SMCA5_HUMAN
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 03-AUG-2022, entry version 209.
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.- {ECO:0000269|PubMed:12972596, ECO:0000269|PubMed:28801535};
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 homologue of
RT 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP FUNCTION, IDENTIFICATION IN THE CHRAC ISWI CHROMATIN REMODELING COMPLEX,
RP AND INTERACTION WITH BAZ1A; CHRAC1 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 and two
RT 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, IDENTIFICATION IN THE WICH-5 ISWI CHROMATIN REMODELING COMPLEX,
RP AND INTERACTION 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 replication
RT foci.";
RL EMBO J. 21:2231-2241(2002).
RN [8]
RP FUNCTION, IDENTIFICATION IN THE CHRAC ISWI CHROMATIN REMODELING COMPLEX,
RP INTERACTION WITH BAZ1A; CHRAC1 AND POLE3, AND SUBCELLULAR LOCATION.
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 replication
RT through heterochromatin.";
RL Nat. Genet. 32:627-632(2002).
RN [9]
RP FUNCTION, IDENTIFICATION IN THE ACF-5 ISWI CHROMATIN REMODELING COMPLEX,
RP INTERACTION WITH BAZ1A; RAD21; HDAC2; RBBP4 AND CHD4, AND MUTAGENESIS OF
RP 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, CATALYTIC ACTIVITY, IDENTIFICATION IN THE RSF-5 ISWI CHROMATIN
RP REMODELING COMPLEX, INTERACTION WITH RSF-1, AND SUBCELLULAR LOCATION.
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 IDENTIFICATION IN THE CHRAC ISWI CHROMATIN REMODELING COMPLEX, AND
RP INTERACTION WITH BAZ1A.
RX PubMed=14759371; DOI=10.1016/s1097-2765(03)00523-9;
RA Kukimoto I., Elderkin S., Grimaldi M., Oelgeschlager T., Varga-Weisz P.D.;
RT "The histone-fold protein complex CHRAC-15/17 enhances nucleosome sliding
RT and assembly mediated by ACF.";
RL Mol. Cell 13:265-277(2004).
RN [13]
RP FUNCTION, INTERACTION WITH BAZ1B AND PCNA, AND SUBCELLULAR LOCATION.
RX PubMed=15543136; DOI=10.1038/ncb1196;
RA Poot R.A., Bozhenok L., van den Berg D.L.C., Steffensen S., Ferreira F.,
RA Grimaldi M., Gilbert N., Ferreira J., Varga-Weisz P.D.;
RT "The Williams syndrome transcription factor interacts with PCNA to target
RT chromatin remodelling by ISWI to replication foci.";
RL Nat. Cell Biol. 6:1236-1244(2004).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [15]
RP FUNCTION, IDENTIFICATION IN THE B-WICH COMPLEX, AND SUBCELLULAR LOCATION.
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 nuclear
RT proteins in transcription.";
RL J. Biol. Chem. 281:16264-16271(2006).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP 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., Li S.-J.,
RA 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 reductase
RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal
RT transduction.";
RL Mol. Cell. Proteomics 6:1952-1967(2007).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP 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 the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-116 AND SER-137, AND
RP 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 [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP 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 [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-440, AND IDENTIFICATION BY MASS
RP 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-113; SER-137 AND SER-825, AND
RP 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 [23]
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-137; SER-171 AND
RP SER-755, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [26]
RP FUNCTION, AND INTERACTION WITH SIRT6.
RX PubMed=23911928; DOI=10.1016/j.molcel.2013.06.018;
RA Toiber D., Erdel F., Bouazoune K., Silberman D.M., Zhong L., Mulligan P.,
RA Sebastian C., Cosentino C., Martinez-Pastor B., Giacosa S., D'Urso A.,
RA Naeaer A.M., Kingston R., Rippe K., Mostoslavsky R.;
RT "SIRT6 recruits SNF2H to DNA break sites, preventing genomic instability
RT through chromatin remodeling.";
RL Mol. Cell 51:454-468(2013).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, AND IDENTIFICATION BY
RP 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 [28]
RP INTERACTION WITH BEND3.
RX PubMed=26100909; DOI=10.1073/pnas.1424705112;
RA Khan A., Giri S., Wang Y., Chakraborty A., Ghosh A.K., Anantharaman A.,
RA Aggarwal V., Sathyan K.M., Ha T., Prasanth K.V., Prasanth S.G.;
RT "BEND3 represses rDNA transcription by stabilizing a NoRC component via
RT USP21 deubiquitinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:8338-8343(2015).
RN [29]
RP FUNCTION, IDENTIFICATION IN THE ACF-5 ISWI CHROMATIN REMODELING COMPLEX,
RP IDENTIFICATION IN THE WICH-5 ISWI CHROMATIN REMODELING COMPLEX,
RP IDENTIFICATION IN THE NORC-5 ISWI CHROMATIN REMODELING COMPLEX,
RP IDENTIFICATION IN THE BRF-5 ISWI CHROMATIN REMODELING COMPLEX,
RP IDENTIFICATION IN THE NURF-5 ISWI CHROMATIN REMODELING COMPLEX,
RP IDENTIFICATION IN THE CERF-5 ISWI CHROMATIN REMODELING COMPLEX,
RP IDENTIFICATION IN THE RSF-5 ISWI CHROMATIN REMODELING COMPLEX, AND
RP INTERACTION WITH BAZ1A; BAZ1B; BAZ2A; BAZ2B; BPFT; CECR2 AND RSF1.
RX PubMed=28801535; DOI=10.15252/embr.201744011;
RA Oppikofer M., Bai T., Gan Y., Haley B., Liu P., Sandoval W., Ciferri C.,
RA Cochran A.G.;
RT "Expansion of the ISWI chromatin remodeler family with new active
RT complexes.";
RL EMBO Rep. 18:1697-1706(2017).
RN [30]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-83; LYS-644; LYS-647; LYS-694;
RP LYS-722; LYS-735 AND LYS-966, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [31]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH JC VIRUS SMALL T ANTIGEN
RP (MICROBIAL INFECTION).
RX PubMed=33092197; DOI=10.3390/v12101192;
RA Saribas S., Safak M.;
RT "A Comprehensive Proteomics Analysis of the JC Virus (JCV) Large and Small
RT Tumor Antigen Interacting Proteins: Large T Primarily Targets the Host
RT Protein Complexes with V-ATPase and Ubiquitin Ligase Activities While Small
RT t Mostly Associates with Those Having Phosphatase and Chromatin-Remodeling
RT Functions.";
RL Viruses 12:0-0(2020).
CC -!- FUNCTION: Helicase that possesses intrinsic ATP-dependent nucleosome-
CC remodeling activity (PubMed:12972596, PubMed:28801535). Catalytic
CC subunit of ISWI chromatin-remodeling complexes, which form ordered
CC nucleosome arrays on chromatin and facilitate access to DNA during DNA-
CC templated processes such as DNA replication, transcription, and repair;
CC this may require intact histone H4 tails (PubMed:10880450,
CC PubMed:12434153, PubMed:28801535, PubMed:12198550, PubMed:12972596,
CC PubMed:23911928). Within the ISWI chromatin-remodeling complexes,
CC slides edge- and center-positioned histone octamers away from their
CC original location on the DNA template (PubMed:28801535). Catalytic
CC activity and histone octamer sliding propensity is regulated and
CC determined by components of the ISWI chromatin-remodeling complexes
CC (PubMed:28801535). The BAZ1A/ACF1-, BAZ1B/WSTF-, BAZ2A/TIP5- and BAZ2B-
CC containing ISWI chromatin-remodeling complexes regulate the spacing of
CC nucleosomes along the chromatin and have the ability to slide
CC mononucleosomes to the center of a DNA template in an ATP-dependent
CC manner (PubMed:14759371, PubMed:15543136, PubMed:28801535). The
CC CECR2- and RSF1-containing ISWI chromatin-remodeling complexes do not
CC have the ability to slide mononucleosomes to the center of a DNA
CC template (PubMed:28801535). Binds to core histones together with RSF1,
CC and is required for the assembly of regular nucleosome arrays by the
CC RSF-5 ISWI chromatin-remodeling complex (PubMed:12972596). Involved in
CC DNA replication and together with BAZ1A/ACF1 is required for
CC replication of pericentric heterochromatin in S-phase
CC (PubMed:12434153). Probably plays a role in repression of RNA
CC polymerase I dependent transcription of the rDNA locus, through the
CC recruitment of the SIN3/HDAC1 corepressor complex to the rDNA promoter
CC (By similarity). Essential component of the WICH-5 ISWI chromatin-
CC remodeling complex (also called the WICH complex), a chromatin-
CC remodeling complex that mobilizes nucleosomes and reconfigures
CC irregular chromatin to a regular nucleosomal array structure
CC (PubMed:11980720, PubMed:15543136). The WICH-5 ISWI chromatin-
CC remodeling complex regulates the transcription of various genes, has a
CC role in RNA polymerase I transcription (By similarity). Within the B-
CC WICH complex has a role in RNA polymerase III transcription
CC (PubMed:16603771). Mediates the histone H2AX phosphorylation at 'Tyr-
CC 142', and is involved in the maintenance of chromatin structures during
CC DNA replication processes (By similarity). Essential component of NoRC-
CC 5 ISWI chromatin-remodeling complex, a complex that mediates silencing
CC of a fraction of rDNA by recruiting histone-modifying enzymes and DNA
CC methyltransferases, leading to heterochromatin formation and
CC transcriptional silencing (By similarity).
CC {ECO:0000250|UniProtKB:Q91ZW3, 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:14759371, ECO:0000269|PubMed:15543136,
CC ECO:0000269|PubMed:16603771, ECO:0000269|PubMed:23911928,
CC ECO:0000269|PubMed:28801535}.
CC -!- SUBUNIT: Component of the ACF-5 ISWI chromatin-remodeling complex (also
CC called the ACF/WCRF complex) at least composed of SMARCA5/SNF2H and
CC BAZ1A/ACF1, which regulates the spacing of histone octamers on the DNA
CC template to facilitate access to DNA (PubMed:10880450, PubMed:12434153,
CC PubMed:12198550, PubMed:28801535). Within the complex interacts with
CC BAZ1A/ACF1; the interaction is direct and is required to slide
CC nucleosomes from end to center positions on a DNA template in an ATP-
CC dependent manner (PubMed:10880450, PubMed:12434153, PubMed:12198550,
CC PubMed:28801535). Component of the CHRAC ISWI chromatin-remodeling
CC complex at least composed of SMARCA5/SNF2H, BAZ1A/ACF1, CHRAC1 and
CC POLE3; the complex preferentially binds DNA through the CHRAC1-POLE3
CC heterodimer and possesses ATP-dependent nucleosome-remodeling activity
CC (PubMed:10880450, PubMed:12434153). Within the complex interacts with
CC BAZ1A/ACF1; the interaction is direct and promotes the interaction with
CC the POLE3-CHRAC1 heterodimer (PubMed:10880450, PubMed:12434153,
CC PubMed:14759371). Within the complex interacts with the POLE3-CHRAC1
CC heterodimer; the interaction is direct and enhances nucleosome sliding
CC activity by the SMARCA5/SNF2H and BAZ1A/ACF1 interaction
CC (PubMed:10880450, PubMed:14759371). Neither POLE3 nor CHRAC1 enhances
CC nucleosome sliding activity of the ACF-5 ISWI chromatin remodeling
CC complex (PubMed:14759371). Component of the WICH-5 ISWI chromatin-
CC remodeling complex (also called the WICH complex) at least composed of
CC SMARCA5/SNF2H and BAZ1B/WSTF, which regulates the spacing of histone
CC octamers on the DNA template to facilitate access to DNA
CC (PubMed:11980720, PubMed:28801535). Within the complex interacts with
CC BAZ1B/WSTF (PubMed:11980720, PubMed:15543136, PubMed:28801535).
CC Component of the NoRC-5 ISWI chromatin-remodeling complex (also called
CC the NoRC chromatin-remodeling complex) at least composed of
CC SMARCA5/SNF2H and BAZ2A/TIP5; the complex suppresses rDNA transcription
CC by a combination of nucleosome remodeling, histone deacetylation, and
CC DNA methylation (PubMed:28801535). Within the complex interacts with
CC BAZ2A/TIP5 (PubMed:28801535). Within the complex interacts with HDAC1
CC (By similarity). Component of the BRF-5 ISWI chromatin-remodeling
CC complex at least composed of SMARCA5/SNF2H and BAZ2B (PubMed:28801535).
CC Within the complex interacts with BAZ2B (PubMed:28801535). Component of
CC the NURF-5 ISWI chromatin-remodeling complex at least composed of
CC SMARCA5/SNF2H and BPTF (PubMed:28801535). Within the complex interacts
CC with BPFT (PubMed:28801535). Component of the CERF-5 ISWI chromatin-
CC remodeling complex at least composed of SMARCA5/SNF2H and CECR2
CC (PubMed:28801535). Within the complex interacts with CECR2
CC (PubMed:28801535). Component of the RSF-5 ISWI chromatin-remodeling
CC complex (also called the RSF complex) at least composed of
CC SMARCA5/SNF2H and RSF1 (PubMed:12972596, PubMed:28801535). Within the
CC complex interacts with RSF1 (PubMed:12972596, PubMed:28801535).
CC Interacts with the cohesin complex component RAD21; the interaction is
CC direct (PubMed:12198550). Interacts with the NuRD complex components
CC HDAC2, RBBP4 and CHD4; the interactions are direct (PubMed:12198550).
CC Interacts with PCNA (PubMed:15543136). Component of the B-WICH complex,
CC at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C,
CC ERCC6, MYBBP1A and DDX21 which positively regulates RNA polymerase III
CC transcription (PubMed:16603771). Interacts with MYO1C (By similarity).
CC Interacts with BEND3 (PubMed:26100909). Interacts with SIRT6; promoting
CC recruitment to DNA damage sites (PubMed:23911928).
CC {ECO:0000250|UniProtKB:Q91ZW3, 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:14759371, ECO:0000269|PubMed:15543136,
CC ECO:0000269|PubMed:16603771, ECO:0000269|PubMed:23911928,
CC ECO:0000269|PubMed:26100909, ECO:0000269|PubMed:28801535}.
CC -!- SUBUNIT: (Microbial infection) Interacts with JC virus small t antigen.
CC {ECO:0000269|PubMed:33092197}.
CC -!- INTERACTION:
CC O60264; Q9NRL2: BAZ1A; NbExp=3; IntAct=EBI-352588, EBI-927511;
CC O60264; Q9UIG0: BAZ1B; NbExp=7; IntAct=EBI-352588, EBI-927482;
CC O60264; P62805: H4C9; NbExp=2; IntAct=EBI-352588, EBI-302023;
CC O60264; Q96T23: RSF1; NbExp=5; IntAct=EBI-352588, EBI-926768;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624,
CC ECO:0000269|PubMed:12434153, ECO:0000269|PubMed:12972596,
CC ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:33092197}. Chromosome
CC {ECO:0000269|PubMed:12972596, ECO:0000269|PubMed:23911928}.
CC Note=Localizes to mitotic chromosomes (PubMed:12972596). Co-localizes
CC with RSF1 in the nucleus (PubMed:12972596). Co-localizes with PCNA at
CC replication foci during S phase (PubMed:15543136). Co-localizes with
CC BAZ1B/WSTF at replication foci during late-S phase (PubMed:15543136).
CC Recruited to DNA damage sites following interactiuon with SIRT6
CC (PubMed:23911928). {ECO:0000269|PubMed:12972596,
CC ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:23911928}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DEVELOPMENTAL STAGE: Overexpressed in CD34-positive erythrocyte
CC progenitor cells in acute myeloid leukemia. Down-regulation correlates
CC with hematologic remission following chemotherapy.
CC {ECO:0000269|PubMed:10914549}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000305}.
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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 AlphaFoldDB; O60264; -.
DR SMR; O60264; -.
DR BioGRID; 114045; 279.
DR ComplexPortal; CPX-1099; B-WICH chromatin remodelling complex.
DR ComplexPortal; CPX-432; NoRC complex.
DR ComplexPortal; CPX-434; ACF chromatin remodeling 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; 81.
DR MINT; O60264; -.
DR STRING; 9606.ENSP00000283131; -.
DR DrugBank; DB02670; 4-Deoxy-Alpha-D-Glucose.
DR DrugBank; DB02379; Beta-D-Glucose.
DR GlyGen; O60264; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60264; -.
DR MetOSite; O60264; -.
DR PhosphoSitePlus; O60264; -.
DR SwissPalm; O60264; -.
DR BioMuta; SMARCA5; -.
DR CPTAC; CPTAC-1636; -.
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 Antibodypedia; 1804; 396 antibodies from 37 providers.
DR DNASU; 8467; -.
DR Ensembl; ENST00000283131.4; ENSP00000283131.3; ENSG00000153147.6.
DR GeneID; 8467; -.
DR KEGG; hsa:8467; -.
DR MANE-Select; ENST00000283131.4; ENSP00000283131.3; NM_003601.4; NP_003592.3.
DR UCSC; uc003ijg.4; human.
DR CTD; 8467; -.
DR DisGeNET; 8467; -.
DR GeneCards; SMARCA5; -.
DR HGNC; HGNC:11101; SMARCA5.
DR HPA; ENSG00000153147; Low tissue specificity.
DR MalaCards; SMARCA5; -.
DR MIM; 603375; gene.
DR neXtProt; NX_O60264; -.
DR OpenTargets; ENSG00000153147; -.
DR Orphanet; 370334; Extraskeletal Ewing sarcoma.
DR PharmGKB; PA35951; -.
DR VEuPathDB; HostDB:ENSG00000153147; -.
DR eggNOG; KOG0385; Eukaryota.
DR GeneTree; ENSGT00940000156733; -.
DR HOGENOM; CLU_000315_0_2_1; -.
DR InParanoid; O60264; -.
DR OMA; GWINPGK; -.
DR OrthoDB; 61251at2759; -.
DR PhylomeDB; O60264; -.
DR TreeFam; TF300674; -.
DR PathwayCommons; O60264; -.
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 SignaLink; O60264; -.
DR SIGNOR; O60264; -.
DR BioGRID-ORCS; 8467; 431 hits in 1089 CRISPR screens.
DR ChiTaRS; SMARCA5; human.
DR GeneWiki; SMARCA5; -.
DR GenomeRNAi; 8467; -.
DR Pharos; O60264; Tbio.
DR PRO; PR:O60264; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O60264; protein.
DR Bgee; ENSG00000153147; Expressed in ventricular zone and 223 other tissues.
DR Genevisible; O60264; HS.
DR GO; GO:0016590; C:ACF complex; IPI:ComplexPortal.
DR GO; GO:0110016; C:B-WICH complex; IDA:ComplexPortal.
DR GO; GO:0008623; C:CHRAC; IC:ComplexPortal.
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:0090536; C:NoRC complex; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016589; C:NURF complex; IDA:UniProtKB.
DR GO; GO:0005721; C:pericentric heterochromatin; IC:ComplexPortal.
DR GO; GO:0031213; C:RSF complex; IPI:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR GO; GO:0090535; C:WICH complex; IDA:ComplexPortal.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0004386; F:helicase activity; TAS:ProtInc.
DR GO; GO:0140751; F:histone octamer slider activity; IDA:GO_Central.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0031497; P:chromatin assembly; IDA:ComplexPortal.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; IDA:UniProtKB.
DR GO; GO:1990164; P:histone H2A phosphorylation; IDA:ComplexPortal.
DR GO; GO:1905213; P:negative regulation of mitotic chromosome condensation; IDA:ComplexPortal.
DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; IEA:Ensembl.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:ComplexPortal.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IC:ComplexPortal.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; IEA:Ensembl.
DR GO; GO:0031062; P:positive regulation of histone methylation; IEA:Ensembl.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IDA:ComplexPortal.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IEA:Ensembl.
DR GO; GO:0044030; P:regulation of DNA methylation; IEA:Ensembl.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:ComplexPortal.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR CDD; cd00167; SANT; 2.
DR Gene3D; 1.10.1040.30; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; SSF101224; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Chromatin regulator; Chromosome;
KW Helicase; Host-virus interaction; Hydrolase; Isopeptide bond;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..1052
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily A member 5"
FT /id="PRO_0000074354"
FT DOMAIN 192..357
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 487..638
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 840..892
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 943..1007
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 308..311
FT /note="DEAH box"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 205..212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17693683,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 113
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 440
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 825
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 83
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 644
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 647
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 694
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 722
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 735
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 966
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MUTAGEN 211
FT /note="K->R: Abolishes ATP hydrolysis. Binds to chromatin
FT itself, but abolishes the chromatin binding of the cohesin
FT complex component RAD21."
FT /evidence="ECO:0000269|PubMed:12198550,
FT ECO:0007744|PubMed:28112733"
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
