UB2V2_MOUSE
ID UB2V2_MOUSE Reviewed; 145 AA.
AC Q9D2M8; A6X924; Q8BGH6; Q8CE99; Q8K2V7; Q9CYD7; Q9ERI8;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 variant 2;
DE AltName: Full=Ubc-like protein MMS2;
GN Name=Ube2v2; Synonyms=Mms2, Uev2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RX PubMed=11406273; DOI=10.1016/s0167-4781(01)00223-8;
RA Franko J., Ashley C., Xiao W.;
RT "Molecular cloning and functional characterization of two murine cDNAs
RT which encode Ubc variants involved in DNA repair and mutagenesis.";
RL Biochim. Biophys. Acta 1519:70-77(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, Fetus, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RC TISSUE=Embryonic germ cell, Fetal brain, and Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:11406273}.
CC -!- SUBUNIT: Heterodimer with UBE2N. Binds CHFR (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D2M8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D2M8-2; Sequence=VSP_011529;
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH29742.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF303828; AAG22084.1; -; mRNA.
DR EMBL; AK017786; BAB30932.1; -; mRNA.
DR EMBL; AK019486; BAB31753.1; -; mRNA.
DR EMBL; AK028472; BAC25968.1; -; mRNA.
DR EMBL; AK028742; BAC26094.1; -; mRNA.
DR EMBL; AK031233; BAC27311.1; -; mRNA.
DR EMBL; AK033016; BAC28128.1; -; mRNA.
DR EMBL; CT010522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029742; AAH29742.1; ALT_INIT; mRNA.
DR EMBL; BC058374; AAH58374.1; -; mRNA.
DR EMBL; BC083098; AAH83098.1; -; mRNA.
DR CCDS; CCDS37265.1; -. [Q9D2M8-1]
DR CCDS; CCDS49771.1; -. [Q9D2M8-2]
DR RefSeq; NP_001152823.1; NM_001159351.1. [Q9D2M8-2]
DR RefSeq; NP_076074.2; NM_023585.4. [Q9D2M8-1]
DR AlphaFoldDB; Q9D2M8; -.
DR SMR; Q9D2M8; -.
DR BioGRID; 214171; 5.
DR ComplexPortal; CPX-604; UBC13-MMS2 ubiquitin-conjugating enzyme E2 complex.
DR IntAct; Q9D2M8; 5.
DR MINT; Q9D2M8; -.
DR STRING; 10090.ENSMUSP00000111443; -.
DR iPTMnet; Q9D2M8; -.
DR PhosphoSitePlus; Q9D2M8; -.
DR SwissPalm; Q9D2M8; -.
DR EPD; Q9D2M8; -.
DR jPOST; Q9D2M8; -.
DR MaxQB; Q9D2M8; -.
DR PaxDb; Q9D2M8; -.
DR PeptideAtlas; Q9D2M8; -.
DR PRIDE; Q9D2M8; -.
DR ProteomicsDB; 297777; -. [Q9D2M8-1]
DR ProteomicsDB; 297778; -. [Q9D2M8-2]
DR Antibodypedia; 24348; 317 antibodies from 33 providers.
DR DNASU; 70620; -.
DR Ensembl; ENSMUST00000115776; ENSMUSP00000111442; ENSMUSG00000022674. [Q9D2M8-2]
DR Ensembl; ENSMUST00000115777; ENSMUSP00000111443; ENSMUSG00000022674. [Q9D2M8-1]
DR GeneID; 70620; -.
DR KEGG; mmu:70620; -.
DR UCSC; uc007yhp.2; mouse. [Q9D2M8-1]
DR UCSC; uc007yhq.2; mouse. [Q9D2M8-2]
DR CTD; 7336; -.
DR MGI; MGI:1917870; Ube2v2.
DR VEuPathDB; HostDB:ENSMUSG00000022674; -.
DR eggNOG; KOG0896; Eukaryota.
DR GeneTree; ENSGT00740000115534; -.
DR HOGENOM; CLU_063065_3_0_1; -.
DR InParanoid; Q9D2M8; -.
DR OMA; WQSSYSI; -.
DR PhylomeDB; Q9D2M8; -.
DR TreeFam; TF316971; -.
DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR BioGRID-ORCS; 70620; 6 hits in 107 CRISPR screens.
DR ChiTaRS; Ube2v2; mouse.
DR PRO; PR:Q9D2M8; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9D2M8; protein.
DR Bgee; ENSMUSG00000022674; Expressed in dentate gyrus of hippocampal formation granule cell and 234 other tissues.
DR ExpressionAtlas; Q9D2M8; baseline and differential.
DR Genevisible; Q9D2M8; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0031372; C:UBC13-MMS2 complex; ISO:MGI.
DR GO; GO:0000729; P:DNA double-strand break processing; ISO:MGI.
DR GO; GO:0042275; P:error-free postreplication DNA repair; IGI:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:MGI.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; ISO:MGI.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
DR GO; GO:1902523; P:positive regulation of protein K63-linked ubiquitination; ISO:MGI.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISO:MGI.
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 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 Acetylation; Alternative splicing; Reference proteome;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q15819"
FT CHAIN 2..145
FT /note="Ubiquitin-conjugating enzyme E2 variant 2"
FT /id="PRO_0000082603"
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:0000250|UniProtKB:Q15819"
FT VAR_SEQ 56..97
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011529"
FT CONFLICT 16
FT /note="L -> W (in Ref. 2; BAC26094)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="D -> N (in Ref. 2; BAC25968/BAC27311/BAC28128 and 3;
FT BAB31753)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="A -> D (in Ref. 1; AAG22084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 145 AA; 16367 MW; 98D63173902C6611 CRC64;
MAVSTGVKVP RNFRLLEELE EGQKGVGDGT VSWGLEDDED MTLTRWTGMI IGPPRTNYEN
RIYSLKVECG SKYPEAPPSV RFVTKINMNG INNSSGMVDA RSIPVLAKWQ NSYSIKVILQ
ELRRLMMSKE NMKLPQPPEG QTYNN
