SMRC2_MOUSE
ID SMRC2_MOUSE Reviewed; 1213 AA.
AC Q6PDG5; Q6P6P3;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=SWI/SNF complex subunit SMARCC2;
DE AltName: Full=BRG1-associated factor 170;
DE Short=BAF170;
DE AltName: Full=SWI/SNF complex 170 kDa subunit;
DE AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily C member 2;
GN Name=Smarcc2; Synonyms=Baf170;
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 MRNA] (ISOFORMS 1 AND 2).
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-347, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [3]
RP IDENTIFICATION BY 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 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-283; SER-286 AND SER-347, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-283; SER-286; SER-302;
RP SER-304; SER-347 AND SER-387, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [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 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 [10]
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 [11]
RP INTERACTION WITH FOS.
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).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=28369036; DOI=10.1038/ng.3833;
RA Witzel M., Petersheim D., Fan Y., Bahrami E., Racek T., Rohlfs M.,
RA Puchalka J., Mertes C., Gagneur J., Ziegenhain C., Enard W.,
RA Stray-Pedersen A., Arkwright P.D., Abboud M.R., Pazhakh V., Lieschke G.J.,
RA Krawitz P.M., Dahlhoff M., Schneider M.R., Wolf E., Horny H.P., Schmidt H.,
RA Schaeffer A.A., Klein C.;
RT "Chromatin-remodeling factor SMARCD2 regulates transcriptional networks
RT controlling differentiation of neutrophil granulocytes.";
RL Nat. Genet. 49:742-752(2017).
RN [13]
RP FUNCTION, ADP-RIBOSYLATION AT LYS-312, AND MUTAGENESIS OF LYS-312.
RX PubMed=31216030; DOI=10.1093/nar/gkz528;
RA Rezazadeh S., Yang D., Tombline G., Simon M., Regan S.P., Seluanov A.,
RA Gorbunova V.;
RT "SIRT6 promotes transcription of a subset of NRF2 targets by mono-ADP-
RT ribosylating BAF170.";
RL Nucleic Acids Res. 47:7914-7928(2019).
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. Can stimulate the ATPase activity of the catalytic subunit of
CC these complexes. May be required for CoREST dependent repression of
CC neuronal specific gene promoters in non-neuronal cells. Belongs to the
CC neural progenitors-specific chromatin remodeling complex (npBAF
CC complex) and the neuron-specific chromatin remodeling complex (nBAF
CC complex). During neural development a switch from a stem/progenitor to
CC a postmitotic chromatin remodeling mechanism occurs as neurons exit the
CC cell cycle and become committed to their adult state. The transition
CC from proliferating neural stem/progenitor cells to postmitotic neurons
CC requires a switch in subunit composition of the npBAF and nBAF
CC complexes. As neural progenitors exit mitosis and differentiate into
CC neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A,
CC are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B
CC or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF
CC complex is 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 (PubMed:17640523). Critical regulator of myeloid differentiation,
CC controlling granulocytopoiesis and the expression of genes involved in
CC neutrophil granule formation (PubMed:28369036).
CC {ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:28369036,
CC ECO:0000269|PubMed:31216030, ECO:0000303|PubMed:22952240,
CC 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. Component of neural progenitors-
CC specific chromatin remodeling complex (npBAF complex) composed of at
CC 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). May also interact with the SIN3A
CC histone deacetylase transcription repressor complex in conjunction with
CC SMARCA2 and SMARCA4. Interacts with SMARD1 (By similarity). Interacts
CC with KDM6B (PubMed:21095589). Interaction with RCOR1 (By similarity).
CC Interacts with DPF2 (By similarity). Interacts with ERCC6 (By
CC similarity). Interacts with FOS (PubMed:29272704).
CC {ECO:0000250|UniProtKB:Q8TAQ2, ECO:0000269|PubMed:17640523,
CC ECO:0000269|PubMed:21095589, ECO:0000269|PubMed:29272704,
CC ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PDG5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PDG5-2; Sequence=VSP_012492;
CC -!- DEVELOPMENTAL STAGE: Expressed ubiquitously throughout the developing
CC spinal cord, brain and other embryonic tissues at 10.5-16.5 dpc.
CC {ECO:0000269|PubMed:17640523}.
CC -!- PTM: Mono-ADP-ribosylation at Lys-312 by SIRT6 promotes recruitment to
CC the enhancer region of the Heme oxygenase-1 (HO-1) locus, leading to
CC transcription activation of the locus. {ECO:0000269|PubMed:31216030}.
CC -!- DISRUPTION PHENOTYPE: SMARCD2 knockout mice show aberrant
CC hematopoiesis, characterized by defective myeloid and erythroid
CC differentiation, a reduction in granulocyte/macrophage progenitors as
CC well as reduced neutrophil granulocytes and monocytes. Knockout embryos
CC die late during fetal development and are characterized by reduced
CC size, pallor, and decreased temporal vascularization.
CC {ECO:0000269|PubMed:28369036}.
CC -!- SIMILARITY: Belongs to the SMARCC family. {ECO:0000305}.
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DR EMBL; BC058720; AAH58720.1; -; mRNA.
DR EMBL; BC062102; AAH62102.1; -; mRNA.
DR CCDS; CCDS24278.1; -. [Q6PDG5-2]
DR CCDS; CCDS48727.1; -. [Q6PDG5-1]
DR RefSeq; NP_001107568.1; NM_001114096.1.
DR RefSeq; NP_001107569.1; NM_001114097.1. [Q6PDG5-1]
DR RefSeq; NP_937803.1; NM_198160.2. [Q6PDG5-2]
DR AlphaFoldDB; Q6PDG5; -.
DR SMR; Q6PDG5; -.
DR BioGRID; 212652; 27.
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-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; Q6PDG5; -.
DR DIP; DIP-48884N; -.
DR IntAct; Q6PDG5; 12.
DR MINT; Q6PDG5; -.
DR STRING; 10090.ENSMUSP00000100868; -.
DR iPTMnet; Q6PDG5; -.
DR PhosphoSitePlus; Q6PDG5; -.
DR SwissPalm; Q6PDG5; -.
DR EPD; Q6PDG5; -.
DR jPOST; Q6PDG5; -.
DR MaxQB; Q6PDG5; -.
DR PaxDb; Q6PDG5; -.
DR PeptideAtlas; Q6PDG5; -.
DR PRIDE; Q6PDG5; -.
DR ProteomicsDB; 261278; -. [Q6PDG5-1]
DR ProteomicsDB; 261279; -. [Q6PDG5-2]
DR Antibodypedia; 3811; 263 antibodies from 31 providers.
DR DNASU; 68094; -.
DR Ensembl; ENSMUST00000026433; ENSMUSP00000026433; ENSMUSG00000025369. [Q6PDG5-2]
DR Ensembl; ENSMUST00000105235; ENSMUSP00000100868; ENSMUSG00000025369. [Q6PDG5-1]
DR GeneID; 68094; -.
DR KEGG; mmu:68094; -.
DR UCSC; uc007hmw.2; mouse. [Q6PDG5-2]
DR UCSC; uc007hmx.2; mouse. [Q6PDG5-1]
DR CTD; 6601; -.
DR MGI; MGI:1915344; Smarcc2.
DR VEuPathDB; HostDB:ENSMUSG00000025369; -.
DR eggNOG; KOG1279; Eukaryota.
DR GeneTree; ENSGT00940000155746; -.
DR HOGENOM; CLU_004447_0_1_1; -.
DR InParanoid; Q6PDG5; -.
DR OMA; RFPSSMY; -.
DR OrthoDB; 683891at2759; -.
DR PhylomeDB; Q6PDG5; -.
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; 68094; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Smarcc2; mouse.
DR PRO; PR:Q6PDG5; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q6PDG5; protein.
DR Bgee; ENSMUSG00000025369; Expressed in embryonic brain and 232 other tissues.
DR ExpressionAtlas; Q6PDG5; baseline and differential.
DR Genevisible; Q6PDG5; MM.
DR GO; GO:0140092; C:bBAF complex; IC:ComplexPortal.
DR GO; GO:0035060; C:brahma complex; IC:ComplexPortal.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
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:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0016586; C:RSC-type complex; IC:ComplexPortal.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; 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:0045597; P:positive regulation of cell differentiation; 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:0045582; P:positive regulation of T cell differentiation; IC:ComplexPortal.
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; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IGI:MGI.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 1.10.10.10; -; 1.
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; IPR038044; SMARCC2.
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:SF105; PTHR12802:SF105; 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; ADP-ribosylation; Alternative splicing; Chromatin regulator;
KW Coiled coil; Isopeptide bond; Neurogenesis; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..1213
FT /note="SWI/SNF complex subunit SMARCC2"
FT /id="PRO_0000197118"
FT DOMAIN 424..521
FT /note="SWIRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT DOMAIN 596..647
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 256..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 907..934
FT /evidence="ECO:0000255"
FT COMPBIAS 258..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..978
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1064
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1213
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TAQ2"
FT MOD_RES 312
FT /note="N6-(ADP-ribosyl)lysine"
FT /evidence="ECO:0000269|PubMed:31216030"
FT MOD_RES 326
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8TAQ2"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 813
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TAQ2"
FT CROSSLNK 564
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TAQ2"
FT CROSSLNK 566
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TAQ2"
FT CROSSLNK 568
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TAQ2"
FT CROSSLNK 592
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TAQ2"
FT CROSSLNK 704
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TAQ2"
FT CROSSLNK 787
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TAQ2"
FT CROSSLNK 848
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8TAQ2"
FT VAR_SEQ 1075..1188
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012492"
FT MUTAGEN 312
FT /note="K->A: Abolished mono-ADP-ribosylation by SIRT6 and
FT recruitment to the enhancer region of the Heme oxygenase-1
FT (HO-1) locus."
FT /evidence="ECO:0000269|PubMed:31216030"
FT CONFLICT 550
FT /note="Missing (in Ref. 1; AAH62102)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1213 AA; 132604 MW; 6239489440320676 CRC64;
MAVRKKDGGP NVKYYEAADT VTQFDNVRLW LGKNYKKYIQ AEPPTNKSLS SLVVQLLQFQ
EEVFGKHVSN APLTKLPIKC FLDFKAGGSL CHILAAAYKF KSDQGWRRYD FQNPSRMDRN
VEMFMTIEKS LVQNNCLSRP NIFLCPEIEP KLLGKLKDIV KRHQGTISED KSNASHVVYP
VPGNLEEEEW VRPVMKRDKQ VLLHWGYYPD SYDTWIPASE IEASVEDAPT PEKPRKVHAK
WILDTDTFNE WMNEEDYEVS DDKSPVSRRK KISAKTLTDE VNSPDSDRRD KKGGNYKKRK
RSPSPSPTPE AKKKNAKKGP STPYTKSKRG HREEEQEDLT KDMDEPSPVP NVEEVTLPKT
VNTKKDSESA PVKGGTMTDL DEQDDESMET TGKDEDENST GNKGEQTKNP DLHEDNVTEQ
THHIIIPSYA AWFDYNSVHA IERRALPEFF NGKNKSKTPE IYLAYRNFMI DTYRLNPQEY
LTSTACRRNL AGDVCAIMRV HAFLEQWGLI NYQVDAESRP TPMGPPPTSH FHVLADTPSG
LVPLQPKPPQ QSSASQQMLN FPEKGKEKPA DMQNFGLRTD MYTKKNVPSK SKAAASATRE
WTEQETLLLL EALEMYKDDW NKVSEHVGSR TQDECILHFL RLPIEDPYLE DSEASLGPLA
YQPIPFSQSG NPVMSTVAFL ASVVDPRVAS AAAKSALEEF SKMKEEVPTA LVEAHVRKVE
EAAKVTGKAD PAFGLESSGI AGTASDEPER IEESGTEEAR PEGQAADEKK EPKEPREGGG
AVEEEAKEEI SEVPKKDEEK GKEGDSEKES EKSDGDPIVD PEKDKEPTEG QEEVLKEVAE
PEGERKTKVE RDIGEGNLST AAAAALAAAA VKAKHLAAVE ERKIKSLVAL LVETQMKKLE
IKLRHFEELE TIMDREREAL EYQRQQLLAD RQAFHMEQLK YAEMRARQQH FQQMHQQQQQ
QPPTLPPGSQ PIPPTGAAGP PTVHGLAVPP AAVASAPPGS GAPPGSLGPS EQIGQAGTTA
GPQQPQQAGA PQPGAVPPGV PPPGPHGPSP FPNQPTPPSM MPGAVPGSGH PGVAGNAPLG
LPFGMPPPPP AAPSVIPFGS LADSISINLP PPPNLHGHHH HLPFAPGTIP PPNLPVSMAN
PLHPNLPATT TMPSSLPLGP GLGSAAAQSP AIVAAVQGNL LPSASPLPDP GTPLPPDPTA
PSPGTVTPVP PPQ
