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SNF5_MOUSE
ID   SNF5_MOUSE              Reviewed;         385 AA.
AC   Q9Z0H3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 171.
DE   RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;
DE   AltName: Full=BRG1-associated factor 47;
DE            Short=BAF47;
DE   AltName: Full=Integrase interactor 1 protein;
DE   AltName: Full=SNF5 homolog;
DE            Short=mSNF5;
GN   Name=Smarcb1; Synonyms=Baf47, Ini1, Snf5l1;
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] (ISOFORMS A AND B).
RX   PubMed=10208879; DOI=10.1006/bbrc.1999.0563;
RA   Bruder C.E., Dumanski J.P., Kedra D.;
RT   "The mouse ortholog of the human SMARCB1 gene encodes two splice forms.";
RL   Biochem. Biophys. Res. Commun. 257:886-890(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC   STRAIN=C57BL/6J; TISSUE=Tongue;
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   INTERACTION WITH MAEL.
RX   PubMed=16787967; DOI=10.1093/hmg/ddl158;
RA   Costa Y., Speed R.M., Gautier P., Semple C.A., Maratou K., Turner J.M.A.,
RA   Cooke H.J.;
RT   "Mouse MAELSTROM: the link between meiotic silencing of unsynapsed
RT   chromatin and microRNA pathway?";
RL   Hum. Mol. Genet. 15:2324-2334(2006).
RN   [4]
RP   FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS
RP   SPECTROMETRY, IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
RA   Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T., Wu H.,
RA   Aebersold R., Graef I.A., Crabtree G.R.;
RT   "An essential switch in subunit composition of a chromatin remodeling
RT   complex during neural development.";
RL   Neuron 55:201-215(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Spleen, 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).
RN   [6]
RP   INTERACTION WITH CEBPB.
RX   PubMed=20111005; DOI=10.1038/emboj.2010.3;
RA   Kowenz-Leutz E., Pless O., Dittmar G., Knoblich M., Leutz A.;
RT   "Crosstalk between C/EBPbeta phosphorylation, arginine methylation, and
RT   SWI/SNF/Mediator implies an indexing transcription factor code.";
RL   EMBO J. 29:1105-1115(2010).
RN   [7]
RP   REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
RX   PubMed=22952240; DOI=10.1074/jbc.r111.309302;
RA   Euskirchen G., Auerbach R.K., Snyder M.;
RT   "SWI/SNF chromatin-remodeling factors: multiscale analyses and diverse
RT   functions.";
RL   J. Biol. Chem. 287:30897-30905(2012).
RN   [8]
RP   REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
RX   PubMed=26601204; DOI=10.1126/sciadv.1500447;
RA   Kadoch C., Crabtree G.R.;
RT   "Mammalian SWI/SNF chromatin remodeling complexes and cancer: Mechanistic
RT   insights gained from human genomics.";
RL   Sci. Adv. 1:E1500447-E1500447(2015).
RN   [9]
RP   INTERACTION WITH FOS; FOSB; FOSL1 AND FOSL2.
RX   PubMed=29272704; DOI=10.1016/j.molcel.2017.11.026;
RA   Vierbuchen T., Ling E., Cowley C.J., Couch C.H., Wang X., Harmin D.A.,
RA   Roberts C.W.M., Greenberg M.E.;
RT   "AP-1 Transcription Factors and the BAF Complex Mediate Signal-Dependent
RT   Enhancer Selection.";
RL   Mol. Cell 68:1067-1082.e12(2017).
CC   -!- FUNCTION: Core component of the BAF (SWI/SNF) complex. This ATP-
CC       dependent chromatin-remodeling complex plays important roles in cell
CC       proliferation and differentiation, in cellular antiviral activities and
CC       inhibition of tumor formation. The BAF complex is able to create a
CC       stable, altered form of chromatin that constrains fewer negative
CC       supercoils than normal. This change in supercoiling would be due to the
CC       conversion of up to one-half of the nucleosomes on polynucleosomal
CC       arrays into asymmetric structures, termed altosomes, each composed of 2
CC       histones octamers. Stimulates in vitro the remodeling activity of
CC       SMARCA4/BRG1/BAF190A. Plays a key role in cell-cycle control and causes
CC       cell cycle arrest in G0/G1. Belongs to the neural progenitors-specific
CC       chromatin remodeling complex (npBAF complex) and the neuron-specific
CC       chromatin remodeling complex (nBAF complex). During neural development
CC       a switch from a stem/progenitor to a postmitotic chromatin remodeling
CC       mechanism occurs as neurons exit the cell cycle and become committed to
CC       their adult state. The transition from proliferating neural
CC       stem/progenitor cells to postmitotic neurons requires a switch in
CC       subunit composition of the npBAF and nBAF complexes. As neural
CC       progenitors exit mitosis and differentiate into neurons, npBAF
CC       complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged
CC       for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C
CC       subunits in neuron-specific complexes (nBAF). The npBAF complex is
CC       essential for the self-renewal/proliferative capacity of the
CC       multipotent neural stem cells. The nBAF complex along with CREST plays
CC       a role regulating the activity of genes essential for dendrite growth.
CC       {ECO:0000250|UniProtKB:Q12824, ECO:0000269|PubMed:17640523,
CC       ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
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 (Probable). Component of the BAF complex, which includes at
CC       least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM,
CC       SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57
CC       SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
CC       SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C (By similarity). In
CC       muscle cells, the BAF complex also contains DPF3. Component of neural
CC       progenitors-specific chromatin remodeling complex (npBAF complex)
CC       composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A,
CC       SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A,
CC       SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170,
CC       PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific
CC       chromatin remodeling complex (nBAF complex) composed of at least,
CC       ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
CC       SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
CC       SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
CC       DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523). Component of
CC       the SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of
CC       SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B,
CC       SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C,
CC       SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin
CC       (PubMed:26601204). Binds to double-stranded DNA. Interacts with CEBPB
CC       (when not methylated) (PubMed:20111005). Interacts with PIH1D1.
CC       Interacts with MYK and MAEL (PubMed:16787967). Interacts with PPP1R15A
CC       (By similarity). Interacts with DPF2 (By similarity). Interacts with
CC       YWHAZ (By similarity). Interacts with ERCC6 (By similarity). Interacts
CC       with FOS, FOSB isoform 1 and 2, FOSL1 and FOSL2 (PubMed:29272704).
CC       {ECO:0000250|UniProtKB:Q12824, ECO:0000269|PubMed:16787967,
CC       ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:20111005,
CC       ECO:0000269|PubMed:29272704, ECO:0000303|PubMed:22952240,
CC       ECO:0000303|PubMed:26601204}.
CC   -!- INTERACTION:
CC       Q9Z0H3; P97496: Smarcc1; NbExp=5; IntAct=EBI-689365, EBI-648047;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A; Synonyms=INI1A;
CC         IsoId=Q9Z0H3-1; Sequence=Displayed;
CC       Name=B; Synonyms=INI1B;
CC         IsoId=Q9Z0H3-2; Sequence=VSP_004400;
CC   -!- DEVELOPMENTAL STAGE: Expressed ubiquitously throughout the developing
CC       spinal cord, brain and other embryonic tissues at 10.5 dpc-16.5 dpc.
CC       {ECO:0000269|PubMed:17640523}.
CC   -!- DOMAIN: The N-terminal DNA-binding region is structurally similar to
CC       winged helix domains. {ECO:0000250|UniProtKB:Q12824}.
CC   -!- SIMILARITY: Belongs to the SNF5 family. {ECO:0000305}.
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DR   EMBL; AJ011740; CAA09761.1; -; mRNA.
DR   EMBL; AJ011739; CAA09760.1; -; mRNA.
DR   EMBL; BC025163; AAH25163.1; -; mRNA.
DR   CCDS; CCDS23936.1; -. [Q9Z0H3-1]
DR   CCDS; CCDS48602.1; -. [Q9Z0H3-2]
DR   RefSeq; NP_035548.1; NM_011418.2. [Q9Z0H3-1]
DR   AlphaFoldDB; Q9Z0H3; -.
DR   BMRB; Q9Z0H3; -.
DR   SMR; Q9Z0H3; -.
DR   BioGRID; 203337; 17.
DR   ComplexPortal; CPX-1232; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1233; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1234; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1235; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1236; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1237; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1238; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1239; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1240; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1241; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1242; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1243; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1244; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1245; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1246; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1247; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1248; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
DR   ComplexPortal; CPX-1250; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
DR   ComplexPortal; CPX-1251; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
DR   ComplexPortal; CPX-1252; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1253; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1254; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1255; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1256; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1257; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1258; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1259; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1261; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1262; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1263; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1264; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR   CORUM; Q9Z0H3; -.
DR   DIP; DIP-34373N; -.
DR   IntAct; Q9Z0H3; 12.
DR   STRING; 10090.ENSMUSP00000000925; -.
DR   iPTMnet; Q9Z0H3; -.
DR   PhosphoSitePlus; Q9Z0H3; -.
DR   EPD; Q9Z0H3; -.
DR   MaxQB; Q9Z0H3; -.
DR   PaxDb; Q9Z0H3; -.
DR   PRIDE; Q9Z0H3; -.
DR   ProteomicsDB; 261592; -. [Q9Z0H3-1]
DR   ProteomicsDB; 261593; -. [Q9Z0H3-2]
DR   Antibodypedia; 3973; 546 antibodies from 44 providers.
DR   DNASU; 20587; -.
DR   Ensembl; ENSMUST00000000925; ENSMUSP00000000925; ENSMUSG00000000902. [Q9Z0H3-1]
DR   Ensembl; ENSMUST00000121304; ENSMUSP00000112463; ENSMUSG00000000902. [Q9Z0H3-2]
DR   GeneID; 20587; -.
DR   KEGG; mmu:20587; -.
DR   UCSC; uc007ftm.2; mouse. [Q9Z0H3-1]
DR   CTD; 6598; -.
DR   MGI; MGI:1328366; Smarcb1.
DR   VEuPathDB; HostDB:ENSMUSG00000000902; -.
DR   eggNOG; KOG1649; Eukaryota.
DR   GeneTree; ENSGT00440000038585; -.
DR   HOGENOM; CLU_035084_0_0_1; -.
DR   InParanoid; Q9Z0H3; -.
DR   OMA; QLWKRMA; -.
DR   PhylomeDB; Q9Z0H3; -.
DR   TreeFam; TF105993; -.
DR   Reactome; R-MMU-3214858; RMTs methylate histone arginines.
DR   Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR   BioGRID-ORCS; 20587; 20 hits in 116 CRISPR screens.
DR   ChiTaRS; Smarcb1; mouse.
DR   PRO; PR:Q9Z0H3; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q9Z0H3; protein.
DR   Bgee; ENSMUSG00000000902; Expressed in rostral migratory stream and 275 other tissues.
DR   ExpressionAtlas; Q9Z0H3; baseline and differential.
DR   Genevisible; Q9Z0H3; MM.
DR   GO; GO:0140092; C:bBAF complex; IC:ComplexPortal.
DR   GO; GO:0035060; C:brahma complex; IBA:GO_Central.
DR   GO; GO:0000785; C:chromatin; ISO:MGI.
DR   GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:0043073; C:germ cell nucleus; IDA:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR   GO; GO:0071565; C:nBAF complex; IDA:UniProtKB.
DR   GO; GO:0071564; C:npBAF complex; IDA:UniProtKB.
DR   GO; GO:0000228; C:nuclear chromosome; IEA:InterPro.
DR   GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0016586; C:RSC-type complex; IC:ComplexPortal.
DR   GO; GO:0016514; C:SWI/SNF complex; IDA:MGI.
DR   GO; GO:0001741; C:XY body; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0002039; F:p53 binding; ISO:MGI.
DR   GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0030957; F:Tat protein binding; ISO:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0001824; P:blastocyst development; IMP:MGI.
DR   GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR   GO; GO:0070365; P:hepatocyte differentiation; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:1900110; P:negative regulation of histone H3-K9 dimethylation; ISO:MGI.
DR   GO; GO:1900113; P:negative regulation of histone H3-K9 trimethylation; ISO:MGI.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0006337; P:nucleosome disassembly; ISO:MGI.
DR   GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR   GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR   GO; GO:1902661; P:positive regulation of glucose mediated signaling pathway; ISO:MGI.
DR   GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; ISO:MGI.
DR   GO; GO:0090240; P:positive regulation of histone H4 acetylation; ISO:MGI.
DR   GO; GO:0045663; P:positive regulation of myoblast differentiation; IC:ComplexPortal.
DR   GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR   GO; GO:0045582; P:positive regulation of T cell differentiation; IC:ComplexPortal.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISO:MGI.
DR   GO; GO:0070316; P:regulation of G0 to G1 transition; IC:ComplexPortal.
DR   GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR   GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR   GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0039692; P:single stranded viral RNA replication via double stranded DNA intermediate; ISO:MGI.
DR   InterPro; IPR017393; Sfh1/SNF5.
DR   InterPro; IPR006939; SNF5.
DR   Pfam; PF04855; SNF5; 1.
DR   PIRSF; PIRSF038126; SWI_SNF; 1.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Cell cycle; Chromatin regulator;
KW   DNA-binding; Isopeptide bond; Neurogenesis; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Transcription; Transcription regulation;
KW   Tumor suppressor; Ubl conjugation.
FT   CHAIN           1..385
FT                   /note="SWI/SNF-related matrix-associated actin-dependent
FT                   regulator of chromatin subfamily B member 1"
FT                   /id="PRO_0000205949"
FT   REPEAT          186..245
FT                   /note="1"
FT   REPEAT          259..319
FT                   /note="2"
FT   REGION          1..113
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q12824"
FT   REGION          186..319
FT                   /note="2 X approximate tandem repeats"
FT   REGION          186..245
FT                   /note="MYC-binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q12824"
FT   REGION          304..318
FT                   /note="Interaction with PPP1R15A"
FT                   /evidence="ECO:0000250|UniProtKB:Q12824"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12824"
FT   CROSSLNK        106
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q12824"
FT   CROSSLNK        108
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q12824"
FT   CROSSLNK        124
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q12824"
FT   CROSSLNK        161
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q12824"
FT   VAR_SEQ         69..77
FT                   /note="Missing (in isoform B)"
FT                   /evidence="ECO:0000303|PubMed:10208879"
FT                   /id="VSP_004400"
SQ   SEQUENCE   385 AA;  44141 MW;  B7BCA26875BD943D CRC64;
     MMMMALSKTF GQKPVKFQLE DDGEFYMIGS EVGNYLRMFR GSLYKRYPSL WRRLATVEER
     KKIVASSHGK KTKPNTKDHG YTTLATSVTL LKASEVEEIL DGNDEKYKAV SISTEPPTYL
     REQKAKRNSQ WVPTLPNSSH HLDAVPCSTT INRNRMGRDK KRTFPLCFDD HDPAVIHENA
     SQPEVLVPIR LDMEIDGQKL RDAFTWNMNE KLMTPEMFSE ILCDDLDLNP LTFVPAIASA
     IRQQIESYPT DSILEDQSDQ RVIIKLNIHV GNISLVDQFE WDMSEKENSP EKFALKLCSE
     LGLGGEFVTT IAYSIRGQLS WHQKTYAFSE NPLPTVEIAI RNTGDADQWC PLLETLTDAE
     MEKKIRDQDR NTRRMRRLAN TAPAW
 
 
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