CHD9_HUMAN
ID CHD9_HUMAN Reviewed; 2897 AA.
AC Q3L8U1; B2RTU2; B9ZVQ0; O15025; Q1WF12; Q6DTK9; Q9H9V7; Q9UHM2;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 9;
DE Short=CHD-9;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase CHD9;
DE AltName: Full=Chromatin-related mesenchymal modulator;
DE Short=CReMM;
DE AltName: Full=Chromatin-remodeling factor CHROM1;
DE AltName: Full=Kismet homolog 2;
DE AltName: Full=PPAR-alpha-interacting complex protein 320 kDa;
DE AltName: Full=Peroxisomal proliferator-activated receptor A-interacting complex 320 kDa protein;
GN Name=CHD9; Synonyms=KIAA0308, KISH2, PRIC320; ORFNames=AD-013, x0008;
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), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, PHOSPHORYLATION, AND VARIANT GLU-2312.
RC TISSUE=Bone marrow stroma;
RX PubMed=16095617; DOI=10.1016/j.jmb.2005.06.049;
RA Shur I., Benayahu D.;
RT "Characterization and functional analysis of CReMM, a novel chromodomain
RT helicase DNA-binding protein.";
RL J. Mol. Biol. 352:646-655(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY,
RP VARIANT GLU-2312, AND INTERACTION WITH PPARA; ESR1 AND NR1I3.
RX PubMed=16554032; DOI=10.1016/j.bbrc.2006.02.160;
RA Surapureddi S., Viswakarma N., Yu S., Guo D., Rao M.S., Reddy J.K.;
RT "PRIC320, a transcription coactivator, isolated from peroxisome
RT proliferator-binding protein complex.";
RL Biochem. Biophys. Res. Commun. 343:535-543(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Pharynx carcinoma;
RA Colin C., Dahia P.L.M., Stiles C.D., Sogayar M.C.;
RT "Cloning of the mammalian orthologs of Drosophila melanogaster gene
RT KISMET.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-2897 (ISOFORM 3), AND VARIANT
RP GLU-2312.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 485-639.
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 886-1616.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1468 AND SER-1472, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550; SER-611 AND SER-2026,
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550; SER-2058 AND SER-2059,
RP AND 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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-499, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550; SER-1468 AND SER-1472,
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550; SER-1468; SER-1472;
RP SER-2058; SER-2059; SER-2075 AND SER-2079, AND IDENTIFICATION BY MASS
RP 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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2350, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2038, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-197; LYS-596; LYS-1588; LYS-1738;
RP LYS-1903; LYS-2038; LYS-2074; LYS-2350; LYS-2356; LYS-2361 AND LYS-2843,
RP AND IDENTIFICATION BY MASS 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: Acts as a transcriptional coactivator for PPARA and possibly
CC other nuclear receptors. Proposed to be a ATP-dependent chromatin
CC remodeling protein. Has DNA-dependent ATPase activity and binds to A/T-
CC rich DNA. Associates with A/T-rich regulatory regions in promoters of
CC genes that participate in the differentiation of progenitors during
CC osteogenesis (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:16095617, ECO:0000269|PubMed:16554032}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC -!- SUBUNIT: Interacts with PPARA. Probably interacts with ESR1 and NR1I3.
CC {ECO:0000269|PubMed:16554032}.
CC -!- INTERACTION:
CC Q3L8U1-3; Q07869: PPARA; NbExp=2; IntAct=EBI-960730, EBI-78615;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16095617}. Nucleus
CC {ECO:0000269|PubMed:16095617}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q3L8U1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3L8U1-2; Sequence=VSP_018086;
CC Name=3;
CC IsoId=Q3L8U1-3; Sequence=VSP_018085, VSP_018086;
CC -!- TISSUE SPECIFICITY: Widely expressed at low levels. In bone marrow,
CC expression is restricted to osteoprogenitor cells adjacent to mature
CC osteoblasts. {ECO:0000269|PubMed:16095617,
CC ECO:0000269|PubMed:16554032}.
CC -!- PTM: Phosphorylated on serine and tyrosine residues.
CC {ECO:0000269|PubMed:16095617}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF24170.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=BAB14112.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY243500; AAQ24287.1; -; mRNA.
DR EMBL; DQ333316; ABD24032.1; -; mRNA.
DR EMBL; AY647157; AAT66509.1; -; mRNA.
DR EMBL; AC007906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC079416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC140815; AAI40816.1; -; mRNA.
DR EMBL; AB002306; BAA20767.3; -; mRNA.
DR EMBL; AF150735; AAF24170.1; ALT_SEQ; mRNA.
DR EMBL; AK022582; BAB14112.1; ALT_INIT; mRNA.
DR CCDS; CCDS45485.1; -. [Q3L8U1-2]
DR CCDS; CCDS76865.1; -. [Q3L8U1-1]
DR RefSeq; NP_001295248.1; NM_001308319.1. [Q3L8U1-1]
DR RefSeq; NP_079410.4; NM_025134.4. [Q3L8U1-2]
DR RefSeq; XP_005256229.1; XM_005256172.3.
DR RefSeq; XP_016879210.1; XM_017023721.1. [Q3L8U1-1]
DR RefSeq; XP_016879211.1; XM_017023722.1. [Q3L8U1-3]
DR RefSeq; XP_016879212.1; XM_017023723.1. [Q3L8U1-2]
DR SMR; Q3L8U1; -.
DR BioGRID; 123174; 58.
DR IntAct; Q3L8U1; 28.
DR MINT; Q3L8U1; -.
DR STRING; 9606.ENSP00000457466; -.
DR iPTMnet; Q3L8U1; -.
DR PhosphoSitePlus; Q3L8U1; -.
DR BioMuta; CHD9; -.
DR DMDM; 215273951; -.
DR EPD; Q3L8U1; -.
DR jPOST; Q3L8U1; -.
DR MassIVE; Q3L8U1; -.
DR MaxQB; Q3L8U1; -.
DR PaxDb; Q3L8U1; -.
DR PeptideAtlas; Q3L8U1; -.
DR PRIDE; Q3L8U1; -.
DR ProteomicsDB; 61749; -. [Q3L8U1-1]
DR ProteomicsDB; 61750; -. [Q3L8U1-2]
DR ProteomicsDB; 61751; -. [Q3L8U1-3]
DR Antibodypedia; 28339; 74 antibodies from 22 providers.
DR DNASU; 80205; -.
DR Ensembl; ENST00000398510.7; ENSP00000381522.3; ENSG00000177200.18. [Q3L8U1-1]
DR Ensembl; ENST00000447540.6; ENSP00000396345.2; ENSG00000177200.18. [Q3L8U1-1]
DR Ensembl; ENST00000564845.5; ENSP00000455307.1; ENSG00000177200.18. [Q3L8U1-2]
DR Ensembl; ENST00000566029.5; ENSP00000457466.1; ENSG00000177200.18. [Q3L8U1-2]
DR GeneID; 80205; -.
DR KEGG; hsa:80205; -.
DR MANE-Select; ENST00000447540.6; ENSP00000396345.2; NM_001308319.2; NP_001295248.1.
DR UCSC; uc002egy.4; human. [Q3L8U1-1]
DR CTD; 80205; -.
DR DisGeNET; 80205; -.
DR GeneCards; CHD9; -.
DR HGNC; HGNC:25701; CHD9.
DR HPA; ENSG00000177200; Low tissue specificity.
DR neXtProt; NX_Q3L8U1; -.
DR OpenTargets; ENSG00000177200; -.
DR PharmGKB; PA128394727; -.
DR VEuPathDB; HostDB:ENSG00000177200; -.
DR eggNOG; KOG0384; Eukaryota.
DR GeneTree; ENSGT00940000155706; -.
DR HOGENOM; CLU_000315_5_1_1; -.
DR InParanoid; Q3L8U1; -.
DR OMA; KMAHSKT; -.
DR OrthoDB; 7181at2759; -.
DR PhylomeDB; Q3L8U1; -.
DR TreeFam; TF313572; -.
DR PathwayCommons; Q3L8U1; -.
DR Reactome; R-HSA-1368082; RORA activates gene expression.
DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR Reactome; R-HSA-9707616; Heme signaling.
DR SignaLink; Q3L8U1; -.
DR BioGRID-ORCS; 80205; 14 hits in 1093 CRISPR screens.
DR ChiTaRS; CHD9; human.
DR GeneWiki; CHD9; -.
DR GenomeRNAi; 80205; -.
DR Pharos; Q3L8U1; Tbio.
DR PRO; PR:Q3L8U1; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q3L8U1; protein.
DR Bgee; ENSG00000177200; Expressed in calcaneal tendon and 214 other tissues.
DR ExpressionAtlas; Q3L8U1; baseline and differential.
DR Genevisible; Q3L8U1; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.5.120; -; 2.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006576; BRK_domain.
DR InterPro; IPR037259; BRK_sf.
DR InterPro; IPR042850; CHD9.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623:SF2; PTHR45623:SF2; 1.
DR Pfam; PF07533; BRK; 2.
DR Pfam; PF00385; Chromo; 2.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00592; BRK; 2.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF160481; SSF160481; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54160; SSF54160; 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 Acetylation; Alternative splicing; ATP-binding; Chromatin regulator;
KW Cytoplasm; DNA-binding; Helicase; Hydrolase; Isopeptide bond;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..2897
FT /note="Chromodomain-helicase-DNA-binding protein 9"
FT /id="PRO_0000233172"
FT DOMAIN 690..761
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 773..839
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 872..1046
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1186..1337
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 173..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..671
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1461..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2050..2238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2305..2337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2332..2481
FT /note="Binds A/T-rich DNA"
FT REGION 2429..2436
FT /note="A.T hook-like"
FT REGION 2729..2777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2827..2897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 868..872
FT /note="LXXLL motif 1"
FT MOTIF 997..1000
FT /note="DEAH box"
FT MOTIF 1036..1040
FT /note="LXXLL motif 2"
FT MOTIF 2031..2035
FT /note="LXXLL motif 3"
FT MOTIF 2721..2725
FT /note="LXXLL motif 4"
FT MOTIF 2793..2798
FT /note="LXXLL motif 5"
FT COMPBIAS 482..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..663
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2062..2076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2122..2140
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2141..2193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2219..2238
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2736..2760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2761..2777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2837..2858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 885..892
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 499
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 611
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1468
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 2026
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 2058
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2059
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2075
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2079
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 197
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 596
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1588
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1738
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1903
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2038
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 2074
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2350
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 2356
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2361
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 2843
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 2206
FT /note="R -> RA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9205841"
FT /id="VSP_018085"
FT VAR_SEQ 2336..2351
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16554032,
FT ECO:0000303|PubMed:9205841, ECO:0000303|Ref.3"
FT /id="VSP_018086"
FT VARIANT 2312
FT /note="D -> E (in dbSNP:rs6499548)"
FT /evidence="ECO:0000269|PubMed:16095617,
FT ECO:0000269|PubMed:16554032, ECO:0000269|PubMed:9205841"
FT /id="VAR_047355"
FT CONFLICT 98..100
FT /note="SQF -> PQL (in Ref. 3; AAT66509)"
FT /evidence="ECO:0000305"
FT CONFLICT 119
FT /note="S -> P (in Ref. 3; AAT66509)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="V -> A (in Ref. 3; AAT66509)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="L -> I (in Ref. 3; AAT66509)"
FT /evidence="ECO:0000305"
FT CONFLICT 836
FT /note="R -> C (in Ref. 2; ABD24032 and 6; BAA20767)"
FT /evidence="ECO:0000305"
FT CONFLICT 1072
FT /note="A -> V (in Ref. 2; ABD24032 and 8; BAB14112)"
FT /evidence="ECO:0000305"
FT CONFLICT 1122
FT /note="S -> F (in Ref. 3; AAT66509)"
FT /evidence="ECO:0000305"
FT CONFLICT 1372
FT /note="S -> P (in Ref. 3; AAT66509)"
FT /evidence="ECO:0000305"
FT CONFLICT 1442
FT /note="S -> G (in Ref. 2; ABD24032 and 8; BAB14112)"
FT /evidence="ECO:0000305"
FT CONFLICT 1724
FT /note="A -> T (in Ref. 3; AAT66509)"
FT /evidence="ECO:0000305"
FT CONFLICT 1754
FT /note="S -> L (in Ref. 3; AAT66509)"
FT /evidence="ECO:0000305"
FT CONFLICT 1867
FT /note="T -> A (in Ref. 3; AAT66509)"
FT /evidence="ECO:0000305"
FT CONFLICT 2025
FT /note="A -> V (in Ref. 3; AAT66509)"
FT /evidence="ECO:0000305"
FT CONFLICT 2069
FT /note="T -> A (in Ref. 3; AAT66509)"
FT /evidence="ECO:0000305"
FT CONFLICT 2078
FT /note="V -> G (in Ref. 3; AAT66509)"
FT /evidence="ECO:0000305"
FT CONFLICT 2189
FT /note="S -> F (in Ref. 3; AAT66509)"
FT /evidence="ECO:0000305"
FT CONFLICT 2759
FT /note="S -> N (in Ref. 3; AAT66509)"
FT /evidence="ECO:0000305"
FT CONFLICT 2776
FT /note="T -> A (in Ref. 1; AAQ24287 and 6; BAA20767)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2897 AA; 326022 MW; 91884A5E2F8ED183 CRC64;
MTDPMMDFFD DANLFGETLE GLSDDAFVQP GPVSLVDELN LGAEFEPLHI DSLNHVQGTP
THQKMTDFEQ LNQFDSIKFH HVNQSFGSPA EHVLSPHSQF NCSPIHPQNQ PNGLFPDVSD
GSPMWGHQTA TTISNQNGSP FHQQGHSHSM HQNKSFVAHH DFALFQANEQ QTQCTSLRSQ
QNRNNLNPGQ NSLSQSKNFM NVSGPHRVNV NHPPQMTNAS NSQQSISMQQ FSQTSNPSAH
FHKCSSHQEG NFNGPSPNMT SCSVSNSQQF SSHYSFSSNH ISPNSLLQSS AVLASNHTNQ
TLSDFTGSNS FSPHRGIKQE STQHILNPNT SLNSNNFQIL HSSHPQGNYS NSKLSPVHMN
FPDPVDSGTQ MGHFNDHVET NGFSSLEENL LHQVESQTEP FTGLDPEDLL QEGLLPHFDE
STFGQDNSSH ILDHDLDRQF TSHLVTRPSD MAQTQLQSQA RSWHSSFSNH QHLHDRNHLC
LQRQPPSSKK SDGSGTYTKL QNTQVRVMSE KKQRKKVESE SKQEKANRII SEAIAKAKER
GERNIPRVMS PENFPTASVE GKEEKKGRRM KSKPKDKDSK KTKTCSKLKE KTKIGKLIIT
LGKKQKRKNE SSDEISDAEQ MPQHTLKDQD SQKRRSNRQI KRKKYAEDIE GKQSEEEVKG
SMKIKKNSAP LPGEQPLQLF VENPSEEDAA IVDKILSSRT VKKEISPGVM IDTEEFFVKY
KNYSYLHCEW ATEEQLLKDK RIQQKIKRFK LRQAQRAHFF ADMEEEPFNP DYVEVDRVLE
VSFCEDKDTG EPVIYYLVKW CSLPYEDSTW ELKEDVDLAK IEEFEQLQAS RPDTRRLDRP
PSNIWKKIDQ SRDYKNGNQL REYQLEGLNW LLFNWYNRRN CILADEMGLG KTIQSITFLY
EILLTGIRGP FLIIAPLSTI ANWEREFRTW TDINVVVYHG SLISRQMIQQ YEMYFRDSQG
RIIRGAYRFQ AIITTFEMIL GGCGELNAIE WRCVIIDEAH RLKNKNCKLL EGLKLMNLEH
KVLLTGTPLQ NTVEELFSLL HFLEPLRFPS ESTFMQEFGD LKTEEQVQKL QAILKPMMLR
RLKEDVEKKL APKEETIIEV ELTNIQKKYY RAILEKNFSF LSKGAGQTNV PNLVNTMMEL
RKCCNHPYLI KGAEEKILGE FRDTYNPAAS DFHLQAMIQS AGKLVLIDKL LPKMKAGGHK
VLIFSQMVRC LDILEDYLIH KRYLYERIDG RVRGNLRQAA IDRFSKPDSD RFVFLLCTRA
GGLGINLTAA DTCIIFDSDW NPQNDLQAQA RCHRIGQNKA VKVYRLVTRN SYEREMFDRA
SLKLGLDKAV LQSMSGRESN VGGIQQLSKK EIEDLLRRGA YGAIMEEEDE GSKFCEEDID
QILLRRTKTI TIESEGRGST FAKASFVASG NRTDISLDDP NFWQKWAKKA EIDIEAISGR
NSLVIDTPRI RKQTRPFSAT KDELAELSEA ESEGDEKPKL RRPCDRSNGY GRTECFRVEK
NLLVYGWGRW REILSHGRFK RQLNEHDVEI ICRALLAYCL VHYRGDEKIK GFIWDLITPT
EDGQTRELQN HLGLSAPVPR GRKGKKVKTQ TSSFDIQKAE WLRKYNPEQL LQDEGYKKHI
KHHCNKVLLR VRMLYYLKQE VIGNECQKVF DGVDASDIDV WVPEPDHSEV PAEWWDFDAD
KSLLIGVFKH GYEKYNTIRA DPALCFLERV GKPDEKAVAA EQRANDYMDG DVEDPEYKPA
PAIFKDDIED DVSSPGDLVI ADGDGQLMEG DKVYWPTQSA LTTRLRRLIT AYQRTNKNRQ
IQQIQPTFSV PTSVMQPIYE EATLNPKMAA KIERQQRWTR REEADFYRVV STFGVVFDPD
RGQFDWTKFR AMARLHKKTD DSLEKYLYAF MSMCRRVCRL PSKEELVDPN IFIQPITEER
ASRTLYRIEL LRKVREQALR HPQLFERLKL CHPNPDLPVW WECGPHDRDL LIGAAKHGVS
RTDYHILRDP ELSFMAAQRN YSQSKMAHSR TSTPLLQQYQ VALSASPLTS LPRLLDAKGI
ILEEMKVKSE NLKEEPQSSE EESMSSVETR TLIKSEPVSP KNGVLPQATG DQKSGGKCET
DRRMVAARTE PLTPNPASKK PRVHKRGSES SSDSDSDSER SSCSSRSSSS SSSSSCSHSR
SGSSSSSSSS CSSASSSSSS STSSSSSSSS SSSEESDSDE EEAQKRESTT HMKAYDEESV
ASLSTTQDET QDSFQMNNGT PESAYILQGG YMLAASYWPK DRVMINRLDS ICQTVLKGKW
PSARRSYDAN TVASFYTTKL LDSPGAATEY SDPSVPTPPG AGVKEEHDQS TQMSKVKKHV
REKEFTVKIK DEGGLKLTFQ KQGLAQKRPF DGEDGALGQQ QYLTRLRELQ SASETSLVNF
PKSIPVSGTS IQPTLGANGV ILDNQPIVKK RRGRRKNVEG VDIFFFNRNK PPNHVSLGLT
SSQISTGINP ALSYTQPQGI PDTESPVPVI NLKDGTRLAG DDAPKRKDLE KWLKEHPGYV
EDLGAFIPRM QLHEGRPKQK RHRCRNPNKL DVNSLTGEER VQLINRRNAR KVGGAFAPPL
KDLCRFLKEN SEYGVAPEWG DVVKQSGFLP ESMYERILTG PVVREEVSRR GRRPKSGIAK
ATAAAAAASA TSVSGNPLLA NGLLPGVDLT TLQALQQNLQ NLQSLQVTAG LMGMPTGLPS
GGEAKNMAAM FPMLLSGMAG LPNLLGMGGL LTKPTESGTE DKKGSDSKES EGKTERTESQ
SSENGGENSV SSSPSTSSTA ALNTAAAANP LALNPLLLSN ILYPGMLLTP GLNLHIPTLS
QSNTFDVQNK NSDLGSSKSV EVKEEDSRIK DQEDKGGTEP SPLNENSTDE GSEKADASSG
SDSTSSSSED SDSSNED
