ID SMCA2_HUMAN Reviewed; 1590 AA.
AC P51531; B1ALG3; B1ALG4; D3DRH4; D3DRH5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 27-MAR-2024, entry version 232.
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 Short=hBRM;
DE AltName: Full=SNF2-alpha;
DE AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2 {ECO:0000312|HGNC:HGNC:11098};
GN Name=SMARCA2 {ECO:0000312|HGNC:HGNC:11098};
GN Synonyms=BAF190B, BRM, SNF2A, SNF2L2;
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 LONG).
RC TISSUE=Liver;
RX PubMed=8223438; DOI=10.1002/j.1460-2075.1993.tb06112.x;
RA Muchardt C., Yaniv M.;
RT "A human homologue of Saccharomyces cerevisiae SNF2/SWI2 and Drosophila brm
RT genes potentiates transcriptional activation by the glucocorticoid
RT receptor.";
RL EMBO J. 12:4279-4290(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RC TISSUE=Brain;
RX PubMed=8208605; DOI=10.1093/nar/22.10.1815;
RA Chiba H., Muramatsu M., Nomoto A., Kato H.;
RT "Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and Drosophila
RT brahma are transcriptional coactivators cooperating with the estrogen
RT receptor and the retinoic acid receptor.";
RL Nucleic Acids Res. 22:1815-1820(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, AND UBIQUITINATION.
RX PubMed=11259672; DOI=10.1073/pnas.071057398;
RA Biggs J.R., Yang J., Gullberg U., Muchardt C., Yaniv M., Kraft A.S.;
RT "The human brm protein is cleaved during apoptosis: the role of cathepsin
RT G.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3814-3819(2001).
RN [6]
RP INTERACTION WITH TOPBP1.
RX PubMed=15075294; DOI=10.1101/gad.1180204;
RA Liu K., Luo Y., Lin F.-T., Lin W.-C.;
RT "TopBP1 recruits Brg1/Brm to repress E2F1-induced apoptosis, a novel pRb-
RT independent and E2F1-specific control for cell survival.";
RL Genes Dev. 18:673-686(2004).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-329; SER-1568 AND SER-1572,
RP AND 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [10]
RP IDENTIFICATION IN THE BAF COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18765789; DOI=10.1101/gad.471408;
RA Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C.,
RA Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H.,
RA Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.;
RT "Regulation of muscle development by DPF3, a novel histone acetylation and
RT methylation reader of the BAF chromatin remodeling complex.";
RL Genes Dev. 22:2370-2384(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175; SER-1512; SER-1516 AND
RP SER-1528, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1568 AND SER-1572, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [13]
RP PROBABLE INVOLVEMENT IN SCZD, VARIANT GLU-1546, AND CHARACTERIZATION OF
RP VARIANT GLU-1546.
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1512 AND SER-1516, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-997 AND LYS-999, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [16]
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 [17]
RP INTERACTION WITH DEPF2.
RX PubMed=20460684; DOI=10.1074/jbc.m109.087783;
RA Tando T., Ishizaka A., Watanabe H., Ito T., Iida S., Haraguchi T.,
RA Mizutani T., Izumi T., Isobe T., Akiyama T., Inoue J., Iba H.;
RT "Requiem protein links RelB/p52 and the Brm-type SWI/SNF complex in a
RT noncanonical NF-kappaB pathway.";
RL J. Biol. Chem. 285:21951-21960(2010).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175; SER-329; SER-1568 AND
RP SER-1572, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
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 [20]
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 [21]
RP INVOLVEMENT IN NCBRS.
RX PubMed=22426308; DOI=10.1038/ng.2219;
RA Tsurusaki Y., Okamoto N., Ohashi H., Kosho T., Imai Y., Hibi-Ko Y.,
RA Kaname T., Naritomi K., Kawame H., Wakui K., Fukushima Y., Homma T.,
RA Kato M., Hiraki Y., Yamagata T., Yano S., Mizuno S., Sakazume S., Ishii T.,
RA Nagai T., Shiina M., Ogata K., Ohta T., Niikawa N., Miyatake S., Okada I.,
RA Mizuguchi T., Doi H., Saitsu H., Miyake N., Matsumoto N.;
RT "Mutations affecting components of the SWI/SNF complex cause Coffin-Siris
RT syndrome.";
RL Nat. Genet. 44:376-378(2012).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175; SER-329; SER-591;
RP SER-666 AND SER-1377, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172; SER-591; SER-1377 AND
RP SER-1572, AND 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 [24]
RP SUBCELLULAR LOCATION.
RX PubMed=25593309; DOI=10.1101/gad.252189.114;
RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W.,
RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.;
RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of
RT transcription-associated DNA damage that promotes homologous
RT recombination.";
RL Genes Dev. 29:197-211(2015).
RN [25]
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 [26]
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).
RN [27]
RP VARIANTS NCBRS LYS-852; GLN-855 AND ILE-880.
RX PubMed=23906836; DOI=10.1093/hmg/ddt366;
RA Wieczorek D., Boegershausen N., Beleggia F., Steiner-Haldenstaett S.,
RA Pohl E., Li Y., Milz E., Martin M., Thiele H., Altmueller J., Alanay Y.,
RA Kayserili H., Klein-Hitpass L., Boehringer S., Wollstein A., Albrecht B.,
RA Boduroglu K., Caliebe A., Chrzanowska K., Cogulu O., Cristofoli F.,
RA Czeschik J.C., Devriendt K., Dotti M.T., Elcioglu N., Gener B.,
RA Goecke T.O., Krajewska-Walasek M., Guillen-Navarro E., Hayek J., Houge G.,
RA Kilic E., Simsek-Kiper P.O., Lopez-Gonzalez V., Kuechler A., Lyonnet S.,
RA Mari F., Marozza A., Mathieu Dramard M., Mikat B., Morin G.,
RA Morice-Picard F., Ozkinay F., Rauch A., Renieri A., Tinschert S.,
RA Utine G.E., Vilain C., Vivarelli R., Zweier C., Nuernberg P., Rahmann S.,
RA Vermeesch J., Luedecke H.J., Zeschnigk M., Wollnik B.;
RT "A comprehensive molecular study on Coffin-Siris and Nicolaides-Baraitser
RT syndromes identifies a broad molecular and clinical spectrum converging on
RT altered chromatin remodeling.";
RL Hum. Mol. Genet. 22:5121-5135(2013).
RN [28]
RP STRUCTURE BY NMR OF 1377-1486.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the bromodomain of human SWI/SNF related matrix
RT associated actin dependent regulator of chromatin subfamily A member 2.";
RL Submitted (JAN-2007) to the PDB data bank.
RN [29]
RP VARIANTS NCBRS ALA-752; ARG-755; ILE-756; HIS-851; ASP-852; LYS-852;
RP ARG-854; ASN-854; GLY-855; ARG-881; VAL-881; LEU-883; TYR-939; SER-946;
RP PHE-946; CYS-1105; PRO-1105; PRO-1135; ARG-1146; VAL-1158; GLY-1159;
RP LEU-1159; GLN-1159; HIS-1162; PRO-1188; VAL-1201; CYS-1202; GLY-1205 AND
RP TRP-1213.
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 [30]
RP VARIANT NCBRS GLU-1241.
RX PubMed=27665729; DOI=10.1002/ajmg.a.37935;
RG EuroEPINOMICS RES myoclonic astatic epilepsy working group;
RA Tang S., Hughes E., Lascelles K., Simpson M.A., Pal D.K.;
RT "New SMARCA2 mutation in a patient with Nicolaides-Baraitser syndrome and
RT myoclonic astatic epilepsy.";
RL Am. J. Med. Genet. A 173:195-199(2017).
RN [31]
RP VARIANTS ASN-484; LYS-486; PRO-719; THR-932 AND GLU-1014, VARIANTS BIS
RP GLN-505; VAL-513; CYS-525; HIS-525; VAL-529; ASN-534; VAL-929; CYS-937;
RP HIS-937 AND LEU-937, AND INVOLVEMENT IN BIS.
RX PubMed=32694869; DOI=10.1038/s41436-020-0898-y;
RG Telethon Undiagnosed Diseases Program;
RA Cappuccio G., Sayou C., Tanno P.L., Tisserant E., Bruel A.L., Kennani S.E.,
RA Sa J., Low K.J., Dias C., Havlovicova M., Hancarova M., Eichler E.E.,
RA Devillard F., Moutton S., Van-Gils J., Dubourg C., Odent S., Gerard B.,
RA Piton A., Yamamoto T., Okamoto N., Firth H., Metcalfe K., Moh A.,
RA Chapman K.A., Aref-Eshghi E., Kerkhof J., Torella A., Nigro V., Perrin L.,
RA Piard J., Le Guyader G., Jouan T., Thauvin-Robinet C., Duffourd Y.,
RA George-Abraham J.K., Buchanan C.A., Williams D., Kini U., Wilson K.,
RA Sousa S.B., Hennekam R.C.M., Sadikovic B., Thevenon J., Govin J.,
RA Vitobello A., Brunetti-Pierri N.;
RT "De novo SMARCA2 variants clustered outside the helicase domain cause a new
RT recognizable syndrome with intellectual disability and blepharophimosis
RT distinct from Nicolaides-Baraitser syndrome.";
RL Genet. Med. 22:1838-1850(2020).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q6DIC0, 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 (PubMed:18765789). In
CC muscle cells, the BAF complex also contains DPF3. Component of neural
CC progenitors-specific chromatin remodeling complex (npBAF complex)
CC composed of 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 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. Interacts with PHF10/BAF45A (By
CC similarity). Interacts with CEBPB (when not
CC methylated)(PubMed:20111005). Interacts with TOPBP1 (PubMed:15075294).
CC Interacts with CEBPA (when phosphorylated) (PubMed:15107404). Interacts
CC with DPF2 (PubMed:20460684). Interacts with ERCC6 (PubMed:26030138).
CC {ECO:0000250|UniProtKB:Q6DIC0, ECO:0000269|PubMed:15075294,
CC ECO:0000269|PubMed:15107404, ECO:0000269|PubMed:18765789,
CC ECO:0000269|PubMed:20111005, ECO:0000269|PubMed:20460684,
CC ECO:0000269|PubMed:26030138, ECO:0000303|PubMed:22952240,
CC ECO:0000303|PubMed:26601204}.
CC -!- INTERACTION:
CC P51531; O14497: ARID1A; NbExp=5; IntAct=EBI-679562, EBI-637887;
CC P51531; Q8NFD5: ARID1B; NbExp=3; IntAct=EBI-679562, EBI-679921;
CC P51531; Q07666: KHDRBS1; NbExp=2; IntAct=EBI-679562, EBI-1364;
CC P51531; P51608: MECP2; NbExp=4; IntAct=EBI-679562, EBI-1189067;
CC P51531; Q9NRD5: PICK1; NbExp=2; IntAct=EBI-679562, EBI-79165;
CC P51531; O00560: SDCBP; NbExp=2; IntAct=EBI-679562, EBI-727004;
CC P51531; Q8TAQ2: SMARCC2; NbExp=2; IntAct=EBI-679562, EBI-357418;
CC P51531; P04326: tat; Xeno; NbExp=8; IntAct=EBI-679562, EBI-7333987;
CC P51531-2; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-10212306, EBI-10181188;
CC P51531-2; O00560: SDCBP; NbExp=3; IntAct=EBI-10212306, EBI-727004;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11259672,
CC ECO:0000269|PubMed:25593309}. Note=Localizes to sites of DNA damage.
CC {ECO:0000269|PubMed:25593309}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=P51531-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P51531-2; Sequence=VSP_000577;
CC -!- PTM: During apoptosis, cleaved by cathepsin CTSG to produce a 160 kDa
CC cleavage product which localizes to the cytosol.
CC {ECO:0000269|PubMed:11259672}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:11259672}.
CC -!- DISEASE: Nicolaides-Baraitser syndrome (NCBRS) [MIM:601358]: A rare
CC disorder characterized by severe intellectual disability with absent or
CC limited speech, seizures, short stature, sparse hair, typical facial
CC characteristics, brachydactyly, prominent finger joints and broad
CC distal phalanges. Some of the features are progressive with time.
CC {ECO:0000269|PubMed:22366787, ECO:0000269|PubMed:22426308,
CC ECO:0000269|PubMed:23906836, ECO:0000269|PubMed:27665729}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Blepharophimosis-impaired intellectual development syndrome
CC (BIS) [MIM:619293]: An autosomal dominant congenital syndrome
CC characterized by blepharophimosis, facial dysmorphism, global
CC development delay, delayed motor skills, impaired intellectual
CC development with poor or absent speech, and behavioral abnormalities in
CC some patients. Additional variable features include distal skeletal
CC anomalies, feeding difficulties with poor growth, respiratory
CC infections, and hypotonia with peripheral spasticity.
CC {ECO:0000269|PubMed:32694869}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Schizophrenia (SCZD) [MIM:181500]: A complex, multifactorial
CC psychotic disorder or group of disorders characterized by disturbances
CC in the form and content of thought (e.g. delusions, hallucinations), in
CC mood (e.g. inappropriate affect), in sense of self and relationship to
CC the external world (e.g. loss of ego boundaries, withdrawal), and in
CC behavior (e.g bizarre or apparently purposeless behavior). Although it
CC affects emotions, it is distinguished from mood disorders in which such
CC disturbances are primary. Similarly, there may be mild impairment of
CC cognitive function, and it is distinguished from the dementias in which
CC disturbed cognitive function is considered primary. Some patients
CC manifest schizophrenic as well as bipolar disorder symptoms and are
CC often given the diagnosis of schizoaffective disorder.
CC {ECO:0000269|PubMed:19363039}. Note=Disease susceptibility may be
CC associated with variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SWI/SNF related, matrix associated, actin dependent
CC regulator of chromatin, subfamily a, member 2 (SMARCA2); Note=Leiden
CC Open Variation Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/SMARCA2";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X72889; CAA51407.1; -; mRNA.
DR EMBL; D26155; BAA05142.1; -; mRNA.
DR EMBL; AL359076; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL138755; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58811.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58813.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58814.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58815.1; -; Genomic_DNA.
DR CCDS; CCDS34977.1; -. [P51531-1]
DR CCDS; CCDS34978.1; -. [P51531-2]
DR PIR; S39580; S39580.
DR PIR; S45251; S45251.
DR RefSeq; NP_001276325.1; NM_001289396.1. [P51531-1]
DR RefSeq; NP_001276326.1; NM_001289397.1.
DR RefSeq; NP_003061.3; NM_003070.4. [P51531-1]
DR RefSeq; NP_620614.2; NM_139045.3. [P51531-2]
DR PDB; 2DAT; NMR; -; A=1377-1504.
DR PDB; 4QY4; X-ray; 1.97 A; A/B/C=1373-1511.
DR PDB; 5DKC; X-ray; 1.60 A; A=1373-1511.
DR PDB; 5DKH; X-ray; 1.70 A; A/B/C=1373-1511.
DR PDB; 6EG2; X-ray; 2.98 A; A=705-955.
DR PDB; 6EG3; X-ray; 2.84 A; A=705-955.
DR PDB; 6HAX; X-ray; 2.35 A; A/E=1373-1511.
DR PDB; 6HAY; X-ray; 2.24 A; A/E=1373-1511.
DR PDB; 6HAZ; X-ray; 1.31 A; A/B=1373-1511.
DR PDB; 7S4E; X-ray; 2.25 A; A/E=1373-1511.
DR PDB; 7Z6L; X-ray; 2.24 A; A=1373-1511.
DR PDB; 7Z76; X-ray; 1.32 A; D=1373-1511.
DR PDB; 7Z77; X-ray; 1.97 A; D=1373-1511.
DR PDB; 7Z78; X-ray; 1.32 A; A/B/C=1373-1511.
DR PDBsum; 2DAT; -.
DR PDBsum; 4QY4; -.
DR PDBsum; 5DKC; -.
DR PDBsum; 5DKH; -.
DR PDBsum; 6EG2; -.
DR PDBsum; 6EG3; -.
DR PDBsum; 6HAX; -.
DR PDBsum; 6HAY; -.
DR PDBsum; 6HAZ; -.
DR PDBsum; 7S4E; -.
DR PDBsum; 7Z6L; -.
DR PDBsum; 7Z76; -.
DR PDBsum; 7Z77; -.
DR PDBsum; 7Z78; -.
DR AlphaFoldDB; P51531; -.
DR SASBDB; P51531; -.
DR SMR; P51531; -.
DR BioGRID; 112479; 327.
DR ComplexPortal; CPX-1164; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1194; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1201; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1202; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1203; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1205; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1207; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1210; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1213; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1217; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1220; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1223; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1225; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1227; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-4084; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4203; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4223; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4224; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA2 variant.
DR CORUM; P51531; -.
DR DIP; DIP-29005N; -.
DR IntAct; P51531; 140.
DR MINT; P51531; -.
DR STRING; 9606.ENSP00000371638; -.
DR BindingDB; P51531; -.
DR ChEMBL; CHEMBL2362979; -.
DR GuidetoPHARMACOLOGY; 2739; -.
DR GlyGen; P51531; 1 site.
DR iPTMnet; P51531; -.
DR MetOSite; P51531; -.
DR PhosphoSitePlus; P51531; -.
DR SwissPalm; P51531; -.
DR BioMuta; SMARCA2; -.
DR DMDM; 212276472; -.
DR EPD; P51531; -.
DR jPOST; P51531; -.
DR MassIVE; P51531; -.
DR MaxQB; P51531; -.
DR PaxDb; 9606-ENSP00000265773; -.
DR PeptideAtlas; P51531; -.
DR ProteomicsDB; 56325; -. [P51531-1]
DR ProteomicsDB; 56326; -. [P51531-2]
DR Pumba; P51531; -.
DR ABCD; P51531; 1 sequenced antibody.
DR Antibodypedia; 9105; 282 antibodies from 31 providers.
DR DNASU; 6595; -.
DR Ensembl; ENST00000349721.8; ENSP00000265773.5; ENSG00000080503.25. [P51531-1]
DR Ensembl; ENST00000357248.8; ENSP00000349788.2; ENSG00000080503.25. [P51531-2]
DR Ensembl; ENST00000382194.6; ENSP00000371629.1; ENSG00000080503.25. [P51531-2]
DR Ensembl; ENST00000382203.5; ENSP00000371638.1; ENSG00000080503.25. [P51531-1]
DR GeneID; 6595; -.
DR KEGG; hsa:6595; -.
DR MANE-Select; ENST00000349721.8; ENSP00000265773.5; NM_003070.5; NP_003061.3.
DR UCSC; uc003zhc.5; human. [P51531-1]
DR AGR; HGNC:11098; -.
DR CTD; 6595; -.
DR DisGeNET; 6595; -.
DR GeneCards; SMARCA2; -.
DR GeneReviews; SMARCA2; -.
DR HGNC; HGNC:11098; SMARCA2.
DR HPA; ENSG00000080503; Low tissue specificity.
DR MalaCards; SMARCA2; -.
DR MIM; 181500; phenotype.
DR MIM; 600014; gene.
DR MIM; 601358; phenotype.
DR MIM; 619293; phenotype.
DR neXtProt; NX_P51531; -.
DR OpenTargets; ENSG00000080503; -.
DR Orphanet; 3051; Nicolaides-Baraitser syndrome.
DR Orphanet; 637013; SMARCA2-related blepharophimosis-intellectual disability syndrome.
DR PharmGKB; PA35948; -.
DR VEuPathDB; HostDB:ENSG00000080503; -.
DR eggNOG; KOG0386; Eukaryota.
DR GeneTree; ENSGT00940000154821; -.
DR HOGENOM; CLU_000315_15_0_1; -.
DR InParanoid; P51531; -.
DR OMA; VNYISHT; -.
DR OrthoDB; 5482994at2759; -.
DR PhylomeDB; P51531; -.
DR TreeFam; TF300785; -.
DR PathwayCommons; P51531; -.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR SignaLink; P51531; -.
DR SIGNOR; P51531; -.
DR BioGRID-ORCS; 6595; 46 hits in 1169 CRISPR screens.
DR ChiTaRS; SMARCA2; human.
DR EvolutionaryTrace; P51531; -.
DR GeneWiki; SMARCA2; -.
DR GenomeRNAi; 6595; -.
DR Pharos; P51531; Tchem.
DR PRO; PR:P51531; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P51531; Protein.
DR Bgee; ENSG00000080503; Expressed in calcaneal tendon and 210 other cell types or tissues.
DR ExpressionAtlas; P51531; baseline and differential.
DR Genevisible; P51531; HS.
DR GO; GO:0140092; C:bBAF complex; NAS:ComplexPortal.
DR GO; GO:0035060; C:brahma complex; NAS:ComplexPortal.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0140288; C:GBAF complex; NAS:ComplexPortal.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
DR GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; TAS:ProtInc.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; TAS:BHF-UCL.
DR GO; GO:0045596; P:negative regulation of cell differentiation; NAS:ComplexPortal.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0045597; P:positive regulation of cell differentiation; NAS:ComplexPortal.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; NAS:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; NAS:ComplexPortal.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; NAS:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; NAS:ComplexPortal.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; NAS:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:ProtInc.
DR GO; GO:0070316; P:regulation of G0 to G1 transition; NAS:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; NAS:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; NAS:ComplexPortal.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; NAS:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR CDD; cd05516; Bromo_SNF2L2; 1.
DR CDD; cd18063; DEXHc_SMARCA2; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 3.40.5.120; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 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; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF541; GLOBAL TRANSCRIPTION ACTIVATOR SNF2L2-RELATED; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF07533; BRK; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF08880; QLQ; 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; BRK domain-like; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 3D-structure; Acetylation; Activator; Alternative splicing; ATP-binding;
KW Bromodomain; Disease variant; DNA-binding; Helicase; Hydrolase;
KW Hypotrichosis; Intellectual disability; Isopeptide bond; Neurogenesis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Schizophrenia; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1590
FT /note="Probable global transcription activator SNF2L2"
FT /id="PRO_0000074352"
FT DOMAIN 173..208
FT /note="QLQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01001"
FT DOMAIN 436..508
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 736..901
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1054..1216
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1419..1489
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..592
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1344..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1506..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 851..854
FT /note="DEGH box"
FT COMPBIAS 8..36
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..315
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 637..653
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1344..1373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1512..1529
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1530..1552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1571..1590
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 749..756
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 190
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6DIC0"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 604
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6DIC0"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 670
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT MOD_RES 997
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 999
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1512
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 1516
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 1528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231"
FT MOD_RES 1572
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 1302
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P51532"
FT VAR_SEQ 1400..1417
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000303|PubMed:8208605"
FT /id="VSP_000577"
FT VARIANT 484
FT /note="H -> N (found in a patient with non-specific
FT intellectual disability syndrome; likely pathogenic)"
FT /evidence="ECO:0000269|PubMed:32694869"
FT /id="VAR_085660"
FT VARIANT 486
FT /note="N -> K (found in a patient with non-specific
FT intellectual disability syndrome; likely pathogenic)"
FT /evidence="ECO:0000269|PubMed:32694869"
FT /id="VAR_085661"
FT VARIANT 505
FT /note="R -> Q (in BIS)"
FT /evidence="ECO:0000269|PubMed:32694869"
FT /id="VAR_085662"
FT VARIANT 513
FT /note="G -> V (in BIS)"
FT /evidence="ECO:0000269|PubMed:32694869"
FT /id="VAR_085663"
FT VARIANT 525
FT /note="R -> C (in BIS)"
FT /evidence="ECO:0000269|PubMed:32694869"
FT /id="VAR_085664"
FT VARIANT 525
FT /note="R -> H (in BIS)"
FT /evidence="ECO:0000269|PubMed:32694869"
FT /id="VAR_085665"
FT VARIANT 529
FT /note="L -> V (in BIS)"
FT /evidence="ECO:0000269|PubMed:32694869"
FT /id="VAR_085666"
FT VARIANT 534
FT /note="D -> N (in BIS)"
FT /evidence="ECO:0000269|PubMed:32694869"
FT /id="VAR_085667"
FT VARIANT 719
FT /note="L -> P (found in a patient with non-specific
FT intellectual disability syndrome; likely pathogenic)"
FT /evidence="ECO:0000269|PubMed:32694869"
FT /id="VAR_085668"
FT VARIANT 752
FT /note="G -> A (in NCBRS; dbSNP:rs281875198)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068180"
FT VARIANT 755
FT /note="K -> R (in NCBRS; dbSNP:rs281875203)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068181"
FT VARIANT 756
FT /note="T -> I (in NCBRS; dbSNP:rs281875191)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068182"
FT VARIANT 851
FT /note="D -> H (in NCBRS; dbSNP:rs281875206)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068183"
FT VARIANT 852
FT /note="E -> D (in NCBRS; dbSNP:rs281875193)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068184"
FT VARIANT 852
FT /note="E -> K (in NCBRS; dbSNP:rs281875199)"
FT /evidence="ECO:0000269|PubMed:22366787,
FT ECO:0000269|PubMed:23906836"
FT /id="VAR_068185"
FT VARIANT 854
FT /note="H -> N (in NCBRS)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068186"
FT VARIANT 854
FT /note="H -> R (in NCBRS; dbSNP:rs281875202)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068187"
FT VARIANT 855
FT /note="R -> G (in NCBRS; dbSNP:rs281875207)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068188"
FT VARIANT 855
FT /note="R -> Q (in NCBRS; dbSNP:rs1471482709)"
FT /evidence="ECO:0000269|PubMed:23906836"
FT /id="VAR_076936"
FT VARIANT 880
FT /note="T -> I (in NCBRS)"
FT /evidence="ECO:0000269|PubMed:23906836"
FT /id="VAR_076937"
FT VARIANT 881
FT /note="G -> R (in NCBRS; dbSNP:rs281875194)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068189"
FT VARIANT 881
FT /note="G -> V (in NCBRS; dbSNP:rs281875185)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068190"
FT VARIANT 883
FT /note="P -> L (in NCBRS; dbSNP:rs281875188)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068191"
FT VARIANT 929
FT /note="E -> V (in BIS)"
FT /evidence="ECO:0000269|PubMed:32694869"
FT /id="VAR_085669"
FT VARIANT 932
FT /note="I -> T (found in a patient with non-specific
FT intellectual disability syndrome; likely pathogenic)"
FT /evidence="ECO:0000269|PubMed:32694869"
FT /id="VAR_085670"
FT VARIANT 937
FT /note="R -> C (in BIS)"
FT /evidence="ECO:0000269|PubMed:32694869"
FT /id="VAR_085671"
FT VARIANT 937
FT /note="R -> H (in BIS)"
FT /evidence="ECO:0000269|PubMed:32694869"
FT /id="VAR_085672"
FT VARIANT 937
FT /note="R -> L (in BIS)"
FT /evidence="ECO:0000269|PubMed:32694869"
FT /id="VAR_085673"
FT VARIANT 939
FT /note="H -> Y (in NCBRS; dbSNP:rs281875190)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068192"
FT VARIANT 946
FT /note="L -> F (in NCBRS; dbSNP:rs281875205)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068193"
FT VARIANT 946
FT /note="L -> S (in NCBRS; dbSNP:rs281875200)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068194"
FT VARIANT 1014
FT /note="K -> E (found in a patient with non-specific
FT intellectual disability syndrome; likely pathogenic)"
FT /evidence="ECO:0000269|PubMed:32694869"
FT /id="VAR_085674"
FT VARIANT 1105
FT /note="R -> C (in NCBRS; dbSNP:rs281875192)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068195"
FT VARIANT 1105
FT /note="R -> P (in NCBRS; dbSNP:rs281875197)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068196"
FT VARIANT 1135
FT /note="L -> P (in NCBRS; dbSNP:rs281875195)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068197"
FT VARIANT 1146
FT /note="S -> R (in NCBRS; dbSNP:rs281875204)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068198"
FT VARIANT 1158
FT /note="D -> V (in NCBRS; dbSNP:rs281875240)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068199"
FT VARIANT 1159
FT /note="R -> G (in NCBRS; dbSNP:rs281875184)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068200"
FT VARIANT 1159
FT /note="R -> L (in NCBRS; dbSNP:rs281875187)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068201"
FT VARIANT 1159
FT /note="R -> Q (in NCBRS; dbSNP:rs281875187)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068202"
FT VARIANT 1162
FT /note="R -> H (in NCBRS; dbSNP:rs281875186)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068203"
FT VARIANT 1188
FT /note="A -> P (in NCBRS; dbSNP:rs281875196)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068204"
FT VARIANT 1201
FT /note="A -> V (in NCBRS; dbSNP:rs281875189)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068205"
FT VARIANT 1202
FT /note="G -> C (in NCBRS; dbSNP:rs281875239)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068206"
FT VARIANT 1205
FT /note="D -> G (in NCBRS; dbSNP:rs281875201)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068207"
FT VARIANT 1213
FT /note="R -> W (in NCBRS; dbSNP:rs281875238)"
FT /evidence="ECO:0000269|PubMed:22366787"
FT /id="VAR_068208"
FT VARIANT 1241
FT /note="Q -> E (in NCBRS)"
FT /evidence="ECO:0000269|PubMed:27665729"
FT /id="VAR_078815"
FT VARIANT 1416
FT /note="G -> A (in dbSNP:rs3793510)"
FT /id="VAR_049501"
FT VARIANT 1546
FT /note="D -> E (risk factor for schizophrenia in some
FT populations; results in reduced localization to the
FT nucleus; decreased interaction with chromatin;
FT dbSNP:rs2296212)"
FT /evidence="ECO:0000269|PubMed:19363039"
FT /id="VAR_049502"
FT CONFLICT 237..240
FT /note="Missing (in Ref. 1; CAA51407)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="Q -> E (in Ref. 2; BAA05142)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="G -> S (in Ref. 2; BAA05142)"
FT /evidence="ECO:0000305"
FT CONFLICT 711
FT /note="R -> W (in Ref. 1; CAA51407)"
FT /evidence="ECO:0000305"
FT CONFLICT 1139
FT /note="D -> H (in Ref. 2; BAA05142)"
FT /evidence="ECO:0000305"
FT CONFLICT 1394
FT /note="V -> C (in Ref. 1; CAA51407)"
FT /evidence="ECO:0000305"
FT CONFLICT 1400
FT /note="R -> S (in Ref. 1; CAA51407)"
FT /evidence="ECO:0000305"
FT HELIX 726..740
FT /evidence="ECO:0007829|PDB:6EG3"
FT STRAND 745..747
FT /evidence="ECO:0007829|PDB:6EG3"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:6EG3"
FT HELIX 755..768
FT /evidence="ECO:0007829|PDB:6EG3"
FT STRAND 776..779
FT /evidence="ECO:0007829|PDB:6EG3"
FT HELIX 782..795
FT /evidence="ECO:0007829|PDB:6EG3"
FT STRAND 797..799
FT /evidence="ECO:0007829|PDB:6EG2"
FT STRAND 801..804
FT /evidence="ECO:0007829|PDB:6EG3"
FT HELIX 808..812
FT /evidence="ECO:0007829|PDB:6EG3"
FT HELIX 815..820
FT /evidence="ECO:0007829|PDB:6EG3"
FT STRAND 824..828
FT /evidence="ECO:0007829|PDB:6EG3"
FT HELIX 830..835
FT /evidence="ECO:0007829|PDB:6EG3"
FT HELIX 837..840
FT /evidence="ECO:0007829|PDB:6EG3"
FT STRAND 846..855
FT /evidence="ECO:0007829|PDB:6EG3"
FT HELIX 859..870
FT /evidence="ECO:0007829|PDB:6EG3"
FT STRAND 874..882
FT /evidence="ECO:0007829|PDB:6EG3"
FT HELIX 888..898
FT /evidence="ECO:0007829|PDB:6EG3"
FT TURN 900..903
FT /evidence="ECO:0007829|PDB:6EG3"
FT HELIX 909..914
FT /evidence="ECO:0007829|PDB:6EG3"
FT HELIX 915..917
FT /evidence="ECO:0007829|PDB:6EG3"
FT HELIX 928..942
FT /evidence="ECO:0007829|PDB:6EG3"
FT HELIX 943..945
FT /evidence="ECO:0007829|PDB:6EG3"
FT HELIX 951..953
FT /evidence="ECO:0007829|PDB:6EG3"
FT HELIX 1381..1396
FT /evidence="ECO:0007829|PDB:6HAZ"
FT STRAND 1418..1420
FT /evidence="ECO:0007829|PDB:2DAT"
FT HELIX 1425..1427
FT /evidence="ECO:0007829|PDB:6HAZ"
FT TURN 1433..1435
FT /evidence="ECO:0007829|PDB:6HAZ"
FT HELIX 1437..1442
FT /evidence="ECO:0007829|PDB:6HAZ"
FT HELIX 1449..1457
FT /evidence="ECO:0007829|PDB:6HAZ"
FT HELIX 1464..1481
FT /evidence="ECO:0007829|PDB:6HAZ"
FT HELIX 1487..1507
FT /evidence="ECO:0007829|PDB:6HAZ"
SQ SEQUENCE 1590 AA; 181279 MW; CE69BBB287D35AB5 CRC64;
MSTPTDPGAM PHPGPSPGPG PSPGPILGPS PGPGPSPGSV HSMMGPSPGP PSVSHPMPTM
GSTDFPQEGM HQMHKPIDGI HDKGIVEDIH CGSMKGTGMR PPHPGMGPPQ SPMDQHSQGY
MSPHPSPLGA PEHVSSPMSG GGPTPPQMPP SQPGALIPGD PQAMSQPNRG PSPFSPVQLH
QLRAQILAYK MLARGQPLPE TLQLAVQGKR TLPGLQQQQQ QQQQQQQQQQ QQQQQQQQPQ
QQPPQPQTQQ QQQPALVNYN RPSGPGPELS GPSTPQKLPV PAPGGRPSPA PPAAAQPPAA
AVPGPSVPQP APGQPSPVLQ LQQKQSRISP IQKPQGLDPV EILQEREYRL QARIAHRIQE
LENLPGSLPP DLRTKATVEL KALRLLNFQR QLRQEVVACM RRDTTLETAL NSKAYKRSKR
QTLREARMTE KLEKQQKIEQ ERKRRQKHQE YLNSILQHAK DFKEYHRSVA GKIQKLSKAV
ATWHANTERE QKKETERIEK ERMRRLMAED EEGYRKLIDQ KKDRRLAYLL QQTDEYVANL
TNLVWEHKQA QAAKEKKKRR RRKKKAEENA EGGESALGPD GEPIDESSQM SDLPVKVTHT
ETGKVLFGPE APKASQLDAW LEMNPGYEVA PRSDSEESDS DYEEEDEEEE SSRQETEEKI
LLDPNSEEVS EKDAKQIIET AKQDVDDEYS MQYSARGSQS YYTVAHAISE RVEKQSALLI
NGTLKHYQLQ GLEWMVSLYN NNLNGILADE MGLGKTIQTI ALITYLMEHK RLNGPYLIIV
PLSTLSNWTY EFDKWAPSVV KISYKGTPAM RRSLVPQLRS GKFNVLLTTY EYIIKDKHIL
AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH YVAPRRILLT GTPLQNKLPE LWALLNFLLP
TIFKSCSTFE QWFNAPFAMT GERVDLNEEE TILIIRRLHK VLRPFLLRRL KKEVESQLPE
KVEYVIKCDM SALQKILYRH MQAKGILLTD GSEKDKKGKG GAKTLMNTIM QLRKICNHPY
MFQHIEESFA EHLGYSNGVI NGAELYRASG KFELLDRILP KLRATNHRVL LFCQMTSLMT
IMEDYFAFRN FLYLRLDGTT KSEDRAALLK KFNEPGSQYF IFLLSTRAGG LGLNLQAADT
VVIFDSDWNP HQDLQAQDRA HRIGQQNEVR VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ
AGMFDQKSSS HERRAFLQAI LEHEEENEEE DEVPDDETLN QMIARREEEF DLFMRMDMDR
RREDARNPKR KPRLMEEDEL PSWIIKDDAE VERLTCEEEE EKIFGRGSRQ RRDVDYSDAL
TEKQWLRAIE DGNLEEMEEE VRLKKRKRRR NVDKDPAKED VEKAKKRRGR PPAEKLSPNP
PKLTKQMNAI IDTVINYKDR CNVEKVPSNS QLEIEGNSSG RQLSEVFIQL PSRKELPEYY
ELIRKPVDFK KIKERIRNHK YRSLGDLEKD VMLLCHNAQT FNLEGSQIYE DSIVLQSVFK
SARQKIAKEE ESEDESNEEE EEEDEEESES EAKSVKVKIK LNKKDDKGRD KGKGKKRPNR
GKAKPVVSDF DSDEEQDERE QSEGSGTDDE
//
