SMRD1_HUMAN
ID SMRD1_HUMAN Reviewed; 515 AA.
AC Q96GM5; A6NN27; Q92924; Q9Y635;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1;
DE AltName: Full=60 kDa BRG-1/Brm-associated factor subunit A;
DE AltName: Full=BRG1-associated factor 60A;
DE Short=BAF60A;
DE AltName: Full=SWI/SNF complex 60 kDa subunit;
GN Name=SMARCD1 {ECO:0000312|EMBL:AAD23390.1};
GN Synonyms=BAF60A {ECO:0000303|PubMed:8804307};
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] {ECO:0000305, ECO:0000312|EMBL:AAD23390.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Peripheral blood;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH09368.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle;
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 [4] {ECO:0000305}
RP SUBUNIT.
RX PubMed=8895581; DOI=10.1002/j.1460-2075.1996.tb00921.x;
RA Wang W., Cote J., Xue Y., Zhou S., Khavari P.A., Biggar S.R., Muchardt C.,
RA Kalpana G.V., Goff S.P., Yaniv M., Workman J.L., Crabtree G.R.;
RT "Purification and biochemical heterogeneity of the mammalian SWI-SNF
RT complex.";
RL EMBO J. 15:5370-5382(1996).
RN [5] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH THE VITAMIN D RECEPTOR HETERODIMER COMPLEX.
RX PubMed=14698202; DOI=10.1016/j.jsbmb.2003.09.006;
RA Koszewski N.J., Henry K.W., Lubert E.J., Gravatte H., Noonan D.J.;
RT "Use of a modified yeast one-hybrid screen to identify BAF60a interactions
RT with the Vitamin D receptor heterodimer.";
RL J. Steroid Biochem. Mol. Biol. 87:223-231(2003).
RN [6] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH ESR1; NR3C1; NR1H4; PGR; SMARCA4; SMARCC1
RP AND SMARCC2.
RX PubMed=12917342; DOI=10.1128/mcb.23.17.6210-6220.2003;
RA Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
RT "BAF60a mediates critical interactions between nuclear receptors and the
RT BRG1 chromatin-remodeling complex for transactivation.";
RL Mol. Cell. Biol. 23:6210-6220(2003).
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 INTERACTION WITH DEPF2.
RX PubMed=20460684; DOI=10.1074/jbc.m109.087783;
RA Tando T., Ishizaka A., Watanabe H., Ito T., Iida S., Haraguchi T.,
RA Mizutani T., Izumi T., Isobe T., Akiyama T., Inoue J., Iba H.;
RT "Requiem protein links RelB/p52 and the Brm-type SWI/SNF complex in a
RT noncanonical NF-kappaB pathway.";
RL J. Biol. Chem. 285:21951-21960(2010).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-101, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
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 HDGFL2 AND DPF3.
RX PubMed=32459350; DOI=10.1093/nar/gkaa441;
RA Zhu X., Lan B., Yi X., He C., Dang L., Zhou X., Lu Y., Sun Y., Liu Z.,
RA Bai X., Zhang K., Li B., Li M.J., Chen Y., Zhang L.;
RT "HRP2-DPF3a-BAF complex coordinates histone modification and chromatin
RT remodeling to regulate myogenic gene transcription.";
RL Nucleic Acids Res. 48:6563-6582(2020).
RN [14]
RP VARIANTS CSS11 GLU-330; GLY-446; 486-TRP--THR-515 DEL; LEU-495 AND
RP 503-ARG--THR-515 DEL, CHARACTERIZATION OF VARIANTS CSS11 GLU-330;
RP 486-TRP--THR-515 DEL AND LEU-495, INVOLVEMENT IN CSS11, AND INTERACTION
RP WITH SMARCA4 AND SMARCC1.
RX PubMed=30879640; DOI=10.1016/j.ajhg.2019.02.001;
RG DDD Study;
RA Nixon K.C.J., Rousseau J., Stone M.H., Sarikahya M., Ehresmann S.,
RA Mizuno S., Matsumoto N., Miyake N., Baralle D., McKee S., Izumi K.,
RA Ritter A.L., Heide S., Heron D., Depienne C., Titheradge H., Kramer J.M.,
RA Campeau P.M.;
RT "A syndromic neurodevelopmental disorder caused by mutations in SMARCD1, a
RT core SWI/SNF subunit needed for context-dependent neuronal gene regulation
RT in flies.";
RL Am. J. Hum. Genet. 104:596-610(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 (PubMed:8804307, PubMed:29374058). Belongs to the neural
CC progenitors-specific chromatin remodeling complex (npBAF complex) and
CC the neuron-specific chromatin remodeling complex (nBAF complex). During
CC neural development a switch from a stem/progenitor to a postmitotic
CC chromatin remodeling mechanism occurs as neurons exit the cell cycle
CC and become committed to their adult state. The transition from
CC 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). Has a strong influence on vitamin D-mediated
CC transcriptional activity from an enhancer vitamin D receptor element
CC (VDRE). May be a link between mammalian SWI-SNF-like chromatin
CC remodeling complexes and the vitamin D receptor (VDR) heterodimer
CC (PubMed:14698202). Mediates critical interactions between nuclear
CC receptors and the BRG1/SMARCA4 chromatin-remodeling complex for
CC transactivation (PubMed:12917342). Interacts with AKIRIN2 (By
CC similarity). {ECO:0000250|UniProtKB:Q61466,
CC ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:14698202,
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 (PubMed:8895581). Component of the BAF complex, which includes
CC at 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 (PubMed:18765789). In
CC muscle cells, the BAF complex also contains DPF3. 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). Component of the
CC 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 (ACTB) (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).
CC Specifically interacts with the VDR heterodimer complex
CC (PubMed:14698202). Interacts with ESR1, NR3C1, NR1H4, PGR, SMARCA4,
CC SMARCC1 and SMARCC2 (PubMed:12917342, PubMed:30879640). Interacts with
CC DPF2 (PubMed:20460684). Interacts with DPF3a (isoform 2 of DPF3/BAF45C)
CC and with HDGFL2 in a DPF3a-dependent manner (PubMed:32459350).
CC Interacts with FOS, FOSB isoform 1 and 2, FOSL1 and FOSL2 (By
CC similarity). {ECO:0000250|UniProtKB:Q61466,
CC ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:14698202,
CC ECO:0000269|PubMed:18765789, ECO:0000269|PubMed:20460684,
CC ECO:0000269|PubMed:29374058, ECO:0000269|PubMed:30879640,
CC ECO:0000269|PubMed:32459350, ECO:0000269|PubMed:8895581,
CC ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
CC -!- INTERACTION:
CC Q96GM5; Q8IZP0-5: ABI1; NbExp=3; IntAct=EBI-358489, EBI-11743294;
CC Q96GM5; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-358489, EBI-11096309;
CC Q96GM5; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-358489, EBI-742038;
CC Q96GM5; Q7Z6V5: ADAT2; NbExp=3; IntAct=EBI-358489, EBI-2809203;
CC Q96GM5; Q86SG2: ANKRD23; NbExp=3; IntAct=EBI-358489, EBI-5661893;
CC Q96GM5; Q8WVL7: ANKRD49; NbExp=4; IntAct=EBI-358489, EBI-9381820;
CC Q96GM5; Q8N2F6-2: ARMC10; NbExp=3; IntAct=EBI-358489, EBI-12902762;
CC Q96GM5; Q96B67: ARRDC3; NbExp=3; IntAct=EBI-358489, EBI-2875665;
CC Q96GM5; P54253: ATXN1; NbExp=6; IntAct=EBI-358489, EBI-930964;
CC Q96GM5; P46379-2: BAG6; NbExp=3; IntAct=EBI-358489, EBI-10988864;
CC Q96GM5; O75934: BCAS2; NbExp=3; IntAct=EBI-358489, EBI-1050106;
CC Q96GM5; Q7L4P6: BEND5; NbExp=3; IntAct=EBI-358489, EBI-724373;
CC Q96GM5; Q00994: BEX3; NbExp=3; IntAct=EBI-358489, EBI-741753;
CC Q96GM5; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-358489, EBI-11519926;
CC Q96GM5; Q8TDH9: BLOC1S5; NbExp=3; IntAct=EBI-358489, EBI-465861;
CC Q96GM5; Q9NSI6-4: BRWD1; NbExp=3; IntAct=EBI-358489, EBI-10693038;
CC Q96GM5; Q5BKX5-3: C19orf54; NbExp=3; IntAct=EBI-358489, EBI-11976299;
CC Q96GM5; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-358489, EBI-8643161;
CC Q96GM5; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-358489, EBI-739580;
CC Q96GM5; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-358489, EBI-10171570;
CC Q96GM5; Q8NCU1: CCDC197; NbExp=3; IntAct=EBI-358489, EBI-750686;
CC Q96GM5; Q01850: CDR2; NbExp=3; IntAct=EBI-358489, EBI-1181367;
CC Q96GM5; P40199: CEACAM6; NbExp=3; IntAct=EBI-358489, EBI-4314501;
CC Q96GM5; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-358489, EBI-3866319;
CC Q96GM5; P08123: COL1A2; NbExp=3; IntAct=EBI-358489, EBI-983038;
CC Q96GM5; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-358489, EBI-21553822;
CC Q96GM5; Q9NWM3: CUEDC1; NbExp=3; IntAct=EBI-358489, EBI-5838167;
CC Q96GM5; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-358489, EBI-3867333;
CC Q96GM5; Q13561: DCTN2; NbExp=3; IntAct=EBI-358489, EBI-715074;
CC Q96GM5; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-358489, EBI-11988027;
CC Q96GM5; O14645: DNALI1; NbExp=3; IntAct=EBI-358489, EBI-395638;
CC Q96GM5; Q04637-9: EIF4G1; NbExp=3; IntAct=EBI-358489, EBI-12012124;
CC Q96GM5; A0A0A0MR80: EP400; NbExp=3; IntAct=EBI-358489, EBI-12089140;
CC Q96GM5; Q96DF8: ESS2; NbExp=3; IntAct=EBI-358489, EBI-3928124;
CC Q96GM5; Q96C01: FAM136A; NbExp=3; IntAct=EBI-358489, EBI-373319;
CC Q96GM5; Q3B820: FAM161A; NbExp=3; IntAct=EBI-358489, EBI-719941;
CC Q96GM5; P21333-2: FLNA; NbExp=3; IntAct=EBI-358489, EBI-9641086;
CC Q96GM5; P14136: GFAP; NbExp=3; IntAct=EBI-358489, EBI-744302;
CC Q96GM5; O75420: GIGYF1; NbExp=3; IntAct=EBI-358489, EBI-947774;
CC Q96GM5; Q9BRX5: GINS3; NbExp=3; IntAct=EBI-358489, EBI-2857315;
CC Q96GM5; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-358489, EBI-5916454;
CC Q96GM5; Q6IC98: GRAMD4; NbExp=3; IntAct=EBI-358489, EBI-10962409;
CC Q96GM5; Q96HZ4: HES6; NbExp=3; IntAct=EBI-358489, EBI-7469266;
CC Q96GM5; P31249: HOXD3; NbExp=3; IntAct=EBI-358489, EBI-3957655;
CC Q96GM5; O75031: HSF2BP; NbExp=3; IntAct=EBI-358489, EBI-7116203;
CC Q96GM5; O43464: HTRA2; NbExp=3; IntAct=EBI-358489, EBI-517086;
CC Q96GM5; P42858: HTT; NbExp=12; IntAct=EBI-358489, EBI-466029;
CC Q96GM5; Q70UQ0-4: IKBIP; NbExp=3; IntAct=EBI-358489, EBI-12190633;
CC Q96GM5; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-358489, EBI-747204;
CC Q96GM5; Q1MX18: INSC; NbExp=3; IntAct=EBI-358489, EBI-12081118;
CC Q96GM5; Q15051-2: IQCB1; NbExp=3; IntAct=EBI-358489, EBI-11944935;
CC Q96GM5; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-358489, EBI-1055254;
CC Q96GM5; Q9H079: KATNBL1; NbExp=3; IntAct=EBI-358489, EBI-715394;
CC Q96GM5; Q14145: KEAP1; NbExp=3; IntAct=EBI-358489, EBI-751001;
CC Q96GM5; Q2KHM9: KIAA0753; NbExp=3; IntAct=EBI-358489, EBI-2805604;
CC Q96GM5; O14901: KLF11; NbExp=3; IntAct=EBI-358489, EBI-948266;
CC Q96GM5; P19012: KRT15; NbExp=4; IntAct=EBI-358489, EBI-739566;
CC Q96GM5; P08779: KRT16; NbExp=3; IntAct=EBI-358489, EBI-356410;
CC Q96GM5; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-358489, EBI-3044087;
CC Q96GM5; Q15323: KRT31; NbExp=3; IntAct=EBI-358489, EBI-948001;
CC Q96GM5; O76011: KRT34; NbExp=3; IntAct=EBI-358489, EBI-1047093;
CC Q96GM5; O76014: KRT37; NbExp=3; IntAct=EBI-358489, EBI-1045716;
CC Q96GM5; O76015: KRT38; NbExp=3; IntAct=EBI-358489, EBI-1047263;
CC Q96GM5; O95678: KRT75; NbExp=3; IntAct=EBI-358489, EBI-2949715;
CC Q96GM5; O43679: LDB2; NbExp=3; IntAct=EBI-358489, EBI-2865580;
CC Q96GM5; O95751: LDOC1; NbExp=5; IntAct=EBI-358489, EBI-740738;
CC Q96GM5; Q13449: LSAMP; NbExp=3; IntAct=EBI-358489, EBI-4314821;
CC Q96GM5; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-358489, EBI-741037;
CC Q96GM5; P43356: MAGEA2B; NbExp=3; IntAct=EBI-358489, EBI-5650739;
CC Q96GM5; P43360: MAGEA6; NbExp=3; IntAct=EBI-358489, EBI-1045155;
CC Q96GM5; Q9NPJ6: MED4; NbExp=6; IntAct=EBI-358489, EBI-394607;
CC Q96GM5; Q13064: MKRN3; NbExp=3; IntAct=EBI-358489, EBI-2340269;
CC Q96GM5; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-358489, EBI-11522433;
CC Q96GM5; Q15742: NAB2; NbExp=3; IntAct=EBI-358489, EBI-8641936;
CC Q96GM5; P19404: NDUFV2; NbExp=3; IntAct=EBI-358489, EBI-713665;
CC Q96GM5; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-358489, EBI-10172876;
CC Q96GM5; Q9H3P2: NELFA; NbExp=3; IntAct=EBI-358489, EBI-5461341;
CC Q96GM5; Q9BRJ7: NUDT16L1; NbExp=3; IntAct=EBI-358489, EBI-2949792;
CC Q96GM5; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-358489, EBI-2811583;
CC Q96GM5; Q96CV9: OPTN; NbExp=3; IntAct=EBI-358489, EBI-748974;
CC Q96GM5; Q9UKS6: PACSIN3; NbExp=3; IntAct=EBI-358489, EBI-77926;
CC Q96GM5; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-358489, EBI-10302990;
CC Q96GM5; Q8N2W9: PIAS4; NbExp=3; IntAct=EBI-358489, EBI-473160;
CC Q96GM5; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-358489, EBI-79165;
CC Q96GM5; Q9NWS0: PIH1D1; NbExp=3; IntAct=EBI-358489, EBI-357318;
CC Q96GM5; Q96KN3: PKNOX2; NbExp=3; IntAct=EBI-358489, EBI-2692890;
CC Q96GM5; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-358489, EBI-2876622;
CC Q96GM5; Q5JR12: PPM1J; NbExp=3; IntAct=EBI-358489, EBI-13292717;
CC Q96GM5; P41219: PRPH; NbExp=3; IntAct=EBI-358489, EBI-752074;
CC Q96GM5; O43586: PSTPIP1; NbExp=3; IntAct=EBI-358489, EBI-1050964;
CC Q96GM5; Q92753-1: RORB; NbExp=3; IntAct=EBI-358489, EBI-18560266;
CC Q96GM5; Q6ZMJ2-2: SCARA5; NbExp=3; IntAct=EBI-358489, EBI-12823227;
CC Q96GM5; P0DPB3-4: SCHIP1; NbExp=3; IntAct=EBI-358489, EBI-11962426;
CC Q96GM5; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-358489, EBI-748391;
CC Q96GM5; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-358489, EBI-748621;
CC Q96GM5; Q6ZSJ9: SHISA6; NbExp=3; IntAct=EBI-358489, EBI-12037847;
CC Q96GM5; P51532: SMARCA4; NbExp=7; IntAct=EBI-358489, EBI-302489;
CC Q96GM5; Q12824-2: SMARCB1; NbExp=3; IntAct=EBI-358489, EBI-358436;
CC Q96GM5; Q92922: SMARCC1; NbExp=5; IntAct=EBI-358489, EBI-355653;
CC Q96GM5; Q53HV7-2: SMUG1; NbExp=3; IntAct=EBI-358489, EBI-12275818;
CC Q96GM5; Q96H20: SNF8; NbExp=3; IntAct=EBI-358489, EBI-747719;
CC Q96GM5; Q99619: SPSB2; NbExp=3; IntAct=EBI-358489, EBI-2323209;
CC Q96GM5; Q8IWL8: STH; NbExp=3; IntAct=EBI-358489, EBI-12843506;
CC Q96GM5; Q9NZ72: STMN3; NbExp=3; IntAct=EBI-358489, EBI-725557;
CC Q96GM5; Q13148: TARDBP; NbExp=6; IntAct=EBI-358489, EBI-372899;
CC Q96GM5; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-358489, EBI-3923210;
CC Q96GM5; Q6I9Y2: THOC7; NbExp=3; IntAct=EBI-358489, EBI-716286;
CC Q96GM5; Q08117-2: TLE5; NbExp=3; IntAct=EBI-358489, EBI-11741437;
CC Q96GM5; P14373: TRIM27; NbExp=3; IntAct=EBI-358489, EBI-719493;
CC Q96GM5; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-358489, EBI-2130429;
CC Q96GM5; Q6ZMU5: TRIM72; NbExp=3; IntAct=EBI-358489, EBI-2341648;
CC Q96GM5; Q8N6Y0: USHBP1; NbExp=4; IntAct=EBI-358489, EBI-739895;
CC Q96GM5; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-358489, EBI-11975223;
CC Q96GM5; Q9H9H4: VPS37B; NbExp=7; IntAct=EBI-358489, EBI-4400866;
CC Q96GM5; O00308: WWP2; NbExp=3; IntAct=EBI-358489, EBI-743923;
CC Q96GM5; P13994: YJU2B; NbExp=3; IntAct=EBI-358489, EBI-716093;
CC Q96GM5; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-358489, EBI-14104088;
CC Q96GM5; Q9UDW3: ZMAT5; NbExp=3; IntAct=EBI-358489, EBI-7850213;
CC Q96GM5; Q9H0C1: ZMYND12; NbExp=3; IntAct=EBI-358489, EBI-12030590;
CC Q96GM5; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-358489, EBI-740727;
CC Q96GM5; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-358489, EBI-11962468;
CC Q96GM5; Q8NB15: ZNF511; NbExp=3; IntAct=EBI-358489, EBI-10269136;
CC Q96GM5; Q9UEG4: ZNF629; NbExp=3; IntAct=EBI-358489, EBI-9977294;
CC Q96GM5; Q8N720: ZNF655; NbExp=3; IntAct=EBI-358489, EBI-625509;
CC Q96GM5; Q9UC07-2: ZNF69; NbExp=3; IntAct=EBI-358489, EBI-12310821;
CC Q96GM5; A0A1U9X8X8; NbExp=3; IntAct=EBI-358489, EBI-17234977;
CC Q96GM5; P06536: Nr3c1; Xeno; NbExp=2; IntAct=EBI-358489, EBI-1187143;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8804307,
CC ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:8804307};
CC IsoId=Q96GM5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:8804307};
CC IsoId=Q96GM5-2; Sequence=VSP_004179;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues tested, including brain,
CC heart, kidney, liver, lung, muscle, pancreas and placenta.
CC {ECO:0000269|PubMed:8804307}.
CC -!- DISEASE: Coffin-Siris syndrome 11 (CSS11) [MIM:618779]: A form of
CC Coffin-Siris syndrome, a congenital multiple malformation syndrome with
CC broad phenotypic and genetic variability. Cardinal features are
CC intellectual disability, coarse facial features, hypertrichosis, and
CC hypoplastic or absent fifth digit nails or phalanges. Additional
CC features include malformations of the cardiac, gastrointestinal,
CC genitourinary, and/or central nervous systems. Sucking/feeding
CC difficulties, poor growth, ophthalmologic abnormalities, hearing
CC impairment, and spinal anomalies are common findings. CSS11 is an
CC autosomal dominant form characterized by developmental delay,
CC intellectual disability, hypotonia, feeding difficulties, and small
CC hands and feet. {ECO:0000269|PubMed:30879640}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SMARCD family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50695.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAD23390.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH09368.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF109733; AAD23390.1; ALT_INIT; mRNA.
DR EMBL; U66617; AAC50695.1; ALT_FRAME; mRNA.
DR EMBL; AC025154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009368; AAH09368.3; ALT_INIT; mRNA.
DR CCDS; CCDS8797.2; -. [Q96GM5-1]
DR CCDS; CCDS8798.2; -. [Q96GM5-2]
DR RefSeq; NP_003067.3; NM_003076.4. [Q96GM5-1]
DR RefSeq; NP_620710.2; NM_139071.2. [Q96GM5-2]
DR PDB; 6LTH; EM; 3.00 A; P=1-515.
DR PDB; 6LTJ; EM; 3.70 A; P=1-515.
DR PDBsum; 6LTH; -.
DR PDBsum; 6LTJ; -.
DR AlphaFoldDB; Q96GM5; -.
DR SMR; Q96GM5; -.
DR BioGRID; 112486; 322.
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-1195; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
DR ComplexPortal; CPX-1196; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
DR ComplexPortal; CPX-1199; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A 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 ComplexPortal; CPX-4084; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4203; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4206; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4207; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant.
DR ComplexPortal; CPX-4223; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4224; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4225; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4226; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant.
DR CORUM; Q96GM5; -.
DR DIP; DIP-33390N; -.
DR IntAct; Q96GM5; 250.
DR MINT; Q96GM5; -.
DR STRING; 9606.ENSP00000378414; -.
DR GlyGen; Q96GM5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96GM5; -.
DR MetOSite; Q96GM5; -.
DR PhosphoSitePlus; Q96GM5; -.
DR BioMuta; SMARCD1; -.
DR DMDM; 238054318; -.
DR EPD; Q96GM5; -.
DR jPOST; Q96GM5; -.
DR MassIVE; Q96GM5; -.
DR MaxQB; Q96GM5; -.
DR PaxDb; Q96GM5; -.
DR PeptideAtlas; Q96GM5; -.
DR PRIDE; Q96GM5; -.
DR ProteomicsDB; 76645; -. [Q96GM5-1]
DR ProteomicsDB; 76646; -. [Q96GM5-2]
DR Antibodypedia; 1319; 283 antibodies from 31 providers.
DR DNASU; 6602; -.
DR Ensembl; ENST00000381513.8; ENSP00000370924.4; ENSG00000066117.15. [Q96GM5-2]
DR Ensembl; ENST00000394963.9; ENSP00000378414.4; ENSG00000066117.15. [Q96GM5-1]
DR GeneID; 6602; -.
DR KEGG; hsa:6602; -.
DR MANE-Select; ENST00000394963.9; ENSP00000378414.4; NM_003076.5; NP_003067.3.
DR UCSC; uc001rvx.5; human. [Q96GM5-1]
DR CTD; 6602; -.
DR DisGeNET; 6602; -.
DR GeneCards; SMARCD1; -.
DR HGNC; HGNC:11106; SMARCD1.
DR HPA; ENSG00000066117; Low tissue specificity.
DR MalaCards; SMARCD1; -.
DR MIM; 601735; gene.
DR MIM; 618779; phenotype.
DR neXtProt; NX_Q96GM5; -.
DR OpenTargets; ENSG00000066117; -.
DR Orphanet; 1465; Coffin-Siris syndrome.
DR PharmGKB; PA35956; -.
DR VEuPathDB; HostDB:ENSG00000066117; -.
DR eggNOG; KOG2570; Eukaryota.
DR GeneTree; ENSGT00940000156629; -.
DR HOGENOM; CLU_023529_0_1_1; -.
DR InParanoid; Q96GM5; -.
DR OMA; PYFWNSD; -.
DR OrthoDB; 1027566at2759; -.
DR PhylomeDB; Q96GM5; -.
DR TreeFam; TF106486; -.
DR PathwayCommons; Q96GM5; -.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR SignaLink; Q96GM5; -.
DR SIGNOR; Q96GM5; -.
DR BioGRID-ORCS; 6602; 103 hits in 1087 CRISPR screens.
DR ChiTaRS; SMARCD1; human.
DR GeneWiki; SMARCD1; -.
DR GenomeRNAi; 6602; -.
DR Pharos; Q96GM5; Tbio.
DR PRO; PR:Q96GM5; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q96GM5; protein.
DR Bgee; ENSG00000066117; Expressed in ganglionic eminence and 190 other tissues.
DR ExpressionAtlas; Q96GM5; baseline and differential.
DR Genevisible; Q96GM5; HS.
DR GO; GO:0035060; C:brahma complex; IC:ComplexPortal.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
DR GO; GO:0140288; C:GBAF complex; IC:ComplexPortal.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
DR GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016586; C:RSC-type complex; IC:ComplexPortal.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
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:0071398; P:cellular response to fatty acid; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; IDA:BHF-UCL.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; IMP:UniProtKB.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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:0008284; P:positive regulation of cell population proliferation; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IC:ComplexPortal.
DR GO; GO: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; IBA:GO_Central.
DR Gene3D; 1.10.245.10; -; 1.
DR InterPro; IPR038041; SMARCD1.
DR InterPro; IPR019835; SWIB_domain.
DR InterPro; IPR036885; SWIB_MDM2_dom_sf.
DR InterPro; IPR003121; SWIB_MDM2_domain.
DR PANTHER; PTHR13844:SF1; PTHR13844:SF1; 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 3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
KW Coiled coil; Disease variant; Intellectual disability; Isopeptide bond;
KW Methylation; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..515
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily D member 1"
FT /id="PRO_0000071983"
FT DOMAIN 290..367
FT /note="SWIB/MDM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..167
FT /note="Interaction with ESR1, NR1H4, NR3C1, PGR and
FT SMARCA4"
FT /evidence="ECO:0000269|PubMed:12917342"
FT REGION 168..474
FT /note="Interaction with SMARCC1 and SMARCC2"
FT /evidence="ECO:0000269|PubMed:12917342"
FT REGION 180..515
FT /note="Necessary for GR/NR3C1-mediated remodeling and
FT transcription from chromatin; required for GR/NR3C1
FT interaction with the BRG1/SMARCA4 complex in vivo"
FT COILED 412..440
FT /evidence="ECO:0000255"
FT MOD_RES 68
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q92925"
FT MOD_RES 88
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61466"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92925"
FT MOD_RES 223
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61466"
FT CROSSLNK 101
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 423..463
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8804307"
FT /id="VSP_004179"
FT VARIANT 330
FT /note="D -> E (in CSS11; unknown pathological significance;
FT does not affect the interaction with SMARCC1 and SMARCA4;
FT dbSNP:rs1592289150)"
FT /evidence="ECO:0000269|PubMed:30879640"
FT /id="VAR_083801"
FT VARIANT 446
FT /note="R -> G (in CSS11; dbSNP:rs1592294569)"
FT /evidence="ECO:0000269|PubMed:30879640"
FT /id="VAR_083802"
FT VARIANT 486..515
FT /note="Missing (in CSS11; does not affect the interaction
FT with SMARCC1 and SMARCA4)"
FT /evidence="ECO:0000269|PubMed:30879640"
FT /id="VAR_083803"
FT VARIANT 495
FT /note="F -> L (in CSS11; does not affect the interaction
FT with SMARCC1 and SMARCA4; dbSNP:rs1592295914)"
FT /evidence="ECO:0000269|PubMed:30879640"
FT /id="VAR_083804"
FT VARIANT 503..515
FT /note="Missing (in CSS11)"
FT /evidence="ECO:0000269|PubMed:30879640"
FT /id="VAR_083805"
FT CONFLICT 349
FT /note="S -> T (in Ref. 1; AAC50695)"
FT /evidence="ECO:0000305"
FT HELIX 129..131
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 144..172
FT /evidence="ECO:0007829|PDB:6LTH"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 299..305
FT /evidence="ECO:0007829|PDB:6LTH"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 312..326
FT /evidence="ECO:0007829|PDB:6LTH"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:6LTH"
FT TURN 341..346
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 401..410
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 415..446
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 448..467
FT /evidence="ECO:0007829|PDB:6LTH"
FT TURN 473..477
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 479..483
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 487..504
FT /evidence="ECO:0007829|PDB:6LTH"
SQ SEQUENCE 515 AA; 58233 MW; E683AA1E345DA400 CRC64;
MAARAGFQSV APSGGAGASG GAGAAAALGP GGTPGPPVRM GPAPGQGLYR SPMPGAAYPR
PGMLPGSRMT PQGPSMGPPG YGGNPSVRPG LAQSGMDQSR KRPAPQQIQQ VQQQAVQNRN
HNAKKKKMAD KILPQRIREL VPESQAYMDL LAFERKLDQT IMRKRLDIQE ALKRPIKQKR
KLRIFISNTF NPAKSDAEDG EGTVASWELR VEGRLLEDSA LSKYDATKQK RKFSSFFKSL
VIELDKDLYG PDNHLVEWHR TATTQETDGF QVKRPGDVNV RCTVLLMLDY QPPQFKLDPR
LARLLGIHTQ TRPVIIQALW QYIKTHKLQD PHEREFVICD KYLQQIFESQ RMKFSEIPQR
LHALLMPPEP IIINHVISVD PNDQKKTACY DIDVEVDDTL KTQMNSFLLS TASQQEIATL
DNKIHETIET INQLKTQREF MLSFARDPQG FINDWLQSQC RDLKTMTDVV GNPEEERRAE
FYFQPWAQEA VCRYFYSKVQ QRRQELEQAL GIRNT
