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Protein

Ubiquitin-conjugating enzyme E2 variant 2

Gene

UBE2V2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

GO - Biological processi

  • cell proliferation Source: ProtInc
  • DNA double-strand break processing Source: HGNC
  • negative regulation of neuron apoptotic process Source: Ensembl
  • positive regulation of DNA repair Source: Ensembl
  • positive regulation of neuron projection development Source: Ensembl
  • positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
  • positive regulation of synapse assembly Source: Ensembl
  • postreplication repair Source: GO_Central
  • protein K63-linked ubiquitination Source: GO_Central
  • protein polyubiquitination Source: ProtInc
  • protein ubiquitination Source: HGNC
  • regulation of DNA repair Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BRENDAi2.3.2.B6. 2681.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ15819.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:UBE2V2
Synonyms:MMS2, UEV2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:12495. UBE2V2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HGNC
  • extracellular exosome Source: UniProtKB
  • nucleus Source: HGNC
  • UBC13-MMS2 complex Source: HGNC
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37143.

Polymorphism and mutation databases

BioMutaiUBE2V2.
DMDMi51701935.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 145144Ubiquitin-conjugating enzyme E2 variant 2PRO_0000082602Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ15819.
PaxDbiQ15819.
PRIDEiQ15819.

PTM databases

PhosphoSiteiQ15819.

Expressioni

Tissue specificityi

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

Inductioni

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

Gene expression databases

BgeeiQ15819.
CleanExiHS_UBE2V2.
ExpressionAtlasiQ15819. baseline and differential.
GenevisibleiQ15819. HS.

Interactioni

Subunit structurei

Heterodimer with UBE2N. Binds CHFR.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
UBC35Q94A973EBI-714329,EBI-994120From a different organism.
UBE2NP610883EBI-714329,EBI-1052908

Protein-protein interaction databases

BioGridi113184. 50 interactions.
DIPiDIP-29830N.
IntActiQ15819. 19 interactions.
MINTiMINT-1368221.
STRINGi9606.ENSP00000428209.

Structurei

Secondary structure

1
145
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2414Combined sources
Beta strandi29 – 379Combined sources
Beta strandi45 – 517Combined sources
Beta strandi54 – 563Combined sources
Turni57 – 604Combined sources
Beta strandi62 – 687Combined sources
Turni71 – 755Combined sources
Beta strandi79 – 846Combined sources
Turni93 – 953Combined sources
Helixi100 – 1023Combined sources
Helixi104 – 1074Combined sources
Helixi115 – 12612Combined sources
Helixi129 – 1324Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4NR3X-ray1.80A6-145[»]
4NRGX-ray1.95A1-145[»]
4NRIX-ray2.30A6-145[»]
4ONLX-ray1.35A1-145[»]
4ONMX-ray1.35A1-145[»]
4ONNX-ray1.50A1-145[»]
4ORHX-ray4.80A/E/I1-145[»]
ProteinModelPortaliQ15819.
SMRiQ15819. Positions 6-145.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15819.

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG239185.
GeneTreeiENSGT00740000115534.
HOVERGENiHBG054552.
InParanoidiQ15819.
KOiK10704.
OMAiEPPTVRF.
OrthoDBiEOG77M8R5.
PhylomeDBiQ15819.
TreeFamiTF316971.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q15819-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVSTGVKVP RNFRLLEELE EGQKGVGDGT VSWGLEDDED MTLTRWTGMI
60 70 80 90 100
IGPPRTNYEN RIYSLKVECG PKYPEAPPSV RFVTKINMNG INNSSGMVDA
110 120 130 140
RSIPVLAKWQ NSYSIKVVLQ ELRRLMMSKE NMKLPQPPEG QTYNN
Length:145
Mass (Da):16,363
Last modified:January 23, 2007 - v4
Checksum:i98D632A1AEC0AADE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361E → G.
Corresponds to variant rs11557776 [ dbSNP | Ensembl ].
VAR_052431
Natural varianti40 – 401D → H.
Corresponds to variant rs14890 [ dbSNP | Ensembl ].
VAR_052432
Natural varianti78 – 781P → Q.
Corresponds to variant rs11557786 [ dbSNP | Ensembl ].
VAR_052433

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS43738.1.
PIRiJC5525.
RefSeqiNP_003341.1. NM_003350.2.
UniGeneiHs.491695.
Hs.595400.

Genome annotation databases

EnsembliENST00000523111; ENSP00000428209; ENSG00000169139.
GeneIDi7336.
KEGGihsa:7336.
UCSCiuc003xqm.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS43738.1.
PIRiJC5525.
RefSeqiNP_003341.1. NM_003350.2.
UniGeneiHs.491695.
Hs.595400.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
4NR3X-ray1.80A6-145[»]
4NRGX-ray1.95A1-145[»]
4NRIX-ray2.30A6-145[»]
4ONLX-ray1.35A1-145[»]
4ONMX-ray1.35A1-145[»]
4ONNX-ray1.50A1-145[»]
4ORHX-ray4.80A/E/I1-145[»]
ProteinModelPortaliQ15819.
SMRiQ15819. Positions 6-145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113184. 50 interactions.
DIPiDIP-29830N.
IntActiQ15819. 19 interactions.
MINTiMINT-1368221.
STRINGi9606.ENSP00000428209.

PTM databases

PhosphoSiteiQ15819.

Polymorphism and mutation databases

BioMutaiUBE2V2.
DMDMi51701935.

Proteomic databases

MaxQBiQ15819.
PaxDbiQ15819.
PRIDEiQ15819.

Protocols and materials databases

DNASUi7336.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000523111; ENSP00000428209; ENSG00000169139.
GeneIDi7336.
KEGGihsa:7336.
UCSCiuc003xqm.3. human.

Organism-specific databases

CTDi7336.
GeneCardsiGC08P048920.
HGNCiHGNC:12495. UBE2V2.
MIMi603001. gene.
neXtProtiNX_Q15819.
PharmGKBiPA37143.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG239185.
GeneTreeiENSGT00740000115534.
HOVERGENiHBG054552.
InParanoidiQ15819.
KOiK10704.
OMAiEPPTVRF.
OrthoDBiEOG77M8R5.
PhylomeDBiQ15819.
TreeFamiTF316971.

Enzyme and pathway databases

BRENDAi2.3.2.B6. 2681.
ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiQ15819.

Miscellaneous databases

ChiTaRSiUBE2V2. human.
EvolutionaryTraceiQ15819.
GeneWikiiUBE2V2.
GenomeRNAii7336.
NextBioi28718.
PROiQ15819.
SOURCEiSearch...

Gene expression databases

BgeeiQ15819.
CleanExiHS_UBE2V2.
ExpressionAtlasiQ15819. baseline and differential.
GenevisibleiQ15819. HS.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. 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. Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-271 IN COMPLEX WITH UBE2N AND OTUB1.

Entry informationi

Entry nameiUB2V2_HUMAN
AccessioniPrimary (citable) accession number: Q15819
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.