SMRC1_MOUSE
ID SMRC1_MOUSE Reviewed; 1104 AA.
AC P97496; Q7TS80; Q7TT29;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=SWI/SNF complex subunit SMARCC1;
DE AltName: Full=BRG1-associated factor 155;
DE AltName: Full=SWI/SNF complex 155 kDa subunit;
DE AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 1;
DE AltName: Full=SWI3-related protein;
DE Short=BAF155;
GN Name=Smarcc1; Synonyms=Baf155, Srg3;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=9151708; DOI=10.1084/jem.185.10.1827;
RA Jeon S.H., Kang M.G., Kim Y.H., Jin Y.H., Lee C., Chung H.-Y., Kwon H.,
RA Park S.D., Seong R.H.;
RT "A new mouse gene, SRG3, related to the SWI3 of Saccharomyces cerevisiae,
RT is required for apoptosis induced by glucocorticoids in a thymoma cell
RT line.";
RL J. Exp. Med. 185:1827-1836(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-892 (ISOFORM 1).
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 FUNCTION.
RX PubMed=11604513; DOI=10.1128/mcb.21.22.7787-7795.2001;
RA Kim J.K., Huh S.-O., Choi H., Lee K.-S., Shin D., Lee C., Nam J.-S.,
RA Kim H., Chung H., Lee H.W., Park S.D., Seong R.H.;
RT "Srg3, a mouse homolog of yeast SWI3, is essential for early embryogenesis
RT and involved in brain development.";
RL Mol. Cell. Biol. 21:7787-7795(2001).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327 AND SER-329, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-327; SER-329; SER-572;
RP SER-775; SER-821 AND SER-824, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, 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 [7]
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 [8]
RP INTERACTION WITH KDM6B.
RX PubMed=21095589; DOI=10.1016/j.molcel.2010.10.028;
RA Miller S.A., Mohn S.E., Weinmann A.S.;
RT "Jmjd3 and UTX play a demethylase-independent role in chromatin remodeling
RT to regulate T-box family member-dependent gene expression.";
RL Mol. Cell 40:594-605(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-345, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
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 [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1064, 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).
RN [11]
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 [12]
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 [13]
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: Involved in transcriptional activation and repression of
CC select genes by chromatin remodeling (alteration of DNA-nucleosome
CC topology). Component of SWI/SNF chromatin remodeling complexes that
CC carry out key enzymatic activities, changing chromatin structure by
CC altering DNA-histone contacts within a nucleosome in an ATP-dependent
CC manner. May stimulate the ATPase activity of the catalytic subunit of
CC the complex. Belongs to the neural progenitors-specific chromatin
CC remodeling complex (npBAF complex) and the neuron-specific chromatin
CC remodeling complex (nBAF complex). During neural development a switch
CC from a stem/progenitor to a postmitotic chromatin remodeling mechanism
CC occurs as neurons exit the cell cycle and become committed to their
CC adult state. The transition from proliferating neural stem/progenitor
CC cells to postmitotic neurons requires a switch in subunit composition
CC of the npBAF and nBAF complexes. As neural progenitors exit mitosis and
CC differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A
CC and PHF10/BAF45A, are exchanged for homologous alternative
CC ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-
CC specific complexes (nBAF). The npBAF complex is essential for the self-
CC renewal/proliferative capacity of the multipotent neural stem cells.
CC The nBAF complex along with CREST plays a role regulating the activity
CC of genes essential for dendrite growth. {ECO:0000250|UniProtKB:Q92922,
CC ECO:0000269|PubMed:11604513, 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, 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. In muscle cells, the
CC BAF complex also contains DPF3 (By similarity). 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:22952240, PubMed:26601204). Component of SWI/SNF (GBAF)
CC subcomplex, which includes at least BICRA or BICRAL (mutually
CC exclusive), BRD9, SS18, SMARCA2/BRM, SMARCA4/BRG1/BAF190A,
CC ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A (PubMed:29374058). May
CC also interact with the SIN3A histone deacetylase transcription
CC repressor complex in conjunction with SMARCA2 and SMARCA4. The minimal
CC complex composed of SMARCC1 and SMARCA4 seems to be able to associate
CC with cyclin such as CCNE1 or transcription factors such as KLF1 or
CC GATA1. Interacts with NR3C1 and SMARD1. Interacts with TRIP12; leading
CC to disrupt interaction between TRIP12 and SMARCE1 and prevent SMARCE1
CC ubiquitination (By similarity). Interacts with CEBPB (when not
CC methylated) (PubMed:20111005). Interacts with KDM6B (PubMed:21095589).
CC Interacts with MKKS; the interaction takes place predominantly in the
CC cytoplasm and may modulate SMARCC1 location (By similarity). Interacts
CC with DPF2 (By similarity). Interacts with PRDM1/BLIMP1 (By similarity).
CC Interacts with DPF3a (isoform 2 of DPF3/BAF45C) and with HDGFL2 in a
CC DPF3a-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q92922,
CC ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:20111005,
CC ECO:0000269|PubMed:21095589, ECO:0000269|PubMed:29374058,
CC ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
CC -!- INTERACTION:
CC P97496; Q3TKT4: Smarca4; NbExp=7; IntAct=EBI-648047, EBI-1210244;
CC P97496; Q9Z0H3: Smarcb1; NbExp=5; IntAct=EBI-648047, EBI-689365;
CC P97496; Q61466: Smarcd1; NbExp=3; IntAct=EBI-648047, EBI-371529;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q92922}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P97496-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P97496-2; Sequence=VSP_012489;
CC -!- TISSUE SPECIFICITY: Highly expressed in adult brain, testis and thymus.
CC -!- DEVELOPMENTAL STAGE: Highly expressed in all organs except heart and
CC liver (12.5 dpc and 14.5 dpc). The level of expression gradually
CC diminishes as embryos develop, with expression restricted mostly to the
CC CNS and thymus at 18.5 dpc. Expressed ubiquitously throughout the
CC developing spinal cord, brain and other embryonic tissues at 10.5 dpc-
CC 16.5 dpc. {ECO:0000269|PubMed:17640523}.
CC -!- SIMILARITY: Belongs to the SMARCC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB42085.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U85614; AAB42085.1; ALT_FRAME; mRNA.
DR EMBL; BC052423; AAH52423.1; -; mRNA.
DR EMBL; BC053064; AAH53064.1; -; mRNA.
DR CCDS; CCDS23561.1; -. [P97496-1]
DR PIR; T30967; T30967.
DR RefSeq; NP_033237.2; NM_009211.2. [P97496-1]
DR AlphaFoldDB; P97496; -.
DR BMRB; P97496; -.
DR SMR; P97496; -.
DR BioGRID; 203338; 44.
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-4202; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4204; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4221; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4222; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant.
DR ComplexPortal; CPX-4227; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4228; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4229; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4230; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant.
DR CORUM; P97496; -.
DR DIP; DIP-39986N; -.
DR IntAct; P97496; 34.
DR MINT; P97496; -.
DR STRING; 10090.ENSMUSP00000086094; -.
DR iPTMnet; P97496; -.
DR PhosphoSitePlus; P97496; -.
DR SwissPalm; P97496; -.
DR EPD; P97496; -.
DR jPOST; P97496; -.
DR MaxQB; P97496; -.
DR PaxDb; P97496; -.
DR PeptideAtlas; P97496; -.
DR PRIDE; P97496; -.
DR ProteomicsDB; 257277; -. [P97496-1]
DR ProteomicsDB; 257278; -. [P97496-2]
DR Antibodypedia; 3168; 252 antibodies from 36 providers.
DR DNASU; 20588; -.
DR Ensembl; ENSMUST00000088716; ENSMUSP00000086094; ENSMUSG00000032481. [P97496-1]
DR Ensembl; ENSMUST00000197984; ENSMUSP00000142611; ENSMUSG00000032481. [P97496-2]
DR GeneID; 20588; -.
DR KEGG; mmu:20588; -.
DR UCSC; uc009rto.1; mouse. [P97496-2]
DR UCSC; uc009rtp.1; mouse. [P97496-1]
DR CTD; 6599; -.
DR MGI; MGI:1203524; Smarcc1.
DR VEuPathDB; HostDB:ENSMUSG00000032481; -.
DR eggNOG; KOG1279; Eukaryota.
DR GeneTree; ENSGT00940000156347; -.
DR InParanoid; P97496; -.
DR OMA; CLTRPSI; -.
DR PhylomeDB; P97496; -.
DR TreeFam; TF314710; -.
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; 20588; 7 hits in 78 CRISPR screens.
DR ChiTaRS; Smarcc1; mouse.
DR PRO; PR:P97496; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P97496; protein.
DR Bgee; ENSMUSG00000032481; Expressed in urogenital fold and 257 other tissues.
DR ExpressionAtlas; P97496; baseline and differential.
DR Genevisible; P97496; MM.
DR GO; GO:0035060; C:brahma complex; IC:ComplexPortal.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0140288; C:GBAF complex; IC:ComplexPortal.
DR GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0071565; C:nBAF complex; IDA:UniProtKB.
DR GO; GO:0071564; C:npBAF complex; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016586; C:RSC-type complex; IC:ComplexPortal.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0001741; C:XY body; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0051276; P:chromosome organization; TAS:MGI.
DR GO; GO:0008286; P:insulin receptor signaling pathway; IDA:MGI.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:MGI.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006337; P:nucleosome disassembly; ISO:MGI.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
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; IGI:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; 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; IC:ComplexPortal.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR030087; BAF155.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR032451; SMARCC_C.
DR InterPro; IPR032450; SMARCC_N.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR032448; SWIRM-assoc.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR12802:SF9; PTHR12802:SF9; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF04433; SWIRM; 1.
DR Pfam; PF16495; SWIRM-assoc_1; 1.
DR Pfam; PF16496; SWIRM-assoc_2; 1.
DR Pfam; PF16498; SWIRM-assoc_3; 1.
DR SMART; SM00298; CHROMO; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50934; SWIRM; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromatin regulator; Coiled coil;
KW Cytoplasm; Isopeptide bond; Methylation; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1104
FT /note="SWI/SNF complex subunit SMARCC1"
FT /id="PRO_0000197116"
FT DOMAIN 448..545
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT DOMAIN 617..668
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 295..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 955..1022
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 909..945
FT /evidence="ECO:0000255"
FT COMPBIAS 295..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 769..859
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 955..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 991..1022
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1047..1061
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92922"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92922"
FT MOD_RES 344
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92922"
FT MOD_RES 345
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92922"
FT MOD_RES 353
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92922"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92922"
FT MOD_RES 358
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92922"
FT MOD_RES 397
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92922"
FT MOD_RES 572
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 824
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 947
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92922"
FT MOD_RES 1064
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 178
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92922"
FT CROSSLNK 358
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92922"
FT CROSSLNK 591
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92922"
FT CROSSLNK 738
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92922"
FT CROSSLNK 795
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92922"
FT CROSSLNK 828
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92922"
FT CROSSLNK 855
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92922"
FT VAR_SEQ 1074..1104
FT /note="YPPPPQQQQPPPPADGVPPPPAPGPPASATP -> CK (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012489"
FT CONFLICT 132
FT /note="G -> S (in Ref. 1; AAB42085)"
FT /evidence="ECO:0000305"
FT CONFLICT 468
FT /note="R -> G (in Ref. 1; AAB42085)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="R -> C (in Ref. 1; AAB42085)"
FT /evidence="ECO:0000305"
FT CONFLICT 512
FT /note="R -> L (in Ref. 1; AAB42085)"
FT /evidence="ECO:0000305"
FT CONFLICT 883
FT /note="L -> P (in Ref. 1; AAB42085)"
FT /evidence="ECO:0000305"
FT CONFLICT 891
FT /note="I -> K (in Ref. 2; AAH53064)"
FT /evidence="ECO:0000305"
FT CONFLICT 952
FT /note="R -> L (in Ref. 2; AAH52423)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="A -> R (in Ref. 1; AAB42085)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1104 AA; 122890 MW; 9030545104B90CAF CRC64;
MAATAGGGPG AAAGAVGAGG AAAASGLAVY RRKDGGPASK FWESPDTVSQ LDSVRVWLGK
HYKKYVHADA PTNKTLAGLV VQLLQFQEDA FGKHVTNPAF TKLPAKCFMD FKAGGTLCHI
LGAAYKYKNE QGWRRFDLQN PSRMDRNVEM FMNIEKTLVQ NNCLTRPNIY LIPDIDLKLA
NKLKDIIKRH QGTFTDEKSK ASHHIYPYPS SQEDEEWLRP VMRRDKQVLV HWGFYPDSYD
TWVHSNDVDA EIEDAPIPEK PWKVHVKWIL DTDVFNEWMN EEDYEVDENR KPVSFRQRIS
TKNEEPVRSP ERRDRKASAN SRKRKPSPSP PPPTATESRK KSGKKGQASL YGKRRSQKEE
DEQEDLTKDM EDPTPVPNIE EVVLPKNVNP KKDSENTPVK GGTVADLDEQ DEEAVTTGGK
EDEDPSKGDP SRSVDPGEDN VTEQTNHIII PSYASWFDYN CIHVIERRAL PEFFNGKNKS
KTPEIYLAYR NFMIDTYRLN PQEYLTSTAC RRNLTGDVCA VMRVHAFLEQ WGLVNYQVDP
ESRPMAMGPP PTPHFNVLAD TPSGLVPLHL RSPQVPAAQQ MLNFPEKNKE KPIDLQNFGL
RTDIYSKKTL AKSKGASAGR EWTEQETLLL LEALEMYKDD WNKVSEHVGS RTQDECILHF
LRLPIEDPYL ENSDASLGPL AYQPVPFSQS GNPVMSTVAF LASVVDPRVA SAAAKAALEE
FSRVREEVPL ELVEAHVKKV QEAARASGKV DPTYGLESSC IAGTGPDEPE KLEGSEEEKM
ETDPDGQQPE KAENKVENES DEGDKIQDRE NEKNTEKEQD SDVSEDVKPE EKENEENKEL
TDTCKERESD AGKKKVEHEI SEGNVATAAA AALASAATKA KHLAAVEERK IKSLVALLVE
TQMKKLEIKL RHFEELETIM DREKEALEQQ RQQLLTERQN FHMEQLKYAE LRARQQMEQQ
QQHGQTPQQA HQHTGGPGMA PLGATGHPGM MPHQQPPPYP LMHHQMPPPH PPQPGQIPGP
GSMMPGQPMP GRMIPAVAAN IHPTGSGPTP PGMPPMPGNI LGPRVPLTAP NGMYPPPPQQ
QQPPPPADGV PPPPAPGPPA SATP
