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 27-MAR-2024, entry version 218. 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 INTERACTION WITH EPSTEIN-BARR VIRUS BZLF1 (MICROBIAL INFECTION). RX PubMed=30926617; DOI=10.26508/lsa.201800108; RA Schaeffner M., Mrozek-Gorska P., Buschle A., Woellmer A., Tagawa T., RA Cernilogar F.M., Schotta G., Krietenstein N., Lieleg C., Korber P., RA Hammerschmidt W.; RT "BZLF1 interacts with chromatin remodelers promoting escape from latent RT infections with EBV."; RL Life. Sci Alliance 2:0-0(2019). RN [32] 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 -!- SUBUNIT: (Microbial infection) Interacts with Epstein Barr virus (EBV) CC lytic switch protein BZLF1; this interaction participates to the CC activation of early lytic viral genes by BZLF1. CC {ECO:0000269|PubMed:30926617}. 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}. 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; 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 EMDB; EMD-9356; -. DR SMR; O60264; -. DR BioGRID; 114045; 408. DR ComplexPortal; CPX-1099; B-WICH chromatin remodelling complex. DR ComplexPortal; CPX-432; NoRC chromatin remodelling 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; 95. 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; 9606-ENSP00000283131; -. DR PeptideAtlas; O60264; -. DR ProteomicsDB; 49297; -. DR Pumba; O60264; -. DR Antibodypedia; 1804; 437 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 AGR; HGNC:11101; -. 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; HLWENCG; -. DR OrthoDB; 5482994at2759; -. 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; 464 hits in 1176 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 225 other cell types or tissues. 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; NAS: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; ISO:ComplexPortal. DR GO; GO:0005730; C:nucleolus; NAS: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; EXP: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:0006325; P:chromatin organization; IDA:ComplexPortal. DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB. DR GO; GO:0006974; P:DNA damage response; NAS:ComplexPortal. DR GO; GO:0006281; P:DNA repair; IDA:UniProtKB. DR GO; GO:0006352; P:DNA-templated transcription initiation; IDA:UniProtKB. DR GO; GO:0031507; P:heterochromatin formation; ISO: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; ISO:ComplexPortal. 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; NAS:ComplexPortal. DR GO; GO:0031065; P:positive regulation of histone deacetylation; ISO:ComplexPortal. DR GO; GO:0031062; P:positive regulation of histone methylation; ISO:ComplexPortal. DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; NAS: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 formation; ISO:ComplexPortal. DR GO; GO:0044030; P:regulation of DNA methylation; ISO:ComplexPortal. DR GO; GO:0006275; P:regulation of DNA replication; IMP:ComplexPortal. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc. DR CDD; cd18064; DEXHc_SMARCA5; 1. DR CDD; cd00167; SANT; 1. DR CDD; cd18793; SF2_C_SNF; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 2. DR Gene3D; 1.20.5.1190; iswi atpase; 1. DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 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; 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; IPR049730; SNF2/RAD54-like_C. DR InterPro; IPR000330; SNF2_N. DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1. DR PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 1; 1. DR Pfam; PF09110; HAND; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF09111; SLIDE; 1. DR Pfam; PF00176; SNF2-rel_dom; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00717; SANT; 2. DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1. DR SUPFAM; SSF46689; Homeodomain-like; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51293; SANT; 1. DR Genevisible; O60264; HS. 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 //