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BEGIN_MOUSE
ID   BEGIN_MOUSE             Reviewed;         600 AA.
AC   Q68EF6;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Brain-enriched guanylate kinase-associated protein;
GN   Name=Begain;
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 [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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-600.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-137, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229; SER-246; THR-249;
RP   SER-265; SER-483 AND SER-485, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
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).
RN   [6]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-380, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryo;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
CC   -!- FUNCTION: May sustain the structure of the postsynaptic density (PSD).
CC   -!- SUBUNIT: Interacts with DLG4 and DLGAP1 and forms a ternary complex.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC       Peripheral membrane protein {ECO:0000250}.
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DR   EMBL; AC140111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC080282; AAH80282.1; -; mRNA.
DR   CCDS; CCDS88400.1; -.
DR   RefSeq; NP_001156647.1; NM_001163175.1.
DR   RefSeq; XP_006516107.1; XM_006516044.2.
DR   RefSeq; XP_011242432.1; XM_011244130.2.
DR   AlphaFoldDB; Q68EF6; -.
DR   SMR; Q68EF6; -.
DR   BioGRID; 237646; 4.
DR   IntAct; Q68EF6; 4.
DR   MINT; Q68EF6; -.
DR   STRING; 10090.ENSMUSP00000140393; -.
DR   iPTMnet; Q68EF6; -.
DR   PhosphoSitePlus; Q68EF6; -.
DR   PaxDb; Q68EF6; -.
DR   PRIDE; Q68EF6; -.
DR   ProteomicsDB; 273554; -.
DR   Antibodypedia; 146; 171 antibodies from 27 providers.
DR   DNASU; 380785; -.
DR   Ensembl; ENSMUST00000238841; ENSMUSP00000158999; ENSMUSG00000040867.
DR   GeneID; 380785; -.
DR   KEGG; mmu:380785; -.
DR   CTD; 57596; -.
DR   MGI; MGI:3044626; Begain.
DR   VEuPathDB; HostDB:ENSMUSG00000040867; -.
DR   eggNOG; ENOG502QUGW; Eukaryota.
DR   GeneTree; ENSGT00940000161760; -.
DR   InParanoid; Q68EF6; -.
DR   OrthoDB; 443898at2759; -.
DR   PhylomeDB; Q68EF6; -.
DR   BioGRID-ORCS; 380785; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Begain; mouse.
DR   PRO; PR:Q68EF6; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q68EF6; protein.
DR   Bgee; ENSMUSG00000040867; Expressed in hypothalamus and 67 other tissues.
DR   ExpressionAtlas; Q68EF6; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0098794; C:postsynapse; ISO:MGI.
DR   GO; GO:0098793; C:presynapse; IDA:MGI.
DR   GO; GO:0045202; C:synapse; ISO:MGI.
DR   GO; GO:0098817; P:evoked excitatory postsynaptic potential; IDA:MGI.
DR   GO; GO:0098962; P:regulation of postsynaptic neurotransmitter receptor activity; IDA:SynGO.
DR   InterPro; IPR033584; BEGAIN.
DR   InterPro; IPR043441; Tjap1/BEGAIN.
DR   PANTHER; PTHR28664; PTHR28664; 1.
DR   PANTHER; PTHR28664:SF2; PTHR28664:SF2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Membrane; Methylation; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..600
FT                   /note="Brain-enriched guanylate kinase-associated protein"
FT                   /id="PRO_0000064905"
FT   REGION          192..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          537..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..218
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..590
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT   MOD_RES         137
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18034455"
FT   MOD_RES         200
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT   MOD_RES         229
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         246
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16452087,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         249
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         265
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         372
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT   MOD_RES         380
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         463
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT   MOD_RES         473
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT   MOD_RES         483
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         485
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         508
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT   MOD_RES         510
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT   MOD_RES         514
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT   MOD_RES         560
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUH8"
FT   MOD_RES         570
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUH8"
SQ   SEQUENCE   600 AA;  65309 MW;  0BECA620CF2971D0 CRC64;
     MEKLSALQEQ KGELRKRLSY TTHKLEKLET EFDSTRHYLE IELRRAQEEL DKVTEKLRRI
     QSNYMALQRI NQELEDKLYR MGQHYEEEKR AMSHEIVALN SHLLEAKVTI DKLSEDNELY
     RKDCNLAAQL LQCSQTYGRV HKVSELPSDF QQRVSLHMEK HGCSLPSALC HPAYADSVPT
     CVIAKVLEKP DPGSLSSRMS DASARDLGYR DGVEKSGPRP PYKGDIYCSD PALYCPDERE
     HARRPSVDTP VTDVGFLRAQ NSTDSAAEEE EEAEAAAFPE AYRREAYQGY AASLPTSSSY
     SSFSATSEEK EHAQAGTLTA SQQAIYLSSR DEFFNRKPSA TYGSGPRFAK AASTLGSPLE
     AQVAPGFART VSPYPAEPYR YPASPGPQQA LMPPNLWSLR AKPSGNRLAG EDIRGQWRPV
     SVEDVGAYSY QAGAAAGRAA SPCNYSERYY GGGGGGGAAG GGSPGDKAEG RASPLYATYK
     ADSFSEGDDL SQGHLAEPCF LRAGGDLSLS PSRSADALAG YAASDGDGDR LRVQLCGAGS
     SPEPEHGSRE SLEPSSMEAS PEMHPPTRLS PQQAFPRTGG SGLSRKDSLT KAQLYGTLLN
 
 
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