SMCE1_MOUSE
ID SMCE1_MOUSE Reviewed; 411 AA.
AC O54941; Q8BPD9;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;
DE AltName: Full=BRG1-associated factor 57;
DE Short=BAF57;
GN Name=Smarce1; Synonyms=Baf57;
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 [GENOMIC DNA].
RX PubMed=9435219; DOI=10.1073/pnas.95.2.492;
RA Wang W., Chi T., Xue Y., Zhou S., Kuo A., Crabtree G.R.;
RT "Architectural DNA binding by a high-mobility-group/kinesin-like subunit in
RT mammalian SWI/SNF-related complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:492-498(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Colon, and Mammary tumor;
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]
RP FUNCTION, AND DOMAIN.
RX PubMed=12145209; DOI=10.1093/emboj/cdf412;
RA Belandia B., Orford R.L., Hurst H.C., Parker M.G.;
RT "Targeting of SWI/SNF chromatin remodelling complexes to estrogen-
RT responsive genes.";
RL EMBO J. 21:4094-4103(2002).
RN [5]
RP FUNCTION.
RX PubMed=12110891; DOI=10.1038/nature00876;
RA Chi T.H., Wan M., Zhao K., Taniuchi I., Chen L., Littman D.R.,
RA Crabtree G.R.;
RT "Reciprocal regulation of CD4/CD8 expression by SWI/SNF-like BAF
RT complexes.";
RL Nature 418:195-199(2002).
RN [6]
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Spleen;
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).
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:12110891). 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). Also specifically interacts with the CoREST
CC corepressor resulting in repression of neuronal specific gene promoters
CC in non-neuronal cells (By similarity). Required for the coactivation of
CC estrogen responsive promoters by SWI/SNF complexes and the SRC/p160
CC family of histone acetyltransferases (HATs)(PubMed:12145209).
CC {ECO:0000250|UniProtKB:Q969G3, ECO:0000269|PubMed:12110891,
CC ECO:0000269|PubMed:12145209, 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. Component of the BAF complex, which includes at least actin
CC (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM/BAF190B,
CC SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57,
CC SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
CC SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the
CC BAF complex also contains DPF3. Component of neural progenitors-
CC specific chromatin remodeling complex (npBAF complex) composed of at
CC 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. May be a 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:17640523). Interacts with BRDT (By similarity). Also
CC binds to the SRC/p160 family of histone acetyltransferases (HATs)
CC composed of NCOA1, NCOA2, and NCOA3. Interacts with RCOR1/CoREST, NR3C1
CC and ZMIM2/ZIMP7 (By similarity). {ECO:0000250|UniProtKB:Q56A18,
CC ECO:0000250|UniProtKB:Q969G3, ECO:0000269|PubMed:17640523}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
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 -!- DOMAIN: The HMG domain is essential for CD4 silencing and CD8
CC activation; mutation of this domain blocks thymus development.
CC {ECO:0000269|PubMed:12110891}.
CC -!- PTM: Ubiquitinated by TRIP12, leading to its degradation by the
CC proteasome. Ubiquitination is prevented upon interaction between TRIP12
CC and SMARCC1 (By similarity). {ECO:0000250|UniProtKB:Q969G3}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC36233.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC36233.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC36233.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AF035263; AAC04510.1; -; Genomic_DNA.
DR EMBL; AK076177; BAC36233.1; ALT_SEQ; mRNA.
DR EMBL; BC047141; AAH47141.1; -; mRNA.
DR EMBL; BC061498; AAH61498.1; -; mRNA.
DR EMBL; BC065043; AAH65043.1; -; mRNA.
DR CCDS; CCDS25374.1; -.
DR RefSeq; NP_065643.1; NM_020618.4.
DR AlphaFoldDB; O54941; -.
DR SMR; O54941; -.
DR BioGRID; 208275; 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-1261; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1262; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1263; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1264; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR CORUM; O54941; -.
DR DIP; DIP-39985N; -.
DR IntAct; O54941; 14.
DR MINT; O54941; -.
DR STRING; 10090.ENSMUSP00000099422; -.
DR iPTMnet; O54941; -.
DR PhosphoSitePlus; O54941; -.
DR SwissPalm; O54941; -.
DR EPD; O54941; -.
DR MaxQB; O54941; -.
DR PaxDb; O54941; -.
DR PeptideAtlas; O54941; -.
DR PRIDE; O54941; -.
DR ProteomicsDB; 261088; -.
DR Antibodypedia; 1299; 404 antibodies from 43 providers.
DR DNASU; 57376; -.
DR Ensembl; ENSMUST00000103133; ENSMUSP00000099422; ENSMUSG00000037935.
DR GeneID; 57376; -.
DR KEGG; mmu:57376; -.
DR UCSC; uc007lii.1; mouse.
DR CTD; 6605; -.
DR MGI; MGI:1927347; Smarce1.
DR VEuPathDB; HostDB:ENSMUSG00000037935; -.
DR eggNOG; KOG4715; Eukaryota.
DR GeneTree; ENSGT00390000003628; -.
DR HOGENOM; CLU_021772_1_1_1; -.
DR InParanoid; O54941; -.
DR OMA; QEYDIER; -.
DR OrthoDB; 1199500at2759; -.
DR PhylomeDB; O54941; -.
DR TreeFam; TF321146; -.
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; 57376; 11 hits in 80 CRISPR screens.
DR ChiTaRS; Smarce1; mouse.
DR PRO; PR:O54941; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; O54941; protein.
DR Bgee; ENSMUSG00000037935; Expressed in undifferentiated genital tubercle and 282 other tissues.
DR Genevisible; O54941; MM.
DR GO; GO:0140092; C:bBAF complex; IC:ComplexPortal.
DR GO; GO:0035060; C:brahma complex; IC:ComplexPortal.
DR GO; GO:0000785; C:chromatin; IC:ComplexPortal.
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:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008080; F:N-acetyltransferase activity; ISO:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IDA:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0022008; P:neurogenesis; IGI:MGI.
DR GO; GO:0006337; P:nucleosome disassembly; ISO:MGI.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IC:ComplexPortal.
DR GO; GO: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; IC:ComplexPortal.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR030089; BAF57.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR PANTHER; PTHR46232; PTHR46232; 1.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; DNA-binding; Isopeptide bond;
KW Methylation; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..411
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily E member 1"
FT /id="PRO_0000048578"
FT DNA_BIND 66..134
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 294..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 222..319
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT MOD_RES 40
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT CROSSLNK 3
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT CROSSLNK 131
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT CROSSLNK 146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q969G3"
SQ 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
