CHD2_MOUSE
ID CHD2_MOUSE Reviewed; 1827 AA.
AC E9PZM4;
DT 22-JAN-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 2;
DE Short=CHD-2;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent helicase CHD2;
GN Name=Chd2;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=16810678; DOI=10.1002/jcp.20718;
RA Marfella C.G., Ohkawa Y., Coles A.H., Garlick D.S., Jones S.N.,
RA Imbalzano A.N.;
RT "Mutation of the SNF2 family member Chd2 affects mouse development and
RT survival.";
RL J. Cell. Physiol. 209:162-171(2006).
RN [3]
RP ERRATUM OF PUBMED:16810678.
RA Marfella C.G., Ohkawa Y., Coles A.H., Garlick D.S., Jones S.N.,
RA Imbalzano A.N.;
RL J. Cell. Physiol. 212:562-562(2007).
RN [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=19142019; DOI=10.1159/000190788;
RA Marfella C.G., Henninger N., LeBlanc S.E., Krishnan N., Garlick D.S.,
RA Holzman L.B., Imbalzano A.N.;
RT "A mutation in the mouse Chd2 chromatin remodeling enzyme results in a
RT complex renal phenotype.";
RL Kidney Blood Press. Res. 31:421-432(2008).
RN [5]
RP DISRUPTION PHENOTYPE.
RX PubMed=19137022; DOI=10.1038/onc.2008.440;
RA Nagarajan P., Onami T.M., Rajagopalan S., Kania S., Donnell R.,
RA Venkatachalam S.;
RT "Role of chromodomain helicase DNA-binding protein 2 in DNA damage response
RT signaling and tumorigenesis.";
RL Oncogene 28:1053-1062(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; THR-240 AND SER-242, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, 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).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DNA-BINDING.
RX PubMed=22569126; DOI=10.1038/emboj.2012.136;
RA Harada A., Okada S., Konno D., Odawara J., Yoshimi T., Yoshimura S.,
RA Kumamaru H., Saiwai H., Tsubota T., Kurumizaka H., Akashi K., Tachibana T.,
RA Imbalzano A.N., Ohkawa Y.;
RT "Chd2 interacts with H3.3 to determine myogenic cell fate.";
RL EMBO J. 31:2994-3007(2012).
CC -!- FUNCTION: DNA-binding helicase that specifically binds to the promoter
CC of target genes, leading to chromatin remodeling, possibly by promoting
CC deposition of histone H3.3. Involved in myogenesis via interaction with
CC MYOD1: binds to myogenic gene regulatory sequences and mediates
CC incorporation of histone H3.3 prior to the onset of myogenic gene
CC expression, promoting their expression. {ECO:0000269|PubMed:22569126}.
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 MYOD1. Interacts with histone H3.3.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22569126}. Note=Binds
CC to myogenic gene promoters.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:16810678}.
CC -!- DISRUPTION PHENOTYPE: Growth delay late in embryogenesis and perinatal
CC lethality (PubMed:16810678). Heterozygous mice show decreased neonatal
CC viability. Heterozygous mice display glomerulopathy, proteinuria and
CC impaired kidney function. Glomerulopathy may be associated with anemia
CC (PubMed:19142019). Heterozygous mutant also show increased
CC extramedullary hematopoiesis and susceptibility to lymphomas, with
CC defects in hematopoietic stem cell differentiation (PubMed:19137022).
CC {ECO:0000269|PubMed:16810678, ECO:0000269|PubMed:19137022,
CC ECO:0000269|PubMed:19142019}.
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DR EMBL; AC099699; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC154883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS52274.1; -.
DR RefSeq; NP_001074814.2; NM_001081345.2.
DR AlphaFoldDB; E9PZM4; -.
DR SMR; E9PZM4; -.
DR BioGRID; 232602; 4.
DR IntAct; E9PZM4; 1.
DR MINT; E9PZM4; -.
DR STRING; 10090.ENSMUSP00000126352; -.
DR iPTMnet; E9PZM4; -.
DR PhosphoSitePlus; E9PZM4; -.
DR EPD; E9PZM4; -.
DR jPOST; E9PZM4; -.
DR MaxQB; E9PZM4; -.
DR PaxDb; E9PZM4; -.
DR PeptideAtlas; E9PZM4; -.
DR PRIDE; E9PZM4; -.
DR ProteomicsDB; 281208; -.
DR Ensembl; ENSMUST00000169922; ENSMUSP00000126352; ENSMUSG00000078671.
DR GeneID; 244059; -.
DR KEGG; mmu:244059; -.
DR UCSC; uc009hrd.2; mouse.
DR CTD; 1106; -.
DR MGI; MGI:2448567; Chd2.
DR VEuPathDB; HostDB:ENSMUSG00000078671; -.
DR eggNOG; KOG0384; Eukaryota.
DR GeneTree; ENSGT00940000155888; -.
DR HOGENOM; CLU_000315_8_1_1; -.
DR InParanoid; E9PZM4; -.
DR OMA; CDTFNNW; -.
DR OrthoDB; 57339at2759; -.
DR PhylomeDB; E9PZM4; -.
DR TreeFam; TF313461; -.
DR BioGRID-ORCS; 244059; 9 hits in 77 CRISPR screens.
DR ChiTaRS; Chd2; mouse.
DR PRO; PR:E9PZM4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; E9PZM4; protein.
DR Bgee; ENSMUSG00000078671; Expressed in ear vesicle and 255 other tissues.
DR ExpressionAtlas; E9PZM4; baseline and differential.
DR Genevisible; E9PZM4; MM.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:MGI.
DR GO; GO:0007517; P:muscle organ development; IMP:UniProtKB.
DR GO; GO:0034728; P:nucleosome organization; IBA:GO_Central.
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; DNA-binding; Helicase; Hydrolase;
KW Myogenesis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1827
FT /note="Chromodomain-helicase-DNA-binding protein 2"
FT /id="PRO_0000425206"
FT DOMAIN 261..353
FT /note="Chromo 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 378..456
FT /note="Chromo 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DOMAIN 496..666
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 795..946
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1329..1465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1679..1827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 617..620
FT /note="DEAH box"
FT COMPBIAS 14..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..200
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..251
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1079..1124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1556..1577
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1586..1604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1622..1638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1797..1812
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1813..1827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 509..516
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 207
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 208
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14647"
FT MOD_RES 240
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1085
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14647"
FT MOD_RES 1087
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14647"
FT MOD_RES 1365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14647"
FT MOD_RES 1386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14647"
FT MOD_RES 1806
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14647"
SQ SEQUENCE 1827 AA; 210804 MW; 60B317C82F373453 CRC64;
MMRNKDKSQE EDSSLHSNAS SRSASEEVSG SDSGSQSESE QGSEPGSGHG SESNSSSESS
ESQSESESES AGSKSQPVLP EAKEKPASKK ERIADVKKMW EEYPDVYGVR RSNRSRQEPS
RFNVKEEASS GSESGSPKRR GQRQLKKQEK WKQDPSEDEQ EQGTSAESEA EQKKGKARRP
VPRRTVPKPQ VKKQPKIQRG KRKKQESSDD DDDDDEAPKR QTRRRAAKNV SYKEDDDFET
DSDDLIEMTG EGGDEQQDNS ETIEKVLDSR LGKKGATGAS TTVYAVEANG DPSDDFDTER
EEGEVQYLIK WKGWSYIHST WESEDSLQQQ KVKGLKKLEN FKKKEDEVKQ WLGKVSPEDV
EYFSCQQELA SELNKQYQIV ERVIAVKTSK STLGQTDFPA HSRKPAPSNE PEYLCKWMGL
PYSECSWEDE ALIGKKFQNC IDSFHSRNNS KTIPTRECKA LKQRPRFVAL KKQPAYLGGE
SLELRDYQLE GLNWLAHSWC KSNSVILADE MGLGKTIQTI SFLSYLFHQH QLYGPFLIVV
PLSTLTSWQR EFEIWAPEIN VVVYIGDLMS RNTIREYEWI HSQTKRLKFN ALITTYEILL
KDKTVLGSIN WAFLGVDEAH RLKNDDSLLY KTLIDFKSNH RLLITGTPLQ NSLKELWSLL
HFIMPEKFEF WEDFEEDHGK GRENGYQSLH KVLEPFLLRR VKKDVEKSLP AKVEQILRVE
MSALQKQYYK WILTRNYKAL AKGTRGSTSG FLNIVMELKK CCNHCYLIKA PEDSERESGQ
EVLQSLIRSS GKLILLDKLL TRLRERGNRV LIFSQMVRML DILAEYLTIK HYPFQRLDGS
IKGEIRKQAL DHFNADGSED FCFLLSTRAG GLGINLASAD TVVIFDSDWN PQNDLQAQAR
AHRIGQKKQV NIYRLVTKGT VEEEIIERAK KKMVLDHLVI QRMDTTGRTV LENNSGRSNS
NPFNKEELTA ILKFGAEDLF KEIEGEESEP QEMDIDEILR LAETRENEVS TSATDELLSQ
FKVANFATME DEEELEERPH KDWDEIIPEE QRKKVEEEER QKELEEIYML PRIRSSTKKA
QTNDSDSDTE SKRQAQRSSA SESETDDSDD DKKPKRRGRP RSVRKDLVEG FTDAEIRRFI
KAYKKFGLPL ERLECIARDA ELVDKSVADL KRLGELIHNS CVSAMQEYEE QLKESTSEGK
GPGKRRGPTI KISGVQVNVK SIIQHEEEFE MLHKSIPVDP EEKKKYCLTC RVKAAHFDVE
WGVEDDSRLL LGIYEHGYGN WELIKTDPEL KLTDKILPVE TDKKPQGKQL QTRVDYLLKL
LRKGLEKKGT VASGEEAKLK KRKPRVKKEN KAPRLKDEHG LEPASPRHSD NPSEEGEVKD
DGLEKSPTKK KQKKKENKEN KEKPVSSRKD REGDKERKKS KDKKEKVKGG DGKSSSKSKR
SQGPVHITAG SEPVPIGEDE DDDLDQETFS ICKERMRPVK KALKQLDKPD KGLSVQEQLE
HTRNCLLKIG DRIAECLKAY SDQEHIKLWR RNLWIFVSKF TEFDARKLHK LYKMAHKKRS
QEEEEQKKKD DSLGGKKPFR PEASGSSRDS LISQSHTSHN LHPQKPHLPA SHGPQMHGHP
RDNYSHPNKR HFSNADRGDW QRERKFNYGG GNSAPWGGDR HHQYEQHWYK DHHYGDRRHM
DAHRSGSYRP NNMSRKRPYE QYNSDRDHRG HRDYYDRHHH DSKRRRSDDF RPQNYHQQDF
RRMSDHRPTM GYHGQGPSDH YRSFHTDKLG EYKQPMPSLH TALSDPRSPP SQKSPHDSKS
PLDHRSPLER SLEQKNNPDY NWNVRKT
