKgamma) and phosphorylation of TGF-beta-activated kinase 1 (TAK1) were nearly abolished in Ubc13-deficient thymocytes [8].

Anatomical context of UBE2N


Associations of UBE2N with chemical compounds


Physical interactions of UBE2N


Other interactions of UBE2N

  • Nuclear magnetic resonance (NMR) spectroscopy was used to determine the solution state structure of the RING domain from human TRAF6, and the interaction between hUbc13 and TRAF6 was characterized using NMR chemical shift mapping [13].
  • Furthermore, short interfering RNAs that reduced the expression of paracaspase and UBC13 abrogated the effects of Bcl10 [14].
  • Here we report the crystal structure of a complex between hMms2 (Uev1) and hUbc13 at 1.85 A resolution and a structure of free hMms2 at 1.9 A resolution [15].
  • ISG15 modification of ubiquitin E2 Ubc13 disrupts its ability to form thioester bond with ubiquitin [16].
  • The RING finger protein RNF8 recruits UBC13 for lysine 63-based self polyubiquitylation [17].

Analytical, diagnostic and therapeutic context of UBE2N

  • Furthermore, a dissociation constant of 49 +/- 7 nM was determined for the interaction between Mms2 and Ubc13 using isothermal titration calorimetry [18].
  • The method proposed is based on the processing of the residual terms resulting from the BLUP methodology applied to an additive animal model [19].


  1. Frequent epigenetic inactivation of RASSF1A and BLU genes located within the critical 3p21.3 region in gliomas. Hesson, L., Bièche, I., Krex, D., Criniere, E., Hoang-Xuan, K., Maher, E.R., Latif, F. Oncogene (2004) [Pubmed]
  2. Identification of Stk6/STK15 as a candidate low-penetrance tumor-susceptibility gene in mouse and human. Ewart-Toland, A., Briassouli, P., de Koning, J.P., Mao, J.H., Yuan, J., Chan, F., MacCarthy-Morrogh, L., Ponder, B.A., Nagase, H., Burn, J., Ball, S., Almeida, M., Linardopoulos, S., Balmain, A. Nat. Genet. (2003) [Pubmed]
  3. Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain. Deng, L., Wang, C., Spencer, E., Yang, L., Braun, A., You, J., Slaughter, C., Pickart, C., Chen, Z.J. Cell (2000) [Pubmed]
  4. Key function for the Ubc13 E2 ubiquitin-conjugating enzyme in immune receptor signaling. Yamamoto, M., Okamoto, T., Takeda, K., Sato, S., Sanjo, H., Uematsu, S., Saitoh, T., Yamamoto, N., Sakurai, H., Ishii, K.J., Yamaoka, S., Kawai, T., Matsuura, Y., Takeuchi, O., Akira, S. Nat. Immunol. (2006) [Pubmed]
  5. An NMR-based model of the ubiquitin-bound human ubiquitin conjugation complex Mms2.Ubc13. The structural basis for lysine 63 chain catalysis. McKenna, S., Moraes, T., Pastushok, L., Ptak, C., Xiao, W., Spyracopoulos, L., Ellison, M.J. J. Biol. Chem. (2003) [Pubmed]
  6. Protein ubiquitination: CHIPping away the symmetry. Schulman, B.A., Chen, Z.J. Mol. Cell (2005) [Pubmed]
  7. Regulation of p53 Localization and Activity by Ubc13. Laine, A., Topisirovic, I., Zhai, D., Reed, J.C., Borden, K.L., Ronai, Z. Mol. Cell. Biol. (2006) [Pubmed]
  8. Cutting Edge: Pivotal Function of Ubc13 in Thymocyte TCR Signaling. Yamamoto, M., Sato, S., Saitoh, T., Sakurai, H., Uematsu, S., Kawai, T., Ishii, K.J., Takeuchi, O., Akira, S. J. Immunol. (2006) [Pubmed]
  9. Frequent promoter hypermethylation of RASSF1A and CASP8 in neuroblastoma. L??zcoz, P., Mu??oz, J., Nistal, M., Pesta??a, A., Enc??o, I., Castresana, J.S. BMC Cancer (2006) [Pubmed]
  10. Microarray analysis of gene expression in the prefrontal cortex in schizophrenia: a preliminary study. Vawter, M.P., Crook, J.M., Hyde, T.M., Kleinman, J.E., Weinberger, D.R., Becker, K.G., Freed, W.J. Schizophr. Res. (2002) [Pubmed]
  11. Functional studies of the chromosome 3p21.3 candidate tumor suppressor gene BLU/ZMYND10 in nasopharyngeal carcinoma. Yau, W.L., Lung, H.L., Zabarovsky, E.R., Lerman, M.I., Sham, J.S., Chua, D.T., Tsao, S.W., Stanbridge, E.J., Lung, M.L. Int. J. Cancer (2006) [Pubmed]
  12. The N-terminal domain of the Aurora-A Phe-31 variant encodes an E3 ubiquitin ligase and mediates ubiquitination of I{kappa}B{alpha}. Briassouli, P., Chan, F., Linardopoulos, S. Hum. Mol. Genet. (2006) [Pubmed]
  13. Structure, interactions, and dynamics of the RING domain from human TRAF6. Mercier, P., Lewis, M.J., Hau, D.D., Saltibus, L.F., Xiao, W., Spyracopoulos, L. Protein Sci. (2007) [Pubmed]
  14. Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO. Zhou, H., Wertz, I., O'Rourke, K., Ultsch, M., Seshagiri, S., Eby, M., Xiao, W., Dixit, V.M. Nature (2004) [Pubmed]
  15. 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]
  16. ISG15 modification of ubiquitin E2 Ubc13 disrupts its ability to form thioester bond with ubiquitin. Zou, W., Papov, V., Malakhova, O., Kim, K.I., Dao, C., Li, J., Zhang, D.E. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  17. The RING finger protein RNF8 recruits UBC13 for lysine 63-based self polyubiquitylation. Plans, V., Scheper, J., Soler, M., Loukili, N., Okano, Y., Thomson, T.M. J. Cell. Biochem. (2006) [Pubmed]
  18. Energetics and specificity of interactions within Ub.Uev.Ubc13 human ubiquitin conjugation complexes. McKenna, S., Hu, J., Moraes, T., Xiao, W., Ellison, M.J., Spyracopoulos, L. Biochemistry (2003) [Pubmed]
  19. Estimation of dominance components in noninbred populations by using additive animal model residuals. Chalh, A., El Gazzah, M. J. Appl. Genet. (2002) [Pubmed]
WikiGenes - Universities