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BICRA_MOUSE
ID   BICRA_MOUSE             Reviewed;        1578 AA.
AC   F8VPZ9;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=BRD4-interacting chromatin-remodeling complex-associated protein {ECO:0000305};
DE   AltName: Full=Glioma tumor suppressor candidate region gene 1 protein {ECO:0000305};
GN   Name=Bicra {ECO:0000312|MGI:MGI:2154263};
GN   Synonyms=Gltscr1 {ECO:0000312|MGI:MGI:2154263};
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] {ECO:0007744|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   [3] {ECO:0000312|Ensembl:ENSMUSP00000092416}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J;
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [4] {ECO:0007744|PubMed:23806337}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [5] {ECO:0000312|Ensembl:ENSMUSP00000148012}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J;
RG   Ensembl;
RL   Submitted (JUL-2016) to UniProtKB.
RN   [6]
RP   IDENTIFICATION IN THE GBAF COMPLEX.
RX   PubMed=29374058; DOI=10.1074/jbc.ra117.001065;
RA   Alpsoy A., Dykhuizen E.C.;
RT   "Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its paralog
RT   GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes.";
RL   J. Biol. Chem. 293:3892-3903(2018).
CC   -!- FUNCTION: Component of SWI/SNF chromatin remodeling subcomplex GBAF
CC       that carries out key enzymatic activities, changing chromatin structure
CC       by altering DNA-histone contacts within a nucleosome in an ATP-
CC       dependent manner (PubMed:29374058). May play a role in BRD4-mediated
CC       gene transcription (By similarity). {ECO:0000250|UniProtKB:Q9NZM4,
CC       ECO:0000269|PubMed:29374058}.
CC   -!- SUBUNIT: Component of the multiprotein chromatin-remodeling complexes
CC       SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The
CC       canonical complex contains a catalytic subunit (either
CC       SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1,
CC       ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47.
CC       Other subunits specific to each of the complexes may also be present
CC       permitting several possible combinations developmentally and tissue
CC       specific. Component of the SWI/SNF (GBAF) subcomplex, which includes at
CC       least BICRA or BICRAL (mutually exclusive), BRD9, SS18, the core BAF
CC       subunits, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53,
CC       SMARCC1/BAF155, and SMARCD1/BAF60A (PubMed:29374058). Interacts with
CC       BRD4; the interaction bridges BRD4 to the GBAF complex (By similarity).
CC       {ECO:0000250|UniProtKB:Q9NZM4, ECO:0000269|PubMed:29374058}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9NZM4}.
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DR   EMBL; AC148990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC151733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS39780.1; -.
DR   RefSeq; NP_001074887.1; NM_001081418.1.
DR   RefSeq; XP_006539980.1; XM_006539917.3.
DR   AlphaFoldDB; F8VPZ9; -.
DR   ComplexPortal; CPX-4202; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant.
DR   ComplexPortal; CPX-4221; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR   ComplexPortal; CPX-4227; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA2 variant.
DR   ComplexPortal; CPX-4229; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant.
DR   STRING; 10090.ENSMUSP00000092416; -.
DR   iPTMnet; F8VPZ9; -.
DR   PhosphoSitePlus; F8VPZ9; -.
DR   EPD; F8VPZ9; -.
DR   jPOST; F8VPZ9; -.
DR   MaxQB; F8VPZ9; -.
DR   PaxDb; F8VPZ9; -.
DR   PeptideAtlas; F8VPZ9; -.
DR   PRIDE; F8VPZ9; -.
DR   ProteomicsDB; 333221; -.
DR   Antibodypedia; 65070; 78 antibodies from 18 providers.
DR   DNASU; 243842; -.
DR   Ensembl; ENSMUST00000094821; ENSMUSP00000092416; ENSMUSG00000070808.
DR   Ensembl; ENSMUST00000210781; ENSMUSP00000148012; ENSMUSG00000070808.
DR   GeneID; 243842; -.
DR   KEGG; mmu:243842; -.
DR   UCSC; uc009fgu.1; mouse.
DR   CTD; 29998; -.
DR   MGI; MGI:2154263; Bicra.
DR   VEuPathDB; HostDB:ENSMUSG00000070808; -.
DR   eggNOG; ENOG502QU2K; Eukaryota.
DR   GeneTree; ENSGT00940000159112; -.
DR   HOGENOM; CLU_002283_0_0_1; -.
DR   InParanoid; F8VPZ9; -.
DR   OMA; WVGQSHS; -.
DR   OrthoDB; 352636at2759; -.
DR   PhylomeDB; F8VPZ9; -.
DR   TreeFam; TF335495; -.
DR   BioGRID-ORCS; 243842; 9 hits in 71 CRISPR screens.
DR   ChiTaRS; Bicra; mouse.
DR   PRO; PR:F8VPZ9; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; F8VPZ9; protein.
DR   Bgee; ENSMUSG00000070808; Expressed in embryonic brain and 214 other tissues.
DR   Genevisible; F8VPZ9; MM.
DR   GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR   GO; GO:0140288; C:GBAF complex; IC:ComplexPortal.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR   GO; GO:0140537; F:transcription regulator activator activity; ISO:MGI.
DR   GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; IC:ComplexPortal.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IC:ComplexPortal.
DR   GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR   InterPro; IPR038842; BICRA.
DR   InterPro; IPR015671; GSCR1_dom.
DR   PANTHER; PTHR15572:SF1; PTHR15572:SF1; 1.
DR   Pfam; PF15249; GLTSCR1; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..1578
FT                   /note="BRD4-interacting chromatin-remodeling complex-
FT                   associated protein"
FT                   /id="PRO_0000445345"
FT   REGION          80..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          631..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          725..951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1206..1316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1342..1435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1457..1578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        789..841
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        858..891
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        907..951
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1230..1250
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1270..1295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1346..1372
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1499..1531
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1538..1560
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         929
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZM4"
FT   MOD_RES         931
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZM4"
FT   MOD_RES         1067
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZM4"
FT   MOD_RES         1427
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZM4"
FT   CROSSLNK        1327
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NZM4"
SQ   SEQUENCE   1578 AA;  161354 MW;  A9188E16879ADED1 CRC64;
     MDDEDGRCLL DVICDPQALN DFLHGSEKLD SDDLLDAPVE AQSAFYEGPG LHVQEAAANH
     LNPEPSQPAP SVDLDFLEDD ILGSPAAGGG GGGGGAPDQP CDILQQSLQE ANITEQTLEA
     EAELDLGPFQ LPTLQPADNG AGATGAAGAT AVTAGPQALF PGSADLLGLQ APPTVLTHQA
     LVPPQDVVNK ALSVQPFLQP VGLGNVTLQP ISGLQGLPNG SPGNAAAATL GLTPIQVVGQ
     PVMALNPPTS QLLAKQVPVS GYLASAAGPS EPVTLASAGV SPQGAGLVIQ KNLPAAVTTT
     LNGNSVFAGT GAATAAASGA PSGQPLAVAP GLGTSPLVQA PSVILHRTPT PIQPKPTGVL
     PSKLYQLTPK PFPPTGATLT IQGEPGTLPQ QPKAPQNLTF MATGKAGQNV VLSGFPAPAL
     QANVFKQPPV TTTGTAPPQP PGALSKPMSV HLLNQGSSIV IPAQHMLPGQ NQFLLPGTPA
     VQLPQSLSAL PANVGGQILT AAAPHAGGQL IANPILTNQN LAGPLSLGPV LAPHSGAHSA
     AHILSAAPIQ VGQPALFQMP VSLATGSLPT QSQPAPTGPT ATTVLQGVTL PPSAVAMLNT
     PDGLVQPSTP AATTGEATPV LAVQPATQVP PAVTTPLPMG LQQPQAQQPP QVPTPQAATQ
     PQATPPQASP SLASSPEKIV LGQAPPAATT AILTQDSLQM FLPQERSQQP LSTEGPHLSV
     PASVIVSAPP PAQDPALATP VTKGAGLGAQ TPDSRASPAP APQIPAAAPL KAPGPASSPS
     LPHQAPLGDS PHMPSPHPAR PPSRPPSRPH SRPPSQPQSL TCPPSEPTLH PCPPPQGPPT
     LPGIFVIQNQ LGAPPPASTP ASTAPGPPQP PLRPPSQPPE GPLPPASHLP PASTPSAVAS
     SSEPSARLPV PTPPDFQLQF PPSQGPHKSP TPPPALHMVP EPTAPPPPPP RTFQMVTAPF
     PALPQPKALL ERFHQVPSGI ILQNKAGGTP TTPQTSTTLG TLTGPTASVL VSGQAPPGTP
     AASSHVPAST PMATTGLPPL LPAENKAFAS NLPTLSVAKA TVSGPGKPPA IQYDSKLCSL
     KKQPLLQPSK EACFLEHLHK HQGSVLHPDY KTAFPSFEDA LHRLLPYHVY QGALPSPNDY
     HKVDEEFETV STQLLKRTQA MLNKYRLLLL EESRRVSPSA EMVMIDRMFI QEEKTTLALD
     KQLAKEKPDE YVSSSRSLGF PVPVSSEGHR LPSHGQSSSS STSGTSAQPP PHLPTKLVIR
     HGGAGGSPSV TWARASSSLS STSSSSSSSS AASSLDADED GPMPTRNRPP IKTYEARSRI
     GLKLKIKQEA GLSKVVHNTA LDPVHQPLPA PTPAKGAEPP PHPAPPPLPP ATQAQMNGTL
     DHPPPAVRKP TVPASCPRLP LRKTYRENMG NPGAAEGAQG RPRGAGSPTP LPTKVDEATS
     GLIRELAAVE DELYQRVLKG GPPPPETPAS ATSQGPTEPS WEAPVLPPAK RRKSESPDVD
     QASFSSDSPQ DDTLTEHLQS AIDSILNLQQ APGRTPAGPY PHTGPTPGTP TSPAPLHRPD
     AFPPSSHNGG LGARTLNR
 
 
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