SMCA2_MOUSE
ID SMCA2_MOUSE Reviewed; 1577 AA.
AC Q6DIC0;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Probable global transcription activator SNF2L2;
DE EC=3.6.4.-;
DE AltName: Full=ATP-dependent helicase SMARCA2;
DE AltName: Full=BRG1-associated factor 190B;
DE Short=BAF190B;
DE AltName: Full=Protein brahma homolog;
DE AltName: Full=SNF2-alpha;
DE AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2;
GN Name=Smarca2 {ECO:0000312|MGI:MGI:99603};
GN Synonyms=Baf190b, Brm, Snf2a, Snf2l2 {ECO:0000303|PubMed:15107404};
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=Brain;
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 INTERACTION WITH CEBPA.
RX PubMed=15107404; DOI=10.1101/gad.1183304;
RA Wang G.L., Iakova P., Wilde M., Awad S., Timchenko N.A.;
RT "Liver tumors escape negative control of proliferation via PI3K/Akt-
RT mediated block of C/EBP alpha growth inhibitory activity.";
RL Genes Dev. 18:912-925(2004).
RN [3]
RP FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS
RP SPECTROMETRY, IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES, AND
RP INTERACTION WITH PHF10.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334; SER-1499 AND SER-1503,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=19363039; DOI=10.1093/hmg/ddp166;
RA Koga M., Ishiguro H., Yazaki S., Horiuchi Y., Arai M., Niizato K.,
RA Iritani S., Itokawa M., Inada T., Iwata N., Ozaki N., Ujike H., Kunugi H.,
RA Sasaki T., Takahashi M., Watanabe Y., Someya T., Kakita A., Takahashi H.,
RA Nawa H., Muchardt C., Yaniv M., Arinami T.;
RT "Involvement of SMARCA2/BRM in the SWI/SNF chromatin-remodeling complex in
RT schizophrenia.";
RL Hum. Mol. Genet. 18:2483-2494(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-334; SER-596;
RP SER-1499; SER-1503 AND SER-1515, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, Spleen, 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 [7]
RP INTERACTION WITH CEBPB.
RX PubMed=20111005; DOI=10.1038/emboj.2010.3;
RA Kowenz-Leutz E., Pless O., Dittmar G., Knoblich M., Leutz A.;
RT "Crosstalk between C/EBPbeta phosphorylation, arginine methylation, and
RT SWI/SNF/Mediator implies an indexing transcription factor code.";
RL EMBO J. 29:1105-1115(2010).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=22366787; DOI=10.1038/ng.1105;
RA Van Houdt J.K., Nowakowska B.A., Sousa S.B., van Schaik B.D., Seuntjens E.,
RA Avonce N., Sifrim A., Abdul-Rahman O.A., van den Boogaard M.J., Bottani A.,
RA Castori M., Cormier-Daire V., Deardorff M.A., Filges I., Fryer A.,
RA Fryns J.P., Gana S., Garavelli L., Gillessen-Kaesbach G., Hall B.D.,
RA Horn D., Huylebroeck D., Klapecki J., Krajewska-Walasek M., Kuechler A.,
RA Lines M.A., Maas S., Macdermot K.D., McKee S., Magee A., de Man S.A.,
RA Moreau Y., Morice-Picard F., Obersztyn E., Pilch J., Rosser E., Shannon N.,
RA Stolte-Dijkstra I., Van Dijck P., Vilain C., Vogels A., Wakeling E.,
RA Wieczorek D., Wilson L., Zuffardi O., van Kampen A.H., Devriendt K.,
RA Hennekam R., Vermeesch J.R.;
RT "Heterozygous missense mutations in SMARCA2 cause Nicolaides-Baraitser
RT syndrome.";
RL Nat. Genet. 44:445-449(2012).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-609, 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 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).
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. Binds DNA non-specifically (PubMed:22952240, PubMed:26601204).
CC Belongs to the neural progenitors-specific chromatin remodeling complex
CC (npBAF complex) and the neuron-specific chromatin remodeling complex
CC (nBAF complex). During neural development a switch from a
CC stem/progenitor to a postmitotic chromatin remodeling mechanism occurs
CC as neurons exit the cell cycle and become committed to their adult
CC state. The transition from proliferating neural stem/progenitor cells
CC to postmitotic neurons requires a switch in subunit composition of the
CC npBAF and nBAF complexes. As neural progenitors exit mitosis and
CC differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A
CC and PHF10/BAF45A, are exchanged for homologous alternative
CC ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-
CC specific complexes (nBAF). The npBAF complex is essential for the self-
CC renewal/proliferative capacity of the multipotent neural stem cells.
CC The nBAF complex along with CREST plays a role regulating the activity
CC of genes essential for dendrite growth. {ECO:0000250|UniProtKB:P51531,
CC ECO:0000269|PubMed:17640523, ECO:0000303|PubMed:22952240,
CC 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 (Probable). Component of the BAF complex, which includes at
CC 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 (By similarity). In
CC muscle cells, the BAF complex also contains DPF3 (By similarity).
CC Component of neural progenitors-specific chromatin remodeling complex
CC (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B,
CC 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 Interacts with PHF10/BAF45A (By similarity). Interacts with CEBPB (when
CC not methylated) (PubMed:20111005). Interacts with TOPBP1 (By
CC similarity). Interacts with CEBPA (when phosphorylated)
CC (PubMed:15107404). Interacts with DPF2 (By similarity). Interacts with
CC ERCC6 (By similarity). {ECO:0000250|UniProtKB:P51531,
CC ECO:0000269|PubMed:15107404, ECO:0000269|PubMed:17640523,
CC ECO:0000269|PubMed:20111005, ECO:0000303|PubMed:22952240,
CC ECO:0000303|PubMed:26601204}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549}.
CC -!- TISSUE SPECIFICITY: Expressed in the cortex and the hippocampus.
CC Expressed in the cortical plate in the embryo.
CC {ECO:0000269|PubMed:22366787}.
CC -!- PTM: During apoptosis, cleaved by cathepsin CTSG to produce a 160 kDa
CC cleavage product which localizes to the cytosol.
CC {ECO:0000250|UniProtKB:P51531}.
CC -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:P51531}.
CC -!- DISRUPTION PHENOTYPE: Impaired social interaction and prepulse
CC inhibition. {ECO:0000269|PubMed:19363039}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; BC075641; AAH75641.1; -; mRNA.
DR RefSeq; NP_001334368.1; NM_001347439.1.
DR RefSeq; NP_035546.2; NM_011416.2.
DR AlphaFoldDB; Q6DIC0; -.
DR BMRB; Q6DIC0; -.
DR SMR; Q6DIC0; -.
DR BioGRID; 211982; 46.
DR ComplexPortal; CPX-1232; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1234; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1236; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1238; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1240; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1242; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1244; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1246; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1252; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1254; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1256; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1258; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1261; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1263; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 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-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 DIP; DIP-48888N; -.
DR IntAct; Q6DIC0; 3.
DR MINT; Q6DIC0; -.
DR STRING; 10090.ENSMUSP00000025862; -.
DR iPTMnet; Q6DIC0; -.
DR PhosphoSitePlus; Q6DIC0; -.
DR SwissPalm; Q6DIC0; -.
DR EPD; Q6DIC0; -.
DR jPOST; Q6DIC0; -.
DR MaxQB; Q6DIC0; -.
DR PaxDb; Q6DIC0; -.
DR PRIDE; Q6DIC0; -.
DR ProteomicsDB; 261523; -.
DR DNASU; 67155; -.
DR GeneID; 67155; -.
DR KEGG; mmu:67155; -.
DR UCSC; uc012bjw.1; mouse.
DR CTD; 6595; -.
DR MGI; MGI:99603; Smarca2.
DR eggNOG; KOG0386; Eukaryota.
DR InParanoid; Q6DIC0; -.
DR PhylomeDB; Q6DIC0; -.
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; 67155; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Smarca2; mouse.
DR PRO; PR:Q6DIC0; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q6DIC0; protein.
DR GO; GO:0140092; C:bBAF complex; IC:ComplexPortal.
DR GO; GO:0035060; C:brahma complex; IC:ComplexPortal.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0140288; C:GBAF complex; IC:ComplexPortal.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0071565; C:nBAF complex; IDA:UniProtKB.
DR GO; GO:0071564; C:npBAF complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016514; C:SWI/SNF complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0035887; P:aortic smooth muscle cell differentiation; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0006325; P:chromatin organization; TAS:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IMP:MGI.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0006334; P:nucleosome assembly; TAS: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:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
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; 1.20.920.10; -; 1.
DR Gene3D; 3.40.5.120; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR030088; SMARCA2.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF541; PTHR10799:SF541; 1.
DR Pfam; PF07533; BRK; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF160481; SSF160481; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS51666; QLQ; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; ATP-binding; Bromodomain; DNA-binding; Helicase;
KW Hydrolase; Isopeptide bond; Neurogenesis; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1577
FT /note="Probable global transcription activator SNF2L2"
FT /id="PRO_0000391618"
FT DOMAIN 167..202
FT /note="QLQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01001"
FT DOMAIN 441..513
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 741..906
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1059..1221
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1406..1476
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1493..1577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 856..859
FT /note="DEGH box"
FT COMPBIAS 8..36
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..150
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..658
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1516
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1558..1577
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 754..761
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51531"
FT MOD_RES 169
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51531"
FT MOD_RES 184
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 596
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 609
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51531"
FT MOD_RES 675
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 1002
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51531"
FT MOD_RES 1004
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51531"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51531"
FT MOD_RES 1499
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51531"
FT MOD_RES 1559
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51531"
FT CROSSLNK 1307
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P51532"
SQ SEQUENCE 1577 AA; 180253 MW; 5D79E8FFC66085BE CRC64;
MSTPTDPAAM PHPGPSPGPG PSPGPILGPS PGPGPSPGSV HSMMGPSPGP PSVSHPLSTM
GSADFPQEGM HQLHKPMDGI HDKGIVEDVH CGSMKGTSMR PPHPGMGPPQ SPMDQHSQGY
MSPHPSPLGA PEHVSSPTPP QMPPSQPGAL IPGDPQAMNQ PNRGPSPFSP VQLHQLRAQI
LAYKMLARGQ PLPETLQLAV QGKRTLPGMQ QQQQQQQQQQ QQQQQQQQQQ QQQQQPQQPQ
QQAQAQPQQQ QQQQQQPALV SYNRPSGPGQ ELLLSGQSAP QKLSAPAPSG RPSPAPQAAV
QPTATAVPGP SVQQPAPGQP SPVLQLQQKQ SRISPIQKPQ GLDPVEILQE REYRLQARIA
HRIQELESLP GSLPPDLRTK ATVELKALRL LNFQRQLRQE VVACMRRDTT LETALNSKAY
KRSKRQTLRE ARMTEKLEKQ QKIEQERKRR QKHQEYLNSI LQHAKDFKEY HRSVAGKIQK
LSKAVATWHA NTEREQKKET ERIEKERMRR LMAEDEEGYR KLIDQKKDRR LAYLLQQTDE
YVANLTNLVW EHKQAQAAKE KKKRRRRKKK AEENAEGGEP ALGPDGEPID ESSQMSDLPV
KVTHTETGKV LFGPEAPKAS QLDAWLEMNP GYEVAPRSDS EESESDYEEE DEEEESSRQE
TEEKILLDPN SEEVSEKDAK QIIETAKQDV DDEYSMQYSA RGSQSYYTVA HAISERVEKQ
SALLINGTLK HYQLQGLEWM VSLYNNNLNG ILADEMGLGK TIQTIALITY LMEHKRLNGP
YLIIVPLSTL SNWTYEFDKW APSVVKISYK GTPAMRRSLV PQLRSGKFNV LLTTYEYIIK
DKHILAKIRW KYMIVDEGHR MKNHHCKLTQ VLNTHYVAPR RILLTGTPLQ NKLPELWALL
NFLLPTIFKS CSTFEQWFNA PFAMTGERVD LNEEETILII RRLHKVLRPF LLRRLKKEVE
SQLPEKVEYV IKCDMSALQK ILYRHMQAKG ILLTDGSEKD KKGKGGAKTL MNTIMQLRKI
CNHPYMFQHI EESFAEHLGY SNGVINGAEL YRASGKFELL DRILPKLRAT NHRVLLFCQM
TSLMTIMEDY FAFRNFLYLR LDGTTKSEDR AALLKKFNEP GSQYFIFLLS TRAGGLGLNL
QAADTVVIFD SDWNPHQDLQ AQDRAHRIGQ QNEVRVLRLC TVNSVEEKIL AAAKYKLNVD
QKVIQAGMFD QKSSSHERRA FLQAILEHEE ENEEEDEVPD DETLNQMIAR REEEFDLFMR
MDMDRRREDA RNPKRKPRLM EEDELPSWII KDDAEVERLT CEEEEEKIFG RGSRQRRDVD
YSDALTEKQW LRAIEDGNLE EMEEEVRLKK RKRRRNVDKD PVKEDVEKAK KRRGRPPAEK
LSPNPPKLTK QMNAIIDTVI NYKDSSGRQL SEVFIQLPSR KDLPEYYELI RKPVDFKKIK
ERIRNHKYRS LGDLEKDVML LCHNAQTFNL EGSQIYEDSI VLQSVFKSAR QKIAKEEESE
EESNEEEEED DEEESESEAK SVKVKIKLNK KEEKGRDTGK GKKRPNRGKA KPVVSDFDSD
EEQEENEQSE ASGTDNE
