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 27-MAR-2024, entry version 202. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 35. DR MINT; P97496; -. DR STRING; 10090.ENSMUSP00000086094; -. DR GlyGen; P97496; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P97496; -. DR PhosphoSitePlus; P97496; -. DR SwissPalm; P97496; -. DR EPD; P97496; -. DR jPOST; P97496; -. DR MaxQB; P97496; -. DR PaxDb; 10090-ENSMUSP00000086094; -. DR PeptideAtlas; P97496; -. DR ProteomicsDB; 257277; -. [P97496-1] DR ProteomicsDB; 257278; -. [P97496-2] DR Pumba; P97496; -. DR Antibodypedia; 3168; 305 antibodies from 36 providers. DR DNASU; 20588; -. DR Ensembl; ENSMUST00000088716.12; ENSMUSP00000086094.6; ENSMUSG00000032481.18. [P97496-1] DR Ensembl; ENSMUST00000197984.5; ENSMUSP00000142611.2; ENSMUSG00000032481.18. [P97496-2] DR GeneID; 20588; -. DR KEGG; mmu:20588; -. DR UCSC; uc009rto.1; mouse. [P97496-2] DR UCSC; uc009rtp.1; mouse. [P97496-1] DR AGR; MGI:1203524; -. DR CTD; 6599; -. DR MGI; MGI:1203524; Smarcc1. DR VEuPathDB; HostDB:ENSMUSG00000032481; -. DR eggNOG; KOG1279; Eukaryota. DR GeneTree; ENSGT00940000156347; -. DR InParanoid; P97496; -. DR OMA; TTIDMPD; -. DR OrthoDB; 10062at2759; -. 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 84 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 260 other cell types or tissues. DR ExpressionAtlas; P97496; baseline and differential. DR GO; GO:0035060; C:brahma complex; NAS:ComplexPortal. DR GO; GO:0000785; C:chromatin; NAS:ComplexPortal. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0140288; C:GBAF complex; NAS:ComplexPortal. DR GO; GO:0000776; C:kinetochore; NAS: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; NAS: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; NAS: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: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; NAS: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; NAS:ComplexPortal. DR GO; GO:0008284; P:positive regulation of cell population proliferation; NAS:ComplexPortal. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI. DR GO; GO:2000781; P:positive regulation of double-strand break repair; NAS:ComplexPortal. DR GO; GO:0045663; P:positive regulation of myoblast differentiation; NAS:ComplexPortal. DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0045582; P:positive regulation of T cell differentiation; NAS:ComplexPortal. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI. DR GO; GO:0030850; P:prostate gland development; IEA:Ensembl. DR GO; GO:0070316; P:regulation of G0 to G1 transition; NAS:ComplexPortal. DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; NAS:ComplexPortal. DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; NAS:ComplexPortal. DR GO; GO:2000819; P:regulation of nucleotide-excision repair; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:ComplexPortal. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR036420; BRCT_dom_sf. DR InterPro; IPR000953; Chromo/chromo_shadow_dom. DR InterPro; IPR009057; Homeobox-like_sf. 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; SWI/SNF COMPLEX-RELATED; 1. DR PANTHER; PTHR12802:SF9; SWI_SNF COMPLEX SUBUNIT SMARCC1; 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; SSF52113; BRCT domain; 1. DR SUPFAM; SSF46689; Homeodomain-like; 2. DR PROSITE; PS52032; MARR_BRCT_CHROMO; 1. DR PROSITE; PS51293; SANT; 1. DR PROSITE; PS50934; SWIRM; 1. DR Genevisible; P97496; MM. 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 37..163 FT /note="MarR-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01376" FT DOMAIN 167..210 FT /note="BRCT; N-terminus" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01376" FT DOMAIN 216..244 FT /note="Chromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01376" FT DOMAIN 260..284 FT /note="BRCT; C-terminus" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01376" 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 27..301 FT /note="MarR-like, BRCT and chromo domains module" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01376" 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 //