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UBE2A_MOUSE
ID   UBE2A_MOUSE             Reviewed;         152 AA.
AC   Q9Z255;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 A;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme A;
DE   AltName: Full=RAD6 homolog A;
DE            Short=HR6A;
DE            Short=mHR6A;
DE   AltName: Full=Ubiquitin carrier protein A;
DE   AltName: Full=Ubiquitin-protein ligase A;
GN   Name=Ube2a; Synonyms=Rad6a;
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].
RC   STRAIN=BCBA; TISSUE=Brain;
RA   Roest H.P., van Klaveren J., Koken M.H.M., Vermey M., van Cappellen W.A.,
RA   Baarends W.M., Hoogerbrugge J.W., Bootsma D., Hoeijmakers J.H.J.,
RA   Grootegoed J.A., de Wit J.;
RT   "Isolation of mHR6A, a gene highly homologous to the male fertility gene
RT   mHR6B.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skeletal muscle;
RA   Kwon Y.T., Varshavsky A.;
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   INTERACTION WITH RFPL4A AND CCNB1.
RX   PubMed=12525704; DOI=10.1073/pnas.0234474100;
RA   Suzumori N., Burns K.H., Yan W., Matzuk M.M.;
RT   "RFPL4 interacts with oocyte proteins of the ubiquitin-proteasome
RT   degradation pathway.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:550-555(2003).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Lung, Pancreas, 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: Accepts ubiquitin from the E1 complex and catalyzes its
CC       covalent attachment to other proteins. In association with the E3
CC       enzyme BRE1 (RNF20 and/or RNF40), it plays a role in transcription
CC       regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-
CC       120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic
CC       transcriptional activation, elongation by RNA polymerase II, telomeric
CC       silencing, and is also a prerequisite for H3K4me and H3K79me formation.
CC       In vitro catalyzes 'Lys-11', as well as 'Lys-48'-linked
CC       polyubiquitination. Required for postreplication repair of UV-damaged
CC       DNA. {ECO:0000250|UniProtKB:P49459}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC         [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC         activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC         conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC         Evidence={ECO:0000250|UniProtKB:P49459, ECO:0000255|PROSITE-
CC         ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBUNIT: Interacts with RAD18 and WAC (By similarity). Interacts with
CC       RFPL4A and CCNB1 (PubMed:12525704). {ECO:0000250|UniProtKB:P49459,
CC       ECO:0000269|PubMed:12525704}.
CC   -!- PTM: Phosphorylation at Ser-120 by CDK9 increases activity towards
CC       histone H2B. {ECO:0000250|UniProtKB:P49459}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; AF089812; AAC64563.1; -; mRNA.
DR   EMBL; AF383148; AAK62984.1; -; mRNA.
DR   EMBL; BC026053; AAH26053.1; -; mRNA.
DR   CCDS; CCDS30064.1; -.
DR   RefSeq; NP_062642.1; NM_019668.4.
DR   AlphaFoldDB; Q9Z255; -.
DR   SMR; Q9Z255; -.
DR   BioGRID; 204414; 9.
DR   STRING; 10090.ENSMUSP00000016452; -.
DR   iPTMnet; Q9Z255; -.
DR   PhosphoSitePlus; Q9Z255; -.
DR   SwissPalm; Q9Z255; -.
DR   EPD; Q9Z255; -.
DR   MaxQB; Q9Z255; -.
DR   PaxDb; Q9Z255; -.
DR   PRIDE; Q9Z255; -.
DR   ProteomicsDB; 298179; -.
DR   Antibodypedia; 29799; 209 antibodies from 28 providers.
DR   DNASU; 22209; -.
DR   Ensembl; ENSMUST00000016452; ENSMUSP00000016452; ENSMUSG00000016308.
DR   GeneID; 22209; -.
DR   KEGG; mmu:22209; -.
DR   UCSC; uc009sxv.1; mouse.
DR   CTD; 7319; -.
DR   MGI; MGI:102959; Ube2a.
DR   VEuPathDB; HostDB:ENSMUSG00000016308; -.
DR   eggNOG; KOG0419; Eukaryota.
DR   GeneTree; ENSGT00940000155075; -.
DR   HOGENOM; CLU_030988_10_2_1; -.
DR   InParanoid; Q9Z255; -.
DR   OMA; DHKSQYI; -.
DR   OrthoDB; 1292821at2759; -.
DR   PhylomeDB; Q9Z255; -.
DR   TreeFam; TF101128; -.
DR   Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 22209; 17 hits in 113 CRISPR screens.
DR   ChiTaRS; Ube2a; mouse.
DR   PRO; PR:Q9Z255; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q9Z255; protein.
DR   Bgee; ENSMUSG00000016308; Expressed in placenta labyrinth and 263 other tissues.
DR   ExpressionAtlas; Q9Z255; baseline and differential.
DR   Genevisible; Q9Z255; MM.
DR   GO; GO:0000785; C:chromatin; IDA:MGI.
DR   GO; GO:0033503; C:HULC complex; ISS:UniProtKB.
DR   GO; GO:0001741; C:XY body; IDA:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IGI:MGI.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR   GO; GO:0006281; P:DNA repair; ISO:MGI.
DR   GO; GO:0033522; P:histone H2A ubiquitination; ISO:MGI.
DR   GO; GO:0016574; P:histone ubiquitination; IBA:GO_Central.
DR   GO; GO:0001701; P:in utero embryonic development; IGI:MGI.
DR   GO; GO:0060135; P:maternal process involved in female pregnancy; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:MGI.
DR   GO; GO:0009411; P:response to UV; ISO:MGI.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; -; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   Pfam; PF00179; UQ_con; 1.
DR   SUPFAM; SSF54495; SSF54495; 1.
DR   PROSITE; PS00183; UBC_1; 1.
DR   PROSITE; PS50127; UBC_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA damage; DNA repair; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..152
FT                   /note="Ubiquitin-conjugating enzyme E2 A"
FT                   /id="PRO_0000082446"
FT   DOMAIN          4..150
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        88
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   MOD_RES         120
FT                   /note="Phosphoserine; by CDK9"
FT                   /evidence="ECO:0000250|UniProtKB:P49459"
SQ   SEQUENCE   152 AA;  17315 MW;  0AAEB5B7770E47E2 CRC64;
     MSTPARRRLM RDFKRLQEDP PAGVSGAPSE NNIMVWNAVI FGPEGTPFED GTFKLTIEFT
     EEYPNKPPTV RFVSKMFHPN VYADGSICLD ILQNRWSPTY DVSSILTSIQ SLLDEPNPNS
     PANSQAAQLY QENKREYEKR VSAIVEQSWR DC
 
 
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