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P61088 (UBE2N_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 N

EC=6.3.2.19
Alternative name(s):
Bendless-like ubiquitin-conjugating enzyme
Ubc13
UbcH13
Ubiquitin carrier protein N
Ubiquitin-protein ligase N
Gene names
Name:UBE2N
Synonyms:BLU
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes By similarity. Ref.6 Ref.7 Ref.16 Ref.20 Ref.23

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Enzyme regulation

Activity is inhibited by binding to OTUB1, which prevents 'Lys-63'-linked polyubiquitination. Ref.21 Ref.29 Ref.30

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Heterodimer with UBE2V2. Interacts (UBE2V2-UBE2N heterodimer) with the E3 ligase STUB1 (via the U-box domain); the complex has a specific 'Lys-63'-linked polyubiquitination activity. Interacts with RNF8 and RNF168. Interacts with RNF11. Interacts with the E3 ligases, HLTF and SHPRH; the interactions promote the 'Lys-63'-linked polyubiquitination of PCNA upon genotoxic stress and lead to DNA repair. Interacts with ARIH2 (via RING-type 2). Interacts with OTUB1; leading to inhibit E2-conjugating activity. Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.21 Ref.29 Ref.30

Subcellular location

Nucleus. Cytoplasm Ref.17.

Post-translational modification

Conjugation to ISG15 impairs formation of the thioester bond with ubiquitin but not interaction with UBE2V2.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMAcetylation
Disulfide bond
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA double-strand break processing

Inferred from mutant phenotype PubMed 17349954. Source: HGNC

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

T cell receptor signaling pathway

Inferred from mutant phenotype PubMed 15125833. Source: UniProtKB

cellular protein modification process

Traceable author statement Ref.1. Source: ProtInc

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

double-strand break repair via homologous recombination

Inferred from mutant phenotype PubMed 17349954. Source: HGNC

histone ubiquitination

Inferred from mutant phenotype PubMed 17349954. Source: HGNC

innate immune response

Traceable author statement. Source: Reactome

nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway

Traceable author statement. Source: Reactome

nucleotide-binding oligomerization domain containing signaling pathway

Traceable author statement. Source: Reactome

positive regulation of DNA repair

Inferred from mutant phenotype PubMed 16129784. Source: HGNC

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 16129784. Source: HGNC

positive regulation of NF-kappaB transcription factor activity

Inferred from mutant phenotype PubMed 14695475. Source: UniProtKB

positive regulation of histone modification

Inferred from mutant phenotype PubMed 17349954. Source: HGNC

positive regulation of ubiquitin-protein ligase activity

Inferred from mutant phenotype PubMed 17349954. Source: HGNC

postreplication repair

Inferred from mutant phenotype PubMed 17349954. Source: HGNC

protein K63-linked ubiquitination

Inferred from direct assay Ref.27Ref.20Ref.23. Source: UniProtKB

protein ubiquitination

Inferred from mutant phenotype PubMed 17349954. Source: HGNC

proteolysis

Traceable author statement Ref.1. Source: ProtInc

regulation of DNA repair

Traceable author statement Ref.6. Source: ProtInc

regulation of histone ubiquitination

Inferred from mutant phenotype PubMed 17349954. Source: HGNC

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentUBC13-MMS2 complex

Inferred from direct assay PubMed 16129784. Source: HGNC

UBC13-UEV1A complex

Inferred from direct assay Ref.27. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.17. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nucleus

Inferred from direct assay Ref.17. Source: UniProtKB

ubiquitin ligase complex

Inferred from direct assay Ref.27. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

ubiquitin binding

Inferred from direct assay Ref.5. Source: HGNC

ubiquitin-protein ligase activity

Inferred from direct assay Ref.20. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 152152Ubiquitin-conjugating enzyme E2 N
PRO_0000082502

Sites

Active site871Glycyl thioester intermediate

Amino acid modifications

Modified residue821N6-acetyllysine Ref.19
Disulfide bond87Interchain (with C-78 in ISG15) Ref.25
Cross-link92Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) Ref.5 Ref.8

Experimental info

Mutagenesis871C → A: Loss of polyubiquitination of PCNA. Impairs interaction with SHPRH. Ref.9 Ref.12
Mutagenesis921K → R: No ISGylation. Ref.5 Ref.8
Mutagenesis941K → R: No effect on ISGylation. Ref.8

Secondary structure

......................... 152
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P61088 [UniParc].

Last modified April 26, 2004. Version 1.
Checksum: FACD84D883D77407

FASTA15217,138
        10         20         30         40         50         60 
MAGLPRRIIK ETQRLLAEPV PGIKAEPDES NARYFHVVIA GPQDSPFEGG TFKLELFLPE 

        70         80         90        100        110        120 
EYPMAAPKVR FMTKIYHPNV DKLGRICLDI LKDKWSPALQ IRTVLLSIQA LLSAPNPDDP 

       130        140        150 
LANDVAEQWK TNEAQAIETA RAWTRLYAMN NI 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of cDNA encoding a human ubiquitin-conjugating enzyme similar to the Drosophila bendless gene product."
Yamaguchi T., Kim N.-S., Sekine S., Seino H., Osaka F., Yamao F., Kato S.
J. Biochem. 120:494-497(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung, Placenta and Uterus.
[4]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 15-24; 34-68; 86-92 AND 95-102, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[5]"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. 336:61-68(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 86-94, MUTAGENESIS OF LYS-92, ISGYLATION AT LYS-92, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair."
Hofmann R.M., Pickart C.M.
Cell 96:645-653(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH UBE2V2.
[7]"The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form Lys63-linked polyubiquitin chains."
Bothos J., Summers M.K., Venere M., Scolnick D.M., Halazonetis T.D.
Oncogene 22:7101-7107(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH UBE2V2.
[8]"ISG15 modification of Ubc13 suppresses its ubiquitin-conjugating activity."
Takeuchi T., Yokosawa H.
Biochem. Biophys. Res. Commun. 336:9-13(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF LYS-92 AND LYS-94, ISGYLATION AT LYS-92.
[9]"Human SHPRH suppresses genomic instability through proliferating cell nuclear antigen polyubiquitination."
Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K.
J. Cell Biol. 175:703-708(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHPRH, MUTAGENESIS OF CYS-87.
[10]"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. 97:572-582(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF8.
[11]"Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen."
Unk I., Hajdu I., Fatyol K., Szakal B., Blastyak A., Bermudez V., Hurwitz J., Prakash L., Prakash S., Haracska L.
Proc. Natl. Acad. Sci. U.S.A. 103:18107-18112(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHPRH.
[12]"Site-specific Lys-63-linked tumor necrosis factor receptor-associated factor 6 auto-ubiquitination is a critical determinant of I kappa B kinase activation."
Lamothe B., Besse A., Campos A.D., Webster W.K., Wu H., Darnay B.G.
J. Biol. Chem. 282:4102-4112(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-87.
[13]"Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear antigen polyubiquitination."
Unk I., Hajdu I., Fatyol K., Hurwitz J., Yoon J.-H., Prakash L., Prakash S., Haracska L.
Proc. Natl. Acad. Sci. U.S.A. 105:3768-3773(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HLTF.
[14]"Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks."
Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X., Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.
Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HLTF.
[15]"The RIDDLE syndrome protein mediates a ubiquitin-dependent signaling cascade at sites of DNA damage."
Stewart G.S., Panier S., Townsend K., Al-Hakim A.K., Kolas N.K., Miller E.S., Nakada S., Ylanko J., Olivarius S., Mendez M., Oldreive C., Wildenhain J., Tagliaferro A., Pelletier L., Taubenheim N., Durandy A., Byrd P.J., Stankovic T., Taylor A.M.R., Durocher D.
Cell 136:420-434(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF168.
[16]"Regulation of endoplasmic reticulum-associated degradation by RNF5-dependent ubiquitination of JNK-associated membrane protein (JAMP)."
Tcherpakov M., Delaunay A., Toth J., Kadoya T., Petroski M.D., Ronai Z.A.
J. Biol. Chem. 284:12099-12109(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN UBIQUITINATION OF JKAMP.
[17]"The ubiquitin ligase Triad1 inhibits myelopoiesis through UbcH7 and Ubc13 interacting domains."
Marteijn J.A., van der Meer L.T., Smit J.J., Noordermeer S.M., Wissink W., Jansen P., Swarts H.G., Hibbert R.G., de Witte T., Sixma T.K., Jansen J.H., van der Reijden B.A.
Leukemia 23:1480-1489(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARIH2, SUBCELLULAR LOCATION.
[18]"Analysis of electrostatic contributions to the selectivity of interactions between RING-finger domains and ubiquitin-conjugating enzymes."
Scheper J., Oliva B., Villa-Freixa J., Thomson T.M.
Proteins 74:92-103(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF11.
[19]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
David Y., Ziv T., Admon A., Navon A.
J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1."
Nakada S., Tai I., Panier S., Al-Hakim A., Iemura S., Juang Y.C., O'Donnell L., Kumakubo A., Munro M., Sicheri F., Gingras A.C., Natsume T., Suda T., Durocher D.
Nature 466:941-946(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION, INTERACTION WITH OTUB1.
[22]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"TRIM5 is an innate immune sensor for the retrovirus capsid lattice."
Pertel T., Hausmann S., Morger D., Zueger S., Guerra J., Lascano J., Reinhard C., Santoni F.A., Uchil P.D., Chatel L., Bisiaux A., Albert M.L., Strambio-De-Castillia C., Mothes W., Pizzato M., Gruetter M.G., Luban J.
Nature 472:361-365(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[24]"A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1 interacting protein required for ATR signaling."
Cotta-Ramusino C., McDonald E.R. III, Hurov K., Sowa M.E., Harper J.W., Elledge S.J.
Science 332:1313-1317(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[25]"Covalent protein modification with ISG15 via a conserved cysteine in the hinge region."
Bade V.N., Nickels J., Keusekotten K., Praefcke G.J.
PLoS ONE 7:E38294-E38294(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION, DISULFIDE BOND.
[26]"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.M., Ellison M.J.
Nat. Struct. Biol. 8:669-673(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH UBE2V2.
[27]"Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex."
Zhang M., Windheim M., Roe S.M., Peggie M., Cohen P., Prodromou C., Pearl L.H.
Mol. Cell 20:525-538(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 2-152 IN COMPLEX WITH STUB1 AND UBE2V1.
[28]"Molecular insights into the function of RING Finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation."
Campbell S.J., Edwards R.A., Leung C.C., Neculai D., Hodge C.D., Dhe-Paganon S., Glover J.N.
J. Biol. Chem. 287:23900-23910(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (4.8 ANGSTROMS) OF 1-150 IN COMPLEX WITH RNF8 AND UBE2V2.
[29]"OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2 enzyme function."
Juang Y.C., Landry M.C., Sanches M., Vittal V., Leung C.C., Ceccarelli D.F., Mateo A.R., Pruneda J.N., Mao D.Y., Szilard R.K., Orlicky S., Munro M., Brzovic P.S., Klevit R.E., Sicheri F., Durocher D.
Mol. Cell 45:384-397(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-271 IN COMPLEX WITH UBE2V2 AND OTUB1, ENZYME REGULATION, INTERACTION WITH OTUB1.
[30]"The mechanism of OTUB1-mediated inhibition of ubiquitination."
Wiener R., Zhang X., Wang T., Wolberger C.
Nature 483:618-622(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.11 ANGSTROMS) IN COMPLEX WITH OUTB1 AND UBIQUITIN, ENZYME REGULATION, INTERACTION WITH OTUB1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D83004 mRNA. Translation: BAA11675.1.
BT006873 mRNA. Translation: AAP35519.1.
BC000396 mRNA. Translation: AAH00396.1.
BC003365 mRNA. Translation: AAH03365.1.
BC108704 mRNA. Translation: AAI08705.1.
PIRJC4894.
RefSeqNP_003339.1. NM_003348.3.
UniGeneHs.524630.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J7DX-ray1.85B1-152[»]
2C2VX-ray2.90B/E/H/K2-152[»]
3HCTX-ray2.10B1-152[»]
3HCUX-ray2.60B/D1-152[»]
3VONX-ray3.15C/E/G/J/L/N/Q/S/U/X/Z/b/e/g/i/l/n/p3-150[»]
3W31X-ray2.96B1-152[»]
4DHIX-ray1.80D1-152[»]
4DHJX-ray2.35C/G/K/N1-152[»]
4DHZX-ray3.11F1-152[»]
4IP3X-ray2.30B1-152[»]
4ORHX-ray4.80B/F/J1-150[»]
ProteinModelPortalP61088.
SMRP61088. Positions 3-152.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113182. 127 interactions.
DIPDIP-29829N.
IntActP61088. 57 interactions.
MINTMINT-5001139.
STRING9606.ENSP00000316176.

Chemistry

BindingDBP61088.
ChEMBLCHEMBL6089.

PTM databases

PhosphoSiteP61088.

Polymorphism databases

DMDM46577660.

2D gel databases

OGPQ16781.
REPRODUCTION-2DPAGEIPI00003949.

Proteomic databases

PaxDbP61088.
PeptideAtlasP61088.
PRIDEP61088.

Protocols and materials databases

DNASU7334.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318066; ENSP00000316176; ENSG00000177889.
GeneID7334.
KEGGhsa:7334.
UCSCuc001tcp.3. human.

Organism-specific databases

CTD7334.
GeneCardsGC12M093735.
HGNCHGNC:12492. UBE2N.
HPAHPA003962.
HPA044976.
MIM603679. gene.
neXtProtNX_P61088.
PharmGKBPA37141.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000233455.
HOVERGENHBG063308.
InParanoidP61088.
KOK10580.
OMADVAKHYK.
OrthoDBEOG7XWPQB.
PhylomeDBP61088.
TreeFamTF101126.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkP61088.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressP61088.
BgeeP61088.
CleanExHS_UBE2N.
GenevestigatorP61088.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE2N. human.
EvolutionaryTraceP61088.
GeneWikiUBE2N.
GenomeRNAi7334.
NextBio28704.
PROP61088.
SOURCESearch...

Entry information

Entry nameUBE2N_HUMAN
AccessionPrimary (citable) accession number: P61088
Secondary accession number(s): Q16781, Q53Y81
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: April 16, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM