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 Contents Function ; Interactions ; References ; Further reading ;
Identifiers
Aliases	UBE2N , HEL-S-71, UBC13, UBCHBEN; UBC13, UbcH-ben, UbcH13, ubiquitin conjugating enzyme E2 N
External IDs	OMIM: 603679 MGI: 1934835 HomoloGene: 128406 GeneCards: UBE2N
Gene location (Human)
Chr.	Chromosome 12 (human)
End	93,441,947 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	95,545,657 bp
RNA expression pattern
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	• transferase activity ; • nucleotide binding ; • GO:1904264, GO:1904822, GO:0090622, GO:0090302 ubiquitin protein ligase activity ; • ubiquitin binding ; • GO:0001948 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 ; • 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
	7334
	93765
	ENSG00000177889
	ENSMUSG00000074781
	P61088
	P61089
	NM_003348
	NM_080560
	NP_003339
	NP_542127
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated December 08, 2020

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:

Related Research Articles

Ubiquitin is a small regulatory protein found in most tissues of eukaryotic organisms, i.e., it is found ubiquitously. It was discovered in 1975 by Gideon Goldstein and further characterized throughout the 1970s and 1980s. Four genes in the human genome code for ubiquitin: UBB, UBC, UBA52 and RPS27A.

Ubiquitin-protein ligase E3A (UBE3A) also known as E6AP ubiquitin-protein ligase (E6AP) is an enzyme that in humans is encoded by the UBE3A gene. This enzyme is involved in targeting proteins for degradation within cells.

Ubiquitin-conjugating enzymes, also known as E2 enzymes and more rarely as ubiquitin-carrier enzymes, perform the second step in the ubiquitination reaction that targets a protein for degradation via the proteasome. The ubiquitination process covalently attaches ubiquitin, a short protein of 76 amino acids, to a lysine residue on the target protein. Once a protein has been tagged with one ubiquitin molecule, additional rounds of ubiquitination form a polyubiquitin chain that is recognized by the proteasome's 19S regulatory particle, triggering the ATP-dependent unfolding of the target protein that allows passage into the proteasome's 20S core particle, where proteases degrade the target into short peptide fragments for recycling by the cell.

Polyubiquitin-C is a protein encoded by the UBC gene in humans. Polyubiquitin-C is one of the sources of ubiquitin, along with UBB, UBA52, and RPS27A.

Ubiquitin-conjugating enzyme E2 L3 (UBE2L3), also called UBCH7, is a protein that in humans is encoded by the UBE2L3 gene. As an E2 enzyme, UBE2L3 participates in ubiquitination to target proteins for degradation. The role of UBE2L3 in the ubiquitination of the NF-κB precursor implicated it in various major autoimmune diseases, including rheumatoid arthritis (RA), celiac disease, Crohn's disease(CD), and systemic lupus erythematosus.

CDC34 is a gene encoding a protein product that has ubiquitin conjugating activity. CDC34 was originally discovered by work in baker's yeast as a gene that has a role in the cell division cycle. Cdc34 in yeast targets numerous substrates for ubiquitin mediated degradation. Ubiquitin-conjugating enzyme E2 R1 is a protein that in humans is encoded by the CDC34 gene.

Ubiquitin-conjugating enzyme E2 D1 is a protein that in humans is encoded by the UBE2D1 gene.

Ubiquitin-conjugating enzyme E2 D2 is a protein that in humans is encoded by the UBE2D2 gene.

Ubiquitin-conjugating enzyme E2 G2 is a protein that in humans is encoded by the UBE2G2 gene.

Ubiquitin-conjugating enzyme E2 variant 2 is a protein that in humans is encoded by the UBE2V2 gene. Ubiquitin-conjugating enzyme E2 variant proteins constitute a distinct subfamily within the E2 protein family.

Ubiquitin-conjugating enzyme E2 E3 is a protein that in humans is encoded by the UBE2E3 gene.

Ubiquitin/ISG15-conjugating enzyme E2 L6 is a protein that in humans is encoded by the UBE2L6 gene.

Ubiquitin-conjugating enzyme E2 variant 1 is a protein that in humans is encoded by the UBE2V1 gene.

Ubiquitin-conjugating enzyme E2 C is a protein that in humans is encoded by the UBE2C gene.

Ubiquitin-conjugating enzyme E2 G1 is a protein that in humans is encoded by the UBE2G1 gene.

Ubiquitin-conjugating enzyme E2 H is a protein that in humans is encoded by the UBE2H gene.

Ubiquitin-conjugating enzyme E2 E1 is a protein that in humans is encoded by the UBE2E1 gene.

Ubiquitin-conjugating enzyme E2 variant 1, also known as Kua-UEV, is a human gene.

Ubiquitin-conjugating enzyme E2 J1 is a protein that in humans is encoded by the UBE2J1 gene.

NEDD8-conjugating enzyme Ubc12 is a protein that in humans is encoded by the UBE2M gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000177889 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000074781 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
1 2 "Entrez Gene: UBE2N ubiquitin-conjugating enzyme E2N (UBC13 homolog, yeast)".
↑ 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.
↑ 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.
1 2 3 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.

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. 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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000177889 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid8902611-5] 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.

[entrez-6] 1 2 "Entrez Gene: UBE2N ubiquitin-conjugating enzyme E2N (UBC13 homolog, yeast)".

[pmid12881723-7] 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.

[pmid18316726-8] 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.

[pmid11057907-9] 1 2 3 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.

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UBE2N

Contents

Function

Interactions

Related Research Articles

References

Further reading