UBE2N

From Wikipedia, the free encyclopedia

Ubiquitin-conjugating enzyme E2N

PDB rendering based on 1j7d.

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
1J7D, 2C2V, 3HCT, 3HCU, 3VON, 3W31, 4DHI, 4DHJ, 4DHZ, 4EPO, 4IP3

Identifiers

Symbols

UBE2N; UBC13; UbcH-ben; UbcH13

External IDs

OMIM: 603679 MGI: 1934835 HomoloGene: 100734 ChEMBL: 6089 GeneCards: UBE2N Gene

EC number

6.3.2.19

Gene Ontology
Molecular function	• ubiquitin-protein ligase activity • protein binding • ATP binding • ubiquitin binding
Cellular component	• ubiquitin ligase complex • nucleus • cytoplasm • cytosol • UBC13-MMS2 complex • UBC13-UEV1A complex
Biological process	• double-strand break repair via homologous recombination • DNA double-strand break processing • toll-like receptor signaling pathway • MyD88-dependent toll-like receptor signaling pathway • regulation of DNA repair • postreplication repair • cellular protein modification process • proteolysis • ubiquitin-dependent protein catabolic process • protein ubiquitination • histone ubiquitination • cytokine-mediated signaling pathway • positive regulation of histone modification • regulation of histone ubiquitination • toll-like receptor 2 signaling pathway • toll-like receptor 4 signaling pathway • toll-like receptor 5 signaling pathway • toll-like receptor 9 signaling pathway • toll-like receptor 10 signaling pathway • nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway • toll-like receptor TLR1:TLR2 signaling pathway • toll-like receptor TLR6:TLR2 signaling pathway • positive regulation of I-kappaB kinase/NF-kappaB cascade • innate immune response • positive regulation of DNA repair • T cell receptor signaling pathway • positive regulation of NF-kappaB transcription factor activity • positive regulation of ubiquitin-protein ligase activity • nucleotide-binding oligomerization domain containing signaling pathway • protein K63-linked ubiquitination
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 12:
93.8 – 93.84 Mb

Chr 10:
94.98 – 95.01 Mb

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]

Interactions

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

References

↑ 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. PMID 8902611.
↑ 2.0 2.1 "Entrez Gene: UBE2N ubiquitin-conjugating enzyme E2N (UBC13 homolog, yeast)".
↑ 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. doi:10.1038/ng1220. ISSN 1061-4036. PMID 12881723. Cite uses deprecated parameters (help)
↑ 4.0 4.1 4.2 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. doi:10.1016/S0092-8674(00)00126-4. ISSN 0092-8674. PMID 11057907. Cite uses deprecated parameters (help)
↑ 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". Proc. Natl. Acad. Sci. U.S.A. (United States) 105 (10): 3768–73. doi:10.1073/pnas.0800563105. PMC 2268824. PMID 18316726. Cite uses deprecated parameters (help)

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, 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. 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, et al. (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, et al. (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.
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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
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. doi:10.1074/jbc.M212353200. PMID 12569095.
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. doi:10.1016/S1074-7613(03)00084-0. PMID 12705856.
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. doi:10.1038/ng1220. PMID 12881723.
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. doi:10.1038/sj.onc.1206831. PMID 14562038.
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. doi:10.1038/nature02273. PMID 14695475.
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. doi:10.1038/ng1285. PMID 14702039.
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. doi:10.1016/S1097-2765(04)00236-9. PMID 15125833.
Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway.". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
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. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
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, 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. doi:10.1016/j.bbrc.2005.08.038. PMID 16122702.

PDB gallery

1j7d: Crystal Structure of hMms2-hUbc13

2c2v: CRYSTAL STRUCTURE OF THE CHIP-UBC13-UEV1A COMPLEX

Posttranslational modification

Chaperones/
protein folding

Heat shock proteins/ Chaperonins	Hsp10/GroES Early pregnancy factor 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

ATG3
BIRC6
UFC1

Other

Ubiquitin-like modifiers
- SUMO protein
- ISG15
- URM1
- NEDD8
- FAT10
- ATG8
- ATG12
- FUB1
- MUB
- UFM1
- UBL5

See also: posttranslational modification disorders
B bsyn: dna (repl, cycl, reco, repr) · tscr (fact, tcrg, nucl, rnat, rept, ptts) · tltn (risu, pttl, nexn) · dnab, rnab/runp · stru (domn, 1°, 2°, 3°, 4°)

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UBE2N

Interactions

References

Further reading