SMRD1_MOUSE
ID SMRD1_MOUSE Reviewed; 515 AA.
AC Q61466; P70384; Q8R0I7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 173.
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=Protein D15KZ1;
DE AltName: Full=SWI/SNF complex 60 kDa subunit;
GN Name=Smarcd1; Synonyms=Baf60a, D15Kz1;
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].
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 4-515, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Carcinoma;
RX PubMed=2725507; DOI=10.1128/mcb.9.3.935-945.1989;
RA Johnston L.A., Kotarski M.A., Jerry D.J., Kozak L.P.;
RT "An ubiquitously expressed gene 3.5 kilobases upstream of the glycerol-3-
RT phosphate dehydrogenase gene in mice.";
RL Mol. Cell. Biol. 9:935-945(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-515, SUBUNIT, AND TISSUE SPECIFICITY.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 211-515.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP PROTEIN SEQUENCE OF 166-173, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [6]
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 [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-223, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [10]
RP INTERACTION WITH AKIRIN2.
RX PubMed=25107474; DOI=10.15252/embj.201488447;
RA Tartey S., Matsushita K., Vandenbon A., Ori D., Imamura T., Mino T.,
RA Standley D.M., Hoffmann J.A., Reichhart J.M., Akira S., Takeuchi O.;
RT "Akirin2 is critical for inducing inflammatory genes by bridging IkappaB-
RT zeta and the SWI/SNF complex.";
RL EMBO J. 33:2332-2348(2014).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-88, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [12]
RP INTERACTION WITH FOS; FOSB; FOSL1 AND FOSL2.
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 [13]
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 [14]
RP STRUCTURE BY NMR OF 291-370.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SWIB domain of mouse BRG1-associated factor
RT 60A.";
RL Submitted (AUG-2004) to the PDB data bank.
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 (By similarity). Belongs to the neural progenitors-specific
CC chromatin remodeling complex (npBAF complex) and the neuron-specific
CC chromatin remodeling complex (nBAF complex). During neural development
CC a switch from a stem/progenitor to a postmitotic chromatin remodeling
CC mechanism occurs as neurons exit the cell cycle and become committed to
CC their adult state. The transition from proliferating neural
CC stem/progenitor cells to postmitotic neurons requires a switch in
CC subunit composition of the npBAF and nBAF complexes. As neural
CC progenitors exit mitosis and differentiate into neurons, npBAF
CC complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged
CC for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C
CC subunits in neuron-specific complexes (nBAF). The npBAF complex is
CC 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). 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 Mediates critical interactions between nuclear receptors and the
CC BRG1/SMARCA4 chromatin-remodeling complex for transactivation (By
CC similarity). {ECO:0000250|UniProtKB:Q96GM5,
CC ECO:0000269|PubMed:17640523}.
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:8804307, PubMed:8895581). Component of the BAF
CC complex, which includes at least actin (ACTB), ARID1A/BAF250A,
CC ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53,
CC ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170,
CC SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or
CC SMARCD3/BAF60C (By similarity). In muscle cells, the BAF complex also
CC contains DPF3. Component of neural progenitors-specific chromatin
CC remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A
CC or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B,
CC SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57,
CC SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of
CC neuron-specific chromatin remodeling complex (nBAF complex) composed of
CC 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 DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523).
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 (ACTB) (By similarity). 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).
CC Specifically interacts with the VDR heterodimer complex. Interacts with
CC ESR1, NR3C1, NR1H4, PGR, SMARCA4, SMARCC1 and SMARCC2 (By similarity).
CC Interacts with DPF2 (By similarity). Interacts with DPF3a (isoform 2 of
CC DPF3/BAF45C) and with HDGFL2 in a DPF3a-dependent manner (By
CC similarity). Interacts with FOS, FOSB isoform 1 and 2, FOSL1 and FOSL2
CC (PubMed:29272704). Interacts with AKIRIN2 (PubMed:25107474).
CC {ECO:0000250|UniProtKB:Q96GM5, ECO:0000269|PubMed:17640523,
CC ECO:0000269|PubMed:25107474, ECO:0000269|PubMed:29272704,
CC ECO:0000269|PubMed:29374058, ECO:0000269|PubMed:8804307,
CC ECO:0000269|PubMed:8895581}.
CC -!- INTERACTION:
CC Q61466; B1AXD8: Akirin2; NbExp=2; IntAct=EBI-371529, EBI-10107866;
CC Q61466; P97496: Smarcc1; NbExp=3; IntAct=EBI-371529, EBI-648047;
CC Q61466; P70323: Tbx1; NbExp=3; IntAct=EBI-371529, EBI-13635846;
CC Q61466; P02340: Tp53; NbExp=4; IntAct=EBI-371529, EBI-474016;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:2725507,
CC ECO:0000269|PubMed:8804307}.
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 -!- SIMILARITY: Belongs to the SMARCD family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA53377.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA53377.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC52794.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC52794.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH26783.3; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC026783; AAH26783.3; ALT_INIT; mRNA.
DR EMBL; BC059921; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; M25773; AAA53377.1; ALT_SEQ; mRNA.
DR EMBL; U66620; AAC52794.1; ALT_SEQ; mRNA.
DR EMBL; AK075611; BAC35856.1; -; mRNA.
DR CCDS; CCDS37204.1; -.
DR PIR; A30222; A30222.
DR RefSeq; NP_114030.2; NM_031842.2.
DR PDB; 1UHR; NMR; -; A=291-370.
DR PDBsum; 1UHR; -.
DR AlphaFoldDB; Q61466; -.
DR SMR; Q61466; -.
DR BioGRID; 219977; 26.
DR ComplexPortal; CPX-1232; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1233; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1234; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1235; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1236; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1237; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1238; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1239; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1240; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1241; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1242; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1243; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1244; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1245; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1246; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1247; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1248; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
DR ComplexPortal; CPX-1250; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
DR ComplexPortal; CPX-1251; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
DR ComplexPortal; CPX-1252; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1253; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1254; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1255; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1256; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1257; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1258; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1259; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-4202; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4204; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4221; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4222; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant.
DR ComplexPortal; CPX-4227; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4228; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4229; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4230; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant.
DR CORUM; Q61466; -.
DR DIP; DIP-33019N; -.
DR IntAct; Q61466; 13.
DR MINT; Q61466; -.
DR STRING; 10090.ENSMUSP00000023759; -.
DR iPTMnet; Q61466; -.
DR PhosphoSitePlus; Q61466; -.
DR EPD; Q61466; -.
DR MaxQB; Q61466; -.
DR PaxDb; Q61466; -.
DR PeptideAtlas; Q61466; -.
DR PRIDE; Q61466; -.
DR ProteomicsDB; 261528; -.
DR Antibodypedia; 1319; 283 antibodies from 31 providers.
DR DNASU; 83797; -.
DR Ensembl; ENSMUST00000023759; ENSMUSP00000023759; ENSMUSG00000023018.
DR GeneID; 83797; -.
DR KEGG; mmu:83797; -.
DR UCSC; uc007xqb.1; mouse.
DR CTD; 6602; -.
DR MGI; MGI:1933623; Smarcd1.
DR VEuPathDB; HostDB:ENSMUSG00000023018; -.
DR eggNOG; KOG2570; Eukaryota.
DR GeneTree; ENSGT00940000156629; -.
DR HOGENOM; CLU_023529_0_1_1; -.
DR InParanoid; Q61466; -.
DR OMA; PYFWNSD; -.
DR OrthoDB; 1027566at2759; -.
DR PhylomeDB; Q61466; -.
DR TreeFam; TF106486; -.
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; 83797; 13 hits in 81 CRISPR screens.
DR ChiTaRS; Smarcd1; mouse.
DR EvolutionaryTrace; Q61466; -.
DR PRO; PR:Q61466; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q61466; protein.
DR Bgee; ENSMUSG00000023018; Expressed in cortical plate and 223 other tissues.
DR ExpressionAtlas; Q61466; baseline and differential.
DR Genevisible; Q61466; MM.
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; ISO:MGI.
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:0005634; C:nucleus; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0045815; P:epigenetic maintenance of chromatin in transcription-competent conformation; ISO:MGI.
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; ISO:MGI.
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; Chromatin regulator; Coiled coil;
KW Direct protein sequencing; Isopeptide bond; Methylation; Neurogenesis;
KW Nucleus; Phosphoprotein; Reference proteome; 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_0000071984"
FT DOMAIN 290..367
FT /note="SWIB/MDM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01273"
FT REGION 1..128
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:0000250"
FT REGION 168..474
FT /note="Interaction with SMARCC1 and SMARCC2"
FT /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
FT COILED 412..440
FT /evidence="ECO:0000255"
FT COMPBIAS 99..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007744|PubMed:24129315"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92925"
FT MOD_RES 223
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 101
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96GM5"
FT CONFLICT 15
FT /note="G -> A (in Ref. 2; AAA53377 and 3; AAC52794)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="L -> I (in Ref. 4; BAC35856)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="D -> E (in Ref. 4; BAC35856)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="Q -> S (in Ref. 2; AAA53377 and 3; AAC52794)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="D -> G (in Ref. 2; AAA53377 and 3; AAC52794)"
FT /evidence="ECO:0000305"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:1UHR"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:1UHR"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:1UHR"
FT HELIX 312..325
FT /evidence="ECO:0007829|PDB:1UHR"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:1UHR"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:1UHR"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:1UHR"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:1UHR"
FT HELIX 358..364
FT /evidence="ECO:0007829|PDB:1UHR"
SQ SEQUENCE 515 AA; 58245 MW; 166D88566C856A0F CRC64;
MAARAGFQSV APSGGAGASG GAGVAAALGP GGTPGPPVRM GPAPGQGLYR SPMPGAAYPR
PGMLPGSRMT PQGPSMGPPG YGGNPSVRPG LAQSGMDQSR KRPAPQQIQQ VQQQAVQNRN
HNAKKKKMAD KILPQRIREL VPESQAYMDL LAFERKLDQT IMRKRLDIQE ALKRPIKQKR
KLRIFISNTF NPAKSDAEDG EGTVASWELR VEGRLLEDAA LSKYDATKQK RKFSSFFKSL
VIELDKDLYG PDNHLVEWHR TATTQETDGF QVKRPGDVNV RCTVLLMLDY QPPQFKLDPR
LARLLGIHTQ TRPVIIQALW QYIKTHKLQD PHEREFVLCD KYLQQIFESQ RMKFSEIPQR
LHALLMPPEP IIINHVISVD PNDQKKTACY DIDVEVDDTL KTQMNSFLLS TASQQEIATL
DNKIHETIET INQLKTQREF MLSFARDPQG FINDWLQSQC RDLKTMTDVV GNPEEERRAE
FYFQPWAQEA VCRYFYSKVQ QRRQELEQAL GIRNT
