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Q15819 (UB2V2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 variant 2
Alternative name(s):
DDVit 1
Enterocyte differentiation-associated factor 1
Short name=EDAF-1
Enterocyte differentiation-promoting factor 1
Short name=EDPF-1
MMS2 homolog
Vitamin D3-inducible protein
Gene names
Name:UBE2V2
Synonyms:MMS2, UEV2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length145 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 UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination 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. Ref.2 Ref.8 Ref.9 Ref.10

Subunit structure

Heterodimer with UBE2N. Binds CHFR.

Tissue specificity

Detected in placenta, colon, liver and skin. Detected at very low levels in most tissues. Ref.1 Ref.2

Induction

Up-regulated in cultured fresh blood cells upon treatment with vitamin D3. Ref.1

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Coding sequence diversityPolymorphism
   PTMAcetylation
   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

cell proliferation

Traceable author statement PubMed 9418904. Source: ProtInc

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of DNA repair

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of synapse assembly

Inferred from electronic annotation. Source: Ensembl

protein polyubiquitination

Traceable author statement Ref.8. Source: ProtInc

protein ubiquitination

Traceable author statement PubMed 16129784. Source: HGNC

regulation of DNA repair

Traceable author statement Ref.8. Source: ProtInc

   Cellular_componentUBC13-MMS2 complex

Inferred from direct assay PubMed 16129784. Source: HGNC

cytoplasm

Traceable author statement PubMed 16129784. Source: HGNC

nucleus

Inferred from direct assay PubMed 16129784. Source: HGNC

   Molecular_functionacid-amino acid ligase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.13PubMed 16786304PubMed 19549727. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

UBC35Q94A973EBI-714329,EBI-994120From a different organism.
UBE2NP610883EBI-714329,EBI-1052908

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7 Ref.12
Chain2 – 145144Ubiquitin-conjugating enzyme E2 variant 2
PRO_0000082602

Amino acid modifications

Modified residue21N-acetylalanine Ref.12

Natural variations

Natural variant361E → G.
Corresponds to variant rs11557776 [ dbSNP | Ensembl ].
VAR_052431
Natural variant401D → H.
Corresponds to variant rs14890 [ dbSNP | Ensembl ].
VAR_052432
Natural variant781P → Q.
Corresponds to variant rs11557786 [ dbSNP | Ensembl ].
VAR_052433

Secondary structure

......................... 145
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15819 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 98D632A1AEC0AADE

FASTA14516,363
        10         20         30         40         50         60 
MAVSTGVKVP RNFRLLEELE EGQKGVGDGT VSWGLEDDED MTLTRWTGMI IGPPRTNYEN 

        70         80         90        100        110        120 
RIYSLKVECG PKYPEAPPSV RFVTKINMNG INNSSGMVDA RSIPVLAKWQ NSYSIKVVLQ 

       130        140 
ELRRLMMSKE NMKLPQPPEG QTYNN 

« Hide

References

« Hide 'large scale' references
[1]"Molecular Cloning of a 1alpha,25-dihydroxyvitamin D3 inducible transcript (DDVit 1) in human blood monocytes."
Fritsche J., Rehli M., Krause S.W., Andreesen R., Kreutz M.
Biochem. Biophys. Res. Commun. 235:407-412(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, TISSUE SPECIFICITY.
Tissue: Blood.
[2]"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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Colon carcinoma.
[3]"Isolation and characterization of a putative human enterocyte differentiation promoting factor (EDPF-1)."
Faria J., Wild G.E.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"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: Bone marrow, Urinary bladder and Uterus.
[7]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11.
Tissue: Platelet.
[8]"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 UBE2N.
[9]"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 UBE2N AND CHFR.
[10]"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.
[11]"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].
[12]"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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[13]"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 (1.9 ANGSTROMS).
[14]"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 1-144 IN COMPLEX WITH RNF8 AND UBE2N.
[15]"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 UBE2N AND OTUB1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X98091 mRNA. Translation: CAA66717.1.
AF049140 mRNA. Translation: AAC05381.1.
U62136 mRNA. Translation: AAB04758.2.
BT006744 mRNA. Translation: AAP35390.1.
CR407628 mRNA. Translation: CAG28556.1.
BC007051 mRNA. Translation: AAH07051.1.
BC016332 mRNA. Translation: AAH16332.1.
BC016710 mRNA. Translation: AAH16710.1.
BC028673 mRNA. Translation: AAH28673.1.
BC062418 mRNA. Translation: AAH62418.1.
CCDSCCDS43738.1.
PIRJC5525.
RefSeqNP_003341.1. NM_003350.2.
UniGeneHs.491695.
Hs.595400.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J74X-ray1.90A1-145[»]
1J7DX-ray1.85A1-145[»]
1ZGUNMR-A7-145[»]
3VONX-ray3.15B/D/F/I/K/M/P/R/T/W/Y/a/d/f/h/k/m/o6-143[»]
4ORHX-ray4.80A/E/I1-145[»]
ProteinModelPortalQ15819.
SMRQ15819. Positions 6-145.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113184. 47 interactions.
DIPDIP-29830N.
IntActQ15819. 19 interactions.
MINTMINT-1368221.
STRING9606.ENSP00000326473.

PTM databases

PhosphoSiteQ15819.

Polymorphism databases

DMDM51701935.

Proteomic databases

MaxQBQ15819.
PaxDbQ15819.
PRIDEQ15819.

Protocols and materials databases

DNASU7336.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000523111; ENSP00000428209; ENSG00000169139.
GeneID7336.
KEGGhsa:7336.
UCSCuc003xqm.3. human.

Organism-specific databases

CTD7336.
GeneCardsGC08P048970.
HGNCHGNC:12495. UBE2V2.
MIM603001. gene.
neXtProtNX_Q15819.
PharmGKBPA37143.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239185.
HOVERGENHBG054552.
InParanoidQ15819.
KOK10704.
OMAIPILAKW.
OrthoDBEOG77M8R5.
PhylomeDBQ15819.
TreeFamTF316971.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ15819.

Gene expression databases

ArrayExpressQ15819.
BgeeQ15819.
CleanExHS_UBE2V2.
GenevestigatorQ15819.

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

ChiTaRSUBE2V2. human.
EvolutionaryTraceQ15819.
GeneWikiUBE2V2.
GenomeRNAi7336.
NextBio28718.
PROQ15819.
SOURCESearch...

Entry information

Entry nameUB2V2_HUMAN
AccessionPrimary (citable) accession number: Q15819
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 131 of the entry and version 4 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM