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
External IDs	MGI: 1934835 HomoloGene: 128406 GeneCards: UBE2N
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q22 Start 93,405,673 bp[1] End 93,442,262 bp[1]
Gene location (Mouse) Chr. Chromosome 10 (mouse)[2] Band 10|10 C2 Start 95,515,145 bp[2] End 95,545,657 bp[2]
RNA expression pattern 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 • protein complex • nucleoplasm • extracellular exosome • UBC13-MMS2 complex • cell nucleus • fibrillar center • macromolecular 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 • cellular protein modification process • 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 • activation of MAPK activity • 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: 95.52 – 95.55 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Ubiquitin-conjugating enzyme E2 N is a protein that in humans is encoded by the UBE2N gene.^[5][6]

Contents

• 
  1 Function
  


• 
  2 Interactions
  


• 
  3 References
  


• 
  4 Further reading
  

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.^[6]

Interactions

UBE2N has been shown to interact with:

• 
  AURKA,^[7]
  


• 
  HLTF,^[8]
  


• 
  TRAF2,^[9]
  


• 
  TRAF6,^[9] and


• 
  UBE2V1.^[9]
  

References

1. 
   ^ ^abc GRCh38: Ensembl release 89: ENSG00000177889 - Ensembl, May 2017
   


2. 
   ^ ^abc GRCm38: Ensembl release 89: ENSMUSG00000074781 - Ensembl, May 2017
   


3. 
   ^ "Human PubMed Reference:"..mw-parser-output cite.citation{font-style:inherit}.mw-parser-output .citation q{quotes:"""""""'""'"}.mw-parser-output .citation .cs1-lock-free a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/6/65/Lock-green.svg/9px-Lock-green.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-limited a,.mw-parser-output .citation .cs1-lock-registration a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/d/d6/Lock-gray-alt-2.svg/9px-Lock-gray-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .citation .cs1-lock-subscription a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/a/aa/Lock-red-alt-2.svg/9px-Lock-red-alt-2.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration{color:#555}.mw-parser-output .cs1-subscription span,.mw-parser-output .cs1-registration span{border-bottom:1px dotted;cursor:help}.mw-parser-output .cs1-ws-icon a{background:url("//upload.wikimedia.org/wikipedia/commons/thumb/4/4c/Wikisource-logo.svg/12px-Wikisource-logo.svg.png")no-repeat;background-position:right .1em center}.mw-parser-output code.cs1-code{color:inherit;background:inherit;border:inherit;padding:inherit}.mw-parser-output .cs1-hidden-error{display:none;font-size:100%}.mw-parser-output .cs1-visible-error{font-size:100%}.mw-parser-output .cs1-maint{display:none;color:#33aa33;margin-left:0.3em}.mw-parser-output .cs1-subscription,.mw-parser-output .cs1-registration,.mw-parser-output .cs1-format{font-size:95%}.mw-parser-output .cs1-kern-left,.mw-parser-output .cs1-kern-wl-left{padding-left:0.2em}.mw-parser-output .cs1-kern-right,.mw-parser-output .cs1-kern-wl-right{padding-right:0.2em}
   


4. 
   ^ "Mouse PubMed Reference:".
   


5. 
   ^ 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.
   


6. 
   ^ ^ab "Entrez Gene: UBE2N ubiquitin-conjugating enzyme E2N (UBC13 homolog, yeast)".
   


7. 
   ^ 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.
   


8. 
   ^ 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.
   


9. 
   ^ ^abc 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

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• 
  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.
  

‹ The template below (PDB Gallery) is being considered for deletion. See templates for discussion to help reach a consensus. ›

v t e PDB gallery
1j7d: Crystal Structure of hMms2-hUbc13 2c2v: CRYSTAL STRUCTURE OF THE CHIP-UBC13-UEV1A COMPLEX

v t e Posttranslational modification
Chaperones/ protein folding	Heat shock proteins/ Chaperonins Hsp10/GroES Hsp27 Hsp47 HSP60/GroEL Hsp40/DnaJ A1 A2 A3 B1 B2 B11 B4 B6 B9 C1 C3 C5 C6 C7 C10 C11 C13 C14 C19 Hsp70 1A 1B 1L 2 4 4L 5 6 7 8 9 12A 14 Hsp90 α1 α2 β ER TRAP1 Other Alpha crystallin Clusterin Survival of motor neuron SMN1 SMN2
Protein targeting	Signal peptide Mitochondrial targeting signal
Ubiquitin	E1 Ubiquitin-activating enzyme UBA1 UBA2 UBA3 UBA5 UBA6 UBA7 ATG7 NAE1 SAE1 E2 Ubiquitin-conjugating enzyme A B C D1 D2 D3 E1 E2 E3 G1 G2 H I J1 J2 K L1 L2 L3 L4 L6 M N O Q1 Q2 R1 (CDC34) R2 S V1 V2 Z E3 Ubiquitin ligase VHL Cullin CBL MDM2 FANCL UBR1 Deubiquitinating enzyme: Ataxin 3 USP6 CYLD ATG3 BIRC6 UFC1
Other	Ubiquitin-like modifiers SUMO protein ISG15 URM1 NEDD8 FAT10 ATG8 ATG12 FUB1 MUB UFM1 UBL5 Prokaryotic ubiquitin-like protein

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