GenomeNet

Database: UniProt
Entry: O60264
LinkDB: O60264
Original site: O60264 
ID   SMCA5_HUMAN             Reviewed;        1052 AA.
AC   O60264;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-OCT-2019, entry version 194.
DE   RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;
DE            Short=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin A5;
DE            EC=3.6.4.-;
DE   AltName: Full=Sucrose nonfermenting protein 2 homolog;
DE            Short=hSNF2H;
GN   Name=SMARCA5; Synonyms=SNF2H, WCRF135;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RX   PubMed=9730600; DOI=10.1159/000015027;
RA   Aihara T., Miyoshi Y., Koyama K., Suzuki M., Takahashi E., Monden M.,
RA   Nakamura Y.;
RT   "Cloning and mapping of SMARCA5 encoding hSNF2H, a novel human
RT   homologue of Drosophila ISWI.";
RL   Cytogenet. Cell Genet. 81:191-193(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lymph;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, AND IDENTIFICATION IN THE CHRAC COMPLEX WITH BAZ1A; CHRAC1
RP   AND POLE3.
RX   PubMed=10880450; DOI=10.1093/emboj/19.13.3377;
RA   Poot R.A., Dellaire G., Huelsmann B.B., Grimaldi M.A., Corona D.F.V.,
RA   Becker P.B., Bickmore W.A., Varga-Weisz P.D.;
RT   "HuCHRAC, a human ISWI chromatin remodelling complex contains hACF1
RT   and two novel histone-fold proteins.";
RL   EMBO J. 19:3377-3387(2000).
RN   [4]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=10914549; DOI=10.1038/sj.leu.2401807;
RA   Stopka T., Zakova D., Fuchs O., Kubrova O., Blafkova J., Jelinek J.,
RA   Necas E., Zivny J.;
RT   "Chromatin remodeling gene SMARCA5 is dysregulated in primitive
RT   hematopoietic cells of acute leukemia.";
RL   Leukemia 14:1247-1252(2000).
RN   [5]
RP   IDENTIFICATION IN THE ACF/WCRF COMPLEX WITH BAZ1A.
RX   PubMed=10655480; DOI=10.1073/pnas.97.3.1038;
RA   Bochar D.A., Savard J., Wang W., Lafleur D.W., Moore P., Cote J.,
RA   Shiekhattar R.;
RT   "A family of chromatin remodeling factors related to Williams syndrome
RT   transcription factor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:1038-1043(2000).
RN   [6]
RP   CHARACTERIZATION.
RX   PubMed=11435432; DOI=10.1074/jbc.m104163200;
RA   Aalfs J.D., Narlikar G.J., Kingston R.E.;
RT   "Functional differences between the human ATP-dependent nucleosome
RT   remodeling proteins BRG1 and SNF2H.";
RL   J. Biol. Chem. 276:34270-34278(2001).
RN   [7]
RP   FUNCTION, AND IDENTIFICATION IN THE WHICH COMPLEX WITH BAZ1B.
RX   PubMed=11980720; DOI=10.1093/emboj/21.9.2231;
RA   Bozhenok L., Wade P.A., Varga-Weisz P.;
RT   "WSTF-ISWI chromatin remodeling complex targets heterochromatic
RT   replication foci.";
RL   EMBO J. 21:2231-2241(2002).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE ACF/WCRF
RP   COMPLEX WITH BAZ1A.
RX   PubMed=12434153; DOI=10.1038/ng1046;
RA   Collins N., Poot R.A., Kukimoto I., Garcia-Jimenez C., Dellaire G.,
RA   Varga-Weisz P.D.;
RT   "An ACF1-ISWI chromatin-remodeling complex is required for DNA
RT   replication through heterochromatin.";
RL   Nat. Genet. 32:627-632(2002).
RN   [9]
RP   FUNCTION, IDENTIFICATION IN THE SMARCA5/COHESIN/NURD COMPLEX, AND
RP   MUTAGENESIS OF LYS-211.
RX   PubMed=12198550; DOI=10.1038/nature01024;
RA   Hakimi M.-A., Bochar D.A., Schmiesing J.A., Dong Y., Barak O.G.,
RA   Speicher D.W., Yokomori K., Shiekhattar R.;
RT   "A chromatin remodelling complex that loads cohesin onto human
RT   chromosomes.";
RL   Nature 418:994-998(2002).
RN   [10]
RP   FUNCTION, AND IDENTIFICATION IN THE RSF COMPLEX WITH HBXAP.
RX   PubMed=12972596; DOI=10.1128/mcb.23.19.6759-6768.2003;
RA   Loyola A., Huang J.-Y., LeRoy G., Hu S., Wang Y.-H., Donnelly R.J.,
RA   Lane W.S., Lee S.-C., Reinberg D.;
RT   "Functional analysis of the subunits of the chromatin assembly factor
RT   RSF.";
RL   Mol. Cell. Biol. 23:6759-6768(2003).
RN   [11]
RP   REVIEW, AND CHARACTERIZATION OF ISWI COMPLEXES.
RX   PubMed=15284901; DOI=10.1139/o04-044;
RA   Dirscherl S.S., Krebs J.E.;
RT   "Functional diversity of ISWI complexes.";
RL   Biochem. Cell Biol. 82:482-489(2004).
RN   [12]
RP   FUNCTION, AND INTERACTION WITH BAZ1B.
RX   PubMed=15543136; DOI=10.1038/ncb1196;
RA   Poot R.A., Bozhenok L., van den Berg D.L.C., Steffensen S.,
RA   Ferreira F., Grimaldi M., Gilbert N., Ferreira J., Varga-Weisz P.D.;
RT   "The Williams syndrome transcription factor interacts with PCNA to
RT   target chromatin remodelling by ISWI to replication foci.";
RL   Nat. Cell Biol. 6:1236-1244(2004).
RN   [13]
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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [14]
RP   FUNCTION, AND IDENTIFICATION IN THE B-WICH COMPLEX.
RX   PubMed=16603771; DOI=10.1074/jbc.m600233200;
RA   Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.;
RT   "The WSTF-SNF2h chromatin remodeling complex interacts with several
RT   nuclear proteins in transcription.";
RL   J. Biol. Chem. 281:16264-16271(2006).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200;
RA   Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
RA   Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
RT   "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
RT   network: indicating the involvement of ribonucleoside-diphosphate
RT   reductase M2 subunit phosphorylation at residue serine 20 in canonical
RT   Wnt signal transduction.";
RL   Mol. Cell. Proteomics 6:1952-1967(2007).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-116 AND SER-137,
RP   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   [18]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION
RP   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   [20]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-440, AND IDENTIFICATION BY
RP   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.,
RA   Walther T.C., 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   [21]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113; SER-137 AND
RP   SER-825, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [22]
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.,
RA   Buerckstuemmer T., 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   [23]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, AND IDENTIFICATION
RP   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.,
RA   Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA   Blagoev B.;
RT   "System-wide temporal characterization of the proteome and
RT   phosphoproteome of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [24]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-137; SER-171
RP   AND SER-755, 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   [25]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION
RP   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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [26]
RP   INTERACTION WITH BEND3.
RX   PubMed=26100909; DOI=10.1073/pnas.1424705112;
RA   Khan A., Giri S., Wang Y., Chakraborty A., Ghosh A.K.,
RA   Anantharaman A., Aggarwal V., Sathyan K.M., Ha T., Prasanth K.V.,
RA   Prasanth S.G.;
RT   "BEND3 represses rDNA transcription by stabilizing a NoRC component
RT   via USP21 deubiquitinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:8338-8343(2015).
RN   [27]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-83; LYS-644; LYS-647;
RP   LYS-694; LYS-722; LYS-735 AND LYS-966, AND IDENTIFICATION BY MASS
RP   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-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- FUNCTION: Helicase that possesses intrinsic ATP-dependent
CC       nucleosome-remodeling activity. Complexes containing SMARCA5 are
CC       capable of forming ordered nucleosome arrays on chromatin; this
CC       may require intact histone H4 tails. Also required for replication
CC       of pericentric heterochromatin in S-phase specifically in
CC       conjunction with BAZ1A. Probably plays a role in repression of
CC       polI dependent transcription of the rDNA locus, through the
CC       recruitment of the SIN3/HDAC1 corepressor complex to the rDNA
CC       promoter. Essential component of the WICH complex, a chromatin
CC       remodeling complex that mobilizes nucleosomes and reconfigures
CC       irregular chromatin to a regular nucleosomal array structure. The
CC       WICH complex regulates the transcription of various genes, has a
CC       role in RNA polymerase I and RNA polymerase III transcription,
CC       mediates the histone H2AX phosphorylation at 'Tyr-142', and is
CC       involved in the maintenance of chromatin structures during DNA
CC       replication processes. Essential component of the NoRC (nucleolar
CC       remodeling complex) complex, a complex that mediates silencing of
CC       a fraction of rDNA by recruiting histone-modifying enzymes and DNA
CC       methyltransferases, leading to heterochromatin formation and
CC       transcriptional silencing. {ECO:0000269|PubMed:10880450,
CC       ECO:0000269|PubMed:11980720, ECO:0000269|PubMed:12198550,
CC       ECO:0000269|PubMed:12434153, ECO:0000269|PubMed:12972596,
CC       ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:16603771}.
CC   -!- SUBUNIT: Catalytic subunit of the four known chromatin-remodeling
CC       complexes: CHRAC, RSF, ACF/WCRF, and WICH. Each complex contains
CC       subunits which may regulate the specificity or catalytic activity
CC       of SMARCA5. ACF/WCRF contains BAZ1A; CHRAC contains BAZ1A, CHRAC1,
CC       and POLE3; RSF contains RSF1; WICH contains BAZ1B/WSTF. SMARCA5 is
CC       the catalytic subunit of the NoRC chromatin-remodeling complex,
CC       which also contains BAZ2A/TIP5. The BAZ2A/TIP5 subunit of NoRC
CC       also interacts with DNMT1, DNMT3B and HDAC1, which allows NoRC to
CC       actively suppress rDNA transcription by a combination of
CC       nucleosome remodeling, histone deacetylation, and DNA methylation.
CC       Catalytic subunit of SMARCA5/cohesin/NuRD complexes. Component of
CC       the B-WICH complex, at least composed of SMARCA5/SNF2H,
CC       BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts
CC       with MYO1C (By similarity). Interacts with BEND3.
CC       {ECO:0000250|UniProtKB:Q91ZW3, ECO:0000269|PubMed:26100909}.
CC   -!- INTERACTION:
CC       Q9NRL2:BAZ1A; NbExp=3; IntAct=EBI-352588, EBI-927511;
CC       Q9UIG0:BAZ1B; NbExp=7; IntAct=EBI-352588, EBI-927482;
CC       P62805:HIST2H4B; NbExp=2; IntAct=EBI-352588, EBI-302023;
CC       Q96T23:RSF1; NbExp=5; IntAct=EBI-352588, EBI-926768;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00624, ECO:0000269|PubMed:12434153}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC   -!- DEVELOPMENTAL STAGE: Overexpressed in CD34-positive erythrocyte
CC       progenitor cells in acute myeloid leukemia. Down-regulation
CC       correlates with hematologic remission following chemotherapy.
CC       {ECO:0000269|PubMed:10914549}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI
CC       subfamily. {ECO:0000305}.
DR   EMBL; AB010882; BAA25173.1; -; mRNA.
DR   EMBL; BC023144; AAH23144.1; -; mRNA.
DR   CCDS; CCDS3761.1; -.
DR   RefSeq; NP_003592.3; NM_003601.3.
DR   PDB; 6NE3; EM; 3.90 A; W=166-634.
DR   PDBsum; 6NE3; -.
DR   SMR; O60264; -.
DR   BioGrid; 114045; 164.
DR   ComplexPortal; CPX-1099; B-WICH chromatin remodelling complex.
DR   ComplexPortal; CPX-432; NoRC complex.
DR   ComplexPortal; CPX-434; ACF complex.
DR   ComplexPortal; CPX-455; RSF complex.
DR   ComplexPortal; CPX-757; WICH chromatin remodelling complex.
DR   ComplexPortal; CPX-785; CHRAC chromatin remodeling complex.
DR   CORUM; O60264; -.
DR   DIP; DIP-33204N; -.
DR   IntAct; O60264; 72.
DR   MINT; O60264; -.
DR   STRING; 9606.ENSP00000283131; -.
DR   DrugBank; DB02670; 4-Deoxy-Alpha-D-Glucose.
DR   DrugBank; DB02379; Beta-D-Glucose.
DR   iPTMnet; O60264; -.
DR   PhosphoSitePlus; O60264; -.
DR   SwissPalm; O60264; -.
DR   BioMuta; SMARCA5; -.
DR   EPD; O60264; -.
DR   jPOST; O60264; -.
DR   MassIVE; O60264; -.
DR   MaxQB; O60264; -.
DR   PaxDb; O60264; -.
DR   PeptideAtlas; O60264; -.
DR   PRIDE; O60264; -.
DR   ProteomicsDB; 49297; -.
DR   DNASU; 8467; -.
DR   Ensembl; ENST00000283131; ENSP00000283131; ENSG00000153147.
DR   GeneID; 8467; -.
DR   KEGG; hsa:8467; -.
DR   UCSC; uc003ijg.4; human.
DR   CTD; 8467; -.
DR   DisGeNET; 8467; -.
DR   GeneCards; SMARCA5; -.
DR   HGNC; HGNC:11101; SMARCA5.
DR   HPA; CAB005227; -.
DR   HPA; HPA008751; -.
DR   MalaCards; SMARCA5; -.
DR   MIM; 603375; gene.
DR   neXtProt; NX_O60264; -.
DR   OpenTargets; ENSG00000153147; -.
DR   Orphanet; 370334; Extraskeletal Ewing sarcoma.
DR   PharmGKB; PA35951; -.
DR   eggNOG; KOG0385; Eukaryota.
DR   eggNOG; COG0553; LUCA.
DR   GeneTree; ENSGT00940000156733; -.
DR   HOGENOM; HOG000192862; -.
DR   InParanoid; O60264; -.
DR   KO; K11654; -.
DR   OMA; FGDSEVF; -.
DR   OrthoDB; 61251at2759; -.
DR   PhylomeDB; O60264; -.
DR   TreeFam; TF300674; -.
DR   Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR   Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR   Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR   ChiTaRS; SMARCA5; human.
DR   GeneWiki; SMARCA5; -.
DR   GenomeRNAi; 8467; -.
DR   Pharos; O60264; -.
DR   PRO; PR:O60264; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   Bgee; ENSG00000153147; Expressed in 244 organ(s), highest expression level in female gonad.
DR   Genevisible; O60264; HS.
DR   GO; GO:0005677; C:chromatin silencing complex; IEA:Ensembl.
DR   GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
DR   GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0016589; C:NURF complex; IDA:UniProtKB.
DR   GO; GO:0031213; C:RSF complex; IPI:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR   GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central.
DR   GO; GO:0004386; F:helicase activity; TAS:ProtInc.
DR   GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR   GO; GO:0043044; P:ATP-dependent chromatin remodeling; IMP:BHF-UCL.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR   GO; GO:0034080; P:CENP-A containing nucleosome assembly; TAS:Reactome.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR   GO; GO:0000183; P:chromatin silencing at rDNA; IEA:Ensembl.
DR   GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:UniProtKB.
DR   GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR   GO; GO:0016584; P:nucleosome positioning; IDA:UniProtKB.
DR   GO; GO:0045815; P:positive regulation of gene expression, epigenetic; TAS:Reactome.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR   CDD; cd00167; SANT; 2.
DR   Gene3D; 1.10.1040.30; -; 1.
DR   Gene3D; 3.40.50.10810; -; 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; IPR029915; ISWI_metazoa.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   InterPro; IPR015195; SLIDE.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799:SF819; PTHR10799:SF819; 1.
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_N; 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   3D-structure; Acetylation; ATP-binding; Chromatin regulator;
KW   Complete proteome; Helicase; Hydrolase; Isopeptide bond;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:19413330}.
FT   CHAIN         2   1052       SWI/SNF-related matrix-associated actin-
FT                                dependent regulator of chromatin
FT                                subfamily A member 5.
FT                                /FTId=PRO_0000074354.
FT   DOMAIN      192    357       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      487    638       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      840    892       SANT 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00624}.
FT   DOMAIN      943   1007       SANT 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00624}.
FT   NP_BIND     205    212       ATP. {ECO:0000305}.
FT   MOTIF       308    311       DEAH box.
FT   COMPBIAS      7     13       Poly-Pro.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000244|PubMed:19413330}.
FT   MOD_RES      66     66       Phosphoserine.
FT                                {ECO:0000244|PubMed:17693683,
FT                                ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:18691976,
FT                                ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:24275569}.
FT   MOD_RES     113    113       Phosphothreonine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES     116    116       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     137    137       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:23186163}.
FT   MOD_RES     171    171       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     440    440       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES     755    755       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     825    825       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231,
FT                                ECO:0000244|PubMed:21406692}.
FT   CROSSLNK     83     83       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    644    644       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    647    647       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    694    694       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    722    722       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    735    735       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    966    966       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   MUTAGEN     211    211       K->R: Loss of ATP hydrolysis and no
FT                                association of the SMARCA5/cohesin/NuRD
FT                                complex with chromatin.
FT                                {ECO:0000269|PubMed:12198550}.
SQ   SEQUENCE   1052 AA;  121905 MW;  6CC8CB25BAF7A876 CRC64;
     MSSAAEPPPP PPPESAPSKP AASIASGGSN SSNKGGPEGV AAQAVASAAS AGPADAEMEE
     IFDDASPGKQ KEIQEPDPTY EEKMQTDRAN RFEYLLKQTE LFAHFIQPAA QKTPTSPLKM
     KPGRPRIKKD EKQNLLSVGD YRHRRTEQEE DEELLTESSK ATNVCTRFED SPSYVKWGKL
     RDYQVRGLNW LISLYENGIN GILADEMGLG KTLQTISLLG YMKHYRNIPG PHMVLVPKST
     LHNWMSEFKR WVPTLRSVCL IGDKEQRAAF VRDVLLPGEW DVCVTSYEML IKEKSVFKKF
     NWRYLVIDEA HRIKNEKSKL SEIVREFKTT NRLLLTGTPL QNNLHELWSL LNFLLPDVFN
     SADDFDSWFD TNNCLGDQKL VERLHMVLRP FLLRRIKADV EKSLPPKKEV KIYVGLSKMQ
     REWYTRILMK DIDILNSAGK MDKMRLLNIL MQLRKCCNHP YLFDGAEPGP PYTTDMHLVT
     NSGKMVVLDK LLPKLKEQGS RVLIFSQMTR VLDILEDYCM WRNYEYCRLD GQTPHDERQD
     SINAYNEPNS TKFVFMLSTR AGGLGINLAT ADVVILYDSD WNPQVDLQAM DRAHRIGQTK
     TVRVFRFITD NTVEERIVER AEMKLRLDSI VIQQGRLVDQ NLNKIGKDEM LQMIRHGATH
     VFASKESEIT DEDIDGILER GAKKTAEMNE KLSKMGESSL RNFTMDTESS VYNFEGEDYR
     EKQKIAFTEW IEPPKRERKA NYAVDAYFRE ALRVSEPKAP KAPRPPKQPN VQDFQFFPPR
     LFELLEKEIL FYRKTIGYKV PRNPELPNAA QAQKEEQLKI DEAESLNDEE LEEKEKLLTQ
     GFTNWNKRDF NQFIKANEKW GRDDIENIAR EVEGKTPEEV IEYSAVFWER CNELQDIEKI
     MAQIERGEAR IQRRISIKKA LDTKIGRYKA PFHQLRISYG TNKGKNYTEE EDRFLICMLH
     KLGFDKENVY DELRQCIRNS PQFRFDWFLK SRTAMELQRR CNTLITLIER ENMELEEKEK
     AEKKKRGPKP STQKRKMDGA PDGRGRKKKL KL
//
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