CHD1_MOUSE
ID CHD1_MOUSE Reviewed; 1711 AA.
AC P40201; Q14BJ0;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 1;
DE Short=CHD-1;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase CHD1;
GN Name=Chd1; Synonyms=Chd-1;
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].
RX PubMed=8460153; DOI=10.1073/pnas.90.6.2414;
RA Delmas V., Stokes D.G., Perry R.P.;
RT "A mammalian DNA-binding protein that contains a chromodomain and an
RT SNF2/SWI2-like helicase domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:2414-2418(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 SUBCELLULAR LOCATION, AND DNA-BINDING.
RX PubMed=7739555; DOI=10.1128/mcb.15.5.2745;
RA Stokes D.G., Perry R.P.;
RT "DNA-binding and chromatin localization properties of CHD1.";
RL Mol. Cell. Biol. 15:2745-2753(1995).
RN [5]
RP SUBCELLULAR LOCATION, DOMAIN, AND INTERACTION WITH SSRP1.
RX PubMed=10199952; DOI=10.1007/s004120050347;
RA Kelley D.E., Stokes D.G., Perry R.P.;
RT "CHD1 interacts with SSRP1 and depends on both its chromodomain and its
RT ATPase/helicase-like domain for proper association with chromatin.";
RL Chromosoma 108:10-25(1999).
RN [6]
RP INTERACTION WITH BCLAF1; NCOR; SRP20 AND SAF-B, AND FUNCTION.
RX PubMed=12890497; DOI=10.1016/s0006-291x(03)01354-8;
RA Tai H.H., Geisterfer M., Bell J.C., Moniwa M., Davie J.R., Boucher L.,
RA McBurney M.W.;
RT "CHD1 associates with NCoR and histone deacetylase as well as with RNA
RT splicing proteins.";
RL Biochem. Biophys. Res. Commun. 308:170-176(2003).
RN [7]
RP FUNCTION, AND INTERACTION WITH CHROMATIN.
RX PubMed=19587682; DOI=10.1038/nature08212;
RA Gaspar-Maia A., Alajem A., Polesso F., Sridharan R., Mason M.J.,
RA Heidersbach A., Ramalho-Santos J., McManus M.T., Plath K., Meshorer E.,
RA Ramalho-Santos M.;
RT "Chd1 regulates open chromatin and pluripotency of embryonic stem cells.";
RL Nature 460:863-868(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214 AND SER-215, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, 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).
CC -!- FUNCTION: ATP-dependent chromatin-remodeling factor which functions as
CC substrate recognition component of the transcription regulatory histone
CC acetylation (HAT) complex SAGA. Regulates polymerase II transcription.
CC Also required for efficient transcription by RNA polymerase I, and more
CC specifically the polymerase I transcription termination step. Regulates
CC negatively DNA replication. Not only involved in transcription-related
CC chromatin-remodeling, but also required to maintain a specific
CC chromatin configuration across the genome. Required for the bridging of
CC SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex
CC to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing
CC in part through physical bridging of spliceosomal components to H3K4me3
CC (By similarity). Required for maintaining open chromatin and
CC pluripotency in embryonic stem cells (PubMed:19587682). Is also
CC associated with histone deacetylase (HDAC) activity (PubMed:12890497).
CC {ECO:0000250|UniProtKB:O14646, ECO:0000269|PubMed:12890497,
CC ECO:0000269|PubMed:19587682}.
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: Component of the SAGA complex (By similarity). Specifically
CC interacts with methylated H3K4me2 and H3K4me3. Interacts with the FACT
CC complex, the PAF complex and the U2 snRNP. Interacts directly with
CC PAF1, SFA3A1, SFA3A2, SFA3A3, SNF2 and SSRP1 (By similarity). Interacts
CC with BCLAF1, NCoR, SRP20 and SAFB. {ECO:0000250,
CC ECO:0000269|PubMed:10199952, ECO:0000269|PubMed:12890497,
CC ECO:0000269|PubMed:19587682}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10199952,
CC ECO:0000269|PubMed:7739555}. Cytoplasm {ECO:0000269|PubMed:7739555}.
CC Note=Is released into the cytoplasm when cells enter mitosis and is
CC reincorporated into chromatin during telophase-cytokinesis
CC (PubMed:7739555).
CC -!- TISSUE SPECIFICITY: Abundance is higher in cells representing early
CC stages of the B-lymphoid lineage such as pre-B and B-cells, than in
CC cells representing mature plasmacytes or other cell lineages such as
CC fibroblasts.
CC -!- DOMAIN: The 2 chromodomains are involved in the binding to the histone
CC H3 methyllysine at position 4 (H3K4me3). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; L10410; AAB08486.1; -; mRNA.
DR EMBL; CH466630; EDL20454.1; -; Genomic_DNA.
DR EMBL; BC115822; AAI15823.1; -; mRNA.
DR CCDS; CCDS28416.1; -.
DR PIR; A47392; A47392.
DR RefSeq; NP_031716.2; NM_007690.3.
DR AlphaFoldDB; P40201; -.
DR SMR; P40201; -.
DR BioGRID; 198693; 4.
DR IntAct; P40201; 1.
DR STRING; 10090.ENSMUSP00000024627; -.
DR iPTMnet; P40201; -.
DR PhosphoSitePlus; P40201; -.
DR SwissPalm; P40201; -.
DR EPD; P40201; -.
DR jPOST; P40201; -.
DR MaxQB; P40201; -.
DR PaxDb; P40201; -.
DR PeptideAtlas; P40201; -.
DR PRIDE; P40201; -.
DR ProteomicsDB; 279072; -.
DR Antibodypedia; 25129; 210 antibodies from 35 providers.
DR DNASU; 12648; -.
DR Ensembl; ENSMUST00000024627; ENSMUSP00000024627; ENSMUSG00000023852.
DR GeneID; 12648; -.
DR KEGG; mmu:12648; -.
DR UCSC; uc008aou.2; mouse.
DR CTD; 1105; -.
DR MGI; MGI:88393; Chd1.
DR VEuPathDB; HostDB:ENSMUSG00000023852; -.
DR eggNOG; KOG0384; Eukaryota.
DR GeneTree; ENSGT00940000156579; -.
DR HOGENOM; CLU_000315_8_1_1; -.
DR InParanoid; P40201; -.
DR OMA; CSWGARE; -.
DR OrthoDB; 57339at2759; -.
DR PhylomeDB; P40201; -.
DR TreeFam; TF300674; -.
DR BioGRID-ORCS; 12648; 12 hits in 82 CRISPR screens.
DR ChiTaRS; Chd1; mouse.
DR PRO; PR:P40201; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P40201; protein.
DR Bgee; ENSMUSG00000023852; Expressed in embryonic post-anal tail and 254 other tissues.
DR ExpressionAtlas; P40201; baseline and differential.
DR Genevisible; P40201; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0000228; C:nuclear chromosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0004386; F:helicase activity; NAS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; NAS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IGI:MGI.
DR GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR040793; CDH1_2_SANT_HL1.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF18375; CDH1_2_SANT_HL1; 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; 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 ATP-binding; Chromatin regulator; Cytoplasm; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1711
FT /note="Chromodomain-helicase-DNA-binding protein 1"
FT /id="PRO_0000080225"
FT DOMAIN 270..362
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 387..450
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 491..661
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 790..941
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REPEAT 1629..1633
FT /note="1"
FT REPEAT 1635..1639
FT /note="2"
FT REPEAT 1641..1645
FT /note="3"
FT REGION 1..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1078..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1322..1407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1503..1588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1600..1657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1629..1645
FT /note="3 X 5 AA repeats of H-S-D-H-R"
FT REGION 1670..1711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 612..615
FT /note="DEAH box"
FT COMPBIAS 12..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..205
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1342
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1507..1522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1588
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1692..1711
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 504..511
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 248
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 1023
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 1038
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 1079
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 1083
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14647"
FT MOD_RES 1094
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 1096
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 1098
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 1100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 1159
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 1353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 1355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 1356
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 1360
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 1363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 1373
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14647"
FT MOD_RES 1678
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT MOD_RES 1690
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14646"
FT CONFLICT 159
FT /note="S -> L (in Ref. 1; AAB08486)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1711 AA; 196385 MW; 51499636E943A856 CRC64;
MNGHSDEESV RNGSGESSQS GDDCGSASGS GSGSSSGSSS DGSSSQSGSS DSDSGSDSGS
QSESESDTSR ENKVQAKPPK VDGAEFWKSS PSILAVQRSA MLRKQPQQAQ QQRPASSNSG
SEEDSSSSED SDDSSSGAKR KKHNDEDWQM SGSGSPSQSG SDSESEEERD KSSCDGTESD
YEPKNKVRSR KPQNRSKSKN GKKILGQKKR QIDSSEDEDD EDYDNDKRSS RRQATVNVSY
KEDEEMKTDS DDLLEVCGED VPQPEDEEFE TIERVMDCRV GRKGATGATT TIYAVEADGD
PNAGFERNKE PGDIQYLIKW KGWSHIHNTW ETEETLKQQN VRGMKKLDNY KKKDQETKRW
LKNASPEDVE YYNCQQELTD DLHKQYQIVE RIIAHSNQKS AAGLPDYYCK WQGLPYSECS
WEDGALISKK FQTCIDEYFS RNQSKTTPFK DCKVLKQRPR FVALKKQPSY IGGHEGLELR
DYQLNGLNWL AHSWCKGNSC ILADEMGLGK TIQTISFLNY LFHEHQLYGP FLLVVPLSTL
TSWQREIQTW ASQMNAVVYL GDINSRNMIR THEWMHPQTK RLKFNILLTT YEILLKDKAF
LGGLNWAFIG VDEAHRLKND DSLLYKTLID FKSNHRLLIT GTPLQNSLKE LWSLLHFIMP
EKFSSWEDFE EEHGKGREYG YASLHKELEP FLLRRVKKDV EKSLPAKVEQ ILRMEMSALQ
KQYYKWILTR NYKALSKGSK GSTSGFLNIM MELKKCCNHC YLIKPPDNNE FYNKQEALQH
LIRSSGKLIL LDKLLIRLRE RGNRVLIFSQ MVRMLDILAE YLKYRQFPFQ RLDGSIKGEL
RKQALDHFNA EGSEDFCFLL STRAGGLGIN LASADTVVIF DSDWNPQNDL QAQARAHRIG
QKKQVNIYRL VTKGSVEEDI LERAKKKMVL DHLVIQRMDT TGKTVLHTGS APSSSTPFNK
EELSAILKFG AEELFKEPEG EEQEPQEMDI DEILKRAETH ENEPGPLSVG DELLSQFKVA
NFSNMDEDDI ELEPERNSKN WEEIIPEEQR RRLEEEERQK ELEEIYMLPR MRNCAKQISF
NGSEGRRSRS RRYSGSDSDS ISERKRPKKR GRPRTIPREN IKGFSDAEIR RFIKSYKKFG
GPLERLDAIA RDAELVDKSE TDLRRLGELV HNGCVKALKD SSSGTERAGG RLGKVKGPTF
RISGVQVNAK LVIAHEDELI PLHKSIPSDP EERKQYTIPC HTKAAHFDID WGKEDDSNLL
IGIYEYGYGS WEMIKMDPDL SLTHKILPDD PDKKPQAKQL QTRADYLIKL LSRDLAKREA
QRLCGAGGSK RRKTRAKKSK AMKSIKVKEE IKSDSSPLPS EKSDEDDDKL NDSKPESKDR
SKKSVVSDAP VHITASGEPV PIAEESEELD QKTFSICKER MRPVKAALKQ LDRPEKGLSE
REQLEHTRQC LIKIGDHITE CLKEYSNPEQ IKQWRKNLWI FVSKFTEFDA RKLHKLYKHA
IKKRQESQQN SDQNSNVATT HVIRNPDMER LKENTNHDDS SRDSYSSDRH LSQYHDHHKD
RHQGDSYKKS DSRKRPYSSF SNGKDHREWD HYRQDSRYYS DREKHRKLDD HRSREHRPSL
EGGLKDRCHS DHRSHSDHRM HSDHRSSSEH THHKSSRDYR YLSDWQLDHR AASSGPRSPL
DQRSPYGSRS PFEHSAEHRS TPEHTWSSRK T
