UBE2N

Protein-coding gene in the species Homo sapiens
UBE2N
Available structures
PDBOrtholog 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
AliasesUBE2N, HEL-S-71, UBC13, UBCHBEN; UBC13, UbcH-ben, UbcH13, ubiquitin conjugating enzyme E2 N, UBCHBEN
External IDsOMIM: 603679; MGI: 1934835; HomoloGene: 128406; GeneCards: UBE2N; OMA:UBE2N - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for UBE2N
Genomic location for UBE2N
Band12q22Start93,405,673 bp[1]
End93,441,947 bp[1]
Gene location (Mouse)
Chromosome 10 (mouse)
Chr.Chromosome 10 (mouse)[2]
Chromosome 10 (mouse)
Genomic location for UBE2N
Genomic location for UBE2N
Band10|10 C2Start95,351,007 bp[2]
End95,381,519 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • left testis

  • right testis

  • sperm

  • ganglionic eminence

  • islet of Langerhans

  • ventricular zone

  • right ventricle

  • pons

  • human penis

  • myocardium
Top expressed in
  • spermatid

  • spermatocyte

  • ventricular zone

  • tail of embryo

  • esophagus

  • embryo

  • embryo

  • dentate gyrus of hippocampal formation granule cell

  • blastocyst

  • yolk sac
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
SpeciesHumanMouse
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 MbChr 10: 95.35 – 95.38 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

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:

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000177889 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000074781 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  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. ^ a b "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. S2CID 29442841.
  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. Bibcode:2008PNAS..105.3768U. doi:10.1073/pnas.0800563105. PMC 2268824. PMID 18316726.
  9. ^ a b c 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. S2CID 18154645.

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.
  • v
  • t
  • e
  • 1j7d: Crystal Structure of hMms2-hUbc13
    1j7d: Crystal Structure of hMms2-hUbc13
  • 2c2v: CRYSTAL STRUCTURE OF THE CHIP-UBC13-UEV1A COMPLEX
    2c2v: CRYSTAL STRUCTURE OF THE CHIP-UBC13-UEV1A COMPLEX
  • v
  • t
  • e
Chaperones/
protein folding
Heat shock proteins/
Chaperonins
Other
Protein targeting
Ubiquitin
(ubiquitylation)
Ubiquitin-like proteins
(UBL)
SUMO protein
(SUMOylation)
  • E1 SUMO-activating enzyme
  • E2 SUMO-conjugating enzyme
Other


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