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Database: UniProt
Entry: Q15819
LinkDB: Q15819
Original site: Q15819 
ID   UB2V2_HUMAN             Reviewed;         145 AA.
AC   Q15819;
DT   31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   07-APR-2021, entry version 189.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 variant 2;
DE   AltName: Full=DDVit 1;
DE   AltName: Full=Enterocyte differentiation-associated factor 1;
DE            Short=EDAF-1;
DE   AltName: Full=Enterocyte differentiation-promoting factor 1;
DE            Short=EDPF-1;
DE   AltName: Full=MMS2 homolog;
DE   AltName: Full=Vitamin D3-inducible protein;
GN   Name=UBE2V2; Synonyms=MMS2, UEV2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Blood;
RX   PubMed=9199207; DOI=10.1006/bbrc.1997.6798;
RA   Fritsche J., Rehli M., Krause S.W., Andreesen R., Kreutz M.;
RT   "Molecular Cloning of a 1alpha,25-dihydroxyvitamin D3 inducible transcript
RT   (DDVit 1) in human blood monocytes.";
RL   Biochem. Biophys. Res. Commun. 235:407-412(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Colon carcinoma;
RX   PubMed=9705497; DOI=10.1093/nar/26.17.3908;
RA   Xiao W., Lin S.L., Broomfield S., Chow B.L., Wei Y.-F.;
RT   "The products of the yeast MMS2 and two human homologs (hMMS2 and CROC-1)
RT   define a structurally and functionally conserved Ubc-like protein family.";
RL   Nucleic Acids Res. 26:3908-3914(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Faria J., Wild G.E.;
RT   "Isolation and characterization of a putative human enterocyte
RT   differentiation promoting factor (EDPF-1).";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT   "Cloning of human full open reading frames in Gateway(TM) system entry
RT   vector (pDONR201).";
RL   Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bone marrow, Urinary bladder, and Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PROTEIN SEQUENCE OF 2-11.
RC   TISSUE=Platelet;
RX   PubMed=12665801; DOI=10.1038/nbt810;
RA   Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA   Vandekerckhove J.;
RT   "Exploring proteomes and analyzing protein processing by mass spectrometric
RT   identification of sorted N-terminal peptides.";
RL   Nat. Biotechnol. 21:566-569(2003).
RN   [8]
RP   FUNCTION, AND INTERACTION WITH UBE2N.
RX   PubMed=10089880; DOI=10.1016/s0092-8674(00)80575-9;
RA   Hofmann R.M., Pickart C.M.;
RT   "Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in
RT   assembly of novel polyubiquitin chains for DNA repair.";
RL   Cell 96:645-653(1999).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH UBE2N AND CHFR.
RX   PubMed=14562038; DOI=10.1038/sj.onc.1206831;
RA   Bothos J., Summers M.K., Venere M., Scolnick D.M., Halazonetis T.D.;
RT   "The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form
RT   Lys63-linked polyubiquitin chains.";
RL   Oncogene 22:7101-7107(2003).
RN   [10]
RP   FUNCTION.
RX   PubMed=20061386; DOI=10.1074/jbc.m109.089003;
RA   David Y., Ziv T., Admon A., Navon A.;
RT   "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
RT   preferred lysines.";
RL   J. Biol. Chem. 285:8595-8604(2010).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
RX   PubMed=11473255; DOI=10.1038/90373;
RA   Moraes T.F., Edwards R.A., McKenna S., Pastushok L., Xiao W.,
RA   Glover J.N.M., Ellison M.J.;
RT   "Crystal structure of the human ubiquitin conjugating enzyme complex,
RT   hMms2-hUbc13.";
RL   Nat. Struct. Biol. 8:669-673(2001).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (4.8 ANGSTROMS) OF 1-144 IN COMPLEX WITH RNF8 AND
RP   UBE2N.
RX   PubMed=22589545; DOI=10.1074/jbc.m112.359653;
RA   Campbell S.J., Edwards R.A., Leung C.C., Neculai D., Hodge C.D.,
RA   Dhe-Paganon S., Glover J.N.;
RT   "Molecular insights into the function of RING Finger (RNF)-containing
RT   proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation.";
RL   J. Biol. Chem. 287:23900-23910(2012).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-271 IN COMPLEX WITH UBE2N AND
RP   OTUB1.
RX   PubMed=22325355; DOI=10.1016/j.molcel.2012.01.011;
RA   Juang Y.C., Landry M.C., Sanches M., Vittal V., Leung C.C.,
RA   Ceccarelli D.F., Mateo A.R., Pruneda J.N., Mao D.Y., Szilard R.K.,
RA   Orlicky S., Munro M., Brzovic P.S., Klevit R.E., Sicheri F., Durocher D.;
RT   "OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2 enzyme
RT   function.";
RL   Mol. Cell 45:384-397(2012).
CC   -!- FUNCTION: Has no ubiquitin ligase activity on its own. The UBE2V2/UBE2N
CC       heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin
CC       chains that are linked through 'Lys-63'. This type of poly-
CC       ubiquitination does not lead to protein degradation by the proteasome.
CC       Mediates transcriptional activation of target genes. Plays a role in
CC       the control of progress through the cell cycle and differentiation.
CC       Plays a role in the error-free DNA repair pathway and contributes to
CC       the survival of cells after DNA damage. {ECO:0000269|PubMed:10089880,
CC       ECO:0000269|PubMed:14562038, ECO:0000269|PubMed:20061386,
CC       ECO:0000269|PubMed:9705497}.
CC   -!- SUBUNIT: Heterodimer with UBE2N. Binds CHFR.
CC       {ECO:0000269|PubMed:22325355, ECO:0000269|PubMed:22589545}.
CC   -!- INTERACTION:
CC       Q15819; P61088: UBE2N; NbExp=4; IntAct=EBI-714329, EBI-1052908;
CC       Q15819; Q94A97: UBC35; Xeno; NbExp=3; IntAct=EBI-714329, EBI-994120;
CC   -!- TISSUE SPECIFICITY: Detected in placenta, colon, liver and skin.
CC       Detected at very low levels in most tissues.
CC       {ECO:0000269|PubMed:9199207, ECO:0000269|PubMed:9705497}.
CC   -!- INDUCTION: Up-regulated in cultured fresh blood cells upon treatment
CC       with vitamin D3. {ECO:0000269|PubMed:9199207}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; X98091; CAA66717.1; -; mRNA.
DR   EMBL; AF049140; AAC05381.1; -; mRNA.
DR   EMBL; U62136; AAB04758.2; -; mRNA.
DR   EMBL; BT006744; AAP35390.1; -; mRNA.
DR   EMBL; CR407628; CAG28556.1; -; mRNA.
DR   EMBL; BC007051; AAH07051.1; -; mRNA.
DR   EMBL; BC016332; AAH16332.1; -; mRNA.
DR   EMBL; BC016710; AAH16710.1; -; mRNA.
DR   EMBL; BC028673; AAH28673.1; -; mRNA.
DR   EMBL; BC062418; AAH62418.1; -; mRNA.
DR   CCDS; CCDS43738.1; -.
DR   PIR; JC5525; JC5525.
DR   RefSeq; NP_003341.1; NM_003350.2.
DR   PDB; 1J74; X-ray; 1.90 A; A=1-145.
DR   PDB; 1J7D; X-ray; 1.85 A; A=1-145.
DR   PDB; 1ZGU; NMR; -; A=7-145.
DR   PDB; 3VON; X-ray; 3.15 A; B/D/F/I/K/M/P/R/T/W/Y/a/d/f/h/k/m/o=6-143.
DR   PDB; 4NR3; X-ray; 1.80 A; A=6-145.
DR   PDB; 4NRG; X-ray; 1.95 A; A=1-145.
DR   PDB; 4NRI; X-ray; 2.30 A; A=6-145.
DR   PDB; 4ONL; X-ray; 1.35 A; A=1-145.
DR   PDB; 4ONM; X-ray; 1.35 A; A=1-145.
DR   PDB; 4ONN; X-ray; 1.50 A; A=1-145.
DR   PDB; 4ORH; X-ray; 4.80 A; A/E/I=1-145.
DR   PDB; 5AIT; X-ray; 3.40 A; D/G=1-145.
DR   PDBsum; 1J74; -.
DR   PDBsum; 1J7D; -.
DR   PDBsum; 1ZGU; -.
DR   PDBsum; 3VON; -.
DR   PDBsum; 4NR3; -.
DR   PDBsum; 4NRG; -.
DR   PDBsum; 4NRI; -.
DR   PDBsum; 4ONL; -.
DR   PDBsum; 4ONM; -.
DR   PDBsum; 4ONN; -.
DR   PDBsum; 4ORH; -.
DR   PDBsum; 5AIT; -.
DR   SASBDB; Q15819; -.
DR   SMR; Q15819; -.
DR   BioGRID; 113184; 74.
DR   ComplexPortal; CPX-530; UBC13-MMS2 ubiquitin-conjugating enzyme E2 complex.
DR   CORUM; Q15819; -.
DR   DIP; DIP-29830N; -.
DR   IntAct; Q15819; 35.
DR   STRING; 9606.ENSP00000428209; -.
DR   iPTMnet; Q15819; -.
DR   MetOSite; Q15819; -.
DR   PhosphoSitePlus; Q15819; -.
DR   BioMuta; UBE2V2; -.
DR   DMDM; 51701935; -.
DR   EPD; Q15819; -.
DR   jPOST; Q15819; -.
DR   MassIVE; Q15819; -.
DR   MaxQB; Q15819; -.
DR   PaxDb; Q15819; -.
DR   PeptideAtlas; Q15819; -.
DR   PRIDE; Q15819; -.
DR   ProteomicsDB; 60775; -.
DR   TopDownProteomics; Q15819; -.
DR   Antibodypedia; 24348; 301 antibodies.
DR   DNASU; 7336; -.
DR   Ensembl; ENST00000523111; ENSP00000428209; ENSG00000169139.
DR   GeneID; 7336; -.
DR   KEGG; hsa:7336; -.
DR   UCSC; uc003xqm.4; human.
DR   CTD; 7336; -.
DR   DisGeNET; 7336; -.
DR   GeneCards; UBE2V2; -.
DR   HGNC; HGNC:12495; UBE2V2.
DR   HPA; ENSG00000169139; Low tissue specificity.
DR   MIM; 603001; gene.
DR   neXtProt; NX_Q15819; -.
DR   OpenTargets; ENSG00000169139; -.
DR   PharmGKB; PA37143; -.
DR   VEuPathDB; HostDB:ENSG00000169139.11; -.
DR   eggNOG; KOG0896; Eukaryota.
DR   GeneTree; ENSGT00740000115534; -.
DR   HOGENOM; CLU_063065_3_0_1; -.
DR   InParanoid; Q15819; -.
DR   OMA; WQSSYSI; -.
DR   OrthoDB; 1507995at2759; -.
DR   PhylomeDB; Q15819; -.
DR   TreeFam; TF316971; -.
DR   BRENDA; 2.3.2.B6; 2681.
DR   PathwayCommons; Q15819; -.
DR   Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
DR   Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR   Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR   Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; Q15819; -.
DR   BioGRID-ORCS; 7336; 10 hits in 961 CRISPR screens.
DR   ChiTaRS; UBE2V2; human.
DR   EvolutionaryTrace; Q15819; -.
DR   GeneWiki; UBE2V2; -.
DR   GenomeRNAi; 7336; -.
DR   Pharos; Q15819; Tbio.
DR   PRO; PR:Q15819; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q15819; protein.
DR   Bgee; ENSG00000169139; Expressed in anterior cingulate cortex and 248 other tissues.
DR   ExpressionAtlas; Q15819; baseline and differential.
DR   Genevisible; Q15819; HS.
DR   GO; GO:0005737; C:cytoplasm; TAS:HGNC-UCL.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR   GO; GO:0031372; C:UBC13-MMS2 complex; IDA:HGNC-UCL.
DR   GO; GO:0000729; P:DNA double-strand break processing; IMP:HGNC-UCL.
DR   GO; GO:0006302; P:double-strand break repair; TAS:Reactome.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
DR   GO; GO:0042275; P:error-free postreplication DNA repair; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:0045739; P:positive regulation of DNA repair; IEA:Ensembl.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IEA:Ensembl.
DR   GO; GO:0006301; P:postreplication repair; IBA:GO_Central.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; TAS:HGNC-UCL.
DR   GO; GO:0006282; P:regulation of DNA repair; TAS:ProtInc.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Direct protein sequencing; Reference proteome;
KW   Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12665801,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..145
FT                   /note="Ubiquitin-conjugating enzyme E2 variant 2"
FT                   /id="PRO_0000082602"
FT   DOMAIN          10..145
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   VARIANT         36
FT                   /note="E -> G (in dbSNP:rs11557776)"
FT                   /id="VAR_052431"
FT   VARIANT         78
FT                   /note="P -> Q (in dbSNP:rs11557786)"
FT                   /id="VAR_052433"
FT   HELIX           11..24
FT                   /evidence="ECO:0007744|PDB:4ONL"
FT   STRAND          29..37
FT                   /evidence="ECO:0007744|PDB:4ONL"
FT   STRAND          45..51
FT                   /evidence="ECO:0007744|PDB:4ONL"
FT   STRAND          54..56
FT                   /evidence="ECO:0007744|PDB:4NRI"
FT   TURN            57..60
FT                   /evidence="ECO:0007744|PDB:4ONL"
FT   STRAND          62..68
FT                   /evidence="ECO:0007744|PDB:4ONL"
FT   TURN            71..75
FT                   /evidence="ECO:0007744|PDB:4ONL"
FT   STRAND          79..84
FT                   /evidence="ECO:0007744|PDB:4ONL"
FT   TURN            93..95
FT                   /evidence="ECO:0007744|PDB:4ONL"
FT   HELIX           100..102
FT                   /evidence="ECO:0007744|PDB:4ONL"
FT   HELIX           104..107
FT                   /evidence="ECO:0007744|PDB:4ONL"
FT   HELIX           115..126
FT                   /evidence="ECO:0007744|PDB:4ONL"
FT   HELIX           129..132
FT                   /evidence="ECO:0007744|PDB:4ONL"
SQ   SEQUENCE   145 AA;  16363 MW;  98D632A1AEC0AADE CRC64;
     MAVSTGVKVP RNFRLLEELE EGQKGVGDGT VSWGLEDDED MTLTRWTGMI IGPPRTNYEN
     RIYSLKVECG PKYPEAPPSV RFVTKINMNG INNSSGMVDA RSIPVLAKWQ NSYSIKVVLQ
     ELRRLMMSKE NMKLPQPPEG QTYNN
//
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