SMRD3_HUMAN
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 03-AUG-2022, entry version 177.
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; 87.
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; 39.
DR MINT; Q6STE5; -.
DR STRING; 9606.ENSP00000262188; -.
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; Q6STE5; -.
DR PeptideAtlas; Q6STE5; -.
DR PRIDE; Q6STE5; -.
DR ProteomicsDB; 67360; -. [Q6STE5-1]
DR ProteomicsDB; 67361; -. [Q6STE5-2]
DR Antibodypedia; 18748; 263 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 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; PPLYPKF; -.
DR OrthoDB; 1027566at2759; -.
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; 14 hits in 1081 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 185 other tissues.
DR ExpressionAtlas; Q6STE5; baseline and differential.
DR Genevisible; Q6STE5; HS.
DR GO; GO:0035060; C:brahma complex; IC: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: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; 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:0002052; P:positive regulation of neuroblast proliferation; IDA:BHF-UCL.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
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:0043393; P:regulation of protein binding; IEA:Ensembl.
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 Gene3D; 1.10.245.10; -; 1.
DR InterPro; IPR038043; SMARCD3.
DR InterPro; IPR019835; SWIB_domain.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR PANTHER; PTHR13844:SF5; PTHR13844:SF5; 1.
DR Pfam; PF02201; SWIB; 1.
DR SMART; SM00151; SWIB; 1.
DR SUPFAM; SSF47592; SSF47592; 1.
DR PROSITE; PS51925; SWIB_MDM2; 1.
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