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Database: UniProt
Entry: P40201
LinkDB: P40201
Original site: P40201 
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   16-OCT-2019, entry version 159.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   project: 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
RT   its ATPase/helicase-like domain for proper association with
RT   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.,
RA   Meshorer E., Ramalho-Santos M.;
RT   "Chd1 regulates open chromatin and pluripotency of embryonic stem
RT   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
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: ATP-dependent chromatin-remodeling factor which
CC       functions as substrate recognition component of the transcription
CC       regulatory histone acetylation (HAT) complex SAGA. Regulates
CC       polymerase II transcription. Also required for efficient
CC       transcription by RNA polymerase I, and more specifically the
CC       polymerase I transcription termination step. Regulates negatively
CC       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
CC       bridging of SNF2, the FACT complex, the PAF complex as well as the
CC       U2 snRNP complex to H3K4me3. Functions to modulate the efficiency
CC       of pre-mRNA splicing in part through physical bridging of
CC       spliceosomal components to H3K4me3 (By similarity). Required for
CC       maintaining open chromatin and pluripotency in embryonic stem
CC       cells (PubMed:19587682). Is also associated with histone
CC       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).
CC       Specifically interacts with methylated H3K4me2 and H3K4me3.
CC       Interacts with the FACT complex, the PAF complex and the U2 snRNP.
CC       Interacts directly with PAF1, SFA3A1, SFA3A2, SFA3A3, SNF2 and
CC       SSRP1 (By similarity). Interacts with BCLAF1, NCoR, SRP20 and
CC       SAFB. {ECO:0000250, ECO:0000269|PubMed:10199952,
CC       ECO:0000269|PubMed:12890497, ECO:0000269|PubMed:19587682}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10199952,
CC       ECO:0000269|PubMed:7739555}. Cytoplasm
CC       {ECO:0000269|PubMed:7739555}. Note=Is released into the cytoplasm
CC       when cells enter mitosis and is reincorporated into chromatin
CC       during telophase-cytokinesis (PubMed:7739555).
CC   -!- TISSUE SPECIFICITY: Abundance is higher in cells representing
CC       early stages of the B-lymphoid lineage such as pre-B and B-cells,
CC       than in cells representing mature plasmacytes or other cell
CC       lineages such as fibroblasts.
CC   -!- DOMAIN: The 2 chromodomains are involved in the binding to the
CC       histone H3 methyllysine at position 4 (H3K4me3). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
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   SMR; P40201; -.
DR   BioGrid; 198693; 3.
DR   IntAct; P40201; 2.
DR   MINT; P40201; -.
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   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   eggNOG; KOG0383; Eukaryota.
DR   eggNOG; COG0553; LUCA.
DR   GeneTree; ENSGT00940000156579; -.
DR   HOGENOM; HOG000207917; -.
DR   InParanoid; P40201; -.
DR   KO; K11367; -.
DR   OMA; PAWQETF; -.
DR   OrthoDB; 57339at2759; -.
DR   TreeFam; TF300674; -.
DR   ChiTaRS; Chd1; mouse.
DR   PRO; PR:P40201; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   Bgee; ENSMUSG00000023852; Expressed in 288 organ(s), highest expression level in blastocyst.
DR   ExpressionAtlas; P40201; baseline and differential.
DR   Genevisible; P40201; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003682; F:chromatin binding; NAS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004386; F:helicase activity; NAS:UniProtKB.
DR   GO; GO:0035064; F:methylated histone binding; ISO:MGI.
DR   GO; GO:0006333; P:chromatin assembly or disassembly; NAS:UniProtKB.
DR   GO; GO:0006338; P:chromatin remodeling; IGI:MGI.
DR   GO; GO:0016569; P:covalent chromatin modification; ISO:MGI.
DR   GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI.
DR   Gene3D; 3.40.50.10810; -; 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_N; 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; Complete proteome; Cytoplasm;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   1711       Chromodomain-helicase-DNA-binding protein
FT                                1.
FT                                /FTId=PRO_0000080225.
FT   DOMAIN      270    362       Chromo 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      387    450       Chromo 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00053}.
FT   DOMAIN      491    661       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      790    941       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   REPEAT     1629   1633       1.
FT   REPEAT     1635   1639       2.
FT   REPEAT     1641   1645       3.
FT   NP_BIND     504    511       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION     1629   1645       3 X 5 AA repeats of H-S-D-H-R.
FT   MOTIF       612    615       DEAH box.
FT   COMPBIAS      1     70       Ser-rich.
FT   COMPBIAS    116    136       Ser-rich.
FT   MOD_RES     214    214       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     215    215       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     235    235       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES     239    239       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES     248    248       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES     250    250       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES     469    469       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES    1023   1023       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES    1038   1038       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES    1079   1079       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES    1083   1083       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14647}.
FT   MOD_RES    1094   1094       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES    1096   1096       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES    1098   1098       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES    1100   1100       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES    1159   1159       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES    1353   1353       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES    1355   1355       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES    1356   1356       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES    1360   1360       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES    1363   1363       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES    1373   1373       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14647}.
FT   MOD_RES    1678   1678       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   MOD_RES    1690   1690       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O14646}.
FT   CONFLICT    159    159       S -> L (in Ref. 1; AAB08486).
FT                                {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
//
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