SMCA1_HUMAN
ID SMCA1_HUMAN Reviewed; 1054 AA.
AC P28370; Q5JV41; Q5JV42;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 218.
DE RecName: Full=Probable global transcription activator SNF2L1;
DE EC=3.6.4.- {ECO:0000269|PubMed:14609955, ECO:0000269|PubMed:15310751, ECO:0000269|PubMed:15640247, ECO:0000269|PubMed:28801535};
DE AltName: Full=ATP-dependent helicase SMARCA1;
DE AltName: Full=Nucleosome-remodeling factor subunit SNF2L;
DE AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 1;
GN Name=SMARCA1; Synonyms=SNF2L, SNF2L1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-656.
RC TISSUE=Kidney;
RX PubMed=1408766; DOI=10.1093/nar/20.17.4649;
RA Okabe I., Bailey L.C., Attree O.F., Perkel J.M., Nelson D.L.,
RA Nussbaum R.L.;
RT "Cloning of human and bovine homologs of SNF2/SWI2: a global activator of
RT transcription in yeast S. cerevisiae.";
RL Nucleic Acids Res. 20:4649-4655(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, CATALYTIC ACTIVITY,
RP SUBUNIT, IDENTIFICATION IN A COMPLEX WITH BPFT; RBBP4 AND RBBP7,
RP INTERACTION WITH BPTF; RBBP4 AND RBBP7, AND TISSUE SPECIFICITY.
RX PubMed=15310751; DOI=10.1074/jbc.m406212200;
RA Barak O., Lazzaro M.A., Cooch N.S., Picketts D.J., Shiekhattar R.;
RT "A tissue-specific, naturally occurring human SNF2L variant inactivates
RT chromatin remodeling.";
RL J. Biol. Chem. 279:45130-45138(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
RP PHOSPHORYLATION AT TYR-954.
RX PubMed=12112843;
RX DOI=10.1002/1615-9861(200206)2:6<642::aid-prot642>3.0.co;2-i;
RA Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G.,
RA Fitzgerald D.J.;
RT "Identification of the phosphotyrosine proteome from thrombin activated
RT platelets.";
RL Proteomics 2:642-648(2002).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION IN THE NURF-1 ISWI CHROMATIN
RP REMODELING COMPLEX, INTERACTION WITH BPTF; RBBP4 AND RBBP7, MUTAGENESIS OF
RP LYS-214, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14609955; DOI=10.1093/emboj/cdg582;
RA Barak O., Lazzaro M.A., Lane W.S., Speicher D.W., Picketts D.J.,
RA Shiekhattar R.;
RT "Isolation of human NURF: a regulator of Engrailed gene expression.";
RL EMBO J. 22:6089-6100(2003).
RN [7]
RP FUNCTION (ISOFORM 2), CATALYTIC ACTIVITY, IDENTIFICATION IN THE CERF-1 ISWI
RP CHROMATIN REMODELING COMPLEX, IDENTIFICATION IN THE NURF-1 ISWI CHROMATIN
RP REMODELING COMPLEX, AND IDENTIFICATION IN THE RSF-1 ISWI CHROMATIN
RP REMODELING COMPLEX.
RX PubMed=15640247; DOI=10.1093/hmg/ddi048;
RA Banting G.S., Barak O., Ames T.M., Burnham A.C., Kardel M.D., Cooch N.S.,
RA Davidson C.E., Godbout R., McDermid H.E., Shiekhattar R.;
RT "CECR2, a protein involved in neurulation, forms a novel chromatin
RT remodeling complex with SNF2L.";
RL Hum. Mol. Genet. 14:513-524(2005).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP FUNCTION, AND INTERACTION WITH PRLR.
RX PubMed=16740656; DOI=10.1210/me.2005-0213;
RA Lazzaro M.A., Pepin D., Pescador N., Murphy B.D., Vanderhyden B.C.,
RA Picketts D.J.;
RT "The imitation switch protein SNF2L regulates steroidogenic acute
RT regulatory protein expression during terminal differentiation of ovarian
RT granulosa cells.";
RL Mol. Endocrinol. 20:2406-2417(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-119, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-728, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [15]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
RN [16]
RP FUNCTION, IDENTIFICATION IN THE BAZ1A-1-SMARCA1 COMPLEX, IDENTIFICATION IN
RP THE BAZ1B-1-SMARCA1 COMPLEX, IDENTIFICATION IN THE ACF-1 ISWI CHROMATIN
RP REMODELING COMPLEX, IDENTIFICATION IN THE WICH-1 ISWI CHROMATIN REMODELING
RP COMPLEX, IDENTIFICATION IN THE NORC-1 ISWI CHROMATIN REMODELING COMPLEX,
RP IDENTIFICATION IN THE BRF-1 ISWI CHROMATIN REMODELING COMPLEX,
RP IDENTIFICATION IN THE NURF-1 ISWI CHROMATIN REMODELING COMPLEX,
RP IDENTIFICATION IN THE CERF-1 ISWI CHROMATIN REMODELING COMPLEX,
RP IDENTIFICATION IN THE RSF-1 ISWI CHROMATIN REMODELING COMPLEX, AND
RP INTERACTION WITH BPTF; RBBP4; RBBP7; BAZ1A; BAZ1B; BAZ2A; BAZ2B; CECR2 AND
RP RSF1.
RX PubMed=28801535; DOI=10.15252/embr.201744011;
RA Oppikofer M., Bai T., Gan Y., Haley B., Liu P., Sandoval W., Ciferri C.,
RA Cochran A.G.;
RT "Expansion of the ISWI chromatin remodeler family with new active
RT complexes.";
RL EMBO Rep. 18:1697-1706(2017).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-662; LYS-728 AND LYS-750, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [18]
RP VARIANT VAL-978.
RX PubMed=26740508; DOI=10.1136/jmedgenet-2015-103568;
RA Lopes F., Barbosa M., Ameur A., Soares G., de Sa J., Dias A.I.,
RA Oliveira G., Cabral P., Temudo T., Calado E., Cruz I.F., Vieira J.P.,
RA Oliveira R., Esteves S., Sauer S., Jonasson I., Syvaenen A.C.,
RA Gyllensten U., Pinto D., Maciel P.;
RT "Identification of novel genetic causes of Rett syndrome-like phenotypes.";
RL J. Med. Genet. 53:190-199(2016).
CC -!- FUNCTION: [Isoform 1]: Catalytically inactive when either DNA or
CC nucleosomes are the substrate and does not possess chromatin-remodeling
CC activity (PubMed:15310751, PubMed:28801535). Acts as a negative
CC regulator of chromatin remodelers by generating inactive complexes
CC (PubMed:15310751). {ECO:0000269|PubMed:15310751,
CC ECO:0000269|PubMed:28801535}.
CC -!- FUNCTION: [Isoform 2]: Helicase that possesses intrinsic ATP-dependent
CC chromatin-remodeling activity (PubMed:15310751, PubMed:14609955,
CC PubMed:15640247, PubMed:28801535). ATPase activity is substrate-
CC dependent, and is increased when nucleosomes are the substrate, but is
CC also catalytically active when DNA alone is the substrate
CC (PubMed:15310751, PubMed:14609955, PubMed:15640247). Catalytic subunit
CC of ISWI chromatin-remodeling complexes, which form ordered nucleosome
CC arrays on chromatin and facilitate access to DNA during DNA-templated
CC processes such as DNA replication, transcription, and repair
CC (PubMed:15310751, PubMed:14609955, PubMed:15640247, PubMed:28801535).
CC Within the ISWI chromatin-remodeling complexes, slides edge- and
CC center-positioned histone octamers away from their original location on
CC the DNA template (PubMed:28801535). Catalytic activity and histone
CC octamer sliding propensity is regulated and determined by components of
CC the ISWI chromatin-remodeling complexes (PubMed:28801535). The BAZ1A-,
CC BAZ1B-, BAZ2A- and BAZ2B-containing ISWI chromatin-remodeling complexes
CC regulate the spacing of nucleosomes along the chromatin and have the
CC ability to slide mononucleosomes to the center of a DNA template
CC (PubMed:28801535). The CECR2- and RSF1-containing ISWI chromatin-
CC remodeling complexes do not have the ability to slide mononucleosomes
CC to the center of a DNA template (PubMed:28801535). Within the NURF-1
CC and CERF-1 ISWI chromatin remodeling complexes, nucleosomes are the
CC preferred substrate for its ATPase activity (PubMed:14609955,
CC PubMed:15640247). Within the NURF-1 ISWI chromatin-remodeling complex,
CC binds to the promoters of En1 and En2 to positively regulate their
CC expression and promote brain development (PubMed:14609955). May promote
CC neurite outgrowth (PubMed:14609955). May be involved in the development
CC of luteal cells (PubMed:16740656). {ECO:0000269|PubMed:14609955,
CC ECO:0000269|PubMed:15310751, ECO:0000269|PubMed:15640247,
CC ECO:0000269|PubMed:16740656, ECO:0000269|PubMed:28801535}.
CC -!- SUBUNIT: [Isoform 1]: May form homodimers (PubMed:15310751). Component
CC of the BPFT-SMARCA1 complex at least composed of SMARCA1, BPFT, RBBP4
CC and RBBP7; the complex is catalytically inactive and does not remodel
CC chromatin (PubMed:15310751). Within the complex interacts with BPTF,
CC RBBP4 and RBBP7 (PubMed:15310751). Component of the BAZ1A-1-SMARCA1
CC complex at least composed of SMARCA1 and BAZ1A; the complex is
CC catalytically inactive and does not remodel chromatin
CC (PubMed:28801535). Component of the BAZ1B-1-SMARCA1 complex at least
CC composed of SMARCA1 and BAZ1B; the complex is catalytically inactive
CC and does not remodel chromatin (PubMed:28801535).
CC {ECO:0000269|PubMed:15310751, ECO:0000269|PubMed:28801535}.
CC -!- SUBUNIT: [Isoform 2]: May form homodimers (PubMed:15310751). Component
CC of the ACF-1 ISWI chromatin remodeling complex at least composed of
CC SMARCA1 and BAZ1A, which regulates the spacing of histone octamers on
CC the DNA template to facilitate access to DNA (PubMed:28801535). Within
CC the complex interacts with BAZ1A; the interaction is direct
CC (PubMed:28801535). Component of the WICH-1 ISWI chromatin remodeling
CC complex at least composed of SMARCA1 and BAZ1B/WSTF (PubMed:28801535).
CC Within the complex interacts with BAZ1B/WSTF (PubMed:28801535).
CC Component of the NoRC-1 ISWI chromatin remodeling complex at least
CC composed of SMARCA1 and BAZ2A/TIP5 (PubMed:28801535). Within the
CC complex interacts with BAZ2A/TIP5 (PubMed:28801535). Component of the
CC BRF-1 ISWI chromatin remodeling complex at least composed of SMARCA1
CC and BAZ2B (PubMed:28801535). Within the complex interacts with BAZ2B
CC (PubMed:28801535). Component of the NURF-1 ISWI chromatin remodeling
CC complex (also called the nucleosome-remodeling factor (NURF) complex)
CC at least composed of SMARCA1, BPTF, RBBP4 and RBBP7 (PubMed:14609955,
CC PubMed:15640247, PubMed:28801535). Within the complex interacts with
CC BPTF (PubMed:15310751, PubMed:14609955, PubMed:28801535). Within the
CC complex interacts with RBBP4 and RBBP7 (PubMed:15310751,
CC PubMed:14609955). Component of the CERF-1 ISWI chromatin remodeling
CC complex (also called the CECR2-containing-remodeling factor (CERF)
CC complex) at least composed of CECR2 and SMARCA1 (PubMed:15640247,
CC PubMed:28801535). Within the complex interacts with CECR2
CC (PubMed:28801535). Component of the RSF-1 ISWI chromatin remodeling
CC complex at least composed of SMARCA1 and RSF1 (PubMed:15640247,
CC PubMed:28801535). Within the complex interacts with RSF1
CC (PubMed:28801535). Interacts with PRLR (PubMed:16740656). Interacts
CC with ERCC6 (PubMed:26030138). {ECO:0000269|PubMed:14609955,
CC ECO:0000269|PubMed:15310751, ECO:0000269|PubMed:15640247,
CC ECO:0000269|PubMed:28801535}.
CC -!- INTERACTION:
CC P28370; Q12830: BPTF; NbExp=6; IntAct=EBI-2822460, EBI-1560273;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=SMARCA1.13 {ECO:0000303|PubMed:28801535};
CC IsoId=P28370-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28370-2; Sequence=VSP_020406;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Mainly expressed in non-neuronal
CC tissues such as lung, breast, kidney, and ovary.
CC {ECO:0000269|PubMed:15310751}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Expressed in lung, breast, kidney,
CC ovary, skeletal muscle and brain. {ECO:0000269|PubMed:15310751}.
CC -!- MISCELLANEOUS: [Isoform 1]: Inactive as an ATPase due to the presence
CC of exon 13, but retains its ability to correctly fold and incorporate
CC into complexes. {ECO:0000269|PubMed:15310751,
CC ECO:0000269|PubMed:28801535}.
CC -!- MISCELLANEOUS: [Isoform 2]: Active as an ATPase due to the absence of
CC exon 13. {ECO:0000269|PubMed:15310751, ECO:0000269|PubMed:28801535}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA80560.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M88163; AAA80559.1; -; mRNA.
DR EMBL; M89907; AAA80560.1; ALT_INIT; mRNA.
DR EMBL; AL022577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117447; AAI17448.1; -; mRNA.
DR CCDS; CCDS14612.1; -. [P28370-1]
DR PIR; S35457; S35457.
DR PIR; S35458; S35458.
DR RefSeq; NP_001269804.1; NM_001282875.1.
DR RefSeq; NP_003060.2; NM_003069.4. [P28370-1]
DR RefSeq; XP_005262518.1; XM_005262461.2. [P28370-1]
DR RefSeq; XP_006724845.1; XM_006724782.2.
DR RefSeq; XP_016885239.1; XM_017029750.1.
DR AlphaFoldDB; P28370; -.
DR SMR; P28370; -.
DR BioGRID; 112478; 142.
DR ComplexPortal; CPX-446; CERF chromatin remodelling complex.
DR ComplexPortal; CPX-688; NuRF chromatin remodeling complex.
DR CORUM; P28370; -.
DR DIP; DIP-57685N; -.
DR IntAct; P28370; 44.
DR MINT; P28370; -.
DR STRING; 9606.ENSP00000360162; -.
DR iPTMnet; P28370; -.
DR PhosphoSitePlus; P28370; -.
DR SwissPalm; P28370; -.
DR BioMuta; SMARCA1; -.
DR DMDM; 115311627; -.
DR EPD; P28370; -.
DR jPOST; P28370; -.
DR MassIVE; P28370; -.
DR MaxQB; P28370; -.
DR PaxDb; P28370; -.
DR PeptideAtlas; P28370; -.
DR PRIDE; P28370; -.
DR ProteomicsDB; 54483; -. [P28370-1]
DR ProteomicsDB; 54484; -. [P28370-2]
DR Antibodypedia; 518; 205 antibodies from 27 providers.
DR DNASU; 6594; -.
DR Ensembl; ENST00000371122.8; ENSP00000360163.4; ENSG00000102038.16. [P28370-1]
DR GeneID; 6594; -.
DR KEGG; hsa:6594; -.
DR UCSC; uc004eun.6; human. [P28370-1]
DR CTD; 6594; -.
DR DisGeNET; 6594; -.
DR GeneCards; SMARCA1; -.
DR HGNC; HGNC:11097; SMARCA1.
DR HPA; ENSG00000102038; Low tissue specificity.
DR MIM; 300012; gene.
DR neXtProt; NX_P28370; -.
DR OpenTargets; ENSG00000102038; -.
DR PharmGKB; PA35947; -.
DR VEuPathDB; HostDB:ENSG00000102038; -.
DR eggNOG; KOG0385; Eukaryota.
DR GeneTree; ENSGT00940000157297; -.
DR HOGENOM; CLU_000315_0_2_1; -.
DR InParanoid; P28370; -.
DR PhylomeDB; P28370; -.
DR TreeFam; TF300674; -.
DR PathwayCommons; P28370; -.
DR SignaLink; P28370; -.
DR SIGNOR; P28370; -.
DR BioGRID-ORCS; 6594; 3 hits in 694 CRISPR screens.
DR ChiTaRS; SMARCA1; human.
DR GeneWiki; SMARCA1; -.
DR GenomeRNAi; 6594; -.
DR Pharos; P28370; Tbio.
DR PRO; PR:P28370; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P28370; protein.
DR Bgee; ENSG00000102038; Expressed in adrenal tissue and 209 other tissues.
DR ExpressionAtlas; P28370; baseline and differential.
DR Genevisible; P28370; HS.
DR GO; GO:1904949; C:ATPase complex; IDA:ComplexPortal.
DR GO; GO:0090537; C:CERF complex; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0016589; C:NURF complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:MGI.
DR GO; GO:0036310; F:ATP-dependent DNA/DNA annealing activity; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; TAS:ProtInc.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0007420; P:brain development; IMP:HGNC-UCL.
DR GO; GO:0006338; P:chromatin remodeling; IDA:HGNC-UCL.
DR GO; GO:0030182; P:neuron differentiation; ISS:HGNC.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:HGNC-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:HGNC-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR CDD; cd18065; DEXHc_SMARCA1; 1.
DR CDD; cd00167; SANT; 1.
DR Gene3D; 1.10.1040.30; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR020838; DBINO.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR044755; SMARCA1_N.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF13892; DBINO; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; SSF101224; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; ATP-binding; Chromatin regulator;
KW Helicase; Hydrolase; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..1054
FT /note="Probable global transcription activator SNF2L1"
FT /id="PRO_0000074351"
FT DOMAIN 195..360
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 490..653
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 855..907
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 958..1022
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 25..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 819..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 311..314
FT /note="DEAH box"
FT COMPBIAS 827..849
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 208..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 954
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:12112843"
FT CROSSLNK 662
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 728
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 750
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 543..554
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15310751"
FT /id="VSP_020406"
FT VARIANT 656
FT /note="Q -> R (in dbSNP:rs1134838)"
FT /evidence="ECO:0000269|PubMed:1408766"
FT /id="VAR_001242"
FT VARIANT 978
FT /note="G -> V (found in a patient with Rett syndrome-like
FT phenotype; unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:26740508"
FT /id="VAR_079028"
FT MUTAGEN 214
FT /note="K->R: No effect on neurite outgrowth."
FT /evidence="ECO:0000269|PubMed:14609955"
SQ SEQUENCE 1054 AA; 122605 MW; D3FBFCA177F7D3C0 CRC64;
MEQDTAAVAA TVAAADATAT IVVIEDEQPG PSTSQEEGAA AAATEATAAT EKGEKKKEKN
VSSFQLKLAA KAPKSEKEMD PEYEEKMKAD RAKRFEFLLK QTELFAHFIQ PSAQKSPTSP
LNMKLGRPRI KKDEKQSLIS AGDYRHRRTE QEEDEELLSE SRKTSNVCIR FEVSPSYVKG
GPLRDYQIRG LNWLISLYEN GVNGILADEM GLGKTLQTIA LLGYLKHYRN IPGPHMVLVP
KSTLHNWMNE FKRWVPSLRV ICFVGDKDAR AAFIRDEMMP GEWDVCVTSY EMVIKEKSVF
KKFHWRYLVI DEAHRIKNEK SKLSEIVREF KSTNRLLLTG TPLQNNLHEL WALLNFLLPD
VFNSADDFDS WFDTKNCLGD QKLVERLHAV LKPFLLRRIK TDVEKSLPPK KEIKIYLGLS
KMQREWYTKI LMKDIDVLNS SGKMDKMRLL NILMQLRKCC NHPYLFDGAE PGPPYTTDEH
IVSNSGKMVV LDKLLAKLKE QGSRVLIFSQ MTRLLDILED YCMWRGYEYC RLDGQTPHEE
REDKFLEVEF LGQREAIEAF NAPNSSKFIF MLSTRAGGLG INLASADVVI LYDSDWNPQV
DLQAMDRAHR IGQKKPVRVF RLITDNTVEE RIVERAEIKL RLDSIVIQQG RLIDQQSNKL
AKEEMLQMIR HGATHVFASK ESELTDEDIT TILERGEKKT AEMNERLQKM GESSLRNFRM
DIEQSLYKFE GEDYREKQKL GMVEWIEPPK RERKANYAVD AYFREALRVS EPKIPKAPRP
PKQPNVQDFQ FFPPRLFELL EKEILYYRKT IGYKVPRNPD IPNPALAQRE EQKKIDGAEP
LTPEETEEKE KLLTQGFTNW TKRDFNQFIK ANEKYGRDDI DNIAREVEGK SPEEVMEYSA
VFWERCNELQ DIEKIMAQIE RGEARIQRRI SIKKALDAKI ARYKAPFHQL RIQYGTSKGK
NYTEEEDRFL ICMLHKMGFD RENVYEELRQ CVRNAPQFRF DWFIKSRTAM EFQRRCNTLI
SLIEKENMEI EERERAEKKK RATKTPMVKF SAFS
