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SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1 (BRG1-associated factor 57) (BAF57)

 SMCE1_MOUSE             Reviewed;         411 AA.
O54941; Q8BPD9;
25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
25-APR-2018, entry version 149.
RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;
AltName: Full=BRG1-associated factor 57;
Short=BAF57;
Name=Smarce1; Synonyms=Baf57;
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 [GENOMIC DNA].
PubMed=9435219; DOI=10.1073/pnas.95.2.492;
Wang W., Chi T., Xue Y., Zhou S., Kuo A., Crabtree G.R.;
"Architectural DNA binding by a high-mobility-group/kinesin-like
subunit in mammalian SWI/SNF-related complexes.";
Proc. Natl. Acad. Sci. U.S.A. 95:492-498(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Colon, and Mammary tumor;
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).
[4]
FUNCTION, AND DOMAIN.
PubMed=12145209; DOI=10.1093/emboj/cdf412;
Belandia B., Orford R.L., Hurst H.C., Parker M.G.;
"Targeting of SWI/SNF chromatin remodelling complexes to estrogen-
responsive genes.";
EMBO J. 21:4094-4103(2002).
[5]
FUNCTION.
PubMed=12110891; DOI=10.1038/nature00876;
Chi T.H., Wan M., Zhao K., Taniuchi I., Chen L., Littman D.R.,
Crabtree G.R.;
"Reciprocal regulation of CD4/CD8 expression by SWI/SNF-like BAF
complexes.";
Nature 418:195-199(2002).
[6]
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).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, and Spleen;
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).
-!- 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 (PubMed:12110891). 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). Also specifically
interacts with the CoREST corepressor resulting in repression of
neuronal specific gene promoters in non-neuronal cells (By
similarity). Required for the coactivation of estrogen responsive
promoters by SWI/SNF complexes and the SRC/p160 family of histone
acetyltransferases (HATs)(PubMed:12145209).
{ECO:0000250|UniProtKB:Q969G3, ECO:0000269|PubMed:12110891,
ECO:0000269|PubMed:12145209, 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. Component of the
BAF complex, which includes at least actin (ACTB), ARID1A/BAF250A,
ARID1B/BAF250B, SMARCA2/BRM/BAF190B, 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. 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. May be a
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)(PubMed:17640523).
Interacts with BRDT (By similarity). Also binds to the SRC/p160
family of histone acetyltransferases (HATs) composed of NCOA1,
NCOA2, and NCOA3. Interacts with RCOR1/CoREST, NR3C1 and
ZMIM2/ZIMP7 (By similarity). {ECO:0000250|UniProtKB:Q56A18,
ECO:0000250|UniProtKB:Q969G3, ECO:0000269|PubMed:17640523}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00267}.
-!- DEVELOPMENTAL STAGE: Expressed ubiquitously throughout the
developing spinal cord, brain and other embryonic tissues at
E10.5-E16.5. {ECO:0000269|PubMed:17640523}.
-!- DOMAIN: The HMG domain is essential for CD4 silencing and CD8
activation; mutation of this domain blocks thymus development.
{ECO:0000269|PubMed:12110891}.
-!- PTM: Ubiquitinated by TRIP12, leading to its degradation by the
proteasome. Ubiquitination is prevented upon interaction between
TRIP12 and SMARCC1 (By similarity).
{ECO:0000250|UniProtKB:Q969G3}.
-!- SEQUENCE CAUTION:
Sequence=BAC36233.1; Type=Erroneous termination; Positions=408; Note=Translated as Glu.; Evidence={ECO:0000305};
Sequence=BAC36233.1; Type=Frameshift; Positions=184, 212, 255, 316, 353; Evidence={ECO:0000305};
Sequence=BAC36233.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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EMBL; AF035263; AAC04510.1; -; Genomic_DNA.
EMBL; AK076177; BAC36233.1; ALT_SEQ; mRNA.
EMBL; BC047141; AAH47141.1; -; mRNA.
EMBL; BC061498; AAH61498.1; -; mRNA.
EMBL; BC065043; AAH65043.1; -; mRNA.
CCDS; CCDS25374.1; -.
RefSeq; NP_065643.1; NM_020618.4.
UniGene; Mm.379086; -.
UniGene; Mm.389717; -.
ProteinModelPortal; O54941; -.
BioGrid; 208275; 19.
CORUM; O54941; -.
DIP; DIP-39985N; -.
IntAct; O54941; 12.
MINT; O54941; -.
STRING; 10090.ENSMUSP00000099422; -.
iPTMnet; O54941; -.
PhosphoSitePlus; O54941; -.
SwissPalm; O54941; -.
EPD; O54941; -.
MaxQB; O54941; -.
PaxDb; O54941; -.
PeptideAtlas; O54941; -.
PRIDE; O54941; -.
Ensembl; ENSMUST00000103133; ENSMUSP00000099422; ENSMUSG00000037935.
GeneID; 57376; -.
KEGG; mmu:57376; -.
UCSC; uc007lii.1; mouse.
CTD; 6605; -.
MGI; MGI:1927347; Smarce1.
eggNOG; KOG4715; Eukaryota.
eggNOG; ENOG410Y9B3; LUCA.
GeneTree; ENSGT00390000003628; -.
HOGENOM; HOG000230965; -.
HOVERGEN; HBG054558; -.
InParanoid; O54941; -.
KO; K11651; -.
OMA; CCMKVEV; -.
OrthoDB; EOG091G0ER1; -.
PhylomeDB; O54941; -.
TreeFam; TF321146; -.
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.
PRO; PR:O54941; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000037935; -.
Genevisible; O54941; MM.
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; IDA:MGI.
GO; GO:0017053; C:transcriptional repressor complex; ISO:MGI.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0016922; F:ligand-dependent nuclear receptor binding; ISO:MGI.
GO; GO:0008080; F:N-acetyltransferase activity; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0003723; F:RNA binding; IDA:MGI.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; IEA:InterPro.
GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0022008; P:neurogenesis; IGI:MGI.
GO; GO:0006337; P:nucleosome disassembly; ISO:MGI.
Gene3D; 1.10.30.10; -; 1.
InterPro; IPR030089; BAF57.
InterPro; IPR009071; HMG_box_dom.
InterPro; IPR036910; HMG_box_dom_sf.
PANTHER; PTHR13711:SF206; PTHR13711:SF206; 1.
Pfam; PF00505; HMG_box; 1.
SMART; SM00398; HMG; 1.
SUPFAM; SSF47095; SSF47095; 1.
PROSITE; PS50118; HMG_BOX_2; 1.
1: Evidence at protein level;
Chromatin regulator; Coiled coil; Complete proteome; DNA-binding;
Isopeptide bond; Methylation; Neurogenesis; Nucleus; Phosphoprotein;
Reference proteome; Ubl conjugation.
CHAIN 1 411 SWI/SNF-related matrix-associated actin-
dependent regulator of chromatin
subfamily E member 1.
/FTId=PRO_0000048578.
DNA_BIND 66 134 HMG box. {ECO:0000255|PROSITE-
ProRule:PRU00267}.
COILED 222 319 {ECO:0000255}.
COMPBIAS 320 411 Glu-rich.
MOD_RES 4 4 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q969G3}.
MOD_RES 40 40 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q969G3}.
MOD_RES 265 265 Phosphoserine.
{ECO:0000250|UniProtKB:Q969G3}.
CROSSLNK 3 3 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q969G3}.
CROSSLNK 92 92 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate.
{ECO:0000250|UniProtKB:Q969G3}.
CROSSLNK 92 92 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q969G3}.
CROSSLNK 131 131 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q969G3}.
CROSSLNK 146 146 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q969G3}.
CROSSLNK 166 166 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q969G3}.
CROSSLNK 277 277 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q969G3}.
SEQUENCE 411 AA; 46638 MW; 4099B333A0B63709 CRC64;
MSKRPSYAPP PTPAPATQMP STPGFVGYNP YSHLAYNNYR LGGNPGTNSR VTASSGITIP
KPPKPPDKPL MPYMRYSRKV WDQVKASNPD LKLWEIGKII GGMWRDLTDE EKQEYLNEYE
AEKIEYNESM KAYHNSPAYL AYINAKSRAE AALEEESRQR QSRMEKGEPY MSIQPAEDPD
DYDDGFSMKH TATARFQRNH RLISEILSES VVPDVRSVVT TARMQVLKRQ VQSLMVHQRK
LEAELLQIEE RHQEKKRKFL ESTDSFNNEL KRLCGLKVEV DMEKIAAEIA QAEEQARKRQ
EEREKEAAEQ AERSQSSMAP EEEQVANKAE EKKDEESIPM ETEETHLEDT AESQQNGEEG
TSTPEDKESG QEGVDSMEVE GTSDSNTGSE SNSATVEEPP TDPVPEDEKK E


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