Full text data of UBE2V2
UBE2V2
(MMS2, UEV2)
[Confidence: low (only semi-automatic identification from reviews)]
Ubiquitin-conjugating enzyme E2 variant 2 (DDVit 1; Enterocyte differentiation-associated factor 1; EDAF-1; Enterocyte differentiation-promoting factor 1; EDPF-1; MMS2 homolog; Vitamin D3-inducible protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Ubiquitin-conjugating enzyme E2 variant 2 (DDVit 1; Enterocyte differentiation-associated factor 1; EDAF-1; Enterocyte differentiation-promoting factor 1; EDPF-1; MMS2 homolog; Vitamin D3-inducible protein)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q15819
ID UB2V2_HUMAN Reviewed; 145 AA.
AC Q15819;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 125.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT transcript (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
RT CROC-1) define a structurally and functionally conserved Ubc-like
RT 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
RT 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
RT project: 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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric 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.,
RA Buerckstuemmer T., 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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal 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
RP AND 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
RP AND 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.,
RA Durocher D.;
RT "OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2
RT enzyme function.";
RL Mol. Cell 45:384-397(2012).
CC -!- FUNCTION: Has no ubiquitin ligase activity on its own. The
CC UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical
CC poly-ubiquitin chains that are linked through 'Lys-63'. This type
CC of poly-ubiquitination does not lead to protein degradation by the
CC proteasome. Mediates transcriptional activation of target genes.
CC Plays a role in the control of progress through the cell cycle and
CC differentiation. Plays a role in the error-free DNA repair pathway
CC and contributes to the survival of cells after DNA damage.
CC -!- SUBUNIT: Heterodimer with UBE2N. Binds CHFR.
CC -!- INTERACTION:
CC Q94A97:UBC35 (xeno); NbExp=3; IntAct=EBI-714329, EBI-994120;
CC P61088:UBE2N; NbExp=3; IntAct=EBI-714329, EBI-1052908;
CC -!- TISSUE SPECIFICITY: Detected in placenta, colon, liver and skin.
CC Detected at very low levels in most tissues.
CC -!- INDUCTION: Up-regulated in cultured fresh blood cells upon
CC treatment with vitamin D3.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; JC5525; JC5525.
DR RefSeq; NP_003341.1; NM_003350.2.
DR UniGene; Hs.491695; -.
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; 4EPO; X-ray; 4.80 A; A/E/I=1-144.
DR PDBsum; 1J74; -.
DR PDBsum; 1J7D; -.
DR PDBsum; 1ZGU; -.
DR PDBsum; 3VON; -.
DR PDBsum; 4EPO; -.
DR ProteinModelPortal; Q15819; -.
DR SMR; Q15819; 6-145.
DR DIP; DIP-29830N; -.
DR IntAct; Q15819; 19.
DR MINT; MINT-1368221; -.
DR STRING; 9606.ENSP00000326473; -.
DR PhosphoSite; Q15819; -.
DR DMDM; 51701935; -.
DR PaxDb; Q15819; -.
DR PRIDE; Q15819; -.
DR DNASU; 7336; -.
DR Ensembl; ENST00000523111; ENSP00000428209; ENSG00000169139.
DR GeneID; 7336; -.
DR KEGG; hsa:7336; -.
DR UCSC; uc003xqm.3; human.
DR CTD; 7336; -.
DR GeneCards; GC08P048970; -.
DR HGNC; HGNC:12495; UBE2V2.
DR MIM; 603001; gene.
DR neXtProt; NX_Q15819; -.
DR PharmGKB; PA37143; -.
DR eggNOG; NOG239185; -.
DR HOVERGEN; HBG054552; -.
DR InParanoid; Q15819; -.
DR KO; K10704; -.
DR OMA; IPILAKW; -.
DR OrthoDB; EOG77M8R5; -.
DR PhylomeDB; Q15819; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q15819; -.
DR ChiTaRS; UBE2V2; human.
DR EvolutionaryTrace; Q15819; -.
DR GeneWiki; UBE2V2; -.
DR GenomeRNAi; 7336; -.
DR NextBio; 28718; -.
DR PRO; PR:Q15819; -.
DR ArrayExpress; Q15819; -.
DR Bgee; Q15819; -.
DR CleanEx; HS_UBE2V2; -.
DR Genevestigator; Q15819; -.
DR GO; GO:0005737; C:cytoplasm; TAS:HGNC.
DR GO; GO:0005634; C:nucleus; IDA:HGNC.
DR GO; GO:0031372; C:UBC13-MMS2 complex; IDA:HGNC.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0000729; P:DNA double-strand break processing; IMP:HGNC.
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:0000209; P:protein polyubiquitination; TAS:ProtInc.
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; PS00183; UBIQUITIN_CONJUGAT_1; FALSE_NEG.
DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Polymorphism; Reference proteome;
KW Ubl conjugation pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 145 Ubiquitin-conjugating enzyme E2 variant
FT 2.
FT /FTId=PRO_0000082602.
FT MOD_RES 2 2 N-acetylalanine.
FT VARIANT 36 36 E -> G (in dbSNP:rs11557776).
FT /FTId=VAR_052431.
FT VARIANT 40 40 D -> H (in dbSNP:rs14890).
FT /FTId=VAR_052432.
FT VARIANT 78 78 P -> Q (in dbSNP:rs11557786).
FT /FTId=VAR_052433.
FT HELIX 11 24
FT STRAND 29 37
FT STRAND 45 51
FT TURN 57 60
FT STRAND 62 68
FT TURN 71 75
FT STRAND 79 84
FT TURN 93 95
FT HELIX 100 102
FT HELIX 104 107
FT HELIX 115 126
FT HELIX 129 132
SQ SEQUENCE 145 AA; 16363 MW; 98D632A1AEC0AADE CRC64;
MAVSTGVKVP RNFRLLEELE EGQKGVGDGT VSWGLEDDED MTLTRWTGMI IGPPRTNYEN
RIYSLKVECG PKYPEAPPSV RFVTKINMNG INNSSGMVDA RSIPVLAKWQ NSYSIKVVLQ
ELRRLMMSKE NMKLPQPPEG QTYNN
//
ID UB2V2_HUMAN Reviewed; 145 AA.
AC Q15819;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 125.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT transcript (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
RT CROC-1) define a structurally and functionally conserved Ubc-like
RT 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
RT 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
RT project: 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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric 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.,
RA Buerckstuemmer T., 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, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal 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
RP AND 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
RP AND 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.,
RA Durocher D.;
RT "OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2
RT enzyme function.";
RL Mol. Cell 45:384-397(2012).
CC -!- FUNCTION: Has no ubiquitin ligase activity on its own. The
CC UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical
CC poly-ubiquitin chains that are linked through 'Lys-63'. This type
CC of poly-ubiquitination does not lead to protein degradation by the
CC proteasome. Mediates transcriptional activation of target genes.
CC Plays a role in the control of progress through the cell cycle and
CC differentiation. Plays a role in the error-free DNA repair pathway
CC and contributes to the survival of cells after DNA damage.
CC -!- SUBUNIT: Heterodimer with UBE2N. Binds CHFR.
CC -!- INTERACTION:
CC Q94A97:UBC35 (xeno); NbExp=3; IntAct=EBI-714329, EBI-994120;
CC P61088:UBE2N; NbExp=3; IntAct=EBI-714329, EBI-1052908;
CC -!- TISSUE SPECIFICITY: Detected in placenta, colon, liver and skin.
CC Detected at very low levels in most tissues.
CC -!- INDUCTION: Up-regulated in cultured fresh blood cells upon
CC treatment with vitamin D3.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 PIR; JC5525; JC5525.
DR RefSeq; NP_003341.1; NM_003350.2.
DR UniGene; Hs.491695; -.
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; 4EPO; X-ray; 4.80 A; A/E/I=1-144.
DR PDBsum; 1J74; -.
DR PDBsum; 1J7D; -.
DR PDBsum; 1ZGU; -.
DR PDBsum; 3VON; -.
DR PDBsum; 4EPO; -.
DR ProteinModelPortal; Q15819; -.
DR SMR; Q15819; 6-145.
DR DIP; DIP-29830N; -.
DR IntAct; Q15819; 19.
DR MINT; MINT-1368221; -.
DR STRING; 9606.ENSP00000326473; -.
DR PhosphoSite; Q15819; -.
DR DMDM; 51701935; -.
DR PaxDb; Q15819; -.
DR PRIDE; Q15819; -.
DR DNASU; 7336; -.
DR Ensembl; ENST00000523111; ENSP00000428209; ENSG00000169139.
DR GeneID; 7336; -.
DR KEGG; hsa:7336; -.
DR UCSC; uc003xqm.3; human.
DR CTD; 7336; -.
DR GeneCards; GC08P048970; -.
DR HGNC; HGNC:12495; UBE2V2.
DR MIM; 603001; gene.
DR neXtProt; NX_Q15819; -.
DR PharmGKB; PA37143; -.
DR eggNOG; NOG239185; -.
DR HOVERGEN; HBG054552; -.
DR InParanoid; Q15819; -.
DR KO; K10704; -.
DR OMA; IPILAKW; -.
DR OrthoDB; EOG77M8R5; -.
DR PhylomeDB; Q15819; -.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q15819; -.
DR ChiTaRS; UBE2V2; human.
DR EvolutionaryTrace; Q15819; -.
DR GeneWiki; UBE2V2; -.
DR GenomeRNAi; 7336; -.
DR NextBio; 28718; -.
DR PRO; PR:Q15819; -.
DR ArrayExpress; Q15819; -.
DR Bgee; Q15819; -.
DR CleanEx; HS_UBE2V2; -.
DR Genevestigator; Q15819; -.
DR GO; GO:0005737; C:cytoplasm; TAS:HGNC.
DR GO; GO:0005634; C:nucleus; IDA:HGNC.
DR GO; GO:0031372; C:UBC13-MMS2 complex; IDA:HGNC.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
DR GO; GO:0000729; P:DNA double-strand break processing; IMP:HGNC.
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:0000209; P:protein polyubiquitination; TAS:ProtInc.
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; PS00183; UBIQUITIN_CONJUGAT_1; FALSE_NEG.
DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome;
KW Direct protein sequencing; Polymorphism; Reference proteome;
KW Ubl conjugation pathway.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 145 Ubiquitin-conjugating enzyme E2 variant
FT 2.
FT /FTId=PRO_0000082602.
FT MOD_RES 2 2 N-acetylalanine.
FT VARIANT 36 36 E -> G (in dbSNP:rs11557776).
FT /FTId=VAR_052431.
FT VARIANT 40 40 D -> H (in dbSNP:rs14890).
FT /FTId=VAR_052432.
FT VARIANT 78 78 P -> Q (in dbSNP:rs11557786).
FT /FTId=VAR_052433.
FT HELIX 11 24
FT STRAND 29 37
FT STRAND 45 51
FT TURN 57 60
FT STRAND 62 68
FT TURN 71 75
FT STRAND 79 84
FT TURN 93 95
FT HELIX 100 102
FT HELIX 104 107
FT HELIX 115 126
FT HELIX 129 132
SQ SEQUENCE 145 AA; 16363 MW; 98D632A1AEC0AADE CRC64;
MAVSTGVKVP RNFRLLEELE EGQKGVGDGT VSWGLEDDED MTLTRWTGMI IGPPRTNYEN
RIYSLKVECG PKYPEAPPSV RFVTKINMNG INNSSGMVDA RSIPVLAKWQ NSYSIKVVLQ
ELRRLMMSKE NMKLPQPPEG QTYNN
//
MIM
603001
*RECORD*
*FIELD* NO
603001
*FIELD* TI
*603001 UBIQUITIN-CONJUGATING ENZYME E2 VARIANT 2; UBE2V2
;;UEV2;;
1-ALPHA,25-@DIHYDROXYVITAMIN D3-INDUCIBLE TRANSCRIPT 1; DDVIT1;;
read moreENTEROCYTE DIFFERENTIATION-PROMOTING FACTOR 1; EDPF1;;
METHYL METHANESULFONATE SENSITIVE 2, S. CEREVISIAE, HOMOLOG OF; MMS2
*FIELD* TX
CLONING
By mRNA differential display, RACE PCR, and library screening, Fritsche
et al. (1997) isolated human monocyte and macrophage cDNAs encoding
UBE2V2, which they called DDVIT1. The nucleotide sequence of DDVIT1 is
identical to that of the EDPF1 cDNA (GenBank GENBANK U62136). Northern
blot analysis detected DDVIT1 transcripts in all human tissues and cell
lines examined. The authors demonstrated that the 1.4-kb DDVIT1 mRNA was
induced in freshly isolated blood monocytes by short-term incubation
with vitamin D3. The predicted 145-amino acid DDVIT1 protein (see
GenBank GENBANK X98091) does not have hydrophobic regions, and therefore
the authors suggested that it is soluble.
Sancho et al. (1998) found that the UBE2V2 protein, which they named
UEV2, has 90% sequence identity to the C-terminal 140 amino acids of the
221- and 170-amino acid UEV1 isoforms (UBE2V1; 602995). The authors
stated that the UEV1 and UEV2 proteins are similar in sequence and in
predicted structure to the ubiquitin-conjugating enzymes, or E2s (e.g.,
UBE2D1; 602961), but lack a critical cysteine residue essential for the
catalytic activity of E2 enzymes.
GENE FUNCTION
In yeast, Hofmann and Pickart (1999) showed that the MMS2 protein formed
a specific heteromeric complex with UBC13-encoded E2 (603679) and was
required for the UBC13-dependent assembly of polyubiquitin chains linked
through lysine 63. A ubc13 yeast strain was UV sensitive, and single,
double, and triple mutants of the UBC13, MMS2, and ubiquitin genes
displayed a similar phenotype. The findings supported a model in which
an MMS2/UBC13 protein complex assembles novel polyubiquitin chains for
signaling in DNA repair, and suggested that UEV proteins may act to
increase diversity and selectivity in ubiquitin conjugation.
The RAD6 (179095) pathway is central to postreplicative DNA repair in
eukaryotic cells. Two principal elements of this pathway are the
ubiquitin-conjugating enzymes RAD6 and the MMS2-UBC13 heterodimer, which
are recruited to chromatin by the RING finger proteins RAD18 (605256)
and RAD5 (608048), respectively. Hoege et al. (2002) showed that UBC9
(601661), a small ubiquitin-related modifier (SUMO)-conjugating enzyme,
is also affiliated with this pathway and that proliferating cell nuclear
antigen (PCNA; 176740), a DNA polymerase sliding clamp involved in DNA
synthesis and repair, is a substrate. PCNA is monoubiquitinated through
RAD6 and RAD18, modified by lys63-linked multiubiquitination, which
additionally requires MMS2, UBC13, and RAD5, and is conjugated to SUMO
by UBC9. All 3 modifications affect the same lysine residue of PCNA,
K164, suggesting that they label PCNA for alternative functions. Hoege
et al. (2002) demonstrated that these modifications differentially
affect resistance to DNA damage, and that damage-induced PCNA
ubiquitination is elementary for DNA repair and occurs at the same
conserved residue in yeast and humans.
*FIELD* RF
1. Fritsche, J.; Rehli, M.; Krause, S. W.; Andreesen, R.; Kreutz,
M.: Molecular cloning of a 1-alpha,25-dihydroxyvitamin D3-inducible
transcript (DDVit 1) in human blood monocytes. Biochem. Biophys.
Res. Commun. 235: 407-412, 1997.
2. Hoege, C.; Pfander, B.; Moldovan, G.-L.; Pyrowolakis, G.; Jentsch,
S.: RAD6-dependent DNA repair is linked to modification of PCNA by
ubiquitin and SUMO. Nature 419: 135-141, 2002.
3. Hofmann, R. M.; Pickart, C. M.: Noncanonical MMS2-encoded ubiquitin-conjugating
enzyme functions in assembly of novel polyubiquitin chains for DNA
repair. Cell 96: 645-653, 1999.
4. 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.: 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. Molec. Cell. Biol. 18: 576-589,
1998.
*FIELD* CN
Ada Hamosh - updated: 9/30/2002
Stylianos E. Antonarakis - updated: 3/25/1999
*FIELD* CD
Patti M. Sherman: 8/24/1998
*FIELD* ED
alopez: 01/29/2007
alopez: 10/1/2002
tkritzer: 9/30/2002
mgross: 3/31/1999
mgross: 3/29/1999
terry: 3/25/1999
carol: 1/6/1999
alopez: 9/22/1998
*RECORD*
*FIELD* NO
603001
*FIELD* TI
*603001 UBIQUITIN-CONJUGATING ENZYME E2 VARIANT 2; UBE2V2
;;UEV2;;
1-ALPHA,25-@DIHYDROXYVITAMIN D3-INDUCIBLE TRANSCRIPT 1; DDVIT1;;
read moreENTEROCYTE DIFFERENTIATION-PROMOTING FACTOR 1; EDPF1;;
METHYL METHANESULFONATE SENSITIVE 2, S. CEREVISIAE, HOMOLOG OF; MMS2
*FIELD* TX
CLONING
By mRNA differential display, RACE PCR, and library screening, Fritsche
et al. (1997) isolated human monocyte and macrophage cDNAs encoding
UBE2V2, which they called DDVIT1. The nucleotide sequence of DDVIT1 is
identical to that of the EDPF1 cDNA (GenBank GENBANK U62136). Northern
blot analysis detected DDVIT1 transcripts in all human tissues and cell
lines examined. The authors demonstrated that the 1.4-kb DDVIT1 mRNA was
induced in freshly isolated blood monocytes by short-term incubation
with vitamin D3. The predicted 145-amino acid DDVIT1 protein (see
GenBank GENBANK X98091) does not have hydrophobic regions, and therefore
the authors suggested that it is soluble.
Sancho et al. (1998) found that the UBE2V2 protein, which they named
UEV2, has 90% sequence identity to the C-terminal 140 amino acids of the
221- and 170-amino acid UEV1 isoforms (UBE2V1; 602995). The authors
stated that the UEV1 and UEV2 proteins are similar in sequence and in
predicted structure to the ubiquitin-conjugating enzymes, or E2s (e.g.,
UBE2D1; 602961), but lack a critical cysteine residue essential for the
catalytic activity of E2 enzymes.
GENE FUNCTION
In yeast, Hofmann and Pickart (1999) showed that the MMS2 protein formed
a specific heteromeric complex with UBC13-encoded E2 (603679) and was
required for the UBC13-dependent assembly of polyubiquitin chains linked
through lysine 63. A ubc13 yeast strain was UV sensitive, and single,
double, and triple mutants of the UBC13, MMS2, and ubiquitin genes
displayed a similar phenotype. The findings supported a model in which
an MMS2/UBC13 protein complex assembles novel polyubiquitin chains for
signaling in DNA repair, and suggested that UEV proteins may act to
increase diversity and selectivity in ubiquitin conjugation.
The RAD6 (179095) pathway is central to postreplicative DNA repair in
eukaryotic cells. Two principal elements of this pathway are the
ubiquitin-conjugating enzymes RAD6 and the MMS2-UBC13 heterodimer, which
are recruited to chromatin by the RING finger proteins RAD18 (605256)
and RAD5 (608048), respectively. Hoege et al. (2002) showed that UBC9
(601661), a small ubiquitin-related modifier (SUMO)-conjugating enzyme,
is also affiliated with this pathway and that proliferating cell nuclear
antigen (PCNA; 176740), a DNA polymerase sliding clamp involved in DNA
synthesis and repair, is a substrate. PCNA is monoubiquitinated through
RAD6 and RAD18, modified by lys63-linked multiubiquitination, which
additionally requires MMS2, UBC13, and RAD5, and is conjugated to SUMO
by UBC9. All 3 modifications affect the same lysine residue of PCNA,
K164, suggesting that they label PCNA for alternative functions. Hoege
et al. (2002) demonstrated that these modifications differentially
affect resistance to DNA damage, and that damage-induced PCNA
ubiquitination is elementary for DNA repair and occurs at the same
conserved residue in yeast and humans.
*FIELD* RF
1. Fritsche, J.; Rehli, M.; Krause, S. W.; Andreesen, R.; Kreutz,
M.: Molecular cloning of a 1-alpha,25-dihydroxyvitamin D3-inducible
transcript (DDVit 1) in human blood monocytes. Biochem. Biophys.
Res. Commun. 235: 407-412, 1997.
2. Hoege, C.; Pfander, B.; Moldovan, G.-L.; Pyrowolakis, G.; Jentsch,
S.: RAD6-dependent DNA repair is linked to modification of PCNA by
ubiquitin and SUMO. Nature 419: 135-141, 2002.
3. Hofmann, R. M.; Pickart, C. M.: Noncanonical MMS2-encoded ubiquitin-conjugating
enzyme functions in assembly of novel polyubiquitin chains for DNA
repair. Cell 96: 645-653, 1999.
4. 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.: 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. Molec. Cell. Biol. 18: 576-589,
1998.
*FIELD* CN
Ada Hamosh - updated: 9/30/2002
Stylianos E. Antonarakis - updated: 3/25/1999
*FIELD* CD
Patti M. Sherman: 8/24/1998
*FIELD* ED
alopez: 01/29/2007
alopez: 10/1/2002
tkritzer: 9/30/2002
mgross: 3/31/1999
mgross: 3/29/1999
terry: 3/25/1999
carol: 1/6/1999
alopez: 9/22/1998