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Q15819

- UB2V2_HUMAN

UniProt

Q15819 - UB2V2_HUMAN

Protein

Ubiquitin-conjugating enzyme E2 variant 2

Gene

UBE2V2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    1. acid-amino acid ligase activity Source: InterPro
    2. protein binding Source: IntAct

    GO - Biological processi

    1. cell proliferation Source: ProtInc
    2. DNA double-strand break processing Source: HGNC
    3. negative regulation of neuron apoptotic process Source: Ensembl
    4. positive regulation of DNA repair Source: Ensembl
    5. positive regulation of neuron projection development Source: Ensembl
    6. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
    7. positive regulation of synapse assembly Source: Ensembl
    8. protein polyubiquitination Source: ProtInc
    9. protein ubiquitination Source: HGNC
    10. regulation of DNA repair Source: ProtInc

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    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: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:12495. UBE2V2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HGNC
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: HGNC
    4. UBC13-MMS2 complex Source: HGNC

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37143.

    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

    ArrayExpressiQ15819.
    BgeeiQ15819.
    CleanExiHS_UBE2V2.
    GenevestigatoriQ15819.

    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. 47 interactions.
    DIPiDIP-29830N.
    IntActiQ15819. 19 interactions.
    MINTiMINT-1368221.
    STRINGi9606.ENSP00000326473.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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.
    HOVERGENiHBG054552.
    InParanoidiQ15819.
    KOiK10704.
    OMAiIPILAKW.
    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

    MAVSTGVKVP RNFRLLEELE EGQKGVGDGT VSWGLEDDED MTLTRWTGMI    50
    IGPPRTNYEN RIYSLKVECG PKYPEAPPSV RFVTKINMNG INNSSGMVDA 100
    RSIPVLAKWQ NSYSIKVVLQ ELRRLMMSKE NMKLPQPPEG QTYNN 145
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi51701935.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS43738.1.
    PIRi JC5525.
    RefSeqi NP_003341.1. NM_003350.2.
    UniGenei Hs.491695.
    Hs.595400.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1J74 X-ray 1.90 A 1-145 [» ]
    1J7D X-ray 1.85 A 1-145 [» ]
    1ZGU NMR - A 7-145 [» ]
    3VON X-ray 3.15 B/D/F/I/K/M/P/R/T/W/Y/a/d/f/h/k/m/o 6-143 [» ]
    4ORH X-ray 4.80 A/E/I 1-145 [» ]
    ProteinModelPortali Q15819.
    SMRi Q15819. Positions 6-145.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113184. 47 interactions.
    DIPi DIP-29830N.
    IntActi Q15819. 19 interactions.
    MINTi MINT-1368221.
    STRINGi 9606.ENSP00000326473.

    PTM databases

    PhosphoSitei Q15819.

    Polymorphism databases

    DMDMi 51701935.

    Proteomic databases

    MaxQBi Q15819.
    PaxDbi Q15819.
    PRIDEi Q15819.

    Protocols and materials databases

    DNASUi 7336.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000523111 ; ENSP00000428209 ; ENSG00000169139 .
    GeneIDi 7336.
    KEGGi hsa:7336.
    UCSCi uc003xqm.3. human.

    Organism-specific databases

    CTDi 7336.
    GeneCardsi GC08P048970.
    HGNCi HGNC:12495. UBE2V2.
    MIMi 603001. gene.
    neXtProti NX_Q15819.
    PharmGKBi PA37143.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG239185.
    HOVERGENi HBG054552.
    InParanoidi Q15819.
    KOi K10704.
    OMAi IPILAKW.
    OrthoDBi EOG77M8R5.
    PhylomeDBi Q15819.
    TreeFami TF316971.

    Enzyme and pathway databases

    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki Q15819.

    Miscellaneous databases

    ChiTaRSi UBE2V2. human.
    EvolutionaryTracei Q15819.
    GeneWikii UBE2V2.
    GenomeRNAii 7336.
    NextBioi 28718.
    PROi Q15819.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15819.
    Bgeei Q15819.
    CleanExi HS_UBE2V2.
    Genevestigatori Q15819.

    Family and domain databases

    Gene3Di 3.10.110.10. 1 hit.
    InterProi IPR000608. UBQ-conjugat_E2.
    IPR016135. UBQ-conjugating_enzyme/RWD.
    [Graphical view ]
    Pfami PF00179. UQ_con. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54495. SSF54495. 1 hit.
    PROSITEi PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 133 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