BAZ1A_HUMAN
ID BAZ1A_HUMAN Reviewed; 1556 AA.
AC Q9NRL2; Q9NZ15; Q9P065; Q9UIG1; Q9Y3V3;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Bromodomain adjacent to zinc finger domain protein 1A;
DE AltName: Full=ATP-dependent chromatin-remodeling protein;
DE AltName: Full=ATP-utilizing chromatin assembly and remodeling factor 1;
DE Short=hACF1;
DE AltName: Full=CHRAC subunit ACF1;
DE AltName: Full=Williams syndrome transcription factor-related chromatin-remodeling factor 180;
DE Short=WCRF180;
DE AltName: Full=hWALp1;
GN Name=BAZ1A; Synonyms=ACF1, WCRF180; ORFNames=HSPC317;
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] (ISOFORM 1), IDENTIFICATION BY MASS
RP SPECTROMETRY, IDENTIFICATION IN THE CHRAC COMPLEX, AND VARIANT LYS-1366.
RC TISSUE=Cervix carcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=10662543; DOI=10.1006/geno.1999.6071;
RA Jones M.H., Hamana N., Nezu J., Shimane M.;
RT "A novel family of bromodomain genes.";
RL Genomics 63:40-45(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-540 (ISOFORM 1).
RC TISSUE=Umbilical cord blood;
RA Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L.,
RA Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.;
RT "Human partial CDS from CD34+ stem cells.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 746-1556 (ISOFORM 1), AND VARIANT
RP LYS-1366.
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP IDENTIFICATION IN THE ACF-5 ISWI CHROMATIN REMODELING COMPLEX, AND
RP INTERACTION WITH SMARCA5.
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 [9]
RP FUNCTION, IDENTIFICATION IN THE CHRAC ISWI CHROMATIN REMODELING COMPLEX,
RP INTERACTION WITH SMARCA5; CHRAC1 AND POLE3, AND MUTAGENESIS OF
RP 667-ILE--LEU-933.
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 [10]
RP FUNCTION, IDENTIFICATION IN THE CHRAC ISWI CHROMATIN REMODELING COMPLEX,
RP INTERACTION WITH SMARCA5; POLE3 AND CHRAC1, AND MUTAGENESIS OF
RP 1-MET--ASN-128.
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1413 AND SER-1417, AND
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 [12]
RP FUNCTION.
RX PubMed=17099699; DOI=10.1038/nsmb1170;
RA Yang J.G., Madrid T.S., Sevastopoulos E., Narlikar G.J.;
RT "The chromatin-remodeling enzyme ACF is an ATP-dependent DNA length sensor
RT that regulates nucleosome spacing.";
RL Nat. Struct. Mol. Biol. 13:1078-1083(2006).
RN [13]
RP FUNCTION, AND INTERACTION WITH NCOR1.
RX PubMed=17519354; DOI=10.1210/me.2007-0095;
RA Ewing A.K., Attner M., Chakravarti D.;
RT "Novel regulatory role for human Acf1 in transcriptional repression of
RT vitamin D3 receptor-regulated genes.";
RL Mol. Endocrinol. 21:1791-1806(2007).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1402; SER-1413 AND SER-1417,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270; SER-702 AND SER-960, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270; SER-1371 AND SER-1402,
RP AND 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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-731; SER-1281; SER-1339 AND
RP SER-1413, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-731; SER-961; SER-1281;
RP SER-1320; SER-1339; SER-1353; SER-1363; SER-1413; SER-1417 AND THR-1547,
RP 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 [20]
RP FUNCTION, IDENTIFICATION IN THE ACF-1 ISWI CHROMATIN REMODELING COMPLEX,
RP IDENTIFICATION IN THE ACF-5 ISWI CHROMATIN REMODELING COMPLEX, AND
RP INTERACTION WITH SMARCA1 AND SMARCA5.
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 [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-952, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Regulatory subunit of the ATP-dependent ACF-1 and ACF-5 ISWI
CC chromatin remodeling complexes, which form ordered nucleosome arrays on
CC chromatin and slide edge- and center-positioned histone octamers away
CC from their original location on the DNA template to facilitate access
CC to DNA during DNA-templated processes such as DNA replication,
CC transcription, and repair (PubMed:17099699, PubMed:28801535). Both
CC complexes regulate the spacing of nucleosomes along the chromatin and
CC have the ability to slide mononucleosomes to the center of a DNA
CC template in an ATP-dependent manner (PubMed:14759371, PubMed:17099699,
CC PubMed:28801535). The ACF-1 ISWI chromatin remodeling complex has a
CC lower ATP hydrolysis rate than the ACF-5 ISWI chromatin remodeling
CC complex (PubMed:28801535). Has a role in sensing the length of DNA
CC which flank nucleosomes, which modulates the nucleosome spacing
CC activity of the ACF-5 ISWI chromatin remodeling complex
CC (PubMed:17099699). Involved in DNA replication and together with
CC SMARCA5/SNF2H is required for replication of pericentric
CC heterochromatin in S-phase (PubMed:12434153). May have a role in
CC nuclear receptor-mediated transcription repression (PubMed:17519354).
CC {ECO:0000269|PubMed:12434153, ECO:0000269|PubMed:14759371,
CC ECO:0000269|PubMed:17099699, ECO:0000269|PubMed:17519354,
CC ECO:0000269|PubMed:28801535}.
CC -!- SUBUNIT: Component of the ACF-1 ISWI chromatin remodeling complex at
CC least composed of SMARCA1 and BAZ1A, which regulates the spacing of
CC histone octamers on the DNA template to facilitate access to DNA
CC (PubMed:28801535). Within the ACF-1 ISWI chromatin remodeling complex
CC interacts with SMARCA1; the interaction is direct (PubMed:28801535).
CC Component of the ACF-5 ISWI chromatin remodeling complex (also called
CC the ACF complex) at least composed of BAZ1A and SMARCA5/SNF2H, which
CC regulates the spacing of histone octamers on the DNA template to
CC facilitate access to DNA (PubMed:10880450, PubMed:12198550,
CC PubMed:28801535). Within the ACF-5 ISWI chromatin remodeling complex
CC interacts with SMARCA5/SNF2H; the interaction is direct
CC (PubMed:10880450, PubMed:12198550, PubMed:28801535). 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 (PubMed:10880450,
CC PubMed:12434153, PubMed:14759371). Within the complex interacts (via N-
CC terminus) with POLE3-CHRAC1 heterodimer; the interaction is direct and
CC is required for the complex to preferentially bind to DNA
CC (PubMed:10880450, PubMed:12434153, PubMed:14759371). Within the complex
CC interacts with SMARCA5/SNF2H; the interaction is direct and promotes
CC the interaction with the POLE3-CHRAC1 heterodimer (PubMed:10880450,
CC PubMed:12434153, PubMed:14759371). Interacts with NCOR1 (via its RD1
CC domain); the interaction corepresses a number of NCOR1-regulated genes
CC (PubMed:17519354). {ECO:0000269|PubMed:10880450,
CC ECO:0000269|PubMed:12198550, ECO:0000269|PubMed:12434153,
CC ECO:0000269|PubMed:14759371, ECO:0000269|PubMed:17519354,
CC ECO:0000269|PubMed:28801535}.
CC -!- INTERACTION:
CC Q9NRL2; P42858: HTT; NbExp=4; IntAct=EBI-927511, EBI-466029;
CC Q9NRL2; O60264: SMARCA5; NbExp=3; IntAct=EBI-927511, EBI-352588;
CC Q9NRL2; O95365: ZBTB7A; NbExp=2; IntAct=EBI-927511, EBI-2795384;
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=May target the CHRAC complex to
CC heterochromatin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NRL2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NRL2-2; Sequence=VSP_000551;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis and at low or
CC undetectable levels in other tissues analyzed.
CC -!- MISCELLANEOUS: Stimulated by double-stranded DNA and nucleosomal DNA.
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF28995.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF213467; AAF70601.1; -; mRNA.
DR EMBL; AF221130; AAF32366.1; -; mRNA.
DR EMBL; AB032252; BAA89209.1; -; mRNA.
DR EMBL; AL121603; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355885; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW65900.1; -; Genomic_DNA.
DR EMBL; AF161435; AAF28995.1; ALT_FRAME; mRNA.
DR EMBL; AL050089; CAB43261.1; -; mRNA.
DR CCDS; CCDS41943.1; -. [Q9NRL2-2]
DR CCDS; CCDS9651.1; -. [Q9NRL2-1]
DR PIR; T08738; T08738.
DR RefSeq; NP_038476.2; NM_013448.2. [Q9NRL2-1]
DR RefSeq; NP_872589.1; NM_182648.1. [Q9NRL2-2]
DR PDB; 5UIY; X-ray; 1.69 A; A/B/C/D=1425-1538.
DR PDBsum; 5UIY; -.
DR AlphaFoldDB; Q9NRL2; -.
DR SMR; Q9NRL2; -.
DR BioGRID; 116347; 98.
DR ComplexPortal; CPX-434; ACF chromatin remodeling complex.
DR ComplexPortal; CPX-785; CHRAC chromatin remodeling complex.
DR CORUM; Q9NRL2; -.
DR DIP; DIP-36071N; -.
DR IntAct; Q9NRL2; 39.
DR MINT; Q9NRL2; -.
DR STRING; 9606.ENSP00000353458; -.
DR BindingDB; Q9NRL2; -.
DR ChEMBL; CHEMBL4105737; -.
DR iPTMnet; Q9NRL2; -.
DR MetOSite; Q9NRL2; -.
DR PhosphoSitePlus; Q9NRL2; -.
DR SwissPalm; Q9NRL2; -.
DR BioMuta; BAZ1A; -.
DR DMDM; 116241266; -.
DR EPD; Q9NRL2; -.
DR jPOST; Q9NRL2; -.
DR MassIVE; Q9NRL2; -.
DR MaxQB; Q9NRL2; -.
DR PaxDb; Q9NRL2; -.
DR PeptideAtlas; Q9NRL2; -.
DR PRIDE; Q9NRL2; -.
DR ProteomicsDB; 82383; -. [Q9NRL2-1]
DR ProteomicsDB; 82384; -. [Q9NRL2-2]
DR Antibodypedia; 113; 137 antibodies from 25 providers.
DR DNASU; 11177; -.
DR Ensembl; ENST00000358716.8; ENSP00000351555.4; ENSG00000198604.11. [Q9NRL2-2]
DR Ensembl; ENST00000360310.6; ENSP00000353458.1; ENSG00000198604.11. [Q9NRL2-1]
DR Ensembl; ENST00000382422.6; ENSP00000371859.2; ENSG00000198604.11. [Q9NRL2-1]
DR GeneID; 11177; -.
DR KEGG; hsa:11177; -.
DR MANE-Select; ENST00000360310.6; ENSP00000353458.1; NM_013448.3; NP_038476.2.
DR UCSC; uc001wsk.4; human. [Q9NRL2-1]
DR CTD; 11177; -.
DR DisGeNET; 11177; -.
DR GeneCards; BAZ1A; -.
DR HGNC; HGNC:960; BAZ1A.
DR HPA; ENSG00000198604; Tissue enhanced (bone).
DR MIM; 605680; gene.
DR neXtProt; NX_Q9NRL2; -.
DR OpenTargets; ENSG00000198604; -.
DR PharmGKB; PA25270; -.
DR VEuPathDB; HostDB:ENSG00000198604; -.
DR eggNOG; KOG1245; Eukaryota.
DR GeneTree; ENSGT00940000158135; -.
DR HOGENOM; CLU_002479_1_0_1; -.
DR InParanoid; Q9NRL2; -.
DR OMA; CEATGKD; -.
DR OrthoDB; 858930at2759; -.
DR PhylomeDB; Q9NRL2; -.
DR TreeFam; TF316326; -.
DR PathwayCommons; Q9NRL2; -.
DR SignaLink; Q9NRL2; -.
DR BioGRID-ORCS; 11177; 21 hits in 1101 CRISPR screens.
DR ChiTaRS; BAZ1A; human.
DR GenomeRNAi; 11177; -.
DR Pharos; Q9NRL2; Tbio.
DR PRO; PR:Q9NRL2; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9NRL2; protein.
DR Bgee; ENSG00000198604; Expressed in sperm and 194 other tissues.
DR ExpressionAtlas; Q9NRL2; baseline and differential.
DR Genevisible; Q9NRL2; HS.
DR GO; GO:0016590; C:ACF complex; IPI:ComplexPortal.
DR GO; GO:0008623; C:CHRAC; IDA:UniProtKB.
DR GO; GO:0000228; C:nuclear chromosome; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0005721; C:pericentric heterochromatin; IC:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006261; P:DNA-templated DNA replication; IDA:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IDA:ComplexPortal.
DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:ComplexPortal.
DR GO; GO:0031445; P:regulation of heterochromatin assembly; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:BHF-UCL.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd05504; Bromo_Acf1_like; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR037325; Acf1_Bromo.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR013136; WSTF_Acf1_Cbp146.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF10537; WAC_Acf1_DNA_bd; 1.
DR Pfam; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS51136; WAC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Bromodomain; Coiled coil;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1556
FT /note="Bromodomain adjacent to zinc finger domain protein
FT 1A"
FT /id="PRO_0000211167"
FT DOMAIN 22..128
FT /note="WAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00475"
FT DOMAIN 422..487
FT /note="DDT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00063"
FT DOMAIN 1446..1516
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT ZN_FING 1148..1198
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..133
FT /note="Required for interaction with NCOR1"
FT /evidence="ECO:0000269|PubMed:17519354"
FT REGION 1..128
FT /note="Required for interaction with the CHRAC1-POLE3
FT heterodimer. Required for interaction with the CHRAC1-POLE3
FT heterodimer"
FT /evidence="ECO:0000269|PubMed:14759371"
FT REGION 662..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..933
FT /note="Required for interaction with SMARCA5 and formation
FT of the CHRAC ISWI chromatin remodeling complex"
FT /evidence="ECO:0000269|PubMed:12434153"
FT REGION 841..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1202..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1399..1431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 306..397
FT /evidence="ECO:0000255"
FT COILED 634..709
FT /evidence="ECO:0000255"
FT COMPBIAS 662..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..966
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1202..1216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1255
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1274..1340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 702
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 731
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 960
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88379"
FT MOD_RES 961
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1339
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88379"
FT MOD_RES 1353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88379"
FT MOD_RES 1363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 1413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 1547
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 952
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 504..535
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10655480"
FT /id="VSP_000551"
FT VARIANT 344
FT /note="D -> E (in dbSNP:rs1133285)"
FT /id="VAR_028049"
FT VARIANT 1366
FT /note="N -> K (in dbSNP:rs1044140)"
FT /evidence="ECO:0000269|PubMed:10880450,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_048423"
FT MUTAGEN 1..128
FT /note="Missing: Abolishes interaction with the CHRAC1-POLE3
FT heterodimer."
FT /evidence="ECO:0000269|PubMed:14759371"
FT MUTAGEN 667..933
FT /note="Missing: Abolishes interaction with SMARCA5/SNF2H,
FT and abolishes the formation of the CHRAC ISWI chromatin
FT remodeling complex."
FT /evidence="ECO:0000269|PubMed:12434153"
FT CONFLICT 135
FT /note="R -> T (in Ref. 3; BAA89209)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="D -> E (in Ref. 3; BAA89209)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="K -> Q (in Ref. 6; AAF28995)"
FT /evidence="ECO:0000305"
FT CONFLICT 503..508
FT /note="KDLTEA -> QDFTEP (in Ref. 6; AAF28995)"
FT /evidence="ECO:0000305"
FT CONFLICT 525
FT /note="S -> P (in Ref. 6; AAF28995)"
FT /evidence="ECO:0000305"
FT CONFLICT 536..540
FT /note="GCSLK -> AALKF (in Ref. 6; AAF28995)"
FT /evidence="ECO:0000305"
FT CONFLICT 551
FT /note="E -> D (in Ref. 1; AAF70601)"
FT /evidence="ECO:0000305"
FT CONFLICT 730
FT /note="V -> F (in Ref. 3; BAA89209)"
FT /evidence="ECO:0000305"
FT CONFLICT 769
FT /note="P -> L (in Ref. 3; BAA89209)"
FT /evidence="ECO:0000305"
FT CONFLICT 1201
FT /note="S -> C (in Ref. 3; BAA89209)"
FT /evidence="ECO:0000305"
FT CONFLICT 1206
FT /note="S -> F (in Ref. 3; BAA89209)"
FT /evidence="ECO:0000305"
FT CONFLICT 1409
FT /note="R -> K (in Ref. 1; AAF70601 and 7; CAB43261)"
FT /evidence="ECO:0000305"
FT HELIX 1436..1447
FT /evidence="ECO:0007829|PDB:5UIY"
FT HELIX 1449..1454
FT /evidence="ECO:0007829|PDB:5UIY"
FT TURN 1460..1462
FT /evidence="ECO:0007829|PDB:5UIY"
FT HELIX 1466..1469
FT /evidence="ECO:0007829|PDB:5UIY"
FT HELIX 1476..1484
FT /evidence="ECO:0007829|PDB:5UIY"
FT HELIX 1491..1508
FT /evidence="ECO:0007829|PDB:5UIY"
FT HELIX 1514..1532
FT /evidence="ECO:0007829|PDB:5UIY"
SQ SEQUENCE 1556 AA; 178702 MW; 4D78B9A8ADBF715B CRC64;
MPLLHRKPFV RQKPPADLRP DEEVFYCKVT NEIFRHYDDF FERTILCNSL VWSCAVTGRP
GLTYQEALES EKKARQNLQS FPEPLIIPVL YLTSLTHRSR LHEICDDIFA YVKDRYFVEE
TVEVIRNNGA RLQCRILEVL PPSHQNGFAN GHVNSVDGET IIISDSDDSE TQSCSFQNGK
KKDAIDPLLF KYKVQPTKKE LHESAIVKAT QISRRKHLFS RDKLKLFLKQ HCEPQDGVIK
IKASSLSTYK IAEQDFSYFF PDDPPTFIFS PANRRRGRPP KRIHISQEDN VANKQTLASY
RSKATKERDK LLKQEEMKSL AFEKAKLKRE KADALEAKKK EKEDKEKKRE ELKKIVEEER
LKKKEEKERL KVEREKEREK LREEKRKYVE YLKQWSKPRE DMECDDLKEL PEPTPVKTRL
PPEIFGDALM VLEFLNAFGE LFDLQDEFPD GVTLEVLEEA LVGNDSEGPL CELLFFFLTA
IFQAIAEEEE EVAKEQLTDA DTKDLTEALD EDADPTKSAL SAVASLAAAW PQLHQGCSLK
SLDLDSCTLS EILRLHILAS GADVTSANAK YRYQKRGGFD ATDDACMELR LSNPSLVKKL
SSTSVYDLTP GEKMKILHAL CGKLLTLVST RDFIEDYVDI LRQAKQEFRE LKAEQHRKER
EEAAARIRKR KEEKLKEQEQ KMKEKQEKLK EDEQRNSTAD ISIGEEERED FDTSIESKDT
EQKELDQDMV TEDEDDPGSH KRGRRGKRGQ NGFKEFTRQE QINCVTREPL TADEEEALKQ
EHQRKEKELL EKIQSAIACT NIFPLGRDRM YRRYWIFPSI PGLFIEEDYS GLTEDMLLPR
PSSFQNNVQS QDPQVSTKTG EPLMSESTSN IDQGPRDHSV QLPKPVHKPN RWCFYSSCEQ
LDQLIEALNS RGHRESALKE TLLQEKSRIC AQLARFSEEK FHFSDKPQPD SKPTYSRGRS
SNAYDPSQMC AEKQLELRLR DFLLDIEDRI YQGTLGAIKV TDRHIWRSAL ESGRYELLSE
ENKENGIIKT VNEDVEEMEI DEQTKVIVKD RLLGIKTETP STVSTNASTP QSVSSVVHYL
AMALFQIEQG IERRFLKAPL DASDSGRSYK TVLDRWRESL LSSASLSQVF LHLSTLDRSV
IWSKSILNAR CKICRKKGDA ENMVLCDGCD RGHHTYCVRP KLKTVPEGDW FCPECRPKQR
SRRLSSRQRP SLESDEDVED SMGGEDDEVD GDEEEGQSEE EEYEVEQDED DSQEEEEVSL
PKRGRPQVRL PVKTRGKLSS SFSSRGQQQE PGRYPSRSQQ STPKTTVSSK TGRSLRKINS
APPTETKSLR IASRSTRHSH GPLQADVFVE LLSPRRKRRG RKSANNTPEN SPNFPNFRVI
ATKSSEQSRS VNIASKLSLQ ESESKRRCRK RQSPEPSPVT LGRRSSGRQG GVHELSAFEQ
LVVELVRHDD SWPFLKLVSK IQVPDYYDII KKPIALNIIR EKVNKCEYKL ASEFIDDIEL
MFSNCFEYNP RNTSEAKAGT RLQAFFHIQA QKLGLHVTPS NVDQVSTPPA AKKSRI
