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Q13404 (UB2V1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 variant 1

Short name=UEV-1
Alternative name(s):
CROC-1
TRAF6-regulated IKK activator 1 beta Uev1A
Gene names
Name:UBE2V1
Synonyms:CROC1, UBE2V, UEV1
ORF Names:P/OKcl.19
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has no ubiquitin ligase activity on its own. The UBE2V1-UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through Lys-63. This type of poly-ubiquitination activates IKK and does not seem to involve protein degradation by the proteasome. Plays a role in the activation of NF-kappa-B mediated by IL1B, TNF, TRAF6 and TRAF2. 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. 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. Ref.1 Ref.2 Ref.3 Ref.10 Ref.11 Ref.13 Ref.14

Subunit structure

Heterodimer with UBE2N. 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 TRAF6. Ref.3

Subcellular location

Nucleus. Note: Excluded from the nucleolus. Ref.1 Ref.12

Tissue specificity

Highly expressed in thyroid, pancreas, spinal cord, lymph node, trachea, adrenal gland, bone marrow and pancreas. Detected at low levels in heart, breast, placenta, brain, liver, kidney, stomach and lung. Ref.2 Ref.11

Induction

Down-regulated during differentiation of cultured colon adenocarcinoma cells. Ref.2

Miscellaneous

In human, TMEM189/KUA and UBE2V1/UEV1 are adjacent genes which can produce independent proteins and can also be fused to form a TMEM189-UBE2V1 hybrid protein.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence caution

The sequence AAH08944.2 differs from that shown. Reason: Erroneous initiation.

The sequence CAC16955.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-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

Traceable author statement. Source: Reactome

cell differentiation

Non-traceable author statement Ref.2. Source: UniProtKB

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 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 16129784. Source: HGNC

positive regulation of transcription, DNA-templated

Traceable author statement Ref.1. Source: UniProtKB

protein K63-linked ubiquitination

Inferred from direct assay Ref.16Ref.14. Source: UniProtKB

protein polyubiquitination

Traceable author statement PubMed 10089880. Source: ProtInc

regulation of DNA repair

Traceable author statement PubMed 10089880. Source: ProtInc

regulation of transcription, DNA-templated

Traceable author statement Ref.1. Source: UniProtKB

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

   Cellular_componentUBC13-UEV1A complex

Inferred from direct assay Ref.16. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 16129784. Source: HGNC

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nucleus

Traceable author statement Ref.1. Source: UniProtKB

ubiquitin conjugating enzyme complex

Inferred from direct assay PubMed 16129784. Source: HGNC

ubiquitin ligase complex

Inferred from direct assay Ref.16. Source: UniProtKB

   Molecular_functionacid-amino acid ligase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 3 (identifier: Q13404-4)

Also known as: Isoform 2;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 1 (identifier: Q13404-1)

Also known as: CROC-1B; UEV-1B; Isoform 4;

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MAATTGS → MAYKFRTHSP...PHETYFCITT
Isoform 2 (identifier: Q13404-2)

Also known as: CROC-1A; UEV-1A;

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: MAATTGSGVKVPRN → MPGEVQASYLKSQSKLSDEGRLEPRKFHCKGSKSPSQ
Isoform 4 (identifier: Q13404-6)

Also known as: UEV-1As;

The sequence of this isoform differs from the canonical sequence as follows:
     1-44: Missing.
     45-57: LTRWTGMIIGPPR → MKEDLNLENFTAK
Isoform 5 (identifier: Q13404-7)

Also known as: Isoform 3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MAATTGS → MPGEVQASYLKSQSKLSDEGRLEPRKFHCK
Isoform 6 (identifier: Q13404-8)

The sequence of this isoform differs from the canonical sequence as follows:
     58-99: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 147146Ubiquitin-conjugating enzyme E2 variant 1
PRO_0000082600

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.15

Natural variations

Alternative sequence1 – 4444Missing in isoform 4.
VSP_038032
Alternative sequence1 – 1414MAATT…KVPRN → MPGEVQASYLKSQSKLSDEG RLEPRKFHCKGSKSPSQ in isoform 2.
VSP_038033
Alternative sequence1 – 77MAATTGS → MAYKFRTHSPEALEQLYPWE CFVFCLIIFGTFTNQIHKWS HTYFGLPRWVTLLQDWHVIL PRKHHRIHHVSPHETYFCIT T in isoform 1.
VSP_038034
Alternative sequence1 – 77MAATTGS → MPGEVQASYLKSQSKLSDEG RLEPRKFHCK in isoform 5.
VSP_038035
Alternative sequence45 – 5713LTRWT…IGPPR → MKEDLNLENFTAK in isoform 4.
VSP_038036
Alternative sequence58 – 9942Missing in isoform 6.
VSP_044818

Experimental info

Isoform 1:
Sequence conflict71 – 8111SPHETYFCITT → WPTSSAQCYSP in AAC02755. Ref.2

Secondary structure

............................ 147
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 (Isoform 2) [UniParc].

Last modified September 22, 2009. Version 2.
Checksum: BA53837F21977B3F

FASTA14716,495
        10         20         30         40         50         60 
MAATTGSGVK VPRNFRLLEE LEEGQKGVGD GTVSWGLEDD EDMTLTRWTG MIIGPPRTIY 

        70         80         90        100        110        120 
ENRIYSLKIE CGPKYPEAPP FVRFVTKINM NGVNSSNGVV DPRAISVLAK WQNSYSIKVV 

       130        140 
LQELRRLMMS KENMKLPQPP EGQCYSN 

« Hide

Isoform 1 (CROC-1B) (UEV-1B) (Isoform 4) [UniParc].

Checksum: 6EE5C0FCC8CBBEE6
Show »

FASTA22125,797
Isoform 2 (CROC-1A) (UEV-1A) [UniParc].

Checksum: 9D3A8AC1EBEB22A6
Show »

FASTA17019,228
Isoform 4 (UEV-1As) [UniParc].

Checksum: 76C152A73DE9AC40
Show »

FASTA10311,842
Isoform 5 (Isoform 3) [UniParc].

Checksum: 5B2E8C6FFDF51510
Show »

FASTA17019,307
Isoform 6 [UniParc].

Checksum: D7C2659FBA3FC719
Show »

FASTA10511,766

References

« Hide 'large scale' references
[1]"CROC-1 encodes a protein which mediates transcriptional activation of the human FOS promoter."
Rothofsky M.L., Lin S.L.
Gene 195:141-149(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION.
Tissue: Brain.
[2]"Role of UEV-1, an inactive variant of the E2 ubiquitin-conjugating enzymes, in in vitro differentiation and cell cycle behavior of HT-29-M6 intestinal mucosecretory cells."
Sancho E., Vila M.R., Sanchez-Pulido L., Lozano J.J., Paciucci R., Nadal M., Fox M., Harvey C., Bercovich B., Loukili N., Ciechanover A., Lin S.L., Sanz F., Estivill X., Valencia A., Thomson T.M.
Mol. Cell. Biol. 18:576-589(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), FUNCTION, INDUCTION, TISSUE SPECIFICITY.
Tissue: Colon adenocarcinoma.
[3]"Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain."
Deng L., Wang C., Spencer E., Yang L., Braun A., You J., Slaughter C., Pickart C., Chen Z.J.
Cell 103:351-361(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), FUNCTION, INTERACTION WITH TRAF6 AND UBE2N, IDENTIFICATION BY MASS SPECTROMETRY.
[4]"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] (ISOFORM 3).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
Tissue: Lung.
[6]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Bienvenut W.V., Pchelintsev N., Adams P.D.
Submitted (JUL-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13 (ISOFORM 3), CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Lung fibroblast.
[9]"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] OF 8-147 (ISOFORMS 1 AND 3).
Tissue: Muscle.
[10]"Role of UEV-1A, a homologue of the tumor suppressor protein TSG101, in protection from DNA damage."
Thomson T.M., Khalid H., Lozano J.J., Sancho E., Arino J.
FEBS Lett. 423:49-52(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"The products of the yeast MMS2 and two human homologs (hMMS2 and CROC-1) define a structurally and functionally conserved Ubc-like protein family."
Xiao W., Lin S.L., Broomfield S., Chow B.L., Wei Y.-F.
Nucleic Acids Res. 26:3908-3914(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[12]"Fusion of the human gene for the polyubiquitination coeffector UEV1 with Kua, a newly identified gene."
Thomson T.M., Lozano J.J., Loukili N., Carrio R., Serras F., Cormand B., Valeri M., Diaz V.M., Abril J., Burset M., Merino J., Macaya A., Corominas M., Guigo R.
Genome Res. 10:1743-1756(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, IDENTIFICATION OF TMEM189-UBE2V1 FUSION PROTEIN.
Tissue: Colon cancer.
[13]"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.
[14]"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.
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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 8-147 IN COMPLEX WITH STUB1 AND UBE2N.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U39360 mRNA. Translation: AAB72015.1.
U39361 mRNA. Translation: AAB72016.1.
U49278 mRNA. Translation: AAC02757.1.
U97279 mRNA. Translation: AAC02780.1.
U97280 mRNA. Translation: AAC02755.1.
U97281 mRNA. Translation: AAC02756.1.
AY008273 mRNA. Translation: AAG24229.1.
BT007382 mRNA. Translation: AAP36046.1.
DA580976 mRNA. No translation available.
AL034423 Genomic DNA. Translation: CAB76864.1.
AL034423 Genomic DNA. Translation: CAB76865.1.
AL034423 Genomic DNA. Translation: CAC16954.1.
AL034423 Genomic DNA. Translation: CAC16955.2. Different initiation.
AL034423 Genomic DNA. Translation: CAI19382.1.
AL034423 Genomic DNA. Translation: CAI19383.1.
CH471077 Genomic DNA. Translation: EAW75635.1.
CH471077 Genomic DNA. Translation: EAW75634.1.
CH471077 Genomic DNA. Translation: EAW75636.1.
BC000468 mRNA. Translation: AAH00468.1.
BC008944 mRNA. Translation: AAH08944.2. Different initiation.
RefSeqNP_001027459.1. NM_001032288.2.
NP_001244322.1. NM_001257393.1.
NP_001244323.1. NM_001257394.1.
NP_001244325.1. NM_001257396.1.
NP_068823.2. NM_021988.5.
NP_071887.1. NM_022442.5.
NP_954595.1. NM_199144.2.
NP_954673.1. NM_199203.2.
UniGeneHs.420529.
Hs.744839.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A4DX-ray1.69A8-147[»]
2C2VX-ray2.90C/F/I/L8-147[»]
2HLWNMR-A8-147[»]
ProteinModelPortalQ13404.
SMRQ13404. Positions 8-146.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113183. 67 interactions.
132321. 2 interactions.
DIPDIP-41911N.
IntActQ13404. 27 interactions.
MINTMINT-5002796.

Polymorphism databases

DMDM259016163.

Proteomic databases

PaxDbQ13404.
PRIDEQ13404.

Protocols and materials databases

DNASU387522.
7335.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340309; ENSP00000340305; ENSG00000244687. [Q13404-7]
ENST00000371657; ENSP00000360720; ENSG00000244687. [Q13404-8]
ENST00000371674; ENSP00000360739; ENSG00000244687. [Q13404-4]
ENST00000371677; ENSP00000360742; ENSG00000244687. [Q13404-7]
ENST00000415862; ENSP00000407770; ENSG00000244687. [Q13404-6]
ENST00000420027; ENSP00000395264; ENSG00000244687. [Q13404-6]
GeneID387522.
7335.
KEGGhsa:387522.
hsa:7335.
UCSCuc002xva.4. human. [Q13404-4]
uc002xvc.4. human. [Q13404-6]
uc002xvd.4. human. [Q13404-7]
uc031rtz.1. human.

Organism-specific databases

CTD387522.
7335.
GeneCardsGC20M048698.
HGNCHGNC:12494. UBE2V1.
MIM602995. gene.
neXtProtNX_Q13404.
PharmGKBPA37142.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG119330.
HOVERGENHBG054552.
InParanoidQ13404.
KOK10704.
OMATVHENRI.
OrthoDBEOG77M8R5.
TreeFamTF316971.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ13404.

Gene expression databases

BgeeQ13404.
GenevestigatorQ13404.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE2V1. human.
EvolutionaryTraceQ13404.
GeneWikiUBE2V1.
NextBio101372.
PROQ13404.
SOURCESearch...

Entry information

Entry nameUB2V1_HUMAN
AccessionPrimary (citable) accession number: Q13404
Secondary accession number(s): E1P629 expand/collapse secondary AC list , Q13403, Q13532, Q5TGE0, Q5TGE3, Q96H34, Q9GZT0, Q9GZW1, Q9H4J3, Q9H4J4, Q9UKL1, Q9UM48, Q9UM49, Q9UM50
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: September 22, 2009
Last modified: April 16, 2014
This is version 142 of the entry and version 2 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

MIM cross-references

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

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM