CHD1_YEAST
ID CHD1_YEAST Reviewed; 1468 AA.
AC P32657; D3DM72;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Chromo domain-containing protein 1;
DE EC=3.6.4.-;
DE AltName: Full=ATP-dependent helicase CHD1;
GN Name=CHD1; OrderedLocusNames=YER164W; ORFNames=SYGP-ORF4;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
RX PubMed=10026213; DOI=10.1074/jbc.274.9.5895;
RA Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.;
RT "Expanded lysine acetylation specificity of Gcn5 in native complexes.";
RL J. Biol. Chem. 274:5895-5900(1999).
RN [4]
RP FUNCTION.
RX PubMed=10811623; DOI=10.1093/emboj/19.10.2323;
RA Tran H.G., Steger D.J., Iyer V.R., Johnson A.D.;
RT "The chromo domain protein chd1p from budding yeast is an ATP-dependent
RT chromatin-modifying factor.";
RL EMBO J. 19:2323-2331(2000).
RN [5]
RP INTERACTION WITH POB3 AND SPT16.
RX PubMed=12242279; DOI=10.1128/mcb.22.20.6979-6992.2002;
RA Krogan N.J., Kim M., Ahn S.H., Zhong G., Kobor M.S., Cagney G., Emili A.,
RA Shilatifard A., Buratowski S., Greenblatt J.F.;
RT "RNA polymerase II elongation factors of Saccharomyces cerevisiae: a
RT targeted proteomics approach.";
RL Mol. Cell. Biol. 22:6979-6992(2002).
RN [6]
RP IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=12446794; DOI=10.1128/mcb.22.24.8774-8786.2002;
RA Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L.,
RA Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.;
RT "The novel SLIK histone acetyltransferase complex functions in the yeast
RT retrograde response pathway.";
RL Mol. Cell. Biol. 22:8774-8786(2002).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RTF1 AND SPT5.
RX PubMed=12682017; DOI=10.1093/emboj/cdg179;
RA Simic R., Lindstrom D.L., Tran H.G., Roinick K.L., Costa P.J.,
RA Johnson A.D., Hartzog G.A., Arndt K.M.;
RT "Chromatin remodeling protein Chd1 interacts with transcription elongation
RT factors and localizes to transcribed genes.";
RL EMBO J. 22:1846-1856(2003).
RN [8]
RP FUNCTION.
RX PubMed=14585955; DOI=10.1128/mcb.23.22.7937-7946.2003;
RA Robinson K.M., Schultz M.C.;
RT "Replication-independent assembly of nucleosome arrays in a novel yeast
RT chromatin reconstitution system involves antisilencing factor Asf1p and
RT chromodomain protein Chd1p.";
RL Mol. Cell. Biol. 23:7937-7946(2003).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1144, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=SUB592;
RX PubMed=12872131; DOI=10.1038/nbt849;
RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G.,
RA Roelofs J., Finley D., Gygi S.P.;
RT "A proteomics approach to understanding protein ubiquitination.";
RL Nat. Biotechnol. 21:921-926(2003).
RN [11]
RP IDENTIFICATION IN THE SAGA COMPLEX, IDENTIFICATION IN THE SLIK COMPLEX,
RP FUNCTION IN SUBSTRATE RECOGNITION OF THE SLIK COMPLEX, INTERACTION WITH
RP HISTONE H3, AND MUTAGENESIS OF GLU-220; HIS-222; LEU-314 AND TYR-316.
RX PubMed=15647753; DOI=10.1038/nature03242;
RA Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.;
RT "Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-
RT dependent acetylation.";
RL Nature 433:434-438(2005).
RN [12]
RP FUNCTION.
RX PubMed=16606615; DOI=10.1074/jbc.m600682200;
RA Stockdale C., Flaus A., Ferreira H., Owen-Hughes T.;
RT "Analysis of nucleosome repositioning by yeast ISWI and Chd1 chromatin
RT remodeling complexes.";
RL J. Biol. Chem. 281:16279-16288(2006).
RN [13]
RP FUNCTION.
RX PubMed=16468993; DOI=10.1111/j.1365-2958.2005.05031.x;
RA Xella B., Goding C., Agricola E., Di Mauro E., Caserta M.;
RT "The ISWI and CHD1 chromatin remodelling activities influence ADH2
RT expression and chromatin organization.";
RL Mol. Microbiol. 59:1531-1541(2006).
RN [14]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=17949749; DOI=10.1016/j.jmb.2007.09.059;
RA Ferreira H., Flaus A., Owen-Hughes T.;
RT "Histone modifications influence the action of Snf2 family remodelling
RT enzymes by different mechanisms.";
RL J. Mol. Biol. 374:563-579(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [16]
RP INTERACTION WITH RTF1.
RX PubMed=17576814; DOI=10.1128/mcb.00772-07;
RA Warner M.H., Roinick K.L., Arndt K.M.;
RT "Rtf1 is a multifunctional component of the Paf1 complex that regulates
RT gene expression by directing cotranscriptional histone modification.";
RL Mol. Cell. Biol. 27:6103-6115(2007).
RN [17]
RP FUNCTION.
RX PubMed=17620414; DOI=10.1128/mcb.00978-07;
RA Biswas D., Dutta-Biswas R., Stillman D.J.;
RT "Chd1 and yFACT act in opposition in regulating transcription.";
RL Mol. Cell. Biol. 27:6279-6287(2007).
RN [18]
RP ASSOCIATION WITH RDNA, AND FUNCTION.
RX PubMed=17259992; DOI=10.1038/nsmb1199;
RA Jones H.S., Kawauchi J., Braglia P., Alen C.M., Kent N.A., Proudfoot N.J.;
RT "RNA polymerase I in yeast transcribes dynamic nucleosomal rDNA.";
RL Nat. Struct. Mol. Biol. 14:123-130(2007).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1364, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [20]
RP FUNCTION.
RX PubMed=18245327; DOI=10.1534/genetics.107.084202;
RA Biswas D., Takahata S., Xin H., Dutta-Biswas R., Yu Y., Formosa T.,
RA Stillman D.J.;
RT "A role for Chd1 and Set2 in negatively regulating DNA replication in
RT Saccharomyces cerevisiae.";
RL Genetics 178:649-659(2008).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-987; SER-989;
RP SER-1336 AND SER-1372, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-72; SER-987; SER-989
RP AND SER-1336, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
RP 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
RX PubMed=15260971; DOI=10.1016/j.molcel.2004.06.005;
RA Wu P.Y., Ruhlmann C., Winston F., Schultz P.;
RT "Molecular architecture of the S. cerevisiae SAGA complex.";
RL Mol. Cell 15:199-208(2004).
RN [25]
RP STRUCTURE BY NMR OF 172-252, AND DOMAIN.
RX PubMed=17098252; DOI=10.1016/j.jmb.2006.10.039;
RA Okuda M., Horikoshi M., Nishimura Y.;
RT "Structural polymorphism of chromodomains in Chd1.";
RL J. Mol. Biol. 365:1047-1062(2007).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 174-339, DOMAIN, INTERACTION WITH
RP HISTONE H3K4ME3, AND MUTAGENESIS OF GLU-220.
RX PubMed=17433364; DOI=10.1016/j.jmb.2007.03.024;
RA Flanagan J.F., Blus B.J., Kim D., Clines K.L., Rastinejad F.,
RA Khorasanizadeh S.;
RT "Molecular implications of evolutionary differences in CHD double
RT chromodomains.";
RL J. Mol. Biol. 369:334-342(2007).
CC -!- FUNCTION: ATP-dependent chromatin-remodeling factor which functions as
CC substrate recognition component of the transcription regulatory histone
CC acetylation (HAT) complexes SAGA and SLIK. It recognizes H3K4me. SAGA
CC is involved in RNA polymerase II-dependent transcriptional regulation
CC of approximately 10% of yeast genes. At the promoters, SAGA is required
CC for recruitment of the basal transcription machinery. It influences RNA
CC polymerase II transcriptional activity through different activities
CC such as TBP interaction (SPT3, SPT8 and SPT20) and promoter
CC selectivity, interaction with transcription activators (GCN5, ADA2,
CC ADA3 and TRA1), and chromatin modification through histone acetylation
CC (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone
CC H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA
CC interacts with DNA via upstream activating sequences (UASs). SLIK is
CC proposed to have partly overlapping functions with SAGA. It
CC preferentially acetylates methylated histone H3, at least after
CC activation at the GAL1-10 locus. Acts in opposition to the FACT complex
CC in regulating polymerase II transcription. Also required for efficient
CC transcription by RNA polymerase I, and more specifically the pol I
CC transcription termination step. Regulates negatively DNA replication.
CC Not only involved in transcription-related chromatin-remodeling, but
CC also required to maintain a specific chromatin configuration across the
CC genome. {ECO:0000269|PubMed:10026213, ECO:0000269|PubMed:10811623,
CC ECO:0000269|PubMed:12682017, ECO:0000269|PubMed:14585955,
CC ECO:0000269|PubMed:15647753, ECO:0000269|PubMed:16468993,
CC ECO:0000269|PubMed:16606615, ECO:0000269|PubMed:17259992,
CC ECO:0000269|PubMed:17620414, ECO:0000269|PubMed:17949749,
CC ECO:0000269|PubMed:18245327}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.2 nM for ATP {ECO:0000269|PubMed:17949749};
CC -!- SUBUNIT: Component of the 1.8 MDa SAGA complex, which consists of at
CC least of TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12,
CC TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and
CC SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2
CC copies. SAGA is built of 5 distinct domains with specialized functions.
CC Domain I (containing TRA1) probably represents the activator
CC interaction surface. Domain II (containing TAF5 and TAF6, and probably
CC TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and
CC ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing
CC HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily
CC an architectural role. Domain III also harbors the HAT activity. Domain
CC V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-
CC interacting module, which may be associated transiently with SAGA.
CC Component of the SLIK complex, which consists of at least TRA1, CHD1,
CC SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1, UBP8, GCN5, ADA2,
CC SPT3, SGF29, TAF10 and TAF9. Interacts with RTF1, SPT5 and with the
CC FACT subunits POB3 and SPT16. {ECO:0000269|PubMed:12242279,
CC ECO:0000269|PubMed:12446794, ECO:0000269|PubMed:12682017,
CC ECO:0000269|PubMed:15647753, ECO:0000269|PubMed:17433364,
CC ECO:0000269|PubMed:17576814}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:12682017}.
CC -!- MISCELLANEOUS: Present with 1620 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {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; U18917; AAB64691.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07826.1; -; Genomic_DNA.
DR PIR; S30818; S30818.
DR RefSeq; NP_011091.1; NM_001179054.1.
DR PDB; 2DY7; NMR; -; A=172-252.
DR PDB; 2DY8; NMR; -; A=279-347.
DR PDB; 2H1E; X-ray; 2.20 A; A/B=174-339.
DR PDB; 2XB0; X-ray; 2.00 A; X=1009-1274.
DR PDB; 3MWY; X-ray; 3.70 A; W=142-939.
DR PDB; 3TED; X-ray; 2.00 A; A=1006-1274.
DR PDB; 5J70; X-ray; 2.96 A; A/B=1006-1274.
DR PDB; 5O9G; EM; 4.80 A; W=1-1468.
DR PDB; 6FTX; EM; 4.50 A; W=175-1269.
DR PDB; 6G0L; EM; 4.50 A; M/W=1-1468.
DR PDB; 7NKX; EM; 2.90 A; W=1-1468.
DR PDB; 7TN2; EM; 2.30 A; W=118-1274.
DR PDBsum; 2DY7; -.
DR PDBsum; 2DY8; -.
DR PDBsum; 2H1E; -.
DR PDBsum; 2XB0; -.
DR PDBsum; 3MWY; -.
DR PDBsum; 3TED; -.
DR PDBsum; 5J70; -.
DR PDBsum; 5O9G; -.
DR PDBsum; 6FTX; -.
DR PDBsum; 6G0L; -.
DR PDBsum; 7NKX; -.
DR PDBsum; 7TN2; -.
DR AlphaFoldDB; P32657; -.
DR SASBDB; P32657; -.
DR SMR; P32657; -.
DR BioGRID; 36917; 488.
DR ComplexPortal; CPX-656; SAGA complex.
DR ComplexPortal; CPX-675; SLIK (SAGA-like) complex.
DR DIP; DIP-6362N; -.
DR IntAct; P32657; 45.
DR MINT; P32657; -.
DR STRING; 4932.YER164W; -.
DR ChEMBL; CHEMBL4662924; -.
DR iPTMnet; P32657; -.
DR MaxQB; P32657; -.
DR PaxDb; P32657; -.
DR PRIDE; P32657; -.
DR EnsemblFungi; YER164W_mRNA; YER164W; YER164W.
DR GeneID; 856911; -.
DR KEGG; sce:YER164W; -.
DR SGD; S000000966; CHD1.
DR VEuPathDB; FungiDB:YER164W; -.
DR eggNOG; KOG0384; Eukaryota.
DR GeneTree; ENSGT00940000170579; -.
DR HOGENOM; CLU_000315_29_2_1; -.
DR InParanoid; P32657; -.
DR OMA; CSWGARE; -.
DR BioCyc; YEAST:G3O-30325-MON; -.
DR SABIO-RK; P32657; -.
DR EvolutionaryTrace; P32657; -.
DR PRO; PR:P32657; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P32657; protein.
DR GO; GO:0000785; C:chromatin; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0030874; C:nucleolar chromatin; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000124; C:SAGA complex; IDA:SGD.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IDA:SGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:SGD.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:SGD.
DR GO; GO:0003677; F:DNA binding; IDA:SGD.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0035064; F:methylated histone binding; IDA:SGD.
DR GO; GO:0000182; F:rDNA binding; IDA:SGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:ComplexPortal.
DR GO; GO:0016578; P:histone deubiquitination; IC:ComplexPortal.
DR GO; GO:0071894; P:histone H2B conserved C-terminal lysine ubiquitination; IMP:SGD.
DR GO; GO:2000104; P:negative regulation of DNA-templated DNA replication; IGI:SGD.
DR GO; GO:1900050; P:negative regulation of histone exchange; IMP:SGD.
DR GO; GO:0071441; P:negative regulation of histone H3-K14 acetylation; IMP:SGD.
DR GO; GO:2000616; P:negative regulation of histone H3-K9 acetylation; IMP:SGD.
DR GO; GO:0034728; P:nucleosome organization; IMP:SGD.
DR GO; GO:1902275; P:regulation of chromatin organization; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0001178; P:regulation of transcriptional start site selection at RNA polymerase II promoter; IGI:SGD.
DR GO; GO:0007062; P:sister chromatid cohesion; IMP:SGD.
DR GO; GO:0006363; P:termination of RNA polymerase I transcription; IGI:SGD.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IGI:SGD.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR041150; Cdh1_DBD.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR025260; DUF4208.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF18196; Cdh1_DBD_1; 1.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF13907; DUF4208; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 2.
DR PROSITE; PS00598; CHROMO_1; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Chromatin regulator; DNA-binding; Helicase;
KW Hydrolase; Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..1468
FT /note="Chromo domain-containing protein 1"
FT /id="PRO_0000080237"
FT DOMAIN 195..257
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 285..350
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 388..562
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 699..860
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 21..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 974..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1220..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1270..1378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 513..516
FT /note="DEAH box"
FT COMPBIAS 43..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..86
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..157
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1007
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1331..1366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 401..408
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 72
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 987
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 989
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1336
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 1372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 1144
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:12872131"
FT MUTAGEN 220
FT /note="E->L,W: No interaction with methylated histone H3
FT 'K-4'."
FT /evidence="ECO:0000269|PubMed:15647753,
FT ECO:0000269|PubMed:17433364"
FT MUTAGEN 222
FT /note="H->Y: Confers interaction with methylated histone H3
FT 'K-4'."
FT /evidence="ECO:0000269|PubMed:15647753"
FT MUTAGEN 314
FT /note="L->Y: No effect on interaction with methylated
FT histone H3 'K-4'."
FT /evidence="ECO:0000269|PubMed:15647753"
FT MUTAGEN 316
FT /note="Y->E: Disrupts interaction with methylated histone
FT H3 'K-4'; abrogates histone acetylation activity of SLIK."
FT /evidence="ECO:0000269|PubMed:15647753"
FT STRAND 179..187
FT /evidence="ECO:0007829|PDB:2H1E"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:2DY7"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:2H1E"
FT HELIX 204..210
FT /evidence="ECO:0007829|PDB:2H1E"
FT STRAND 211..217
FT /evidence="ECO:0007829|PDB:2H1E"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:2H1E"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:2H1E"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:2H1E"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:2DY7"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:2H1E"
FT HELIX 251..258
FT /evidence="ECO:0007829|PDB:2H1E"
FT HELIX 264..283
FT /evidence="ECO:0007829|PDB:2H1E"
FT STRAND 286..297
FT /evidence="ECO:0007829|PDB:2H1E"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:2DY8"
FT STRAND 303..311
FT /evidence="ECO:0007829|PDB:2H1E"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:2H1E"
FT HELIX 324..330
FT /evidence="ECO:0007829|PDB:2H1E"
FT HELIX 332..338
FT /evidence="ECO:0007829|PDB:2H1E"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 378..393
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 407..420
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 437..447
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 460..470
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 492..497
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 499..503
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 507..514
FT /evidence="ECO:0007829|PDB:7NKX"
FT TURN 515..518
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 524..531
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 534..540
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 549..559
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 576..590
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 591..593
FT /evidence="ECO:0007829|PDB:7NKX"
FT TURN 599..601
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 610..616
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 620..629
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 652..660
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 662..664
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 669..672
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 684..693
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 695..709
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 714..717
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 721..734
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 738..741
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 747..758
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 759..761
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 766..769
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 771..777
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 785..790
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 795..802
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 807..809
FT /evidence="ECO:0007829|PDB:7NKX"
FT STRAND 815..824
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 825..839
FT /evidence="ECO:0007829|PDB:7NKX"
FT HELIX 1012..1025
FT /evidence="ECO:0007829|PDB:2XB0"
FT HELIX 1029..1031
FT /evidence="ECO:0007829|PDB:3TED"
FT HELIX 1032..1037
FT /evidence="ECO:0007829|PDB:2XB0"
FT HELIX 1046..1091
FT /evidence="ECO:0007829|PDB:2XB0"
FT STRAND 1092..1094
FT /evidence="ECO:0007829|PDB:2XB0"
FT STRAND 1096..1098
FT /evidence="ECO:0007829|PDB:3TED"
FT STRAND 1101..1103
FT /evidence="ECO:0007829|PDB:3TED"
FT HELIX 1104..1112
FT /evidence="ECO:0007829|PDB:2XB0"
FT STRAND 1119..1122
FT /evidence="ECO:0007829|PDB:3TED"
FT STRAND 1125..1129
FT /evidence="ECO:0007829|PDB:3TED"
FT HELIX 1130..1150
FT /evidence="ECO:0007829|PDB:2XB0"
FT HELIX 1155..1157
FT /evidence="ECO:0007829|PDB:2XB0"
FT STRAND 1171..1173
FT /evidence="ECO:0007829|PDB:2XB0"
FT HELIX 1177..1190
FT /evidence="ECO:0007829|PDB:2XB0"
FT HELIX 1195..1200
FT /evidence="ECO:0007829|PDB:2XB0"
FT TURN 1202..1204
FT /evidence="ECO:0007829|PDB:2XB0"
FT HELIX 1207..1209
FT /evidence="ECO:0007829|PDB:2XB0"
FT HELIX 1250..1264
FT /evidence="ECO:0007829|PDB:2XB0"
FT TURN 1265..1268
FT /evidence="ECO:0007829|PDB:2XB0"
SQ SEQUENCE 1468 AA; 168241 MW; 78BDB74C7FEC6BE5 CRC64;
MAAKDISTEV LQNPELYGLR RSHRAAAHQQ NYFNDSDDED DEDNIKQSRR KRMTTIEDDE
DEFEDEEGEE DSGEDEDEED FEEDDDYYGS PIKQNRSKPK SRTKSKSKSK PKSQSEKQST
VKIPTRFSNR QNKTVNYNID YSDDDLLESE DDYGSEEALS EENVHEASAN PQPEDFHGID
IVINHRLKTS LEEGKVLEKT VPDLNNCKEN YEFLIKWTDE SHLHNTWETY ESIGQVRGLK
RLDNYCKQFI IEDQQVRLDP YVTAEDIEIM DMERERRLDE FEEFHVPERI IDSQRASLED
GTSQLQYLVK WRRLNYDEAT WENATDIVKL APEQVKHFQN RENSKILPQY SSNYTSQRPR
FEKLSVQPPF IKGGELRDFQ LTGINWMAFL WSKGDNGILA DEMGLGKTVQ TVAFISWLIF
ARRQNGPHII VVPLSTMPAW LDTFEKWAPD LNCICYMGNQ KSRDTIREYE FYTNPRAKGK
KTMKFNVLLT TYEYILKDRA ELGSIKWQFM AVDEAHRLKN AESSLYESLN SFKVANRMLI
TGTPLQNNIK ELAALVNFLM PGRFTIDQEI DFENQDEEQE EYIHDLHRRI QPFILRRLKK
DVEKSLPSKT ERILRVELSD VQTEYYKNIL TKNYSALTAG AKGGHFSLLN IMNELKKASN
HPYLFDNAEE RVLQKFGDGK MTRENVLRGL IMSSGKMVLL DQLLTRLKKD GHRVLIFSQM
VRMLDILGDY LSIKGINFQR LDGTVPSAQR RISIDHFNSP DSNDFVFLLS TRAGGLGINL
MTADTVVIFD SDWNPQADLQ AMARAHRIGQ KNHVMVYRLV SKDTVEEEVL ERARKKMILE
YAIISLGVTD GNKYTKKNEP NAGELSAILK FGAGNMFTAT DNQKKLEDLN LDDVLNHAED
HVTTPDLGES HLGGEEFLKQ FEVTDYKADI DWDDIIPEEE LKKLQDEEQK RKDEEYVKEQ
LEMMNRRDNA LKKIKNSVNG DGTAANSDSD DDSTSRSSRR RARANDMDSI GESEVRALYK
AILKFGNLKE ILDELIADGT LPVKSFEKYG ETYDEMMEAA KDCVHEEEKN RKEILEKLEK
HATAYRAKLK SGEIKAENQP KDNPLTRLSL KKREKKAVLF NFKGVKSLNA ESLLSRVEDL
KYLKNLINSN YKDDPLKFSL GNNTPKPVQN WSSNWTKEED EKLLIGVFKY GYGSWTQIRD
DPFLGITDKI FLNEVHNPVA KKSASSSDTT PTPSKKGKGI TGSSKKVPGA IHLGRRVDYL
LSFLRGGLNT KSPSADIGSK KLPTGPSKKR QRKPANHSKS MTPEITSSEP ANGPPSKRMK
ALPKGPAALI NNTRLSPNSP TPPLKSKVSR DNGTRQSSNP SSGSAHEKEY DSMDEEDCRH
TMSAIRTSLK RLRRGGKSLD RKEWAKILKT ELTTIGNHIE SQKGSSRKAS PEKYRKHLWS
YSANFWPADV KSTKLMAMYD KITESQKK
