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SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5 (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin A5) (EC 3.6.4.-) (Sucrose nonfermenting protein 2 homolog) (hSNF2H)

 SMCA5_HUMAN             Reviewed;        1052 AA.
O60264;
25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
01-AUG-1998, sequence version 1.
23-MAY-2018, entry version 180.
RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;
Short=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin A5;
EC=3.6.4.-;
AltName: Full=Sucrose nonfermenting protein 2 homolog;
Short=hSNF2H;
Name=SMARCA5; Synonyms=SNF2H, WCRF135;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Testis;
PubMed=9730600;
Aihara T., Miyoshi Y., Koyama K., Suzuki M., Takahashi E., Monden M.,
Nakamura Y.;
"Cloning and mapping of SMARCA5 encoding hSNF2H, a novel human
homologue of Drosophila ISWI.";
Cytogenet. Cell Genet. 81:191-193(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, AND IDENTIFICATION IN THE CHRAC COMPLEX WITH BAZ1A; CHRAC1
AND POLE3.
PubMed=10880450; DOI=10.1093/emboj/19.13.3377;
Poot R.A., Dellaire G., Huelsmann B.B., Grimaldi M.A., Corona D.F.V.,
Becker P.B., Bickmore W.A., Varga-Weisz P.D.;
"HuCHRAC, a human ISWI chromatin remodelling complex contains hACF1
and two novel histone-fold proteins.";
EMBO J. 19:3377-3387(2000).
[4]
DEVELOPMENTAL STAGE.
PubMed=10914549; DOI=10.1038/sj.leu.2401807;
Stopka T., Zakova D., Fuchs O., Kubrova O., Blafkova J., Jelinek J.,
Necas E., Zivny J.;
"Chromatin remodeling gene SMARCA5 is dysregulated in primitive
hematopoietic cells of acute leukemia.";
Leukemia 14:1247-1252(2000).
[5]
IDENTIFICATION IN THE ACF/WCRF COMPLEX WITH BAZ1A.
PubMed=10655480; DOI=10.1073/pnas.97.3.1038;
Bochar D.A., Savard J., Wang W., Lafleur D.W., Moore P., Cote J.,
Shiekhattar R.;
"A family of chromatin remodeling factors related to Williams syndrome
transcription factor.";
Proc. Natl. Acad. Sci. U.S.A. 97:1038-1043(2000).
[6]
CHARACTERIZATION.
PubMed=11435432; DOI=10.1074/jbc.M104163200;
Aalfs J.D., Narlikar G.J., Kingston R.E.;
"Functional differences between the human ATP-dependent nucleosome
remodeling proteins BRG1 and SNF2H.";
J. Biol. Chem. 276:34270-34278(2001).
[7]
FUNCTION, AND IDENTIFICATION IN THE WHICH COMPLEX WITH BAZ1B.
PubMed=11980720; DOI=10.1093/emboj/21.9.2231;
Bozhenok L., Wade P.A., Varga-Weisz P.;
"WSTF-ISWI chromatin remodeling complex targets heterochromatic
replication foci.";
EMBO J. 21:2231-2241(2002).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND IDENTIFICATION IN THE ACF/WCRF
COMPLEX WITH BAZ1A.
PubMed=12434153; DOI=10.1038/ng1046;
Collins N., Poot R.A., Kukimoto I., Garcia-Jimenez C., Dellaire G.,
Varga-Weisz P.D.;
"An ACF1-ISWI chromatin-remodeling complex is required for DNA
replication through heterochromatin.";
Nat. Genet. 32:627-632(2002).
[9]
FUNCTION, IDENTIFICATION IN THE SMARCA5/COHESIN/NURD COMPLEX, AND
MUTAGENESIS OF LYS-211.
PubMed=12198550; DOI=10.1038/nature01024;
Hakimi M.-A., Bochar D.A., Schmiesing J.A., Dong Y., Barak O.G.,
Speicher D.W., Yokomori K., Shiekhattar R.;
"A chromatin remodelling complex that loads cohesin onto human
chromosomes.";
Nature 418:994-998(2002).
[10]
FUNCTION, AND IDENTIFICATION IN THE RSF COMPLEX WITH HBXAP.
PubMed=12972596; DOI=10.1128/MCB.23.19.6759-6768.2003;
Loyola A., Huang J.-Y., LeRoy G., Hu S., Wang Y.-H., Donnelly R.J.,
Lane W.S., Lee S.-C., Reinberg D.;
"Functional analysis of the subunits of the chromatin assembly factor
RSF.";
Mol. Cell. Biol. 23:6759-6768(2003).
[11]
REVIEW, AND CHARACTERIZATION OF ISWI COMPLEXES.
PubMed=15284901; DOI=10.1139/o04-044;
Dirscherl S.S., Krebs J.E.;
"Functional diversity of ISWI complexes.";
Biochem. Cell Biol. 82:482-489(2004).
[12]
FUNCTION, AND INTERACTION WITH BAZ1B.
PubMed=15543136; DOI=10.1038/ncb1196;
Poot R.A., Bozhenok L., van den Berg D.L.C., Steffensen S.,
Ferreira F., Grimaldi M., Gilbert N., Ferreira J., Varga-Weisz P.D.;
"The Williams syndrome transcription factor interacts with PCNA to
target chromatin remodelling by ISWI to replication foci.";
Nat. Cell Biol. 6:1236-1244(2004).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[14]
FUNCTION, AND IDENTIFICATION IN THE B-WICH COMPLEX.
PubMed=16603771; DOI=10.1074/jbc.M600233200;
Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.;
"The WSTF-SNF2h chromatin remodeling complex interacts with several
nuclear proteins in transcription.";
J. Biol. Chem. 281:16264-16271(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,
Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling
network: indicating the involvement of ribonucleoside-diphosphate
reductase M2 subunit phosphorylation at residue serine 20 in canonical
Wnt signal transduction.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-116 AND SER-137,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-440, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113; SER-137 AND
SER-825, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-137; SER-171
AND SER-755, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
INTERACTION WITH BEND3.
PubMed=26100909; DOI=10.1073/pnas.1424705112;
Khan A., Giri S., Wang Y., Chakraborty A., Ghosh A.K.,
Anantharaman A., Aggarwal V., Sathyan K.M., Ha T., Prasanth K.V.,
Prasanth S.G.;
"BEND3 represses rDNA transcription by stabilizing a NoRC component
via USP21 deubiquitinase.";
Proc. Natl. Acad. Sci. U.S.A. 112:8338-8343(2015).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-83; LYS-644; LYS-647;
LYS-694; LYS-722; LYS-735 AND LYS-966, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Helicase that possesses intrinsic ATP-dependent
nucleosome-remodeling activity. Complexes containing SMARCA5 are
capable of forming ordered nucleosome arrays on chromatin; this
may require intact histone H4 tails. Also required for replication
of pericentric heterochromatin in S-phase specifically in
conjunction with BAZ1A. Probably plays a role in repression of
polI dependent transcription of the rDNA locus, through the
recruitment of the SIN3/HDAC1 corepressor complex to the rDNA
promoter. Essential component of the WICH complex, a chromatin
remodeling complex that mobilizes nucleosomes and reconfigures
irregular chromatin to a regular nucleosomal array structure. The
WICH complex regulates the transcription of various genes, has a
role in RNA polymerase I and RNA polymerase III transcription,
mediates the histone H2AX phosphorylation at 'Tyr-142', and is
involved in the maintenance of chromatin structures during DNA
replication processes. Essential component of the NoRC (nucleolar
remodeling complex) complex, a complex that mediates silencing of
a fraction of rDNA by recruiting histone-modifying enzymes and DNA
methyltransferases, leading to heterochromatin formation and
transcriptional silencing. {ECO:0000269|PubMed:10880450,
ECO:0000269|PubMed:11980720, ECO:0000269|PubMed:12198550,
ECO:0000269|PubMed:12434153, ECO:0000269|PubMed:12972596,
ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:16603771}.
-!- SUBUNIT: Catalytic subunit of the four known chromatin-remodeling
complexes: CHRAC, RSF, ACF/WCRF, and WICH. Each complex contains
subunits which may regulate the specificity or catalytic activity
of SMARCA5. ACF/WCRF contains BAZ1A; CHRAC contains BAZ1A, CHRAC1,
and POLE3; RSF contains RSF1; WICH contains BAZ1B/WSTF. SMARCA5 is
the catalytic subunit of the NoRC chromatin-remodeling complex,
which also contains BAZ2A/TIP5. The BAZ2A/TIP5 subunit of NoRC
also interacts with DNMT1, DNMT3B and HDAC1, which allows NoRC to
actively suppress rDNA transcription by a combination of
nucleosome remodeling, histone deacetylation, and DNA methylation.
Catalytic subunit of SMARCA5/cohesin/NuRD complexes. Component of
the B-WICH complex, at least composed of SMARCA5/SNF2H,
BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts
with MYO1C (By similarity). Interacts with BEND3.
{ECO:0000250|UniProtKB:Q91ZW3, ECO:0000269|PubMed:26100909}.
-!- INTERACTION:
Q9NRL2:BAZ1A; NbExp=3; IntAct=EBI-352588, EBI-927511;
Q9UIG0:BAZ1B; NbExp=6; IntAct=EBI-352588, EBI-927482;
P62805:HIST2H4B; NbExp=2; IntAct=EBI-352588, EBI-302023;
Q96T23:RSF1; NbExp=5; IntAct=EBI-352588, EBI-926768;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00624, ECO:0000269|PubMed:12434153}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
-!- DEVELOPMENTAL STAGE: Overexpressed in CD34-positive erythrocyte
progenitor cells in acute myeloid leukemia. Down-regulation
correlates with hematologic remission following chemotherapy.
{ECO:0000269|PubMed:10914549}.
-!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI
subfamily. {ECO:0000305}.
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EMBL; AB010882; BAA25173.1; -; mRNA.
EMBL; BC023144; AAH23144.1; -; mRNA.
CCDS; CCDS3761.1; -.
RefSeq; NP_003592.3; NM_003601.3.
UniGene; Hs.558422; -.
ProteinModelPortal; O60264; -.
SMR; O60264; -.
BioGrid; 114045; 138.
CORUM; O60264; -.
DIP; DIP-33204N; -.
IntAct; O60264; 57.
MINT; O60264; -.
STRING; 9606.ENSP00000283131; -.
DrugBank; DB02670; 4-Deoxy-Alpha-D-Glucose.
DrugBank; DB02379; Beta-D-Glucose.
iPTMnet; O60264; -.
PhosphoSitePlus; O60264; -.
SwissPalm; O60264; -.
BioMuta; SMARCA5; -.
EPD; O60264; -.
MaxQB; O60264; -.
PaxDb; O60264; -.
PeptideAtlas; O60264; -.
PRIDE; O60264; -.
DNASU; 8467; -.
Ensembl; ENST00000283131; ENSP00000283131; ENSG00000153147.
GeneID; 8467; -.
KEGG; hsa:8467; -.
UCSC; uc003ijg.4; human.
CTD; 8467; -.
DisGeNET; 8467; -.
EuPathDB; HostDB:ENSG00000153147.5; -.
GeneCards; SMARCA5; -.
HGNC; HGNC:11101; SMARCA5.
HPA; CAB005227; -.
HPA; HPA008751; -.
MalaCards; SMARCA5; -.
MIM; 603375; gene.
neXtProt; NX_O60264; -.
OpenTargets; ENSG00000153147; -.
Orphanet; 370334; Extraskeletal Ewing sarcoma.
PharmGKB; PA35951; -.
eggNOG; KOG0385; Eukaryota.
eggNOG; COG0553; LUCA.
GeneTree; ENSGT00900000140963; -.
HOGENOM; HOG000192862; -.
HOVERGEN; HBG056329; -.
InParanoid; O60264; -.
KO; K11654; -.
OMA; MAFTEWI; -.
OrthoDB; EOG091G01GJ; -.
PhylomeDB; O60264; -.
TreeFam; TF300674; -.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
ChiTaRS; SMARCA5; human.
GeneWiki; SMARCA5; -.
GenomeRNAi; 8467; -.
PRO; PR:O60264; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000153147; -.
CleanEx; HS_SMARCA5; -.
Genevisible; O60264; HS.
GO; GO:0005677; C:chromatin silencing complex; IEA:Ensembl.
GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016589; C:NURF complex; IDA:UniProtKB.
GO; GO:0031213; C:RSF complex; IPI:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0004386; F:helicase activity; TAS:ProtInc.
GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; IMP:BHF-UCL.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
GO; GO:0034080; P:CENP-A containing nucleosome assembly; TAS:Reactome.
GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
GO; GO:0000183; P:chromatin silencing at rDNA; IEA:Ensembl.
GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
GO; GO:0016584; P:nucleosome positioning; IDA:UniProtKB.
GO; GO:0045815; P:positive regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
CDD; cd00079; HELICc; 1.
CDD; cd00167; SANT; 2.
Gene3D; 1.10.1040.30; -; 1.
Gene3D; 3.40.50.10810; -; 1.
InterPro; IPR020838; DBINO.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR029915; ISWI.
InterPro; IPR015194; ISWI_HAND-dom.
InterPro; IPR036306; ISWI_HAND-dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR017884; SANT_dom.
InterPro; IPR015195; SLIDE.
InterPro; IPR038718; SNF2-like_sf.
InterPro; IPR000330; SNF2_N.
PANTHER; PTHR10799:SF887; PTHR10799:SF887; 1.
Pfam; PF13892; DBINO; 1.
Pfam; PF09110; HAND; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF09111; SLIDE; 1.
Pfam; PF00176; SNF2_N; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00717; SANT; 2.
SUPFAM; SSF101224; SSF101224; 1.
SUPFAM; SSF46689; SSF46689; 2.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51293; SANT; 1.
1: Evidence at protein level;
Acetylation; ATP-binding; Chromatin regulator; Complete proteome;
Helicase; Hydrolase; Isopeptide bond; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 1052 SWI/SNF-related matrix-associated actin-
dependent regulator of chromatin
subfamily A member 5.
/FTId=PRO_0000074354.
DOMAIN 192 357 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 487 638 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 840 892 SANT 1. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
DOMAIN 943 1007 SANT 2. {ECO:0000255|PROSITE-
ProRule:PRU00624}.
NP_BIND 205 212 ATP. {ECO:0000305}.
MOTIF 308 311 DEAH box.
COMPBIAS 7 13 Poly-Pro.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 66 66 Phosphoserine.
{ECO:0000244|PubMed:17693683,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:24275569}.
MOD_RES 113 113 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 137 137 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 171 171 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 440 440 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 755 755 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 825 825 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CROSSLNK 83 83 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 644 644 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 647 647 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 694 694 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 722 722 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 735 735 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 966 966 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
MUTAGEN 211 211 K->R: Loss of ATP hydrolysis and no
association of the SMARCA5/cohesin/NuRD
complex with chromatin.
{ECO:0000269|PubMed:12198550}.
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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