SMCA5_MOUSE
ID SMCA5_MOUSE Reviewed; 1051 AA.
AC Q91ZW3; Q8C791; Q8CA22; Q8VDG1; Q925M9;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5;
DE EC=3.6.4.- {ECO:0000250|UniProtKB:O60264};
DE AltName: Full=Sucrose nonfermenting protein 2 homolog;
DE Short=mSnf2h;
GN Name=Smarca5; Synonyms=Snf2h;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Erythroleukemia;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11359880; DOI=10.1046/j.1471-4159.2001.00324.x;
RA Lazzaro M.A., Picketts D.J.;
RT "Cloning and characterization of the murine Imitation Switch (ISWI) genes:
RT differential expression patterns suggest distinct developmental roles for
RT Snf2h and Snf2l.";
RL J. Neurochem. 77:1145-1156(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 440-1007.
RC STRAIN=C57BL/6J; TISSUE=Heart, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN THE NORC-5 ISWI
RP CHROMATIN-REMODELING COMPLEX, AND INTERACTION WITH BAZ2A.
RX PubMed=11532953; DOI=10.1093/emboj/20.17.4892;
RA Strohner R., Nemeth A., Jansa P., Hofmann-Rohrer U., Santoro R.,
RA Laengst G., Grummt I.;
RT "NoRC -- a novel member of mammalian ISWI-containing chromatin remodeling
RT machines.";
RL EMBO J. 20:4892-4900(2001).
RN [6]
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 [7]
RP FUNCTION, IDENTIFICATION IN THE NORC COMPLEX, AND INTERACTION WITH BAZ2A
RP AND HDAC1.
RX PubMed=12198165; DOI=10.1093/emboj/cdf460;
RA Zhou Y., Santoro R., Grummt I.;
RT "The chromatin remodeling complex NoRC targets HDAC1 to the ribosomal gene
RT promoter and represses RNA polymerase I transcription.";
RL EMBO J. 21:4632-4640(2002).
RN [8]
RP FUNCTION.
RX PubMed=12368916; DOI=10.1038/ng1010;
RA Santoro R., Li J., Grummt I.;
RT "The nucleolar remodeling complex NoRC mediates heterochromatin formation
RT and silencing of ribosomal gene transcription.";
RL Nat. Genet. 32:393-396(2002).
RN [9]
RP FUNCTION.
RX PubMed=14617767; DOI=10.1073/pnas.2336105100;
RA Stopka T., Skoultchi A.I.;
RT "The ISWI ATPase Snf2h is required for early mouse development.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:14097-14102(2003).
RN [10]
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 [11]
RP INTERACTION WITH MYO1C.
RX PubMed=16514417; DOI=10.1038/sj.embor.7400657;
RA Percipalle P., Fomproix N., Cavellan E., Voit R., Reimer G., Krueger T.,
RA Thyberg J., Scheer U., Grummt I., Oestlund Farrants A.-K.O.;
RT "The chromatin remodelling complex WSTF-SNF2h interacts with nuclear myosin
RT 1 and has a role in RNA polymerase I transcription.";
RL EMBO Rep. 7:525-530(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [14]
RP FUNCTION, AND INTERACTION WITH BAZ1B.
RX PubMed=19092802; DOI=10.1038/nature07668;
RA Xiao A., Li H., Shechter D., Ahn S.H., Fabrizio L.A., Erdjument-Bromage H.,
RA Ishibe-Murakami S., Wang B., Tempst P., Hofmann K., Patel D.J.,
RA Elledge S.J., Allis C.D.;
RT "WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase
RT activity.";
RL Nature 457:57-62(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55; SER-65 AND THR-112, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-439, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Helicase that possesses intrinsic ATP-dependent nucleosome-
CC remodeling activity (By similarity). Catalytic subunit of ISWI
CC chromatin-remodeling complexes, which form ordered nucleosome arrays on
CC chromatin and facilitate access to DNA during DNA-templated processes
CC such as DNA replication, transcription, and repair; this may require
CC intact histone H4 tails (PubMed:11532953, PubMed:11980720,
CC PubMed:12198165). 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:11532953,
CC PubMed:11980720, PubMed:12198165). Catalytic activity and histone
CC octamer sliding propensity is regulated and determined by components of
CC the ISWI chromatin-remodeling complexes (By similarity). The
CC BAZ1A/ACF1-, BAZ1B/WSTF-, BAZ2A/TIP5- and BAZ2B-containing ISWI
CC chromatin-remodeling complexes regulate the spacing of nucleosomes
CC along the chromatin and have the ability to slide mononucleosomes to
CC the center of a DNA template in an ATP-dependent manner
CC (PubMed:11532953, PubMed:11980720, PubMed:12198165). The CECR2- and
CC RSF1-containing ISWI chromatin-remodeling complexes do not have the
CC ability to slide mononucleosomes to the center of a DNA template (By
CC similarity). Binds to core histones together with RSF1, and is required
CC for the assembly of regular nucleosome arrays by the RSF-5 ISWI
CC chromatin-remodeling complex (By similarity). Involved in DNA
CC replication and together with BAZ1A/ACF1 is required for replication of
CC pericentric heterochromatin in S-phase (By similarity). Probably plays
CC a role in repression of RNA polymerase I dependent transcription of the
CC rDNA locus, through the recruitment of the SIN3/HDAC1 corepressor
CC complex to the rDNA promoter (PubMed:12198165). The WICH-5 ISWI
CC chromatin-remodeling complex regulates the transcription of various
CC genes, has a role in RNA polymerase I and RNA polymerase III
CC transcription, mediates the histone H2AX phosphorylation at 'Tyr-142',
CC and is involved in the maintenance of chromatin structures during DNA
CC replication processes (PubMed:19092802). Essential component of the
CC NoRC-5 ISWI chromatin-remodeling complex, a complex that mediates
CC silencing of a fraction of rDNA by recruiting histone-modifying enzymes
CC and DNA methyltransferases, leading to heterochromatin formation and
CC transcriptional silencing (PubMed:11532953, PubMed:12198165,
CC PubMed:12368916). Required for embryonic development and
CC differentiation, and the proliferation of early blastocyst-derived stem
CC cells (PubMed:14617767). {ECO:0000250|UniProtKB:O60264,
CC ECO:0000269|PubMed:11532953, ECO:0000269|PubMed:11980720,
CC ECO:0000269|PubMed:12198165, ECO:0000269|PubMed:12368916,
CC ECO:0000269|PubMed:14617767, ECO:0000269|PubMed:19092802}.
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 (By similarity). Within the
CC complex interacts with BAZ1A/ACF1; the interaction is direct and is
CC required to slide nucleosomes from end to center positions on a DNA
CC template in an ATP-dependent manner (By similarity). Component of the
CC CHRAC ISWI chromatin-remodeling complex at least composed of
CC SMARCA5/SNF2H, BAZ1A/ACF1, CHRAC1 and POLE3; the complex preferentially
CC binds DNA through the CHRAC1-POLE3 heterodimer and possesses ATP-
CC dependent nucleosome-remodeling activity (By similarity). Within the
CC complex interacts with BAZ1A/ACF1; the interaction is direct and
CC promotes the interaction with the POLE3-CHRAC1 heterodimer (By
CC similarity). 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 (By
CC similarity). Neither POLE3 nor CHRAC1 enhances nucleosome sliding
CC activity of the ACF-5 ISWI chromatin remodeling complex (By
CC similarity). Component of the WICH-5 ISWI chromatin-remodeling complex
CC (also called the WICH complex) at least composed of SMARCA5/SNF2H and
CC BAZ1B/WSTF, which regulates the spacing of histone octamers on the DNA
CC template to facilitate access to DNA (PubMed:11980720). Within the
CC complex interacts with BAZ1B/WSTF (PubMed:19092802). Component of the
CC NoRC-5 ISWI chromatin-remodeling complex (also called the NoRC
CC chromatin-remodeling complex) at least composed of SMARCA5/SNF2H and
CC BAZ2A/TIP5; the complex suppresses rDNA transcription by a combination
CC of nucleosome remodeling, histone deacetylation, and DNA methylation
CC (PubMed:11532953, PubMed:12198165). Within the complex interacts with
CC BAZ2A/TIP5 (PubMed:12198165). Within the complex interacts with HDAC1
CC (PubMed:12198165). Component of the BRF-5 ISWI chromatin-remodeling
CC complex at least composed of SMARCA5/SNF2H and BAZ2B (By similarity).
CC Within the complex interacts with BAZ2B (By similarity). Component of
CC the NURF-5 ISWI chromatin-remodeling complex at least composed of
CC SMARCA5/SNF2H and BPTF (By similarity). Within the complex interacts
CC with BPFT (By similarity). Component of the CERF-5 ISWI chromatin-
CC remodeling complex at least composed of SMARCA5/SNF2H and CECR2 (By
CC similarity). Within the complex interacts with CECR2 (By similarity).
CC Component of the RSF-5 ISWI chromatin-remodeling complex (also called
CC the RSF complex) at least composed of SMARCA5/SNF2H and RSF1 (By
CC similarity). Within the complex interacts with RSF1 (By similarity).
CC Interacts with the cohesin complex component RAD21; the interaction is
CC direct (By similarity). Interacts with the NuRD complex components
CC HDAC2, RBBP4 and CHD4; the interactions are direct (By similarity).
CC Interacts with PCNA (By similarity). 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 (By similarity). Interacts with MYO1C (PubMed:16514417).
CC Interacts with BEND3 (By similarity). Interacts with SIRT6; promoting
CC recruitment to DNA damage sites (By similarity).
CC {ECO:0000250|UniProtKB:O60264, ECO:0000269|PubMed:11532953,
CC ECO:0000269|PubMed:11980720, ECO:0000269|PubMed:12198165,
CC ECO:0000269|PubMed:16514417, ECO:0000269|PubMed:19092802}.
CC -!- INTERACTION:
CC Q91ZW3; Q9Z277: Baz1b; NbExp=2; IntAct=EBI-927547, EBI-927576;
CC Q91ZW3; P54843: Maf; NbExp=2; IntAct=EBI-927547, EBI-3842521;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624,
CC ECO:0000269|PubMed:11532953}. Chromosome
CC {ECO:0000250|UniProtKB:O60264}. Note=Localizes to mitotic chromosomes.
CC Co-localizes with RSF1 in the nucleus. Co-localizes with PCNA at
CC replication foci during S phase. Co-localizes with BAZ1B/WSTF at
CC replication foci during late-S phase. Recruited to DNA damage sites
CC following interactiuon with SIRT6. {ECO:0000250|UniProtKB:O60264}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC -!- DEVELOPMENTAL STAGE: Expressed in CD34-positive erythrocyte progenitor
CC cells. Down-regulated upon differentiation.
CC {ECO:0000269|PubMed:10914549}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21922.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF375046; AAL25793.1; -; mRNA.
DR EMBL; AF325921; AAK52454.1; -; mRNA.
DR EMBL; BC021922; AAH21922.1; ALT_INIT; mRNA.
DR EMBL; BC053069; AAH53069.1; -; mRNA.
DR EMBL; AK039811; BAC30458.1; -; mRNA.
DR EMBL; AK052320; BAC34934.2; -; mRNA.
DR CCDS; CCDS22442.1; -.
DR RefSeq; NP_444354.2; NM_053124.2.
DR AlphaFoldDB; Q91ZW3; -.
DR SMR; Q91ZW3; -.
DR BioGRID; 220300; 28.
DR ComplexPortal; CPX-1133; B-WICH chromatin remodelling complex.
DR ComplexPortal; CPX-424; NoRC complex.
DR ComplexPortal; CPX-444; ACF chromatin remodeling complex.
DR ComplexPortal; CPX-463; RSF complex.
DR ComplexPortal; CPX-841; WICH chromatin remodelling complex.
DR ComplexPortal; CPX-858; CHRAC chromatin remodeling complex.
DR CORUM; Q91ZW3; -.
DR DIP; DIP-36073N; -.
DR IntAct; Q91ZW3; 19.
DR MINT; Q91ZW3; -.
DR STRING; 10090.ENSMUSP00000044361; -.
DR iPTMnet; Q91ZW3; -.
DR PhosphoSitePlus; Q91ZW3; -.
DR SwissPalm; Q91ZW3; -.
DR EPD; Q91ZW3; -.
DR jPOST; Q91ZW3; -.
DR MaxQB; Q91ZW3; -.
DR PaxDb; Q91ZW3; -.
DR PeptideAtlas; Q91ZW3; -.
DR PRIDE; Q91ZW3; -.
DR ProteomicsDB; 257265; -.
DR Antibodypedia; 1804; 396 antibodies from 37 providers.
DR DNASU; 93762; -.
DR Ensembl; ENSMUST00000043359; ENSMUSP00000044361; ENSMUSG00000031715.
DR GeneID; 93762; -.
DR KEGG; mmu:93762; -.
DR UCSC; uc009mja.2; mouse.
DR CTD; 8467; -.
DR MGI; MGI:1935129; Smarca5.
DR VEuPathDB; HostDB:ENSMUSG00000031715; -.
DR eggNOG; KOG0385; Eukaryota.
DR GeneTree; ENSGT00940000156733; -.
DR HOGENOM; CLU_000315_0_3_1; -.
DR InParanoid; Q91ZW3; -.
DR OMA; REINRWT; -.
DR OrthoDB; 61251at2759; -.
DR PhylomeDB; Q91ZW3; -.
DR TreeFam; TF300674; -.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR BioGRID-ORCS; 93762; 36 hits in 113 CRISPR screens.
DR ChiTaRS; Smarca5; mouse.
DR PRO; PR:Q91ZW3; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q91ZW3; protein.
DR Bgee; ENSMUSG00000031715; Expressed in embryonic post-anal tail and 294 other tissues.
DR Genevisible; Q91ZW3; MM.
DR GO; GO:0016590; C:ACF complex; ISO:MGI.
DR GO; GO:0110016; C:B-WICH complex; ISO:MGI.
DR GO; GO:0008623; C:CHRAC; IC:ComplexPortal.
DR GO; GO:0005677; C:chromatin silencing complex; IDA:UniProtKB.
DR GO; GO:0000793; C:condensed chromosome; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0031010; C:ISWI-type complex; IPI:MGI.
DR GO; GO:0090536; C:NoRC complex; IPI:ComplexPortal.
DR GO; GO:0043596; C:nuclear replication fork; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0016589; C:NURF complex; ISO:MGI.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:ComplexPortal.
DR GO; GO:0031213; C:RSF complex; ISO:MGI.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0090535; C:WICH complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0140751; F:histone octamer slider activity; ISO:MGI.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0031497; P:chromatin assembly; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IDA:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
DR GO; GO:0006352; P:DNA-templated transcription, initiation; ISO:MGI.
DR GO; GO:0031507; P:heterochromatin assembly; IDA:ComplexPortal.
DR GO; GO:1990164; P:histone H2A phosphorylation; ISO:MGI.
DR GO; GO:1905213; P:negative regulation of mitotic chromosome condensation; ISO:MGI.
DR GO; GO:0016479; P:negative regulation of transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0006334; P:nucleosome assembly; ISO:MGI.
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; IDA:ComplexPortal.
DR GO; GO:0031062; P:positive regulation of histone methylation; IDA:ComplexPortal.
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; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:MGI.
DR GO; GO:0000183; P:rDNA heterochromatin assembly; IDA:UniProtKB.
DR GO; GO:0044030; P:regulation of DNA methylation; IDA:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR GO; GO:2001020; P:regulation of response to DNA damage stimulus; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
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 Acetylation; ATP-binding; Chromatin regulator; Chromosome; Helicase;
KW Hydrolase; Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O60264"
FT CHAIN 2..1051
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily A member 5"
FT /id="PRO_0000074355"
FT DOMAIN 191..356
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 486..637
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 839..891
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 942..1006
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1051
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 307..310
FT /note="DEAH box"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..81
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1044
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 204..211
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O60264"
FT MOD_RES 55
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60264"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60264"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60264"
FT MOD_RES 439
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 754
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60264"
FT CROSSLNK 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60264"
FT CROSSLNK 643
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60264"
FT CROSSLNK 646
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60264"
FT CROSSLNK 693
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60264"
FT CROSSLNK 721
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60264"
FT CROSSLNK 734
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60264"
FT CROSSLNK 965
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:O60264"
FT CONFLICT 44..45
FT /note="AP -> GS (in Ref. 2; AAK52454)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="R -> C (in Ref. 2; AAK52454)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="S -> R (in Ref. 2; AAK52454)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="K -> R (in Ref. 2; AAK52454)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="K -> N (in Ref. 2; AAK52454)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="C -> S (in Ref. 2; AAK52454)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="G -> S (in Ref. 2; AAK52454)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1051 AA; 121627 MW; C6CB69E7FADE73FC CRC64;
MSSAVEPPPP PPPESAPSKP SAAGAGGSSS GNKGGPEGGA APAAPCAAGS GPADTEMEEV
FDHGSPGKQK EIQEPDPTYE EKMQTDRANR FEYLLKQTEL FAHFIQPAAQ KTPTSPLKMK
PGRPRVKKDE KQNLLSVGDY RHRRTEQEED EELLTESSKA TNVCTRFEDS PSYVKWGKLR
DYQVRGLNWL ISLYENGING ILADEMGLGK TLQTISLLGY MKHYRNIPGP HMVLVPKSTL
HNWMSEFKKW VPTLRSVCLI GDKEQRAAFV RDVLLPGEWD VCVTSYEMLI KEKSVFKKFN
WRYLVIDEAH RIKNEKSKLS EIVREFKTTN RLLLTGTPLQ NNLHELWSLL NFLLPDVFNS
ADDFDSWFDT NNCLGDQKLV ERLHMVLRPF LLRRIKADVE KSLPPKKEVK IYVGLSKMQR
EWYTRILMKD IDILNSAGKM DKMRLLNILM QLRKCCNHPY LFDGAEPGPP YTTDMHLVTN
SGKMVVLDKL LPKLKEQGSR VLIFSQMTRV LDILEDYCMW RNYEYCRLDG QTPHDERQDS
INAYNEPNST KFVFMLSTRA GGLGINLATA DVVILYDSDW NPQVDLQAMD RAHRIGQTKT
VRVFRFITDN TVEERIVERA EMKLRLDSIV IQQGRLVDQN LNKIGKDEML QMIRHGATHV
FASKESEITD EDIDGILERG AKKTAEMNEK LSKMGESSLR NFTMDTESSV YNFEGEDYRE
KQKIAFTEWI EPPKRERKAN YAVDAYFREA LRVSEPKAPK APRPPKQPNV QDFQFFPPRL
FELLEKEILY YRKTIGYKVP RSPDLPNAAQ AQKEEQLKID EAEPLNDEEL EEKEKLLTQG
FTNWNKRDFN QFIKANEKWG RDDIENIARE VEGKTPEEVI EYSAVFWERC NELQDIEKIM
AQIERGEARI QRRISIKKAL DTKIGRYKAP FHQLRISYGT NKGKNYTEEE DRFLICMLHK
LGFDKENVYD ELRQCIRNSP QFRFDWFLKS RTAMELQRRC NTLITLIERE NMELEEKEKA
EKKKRGPKPS TQKRKMDGAP DGRGRKKKLK L
