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SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1 (60 kDa BRG-1/Brm-associated factor subunit A) (BRG1-associated factor 60A) (BAF60A) (Protein D15KZ1) (SWI/SNF complex 60 kDa subunit)

 SMRD1_MOUSE             Reviewed;         515 AA.
Q61466; P70384; Q8R0I7;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
26-MAY-2009, sequence version 3.
10-OCT-2018, entry version 150.
RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1;
AltName: Full=60 kDa BRG-1/Brm-associated factor subunit A;
AltName: Full=BRG1-associated factor 60A;
Short=BAF60A;
AltName: Full=Protein D15KZ1;
AltName: Full=SWI/SNF complex 60 kDa subunit;
Name=Smarcd1; Synonyms=Baf60a, D15Kz1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Retina;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-515, AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Carcinoma;
PubMed=2725507; DOI=10.1128/MCB.9.3.935;
Johnston L.A., Kotarski M.A., Jerry D.J., Kozak L.P.;
"An ubiquitously expressed gene 3.5 kilobases upstream of the
glycerol-3-phosphate dehydrogenase gene in mice.";
Mol. Cell. Biol. 9:935-945(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 4-515, SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=8804307; DOI=10.1101/gad.10.17.2117;
Wang W., Xue Y., Zhou S., Kuo A., Cairns B.R., Crabtree G.R.;
"Diversity and specialization of mammalian SWI/SNF complexes.";
Genes Dev. 10:2117-2130(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 211-515.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
PROTEIN SEQUENCE OF 166-173, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain;
Lubec G., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[6]
SUBUNIT.
PubMed=8895581;
Wang W., Cote J., Xue Y., Zhou S., Khavari P.A., Biggar S.R.,
Muchardt C., Kalpana G.V., Goff S.P., Yaniv M., Workman J.L.,
Crabtree G.R.;
"Purification and biochemical heterogeneity of the mammalian SWI-SNF
complex.";
EMBO J. 15:5370-5382(1996).
[7]
FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS
SPECTROMETRY, IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES, AND
DEVELOPMENTAL STAGE.
PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T.,
Wu H., Aebersold R., Graef I.A., Crabtree G.R.;
"An essential switch in subunit composition of a chromatin remodeling
complex during neural development.";
Neuron 55:201-215(2007).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-223, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[10]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-88, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[11]
FUNCTION, AND IDENTIFICATION IN THE GBAF COMPLEX.
PubMed=29374058; DOI=10.1074/jbc.RA117.001065;
Alpsoy A., Dykhuizen E.C.;
"Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its
paralog GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes.";
J. Biol. Chem. 293:3892-3903(2018).
[12]
STRUCTURE BY NMR OF 291-370.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the SWIB domain of mouse BRG1-associated factor
60A.";
Submitted (AUG-2004) to the PDB data bank.
-!- FUNCTION: Involved in transcriptional activation and repression of
select genes by chromatin remodeling (alteration of DNA-nucleosome
topology). Component of SWI/SNF chromatin remodeling complexes
that carry out key enzymatic activities, changing chromatin
structure by altering DNA-histone contacts within a nucleosome in
an ATP-dependent manner (By similarity). Belongs to the neural
progenitors-specific chromatin remodeling complex (npBAF complex)
and the neuron-specific chromatin remodeling complex (nBAF
complex). During neural development a switch from a
stem/progenitor to a postmitotic chromatin remodeling mechanism
occurs as neurons exit the cell cycle and become committed to
their adult state. The transition from proliferating neural
stem/progenitor cells to postmitotic neurons requires a switch in
subunit composition of the npBAF and nBAF complexes. As neural
progenitors exit mitosis and differentiate into neurons, npBAF
complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are
exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B
or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The
npBAF complex is essential for the self-renewal/proliferative
capacity of the multipotent neural stem cells. The nBAF complex
along with CREST plays a role regulating the activity of genes
essential for dendrite growth (PubMed:17640523). Has a strong
influence on vitamin D-mediated transcriptional activity from an
enhancer vitamin D receptor element (VDRE). May be a link between
mammalian SWI-SNF-like chromatin remodeling complexes and the
vitamin D receptor (VDR) heterodimer. Mediates critical
interactions between nuclear receptors and the BRG1/SMARCA4
chromatin-remodeling complex for transactivation (By similarity).
{ECO:0000250|UniProtKB:Q96GM5, ECO:0000269|PubMed:17640523}.
-!- SUBUNIT: Component of the multiprotein chromatin-remodeling
complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related
complexes. The canonical complex contains a catalytic subunit
(either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B), and at least
SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and
SMARCB1/SNF5/BAF47. Other subunits specific to each of the
complexes may also be present permitting several possible
combinations developmentally and tissue specific (PubMed:8804307,
PubMed:8895581). Component of the BAF complex, which includes at
least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM,
SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57,
SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C (By similarity).
In muscle cells, the BAF complex also contains DPF3. Component of
neural progenitors-specific chromatin remodeling complex (npBAF
complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B,
SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B,
SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155,
SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and
actin. Component of neuron-specific chromatin remodeling complex
(nBAF complex) composed of at least, ARID1A/BAF250A or
ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523). Component
of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least
composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or
ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B,
perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170,
PBRM1/BAF180, ARID2/BAF200 and actin (ACTB) (By similarity).
Component of SWI/SNF (GBAF) subcomplex, which includes at least
BICRA or BICRAL (mutually exclusive), BRD9, SS18, SMARCA2/BRM,
SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and
SMARCD1/BAF60A (PubMed:29374058). Specifically interacts with the
VDR heterodimer complex. Interacts with ESR1, NR3C1, NR1H4, PGR,
SMARCA4, SMARCC1 and SMARCC2 (By similarity).
{ECO:0000250|UniProtKB:Q96GM5, ECO:0000269|PubMed:17640523,
ECO:0000269|PubMed:29374058, ECO:0000269|PubMed:8804307,
ECO:0000269|PubMed:8895581}.
-!- INTERACTION:
B1AXD8:Akirin2; NbExp=2; IntAct=EBI-371529, EBI-10107866;
P97496:Smarcc1; NbExp=3; IntAct=EBI-371529, EBI-648047;
P70323:Tbx1; NbExp=3; IntAct=EBI-371529, EBI-13635846;
P02340:Tp53; NbExp=4; IntAct=EBI-371529, EBI-474016;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:2725507,
ECO:0000269|PubMed:8804307}.
-!- DEVELOPMENTAL STAGE: Expressed ubiquitously throughout the
developing spinal cord, brain and other embryonic tissues at
E10.5-E16.5. {ECO:0000269|PubMed:17640523}.
-!- SIMILARITY: Belongs to the SMARCD family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA53377.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAA53377.1; Type=Frameshift; Positions=29, 445, 447, 462, 473; Evidence={ECO:0000305};
Sequence=AAC52794.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAC52794.1; Type=Frameshift; Positions=29, 445, 447; Evidence={ECO:0000305};
Sequence=AAH26783.3; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; BC026783; AAH26783.3; ALT_INIT; mRNA.
EMBL; BC059921; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; M25773; AAA53377.1; ALT_SEQ; mRNA.
EMBL; U66620; AAC52794.1; ALT_SEQ; mRNA.
EMBL; AK075611; BAC35856.1; -; mRNA.
CCDS; CCDS37204.1; -.
PIR; A30222; A30222.
RefSeq; NP_114030.2; NM_031842.2.
UniGene; Mm.273756; -.
PDB; 1UHR; NMR; -; A=291-370.
PDBsum; 1UHR; -.
ProteinModelPortal; Q61466; -.
SMR; Q61466; -.
BioGrid; 219977; 15.
ComplexPortal; CPX-1232; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1233; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1234; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1235; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1236; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1237; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1238; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1239; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1240; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1241; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1242; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1243; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1244; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1245; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1246; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1247; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1248; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
ComplexPortal; CPX-1250; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
ComplexPortal; CPX-1251; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
ComplexPortal; CPX-1252; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1253; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1254; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1255; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1256; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
ComplexPortal; CPX-1257; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1258; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
ComplexPortal; CPX-1259; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
CORUM; Q61466; -.
DIP; DIP-33019N; -.
IntAct; Q61466; 14.
MINT; Q61466; -.
STRING; 10090.ENSMUSP00000023759; -.
iPTMnet; Q61466; -.
PhosphoSitePlus; Q61466; -.
PaxDb; Q61466; -.
PeptideAtlas; Q61466; -.
PRIDE; Q61466; -.
Ensembl; ENSMUST00000023759; ENSMUSP00000023759; ENSMUSG00000023018.
GeneID; 83797; -.
KEGG; mmu:83797; -.
UCSC; uc007xqb.1; mouse.
CTD; 6602; -.
MGI; MGI:1933623; Smarcd1.
eggNOG; KOG2570; Eukaryota.
eggNOG; COG5531; LUCA.
GeneTree; ENSGT00390000017809; -.
HOGENOM; HOG000240746; -.
HOVERGEN; HBG054046; -.
InParanoid; Q61466; -.
KO; K11650; -.
OMA; FRLPWVE; -.
OrthoDB; EOG091G06WW; -.
PhylomeDB; Q61466; -.
TreeFam; TF106486; -.
Reactome; R-MMU-3214858; RMTs methylate histone arginines.
Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
ChiTaRS; Smarcd1; mouse.
EvolutionaryTrace; Q61466; -.
PRO; PR:Q61466; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000023018; Expressed in 250 organ(s), highest expression level in ear.
Genevisible; Q61466; MM.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0071565; C:nBAF complex; IDA:UniProtKB.
GO; GO:0071564; C:npBAF complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0016514; C:SWI/SNF complex; ISO:MGI.
GO; GO:0003682; F:chromatin binding; ISO:MGI.
GO; GO:0032947; F:protein-containing complex scaffold activity; ISO:MGI.
GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
GO; GO:0048096; P:chromatin-mediated maintenance of transcription; ISO:MGI.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0006337; P:nucleosome disassembly; ISO:MGI.
Gene3D; 1.10.245.10; -; 1.
InterPro; IPR038041; SMARCD1.
InterPro; IPR019835; SWIB_domain.
InterPro; IPR036885; SWIB_MDM2_dom_sf.
InterPro; IPR003121; SWIB_MDM2_domain.
PANTHER; PTHR13844:SF1; PTHR13844:SF1; 1.
Pfam; PF02201; SWIB; 1.
SMART; SM00151; SWIB; 1.
SUPFAM; SSF47592; SSF47592; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromatin regulator; Coiled coil;
Complete proteome; Direct protein sequencing; Isopeptide bond;
Methylation; Neurogenesis; Nucleus; Phosphoprotein;
Reference proteome; Ubl conjugation.
CHAIN 1 515 SWI/SNF-related matrix-associated actin-
dependent regulator of chromatin
subfamily D member 1.
/FTId=PRO_0000071984.
DOMAIN 291 390 SWIB.
REGION 43 167 Interaction with ESR1, NR1H4, NR3C1, PGR
and SMARCA4. {ECO:0000250}.
REGION 168 474 Interaction with SMARCC1 and SMARCC2.
{ECO:0000250}.
REGION 180 515 Necessary for GR/NR3C1-mediated
remodeling and transcription from
chromatin; required for GR/NR3C1
interaction with the BRG1/SMARCA4 complex
in vivo. {ECO:0000250}.
COILED 412 440 {ECO:0000255}.
COMPBIAS 124 127 Poly-Lys.
MOD_RES 68 68 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q92925}.
MOD_RES 88 88 Asymmetric dimethylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 203 203 Phosphothreonine.
{ECO:0000250|UniProtKB:Q92925}.
MOD_RES 223 223 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
CROSSLNK 101 101 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q96GM5}.
CONFLICT 15 15 G -> A (in Ref. 2; AAA53377 and 3;
AAC52794). {ECO:0000305}.
CONFLICT 215 215 L -> I (in Ref. 4; BAC35856).
{ECO:0000305}.
CONFLICT 218 218 D -> E (in Ref. 4; BAC35856).
{ECO:0000305}.
CONFLICT 449 449 Q -> S (in Ref. 2; AAA53377 and 3;
AAC52794). {ECO:0000305}.
CONFLICT 462 462 D -> G (in Ref. 2; AAA53377 and 3;
AAC52794). {ECO:0000305}.
STRAND 294 297 {ECO:0000244|PDB:1UHR}.
HELIX 301 304 {ECO:0000244|PDB:1UHR}.
STRAND 308 311 {ECO:0000244|PDB:1UHR}.
HELIX 312 325 {ECO:0000244|PDB:1UHR}.
STRAND 334 337 {ECO:0000244|PDB:1UHR}.
HELIX 343 346 {ECO:0000244|PDB:1UHR}.
STRAND 350 353 {ECO:0000244|PDB:1UHR}.
HELIX 354 356 {ECO:0000244|PDB:1UHR}.
HELIX 358 364 {ECO:0000244|PDB:1UHR}.
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


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