ID   SMRD3_HUMAN             Reviewed;         483 AA.
AC   Q6STE5; D3DX10; Q2YD86; Q75MJ2; Q75MR8; Q92926; Q9BUH1;
DT   04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 186.
DE   RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 3;
DE   AltName: Full=60 kDa BRG-1/Brm-associated factor subunit C;
DE   AltName: Full=BRG1-associated factor 60C;
DE            Short=BAF60C;
GN   Name=SMARCD3; Synonyms=BAF60C;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RX   PubMed=8804307; DOI=10.1101/gad.10.17.2117;
RA   Wang W., Xue Y., Zhou S., Kuo A., Cairns B.R., Crabtree G.R.;
RT   "Diversity and specialization of mammalian SWI/SNF complexes.";
RL   Genes Dev. 10:2117-2130(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION,
RP   INTERACTION WITH SMARCA4 AND TRANSCRIPTIONAL ACTIVATORS, AND VARIANT
RP   SER-170.
RC   TISSUE=Adipose tissue;
RX   PubMed=14701856; DOI=10.1074/jbc.m312288200;
RA   Debril M.-B., Gelman L., Fayard E., Annicotte J.-S., Rocchi S., Auwerx J.;
RT   "Transcription factors and nuclear receptors interact with the SWI/SNF
RT   complex through the BAF60c subunit.";
RL   J. Biol. Chem. 279:16677-16686(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Blood, and Uterus;
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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-178, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [7]
RP   IDENTIFICATION IN THE BAF COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18765789; DOI=10.1101/gad.471408;
RA   Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C.,
RA   Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H.,
RA   Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.;
RT   "Regulation of muscle development by DPF3, a novel histone acetylation and
RT   methylation reader of the BAF chromatin remodeling complex.";
RL   Genes Dev. 22:2370-2384(2008).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [10]
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   [11]
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   [12]
RP   FUNCTION, AND 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).
RN   [13]
RP   INTERACTION WITH PRDM1.
RX   PubMed=32417234; DOI=10.1016/j.bbagrm.2020.194577;
RA   Fong H.T., Hagen T., Inoue T.;
RT   "LDB1 and the SWI/SNF complex participate in both transcriptional
RT   activation and repression by Caenorhabditis elegans BLIMP1/PRDM1.";
RL   Biochim. Biophys. Acta 1863:194577-194577(2020).
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. Stimulates nuclear receptor mediated transcription. Belongs to
CC       the 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       (By similarity). {ECO:0000250|UniProtKB:Q6P9Z1,
CC       ECO:0000269|PubMed:29374058, ECO:0000269|PubMed:8804307,
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. In muscle cells, the
CC       BAF complex also contains DPF3 (PubMed:18765789). 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 (By similarity). May be a
CC       component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at
CC       least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or
CC       ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps
CC       SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180,
CC       ARID2/BAF200 and actin (PubMed:22952240, PubMed:26601204). Interacts
CC       with SMARCA4/BRG1/BAF190A (PubMed:14701856). Component of SWI/SNF
CC       (GBAF) 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). The
CC       precise distribution of the related SMARCD1, SMARCD2 and SMARCD3
CC       proteins among these and other SWI/SNF nucleosome-remodeling complexes
CC       is not fully known. May allow recruitment of SWI/SNF containing
CC       complexes specifically to promoters where these factors are located.
CC       Also interacts with several nuclear receptors including PPARG/NR1C3,
CC       RXRA/NR1F1, ESR1, NR5A1, NR5A2/LRH1 and other transcriptional
CC       activators including the HLH protein SREBF1/SREBP1 and the homeobox
CC       protein PBX1 (PubMed:14701856). Interacts with PRDM1/BLIMP1
CC       (PubMed:32417234). {ECO:0000250|UniProtKB:Q6P9Z1,
CC       ECO:0000269|PubMed:14701856, ECO:0000269|PubMed:18765789,
CC       ECO:0000269|PubMed:29374058, ECO:0000269|PubMed:32417234,
CC       ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
CC   -!- INTERACTION:
CC       Q6STE5-1; P37231: PPARG; NbExp=3; IntAct=EBI-488506, EBI-781384;
CC       Q6STE5-2; P37231: PPARG; NbExp=3; IntAct=EBI-488511, EBI-781384;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14701856}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=BAF60C2;
CC         IsoId=Q6STE5-1; Sequence=Displayed;
CC       Name=2; Synonyms=BAF60C1;
CC         IsoId=Q6STE5-2; Sequence=VSP_012498;
CC   -!- TISSUE SPECIFICITY: Isoform 2 and isoform 1 are expressed in brain,
CC       heart, kidney, placenta, prostate, salivary gland, spleen, testis,
CC       thyroid, trachea and uterus. Isoform 1 is also expressed in skeletal
CC       muscle and adipose tissue.
CC   -!- SIMILARITY: Belongs to the SMARCD family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC50697.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U66619; AAC50697.1; ALT_FRAME; mRNA.
DR   EMBL; AY450430; AAR88510.1; -; mRNA.
DR   EMBL; AY450431; AAR88511.1; -; mRNA.
DR   EMBL; AC021097; AAS00380.1; -; Genomic_DNA.
DR   EMBL; AC005486; AAS02031.1; -; Genomic_DNA.
DR   EMBL; CH471173; EAW54005.1; -; Genomic_DNA.
DR   EMBL; CH471173; EAW54007.1; -; Genomic_DNA.
DR   EMBL; CH471173; EAW54008.1; -; Genomic_DNA.
DR   EMBL; BC002628; AAH02628.1; -; mRNA.
DR   EMBL; BC110350; AAI10351.1; -; mRNA.
DR   CCDS; CCDS34780.1; -. [Q6STE5-1]
DR   CCDS; CCDS5924.1; -. [Q6STE5-2]
DR   RefSeq; NP_001003801.1; NM_001003801.1. [Q6STE5-1]
DR   RefSeq; NP_001003802.1; NM_001003802.1. [Q6STE5-2]
DR   RefSeq; NP_003069.2; NM_003078.3. [Q6STE5-2]
DR   AlphaFoldDB; Q6STE5; -.
DR   SMR; Q6STE5; -.
DR   BioGRID; 112488; 90.
DR   ComplexPortal; CPX-1164; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1194; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1201; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1202; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1204; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1205; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1206; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1207; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1209; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1210; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1211; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1212; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1213; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1215; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1216; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1217; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1218; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1222; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1223; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1224; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1225; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1226; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1227; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1228; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR   CORUM; Q6STE5; -.
DR   DIP; DIP-33012N; -.
DR   IntAct; Q6STE5; 40.
DR   MINT; Q6STE5; -.
DR   STRING; 9606.ENSP00000262188; -.
DR   GlyGen; Q6STE5; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6STE5; -.
DR   MetOSite; Q6STE5; -.
DR   PhosphoSitePlus; Q6STE5; -.
DR   BioMuta; SMARCD3; -.
DR   DMDM; 57013057; -.
DR   EPD; Q6STE5; -.
DR   jPOST; Q6STE5; -.
DR   MassIVE; Q6STE5; -.
DR   MaxQB; Q6STE5; -.
DR   PaxDb; 9606-ENSP00000262188; -.
DR   PeptideAtlas; Q6STE5; -.
DR   ProteomicsDB; 67360; -. [Q6STE5-1]
DR   ProteomicsDB; 67361; -. [Q6STE5-2]
DR   Pumba; Q6STE5; -.
DR   Antibodypedia; 18748; 296 antibodies from 28 providers.
DR   DNASU; 6604; -.
DR   Ensembl; ENST00000262188.13; ENSP00000262188.8; ENSG00000082014.17. [Q6STE5-1]
DR   Ensembl; ENST00000356800.6; ENSP00000349254.2; ENSG00000082014.17. [Q6STE5-2]
DR   Ensembl; ENST00000392811.6; ENSP00000376558.2; ENSG00000082014.17. [Q6STE5-2]
DR   GeneID; 6604; -.
DR   KEGG; hsa:6604; -.
DR   MANE-Select; ENST00000262188.13; ENSP00000262188.8; NM_001003801.2; NP_001003801.1.
DR   UCSC; uc003wjs.4; human. [Q6STE5-1]
DR   AGR; HGNC:11108; -.
DR   CTD; 6604; -.
DR   DisGeNET; 6604; -.
DR   GeneCards; SMARCD3; -.
DR   HGNC; HGNC:11108; SMARCD3.
DR   HPA; ENSG00000082014; Tissue enhanced (brain, skeletal muscle).
DR   MIM; 601737; gene.
DR   neXtProt; NX_Q6STE5; -.
DR   OpenTargets; ENSG00000082014; -.
DR   PharmGKB; PA35958; -.
DR   VEuPathDB; HostDB:ENSG00000082014; -.
DR   eggNOG; KOG2570; Eukaryota.
DR   GeneTree; ENSGT00940000158945; -.
DR   HOGENOM; CLU_023529_0_2_1; -.
DR   InParanoid; Q6STE5; -.
DR   OMA; RRMYSAK; -.
DR   OrthoDB; 9355at2759; -.
DR   PhylomeDB; Q6STE5; -.
DR   TreeFam; TF106486; -.
DR   PathwayCommons; Q6STE5; -.
DR   Reactome; R-HSA-1368082; RORA activates gene expression.
DR   Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR   Reactome; R-HSA-1989781; PPARA activates gene expression.
DR   Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR   Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR   Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR   Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR   Reactome; R-HSA-400206; Regulation of lipid metabolism by PPARalpha.
DR   Reactome; R-HSA-400253; Circadian Clock.
DR   Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR   Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR   Reactome; R-HSA-9707616; Heme signaling.
DR   SignaLink; Q6STE5; -.
DR   SIGNOR; Q6STE5; -.
DR   BioGRID-ORCS; 6604; 17 hits in 1160 CRISPR screens.
DR   ChiTaRS; SMARCD3; human.
DR   GeneWiki; SMARCD3; -.
DR   GenomeRNAi; 6604; -.
DR   Pharos; Q6STE5; Tbio.
DR   PRO; PR:Q6STE5; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q6STE5; Protein.
DR   Bgee; ENSG00000082014; Expressed in ganglionic eminence and 187 other cell types or tissues.
DR   ExpressionAtlas; Q6STE5; baseline and differential.
DR   GO; GO:0035060; C:brahma complex; NAS:ComplexPortal.
DR   GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR   GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
DR   GO; GO:0071564; C:npBAF complex; IDA:BHF-UCL.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0016922; F:nuclear receptor binding; IPI:BHF-UCL.
DR   GO; GO:0030374; F:nuclear receptor coactivator activity; IMP:BHF-UCL.
DR   GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
DR   GO; GO:0003713; F:transcription coactivator activity; NAS:BHF-UCL.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0001221; F:transcription coregulator binding; IPI:UniProtKB.
DR   GO; GO:0003219; P:cardiac right ventricle formation; IEA:Ensembl.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:BHF-UCL.
DR   GO; GO:0042692; P:muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0003407; P:neural retina development; IEP:BHF-UCL.
DR   GO; GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; NAS:ComplexPortal.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:2000781; P:positive regulation of double-strand break repair; NAS:ComplexPortal.
DR   GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0045663; P:positive regulation of myoblast differentiation; NAS:ComplexPortal.
DR   GO; GO:0002052; P:positive regulation of neuroblast proliferation; IDA:BHF-UCL.
DR   GO; GO:0051152; P:positive regulation of smooth muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0045582; P:positive regulation of T cell differentiation; NAS:ComplexPortal.
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; IMP:BHF-UCL.
DR   GO; GO:0003139; P:secondary heart field specification; IEA:Ensembl.
DR   CDD; cd17676; SWIB_BAF60C; 1.
DR   Gene3D; 1.10.245.10; SWIB/MDM2 domain; 1.
DR   InterPro; IPR038043; SMARCD3_SWIB_dom.
DR   InterPro; IPR019835; SWIB_domain.
DR   InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR   InterPro; IPR003121; SWIB_MDM2_domain.
DR   PANTHER; PTHR13844; SWI/SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY D; 1.
DR   PANTHER; PTHR13844:SF5; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY D MEMBER 3; 1.
DR   Pfam; PF02201; SWIB; 1.
DR   SMART; SM00151; SWIB; 1.
DR   SUPFAM; SSF47592; SWIB/MDM2 domain; 1.
DR   PROSITE; PS51925; SWIB_MDM2; 1.
DR   Genevisible; Q6STE5; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chromatin regulator; Neurogenesis;
KW   Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..483
FT                   /note="SWI/SNF-related matrix-associated actin-dependent
FT                   regulator of chromatin subfamily D member 3"
FT                   /id="PRO_0000071988"
FT   DOMAIN          258..335
FT                   /note="SWIB/MDM2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT   REGION          26..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        76..91
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         178
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983"
FT   VAR_SEQ         1..26
FT                   /note="MAADEVAGGARKATKSKLFEFLVHGV -> MTPGLQHPPTVVQ (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14701856,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8804307"
FT                   /id="VSP_012498"
FT   VARIANT         170
FT                   /note="P -> S (in dbSNP:rs1050101)"
FT                   /evidence="ECO:0000269|PubMed:14701856"
FT                   /id="VAR_020884"
FT   CONFLICT        88
FT                   /note="V -> E (in Ref. 1; AAC50697)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        140
FT                   /note="R -> G (in Ref. 1; AAC50697)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        387
FT                   /note="A -> P (in Ref. 1; AAC50697)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   483 AA;  55016 MW;  B7B28DD11DCD0B5C CRC64;
     MAADEVAGGA RKATKSKLFE FLVHGVRPGM PSGARMPHQG APMGPPGSPY MGSPAVRPGL
     APAGMEPARK RAAPPPGQSQ AQSQGQPVPT APARSRSAKR RKMADKILPQ RIRELVPESQ
     AYMDLLAFER KLDQTIMRKR VDIQEALKRP MKQKRKLRLY ISNTFNPAKP DAEDSDGSIA
     SWELRVEGKL LDDPSKQKRK FSSFFKSLVI ELDKDLYGPD NHLVEWHRTP TTQETDGFQV
     KRPGDLSVRC TLLLMLDYQP PQFKLDPRLA RLLGLHTQSR SAIVQALWQY VKTNRLQDSH
     DKEYINGDKY FQQIFDCPRL KFSEIPQRLT ALLLPPDPIV INHVISVDPS DQKKTACYDI
     DVEVEEPLKG QMSSFLLSTA NQQEISALDS KIHETIESIN QLKIQRDFML SFSRDPKGYV
     QDLLRSQSRD LKVMTDVAGN PEEERRAEFY HQPWSQEAVS RYFYCKIQQR RQELEQSLVV
     RNT
//