UB2V2_RAT
ID UB2V2_RAT Reviewed; 145 AA.
AC Q7M767; Q8CHN0;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 variant 2;
DE AltName: Full=Ubiquitin-conjugating enzyme variant MMS2;
GN Name=Ube2v2; Synonyms=Mms2, Uev2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Fetal cerebellum;
RX PubMed=12750002; DOI=10.1016/s0169-328x(03)00060-3;
RA Hofsaess U., Kapfhammer J.P.;
RT "Identification of numerous genes differentially expressed in rat brain
RT during postnatal development by suppression subtractive hybridization and
RT expression analysis of the novel rat gene rMMS2.";
RL Brain Res. Mol. Brain Res. 113:13-27(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [3]
RP PROTEIN SEQUENCE OF 15-24; 46-55 AND 73-81, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [4]
RP FUNCTION, DEVELOPMENTAL STAGE, AND INDUCTION BY ANGIOTENSIN-II.
RX PubMed=17068200; DOI=10.1210/me.2006-0005;
RA Li J.-M., Mogi M., Tsukuda K., Tomochika H., Iwanami J., Min L.-J.,
RA Nahmias C., Iwai M., Horiuchi M.;
RT "Angiotensin II-induced neural differentiation via angiotensin II type 2
RT (AT2) receptor-MMS2 cascade involving interaction between AT2 receptor-
RT interacting protein and Src homology 2 domain-containing protein-tyrosine
RT phosphatase 1.";
RL Mol. Endocrinol. 21:499-511(2007).
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:17068200}.
CC -!- SUBUNIT: Heterodimer with UBE2N. Binds CHFR (By similarity).
CC {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in embryonic cerebral cortex,
CC hippocampus and cerebellum between day 18 and up to birth. Levels are
CC distictly lower 10 days after birth, and not detectable in adults (at
CC protein level). {ECO:0000269|PubMed:12750002,
CC ECO:0000269|PubMed:17068200}.
CC -!- INDUCTION: By angiotensin-II or its agonist CGP42112A, via MTUS1 and
CC PTPN6 (at protein level). {ECO:0000269|PubMed:17068200}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AJ515244; CAD56165.1; -; mRNA.
DR EMBL; BN000090; CAD56854.1; -; mRNA.
DR EMBL; BC087593; AAH87593.1; -; mRNA.
DR RefSeq; NP_898875.1; NM_183052.2.
DR AlphaFoldDB; Q7M767; -.
DR SMR; Q7M767; -.
DR STRING; 10116.ENSRNOP00000062102; -.
DR SwissPalm; Q7M767; -.
DR jPOST; Q7M767; -.
DR PaxDb; Q7M767; -.
DR PRIDE; Q7M767; -.
DR GeneID; 287927; -.
DR KEGG; rno:287927; -.
DR UCSC; RGD:727838; rat.
DR CTD; 7336; -.
DR RGD; 727838; Ube2v2.
DR eggNOG; KOG0896; Eukaryota.
DR HOGENOM; CLU_063065_3_0_1; -.
DR InParanoid; Q7M767; -.
DR OMA; WQSSYSI; -.
DR OrthoDB; 1507995at2759; -.
DR PhylomeDB; Q7M767; -.
DR TreeFam; TF316971; -.
DR Reactome; R-RNO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-RNO-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-RNO-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-RNO-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-RNO-69473; G2/M DNA damage checkpoint.
DR Reactome; R-RNO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:Q7M767; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001829; Expressed in cerebellum and 20 other tissues.
DR ExpressionAtlas; Q7M767; baseline and differential.
DR Genevisible; Q7M767; RN.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0031372; C:UBC13-MMS2 complex; ISO:RGD.
DR GO; GO:0000729; P:DNA double-strand break processing; ISO:RGD.
DR GO; GO:0042275; P:error-free postreplication DNA repair; ISO:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:0045739; P:positive regulation of DNA repair; IMP:RGD.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; ISO:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:RGD.
DR GO; GO:1902523; P:positive regulation of protein K63-linked ubiquitination; ISO:RGD.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IMP:RGD.
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; Direct protein sequencing; 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_0000082604"
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"
SQ SEQUENCE 145 AA; 16353 MW; 98D6316D61C36611 CRC64;
MAVSTGVKVP RNFRLLEELE EGQKGVGDGT VSWGLEDDED MTLTRWTGMI IGPPRTNYEN
RIYSLKVECG SKYPEAPPSV RFVTKINMNG INNSSGMVDA RSIPVLAKWQ NSYSIKVVLQ
ELRRLMMSKE NMKLPQPPEG QTYNN
