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Q09XV5 (CHD8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromodomain-helicase-DNA-binding protein 8

Short name=CHD-8
EC=3.6.4.12
Alternative name(s):
ATP-dependent helicase CHD8
Axis duplication inhibitor
Short name=Duplin
Gene names
Name:Chd8
Synonyms:Kiaa1564
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2582 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

DNA helicase that acts as a chromatin remodeling factor and regulates transcription. Acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. Suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity. Acts as a negative regulator of Wnt signaling pathway by regulating beta-catenin (CTNNB1) activity. Negatively regulates CTNNB1-targeted gene expression by being recruited specifically to the promoter regions of several CTNNB1 responsive genes. Involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. Acts as a suppressor of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. Also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. Ref.1 Ref.6

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with CHD7 By similarity. Interacts with p53/TP53, histone H1, CTNNB1, CTCF and PIAS3. Component of a multiprotein complex of 900 kDa containing WDR5. Ref.1 Ref.6

Subcellular location

Nucleus. Note: Localizes to the promoter regions of several CTNNB1-responsive genes. Also present at known CTCF target sites. Ref.1

Developmental stage

Expressed predominantly from early- to mid-stage mouse embryogenesis. Detected throughout embryos from E7.5 to E9.5 but localizes predominantly in the brain, faces, branchial arches, limb buds, and tail buds of embryos at E10.5. Ref.2

Post-translational modification

Sumoylated By similarity.

Disruption phenotype

Death during early embryogenesis due to widespread apoptosis. Embryos manifest growth retardation from E5.5 and developmental arrest accompanied by massive apoptosis at E7.5. They develop into an egg cylinder but do not form a primitive streak or mesoderm. Mice lacking both Tp53 and Chd8 ameliorate this developmental arrest. Ref.2 Ref.6

Sequence similarities

Belongs to the SNF2/RAD54 helicase family. CHD8 subfamily.

Contains 2 chromo domains.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Sequence caution

The sequence BAC98203.2 differs from that shown. Reason: Partially unspliced pre-RNA.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
Wnt signaling pathway
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionActivator
Chromatin regulator
Helicase
Hydrolase
Repressor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from sequence or structural similarity. Source: GOC

ATP-dependent chromatin remodeling

Inferred from sequence or structural similarity. Source: UniProtKB

canonical Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

in utero embryonic development

Inferred from mutant phenotype Ref.2. Source: MGI

negative regulation of Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from direct assay Ref.6. Source: UniProtKB

negative regulation of fibroblast apoptotic process

Inferred from direct assay Ref.6. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.6. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase III promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentMLL1 complex

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionATP binding

Inferred from sequence or structural similarity. Source: UniProtKB

DNA binding

Inferred from direct assay Ref.6. Source: UniProtKB

DNA helicase activity

Inferred from sequence or structural similarity. Source: UniProtKB

DNA-dependent ATPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

beta-catenin binding

Inferred from sequence or structural similarity. Source: UniProtKB

histone binding

Inferred from direct assay Ref.6. Source: UniProtKB

methylated histone binding

Inferred from sequence or structural similarity. Source: UniProtKB

p53 binding

Inferred from physical interaction Ref.6. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.1. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CtcfQ611643EBI-1169080,EBI-932785

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q09XV5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q09XV5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     745-751: PVIYYLV → VSWARRT
     752-2582: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25822582Chromodomain-helicase-DNA-binding protein 8
PRO_0000367310

Regions

Domain644 – 71168Chromo 1
Domain726 – 79267Chromo 2
Domain825 – 999175Helicase ATP-binding
Domain1139 – 1290152Helicase C-terminal
Nucleotide binding838 – 8458ATP By similarity
Motif950 – 9534DEAH box
Compositional bias292 – 412121Gln-rich
Compositional bias1777 – 17815Poly-Arg
Compositional bias2070 – 209930Ser-rich
Compositional bias2494 – 250916His-rich
Compositional bias2539 – 258244Asp-rich

Amino acid modifications

Modified residue5551Phosphoserine By similarity
Modified residue5641Phosphoserine By similarity
Modified residue14221Phosphoserine By similarity
Modified residue14261Phosphoserine By similarity
Modified residue19781Phosphoserine By similarity
Modified residue19951Phosphothreonine By similarity
Modified residue20101Phosphoserine By similarity
Modified residue20401Phosphoserine Ref.5
Modified residue20701Phosphoserine By similarity
Modified residue20721Phosphoserine By similarity
Modified residue21841Phosphoserine By similarity
Modified residue22021Phosphoserine By similarity
Modified residue22131Phosphoserine By similarity
Modified residue25201Phosphoserine By similarity
Cross-link611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence745 – 7517PVIYYLV → VSWARRT in isoform 2.
VSP_036676
Alternative sequence752 – 25821831Missing in isoform 2.
VSP_036677

Experimental info

Sequence conflict211T → A in AAW56421. Ref.2
Sequence conflict20201N → S in BAC98203. Ref.3
Sequence conflict22981L → V in BAC98203. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: D9432500F6A8C329

FASTA2,582290,847
        10         20         30         40         50         60 
MADPIMDLFD DPNLFGLDSL TDDSFNQVTQ DPIEEALGLP SSLDSLDQMN QDGGGGDVGN 

        70         80         90        100        110        120 
SSASDLVPPP EETASTELPK ESTAPAPESL TLHDYTTQPT SQEQPAQPVL QTSTPTAGLL 

       130        140        150        160        170        180 
QVSKSQEILS QGNPFMGVSA TGVSPSNTGG QPSQSAPKIV ILKAPPNSSV TGTHVAQIQA 

       190        200        210        220        230        240 
QGITSTAQPL VAGTANGGKV TFTKVLTGTP LRPGVSIVSG NTVLATKVPG NQAAVQRIVQ 

       250        260        270        280        290        300 
PSRPVKQLVL QPVKGSAPAG NPGAAGPPLK PAVTLTSTPT QGESKRITLV LQQPQSGGPQ 

       310        320        330        340        350        360 
GHRHVVLGSL PGKIVLQGNQ LAALTQAKNA QGQPAKVVTI QLQVQQPQQK IQIVPQPPSS 

       370        380        390        400        410        420 
QPQPQPQPPP SAQPLTLSSV QQAQIMGPGQ NPGQRLSVPL KMVLQPQAGS SQGASSGLSV 

       430        440        450        460        470        480 
VKVLSASEVA ALSSPASCAP HTAGKTGMEE NRRLEHQKKQ EKANRIVAEA IARARARGEQ 

       490        500        510        520        530        540 
NIPRVLNEDE LPSVRPEEEG EKKRRKKSSG ERLKEEKPKK SKTAAASKTK GKSKLNTITP 

       550        560        570        580        590        600 
VVGKKRKRNT SSDNSDVEVM PAQSPREDEE SSIQKRRSNR QVKRKKYTED LDIKITDDEE 

       610        620        630        640        650        660 
EEEVDVTGPI KPEPILPEPV QEPDGETLPS MQFFVENPSE EDAAIVDKVL SMRVVKKELP 

       670        680        690        700        710        720 
SGQYTEAEEF FVKYKNYSYL HCEWATISQL EKDKRIHQKL KRFKTKMAQM RHFFHEDEEP 

       730        740        750        760        770        780 
FNPDYVEVDR ILDESHSVDK DNGEPVIYYL VKWCSLPYED STWELKEDVD EGKIREFKRI 

       790        800        810        820        830        840 
QSRHPELRRV NRPQANAWKK LELSHEYKNR NQLREYQLEG VNWLLFNWYN RQNCILADEM 

       850        860        870        880        890        900 
GLGKTIQSIA FLQEVYNVGI HGPFLVIAPL STITNWEREF NTWTEMNTIV YHGSLASRQM 

       910        920        930        940        950        960 
IQQYEMYCKD SRGRLIPGAY KFDALITTFE MILSDCPELR EIEWRCVIID EAHRLKNRNC 

       970        980        990       1000       1010       1020 
KLLDSLKHMD LEHKVLLTGT PLQNTVEELF SLLHFLEPSQ FPSESEFLKD FGDLKTEEQV 

      1030       1040       1050       1060       1070       1080 
QKLQAILKPM MLRRLKEDVE KNLAPKQETI IEVELTNIQK KYYRAILEKN FSFLSKGAGH 

      1090       1100       1110       1120       1130       1140 
TNMPNLLNTM MELRKCCNHP YLINGAEEKI LMEFREACHI IPQDFHLQAM VRSAGKLVLI 

      1150       1160       1170       1180       1190       1200 
DKLLPKLKAG GHKVLIFSQM VRCLDILEDY LIQRRYLYER IDGRVRGNLR QAAIDRFSKP 

      1210       1220       1230       1240       1250       1260 
DSDRFVFLLC TRAGGLGINL TAADTCIIFD SDWNPQNDLQ AQARCHRIGQ SKAVKVYRLI 

      1270       1280       1290       1300       1310       1320 
TRNSYEREMF DKASLKLGLD KAVLQSMSGR DGNITGIQQF SKKEIEDLLR KGAYAAIMEE 

      1330       1340       1350       1360       1370       1380 
DDEGSKFCEE DIDQILLRRT TTITIESEGK GSTFAKASFV ASENRTDISL DDPNFWQKWA 

      1390       1400       1410       1420       1430       1440 
KKADLDMDLL NSKNNLVIDT PRVRKQTRHF STLKDDDLVE FSDLESEDDE RPRSRRHDRH 

      1450       1460       1470       1480       1490       1500 
HTYGRTDCFR VEKHLLVYGW GRWRDILSHG RFKRRMTERD VETICRAILV YCLLHYRGDE 

      1510       1520       1530       1540       1550       1560 
NIKSFIWDLI SPAENGKTKE LQNHSGLSIP VPRGRKGKKV KSQSTFDIHK ADWIRKYNPD 

      1570       1580       1590       1600       1610       1620 
TLFQDESYKK HLKHQCNKVL LRVRMLYYLR QEVIGDQAEK VLGGAIASEI DIWFPVVDQL 

      1630       1640       1650       1660       1670       1680 
EVPTTWWDSE ADKSLLIGVF KHGYEKYNTM RADPALCFLE KAGRPDDKAI AAEHRVLDNF 

      1690       1700       1710       1720       1730       1740 
SDLVEGIDFD KDCEDPEYKP LQGPPKDPDD EGDPLMMMDE EISVIDGEEA QVTQQPGHLF 

      1750       1760       1770       1780       1790       1800 
WPPGSALTAR LRRLVTAYQR SYKREQMKME AAERGDRRRR RCEAAFKLKE IARREKQQRW 

      1810       1820       1830       1840       1850       1860 
TRREQTDFYR VVSTFGVEYD PDNMQFHWDR FRTFARLDKK TDESLTKYFH GFVAMCRQVC 

      1870       1880       1890       1900       1910       1920 
RLPPAAGDEP PDPNLFIEPI TEERASRTLY RIELLRRLRE QVLCHPLLED RLALCQPPGL 

      1930       1940       1950       1960       1970       1980 
ELPKWWEPVR HDGELLRGAA RHGVSQTDCN IMQDPDFSFL AARMNYMQNH QAGASAASLS 

      1990       2000       2010       2020       2030       2040 
RCSTPLLHQQ CTSRTASPSP LRPDAPVEKS PEESTVQVPN LESLTLKLED EVVARSRLTS 

      2050       2060       2070       2080       2090       2100 
QDYEVRVGSS DTAPLSRSVP PVKLEDEDDS DSELDLSKLS PSSSSSSSSS SSSSSTDESE 

      2110       2120       2130       2140       2150       2160 
DEKEEKLTAD RSRPKLYDEE SLLSLTMSQD GFPNEDGEQM TPELLLLQER QRASEWPKDR 

      2170       2180       2190       2200       2210       2220 
VLINRIDLVC QAVLSGKWPS NRRSQEVTAG GILGPGNHLL DSPSLTPGED GDSPVPTPRS 

      2230       2240       2250       2260       2270       2280 
GSAASMAEEE ASAVTTAAAQ FTKLRRGMDE KEFTVQIKDE EGLKLTFQKH RLMANGVMGD 

      2290       2300       2310       2320       2330       2340 
GHPLFHKKKG NRKKLVELEV ECMEEPNHLD LDLETRIPVI NKVDGTLLVG DEAPRRAELE 

      2350       2360       2370       2380       2390       2400 
MWLQGHPEFA VDPRFLAYME ERRKQKWQRC KKNNKAELNC LGMEPVQPAN SRNGKKGHYA 

      2410       2420       2430       2440       2450       2460 
ETAFNRVLPG PVAPENSKKR VRRTRPDLSK MMALMQGGST GSLSLHNTFQ HSSSNLQSVS 

      2470       2480       2490       2500       2510       2520 
SLGHSSTTSA SLPFMPFVMG AAAPPHVDSS TMLHHHHHHP HPHHHHHHHP GLRTTGYPSS 

      2530       2540       2550       2560       2570       2580 
PATTTSGTAL RLPTLQPEDD DEEEDEEDDD LSQGYDSSER DFSLIDDPMM PANSDSSEDA 


DD 

« Hide

Isoform 2 [UniParc].

Checksum: 23F272C1595F2A90
Show »

FASTA75180,950

References

« Hide 'large scale' references
[1]"CTCF-dependent chromatin insulator is linked to epigenetic remodeling."
Ishihara K., Oshimura M., Nakao M.
Mol. Cell 23:733-742(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CTCF, SUBCELLULAR LOCATION.
Tissue: Embryo.
[2]"Early embryonic death in mice lacking the beta-catenin-binding protein Duplin."
Nishiyama M., Nakayama K., Tsunematsu R., Tsukiyama T., Kikuchi A., Nakayama K.I.
Mol. Cell. Biol. 24:8386-8394(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1730-2582.
Tissue: Brain.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2020-2582.
Strain: C57BL/6J.
Tissue: Thymus.
[5]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2040, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"CHD8 suppresses p53-mediated apoptosis through histone H1 recruitment during early embryogenesis."
Nishiyama M., Oshikawa K., Tsukada Y.I., Nakagawa T., Iemura S., Natsume T., Fan Y., Kikuchi A., Skoultchi A.I., Nakayama K.I.
Nat. Cell Biol. 11:172-182(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH TP53 AND HISTONE H1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ190419 mRNA. Translation: ABB02259.1.
AY863219 mRNA. Translation: AAW56421.1.
AK129393 Transcribed RNA. Translation: BAC98203.2. Sequence problems.
AK160299 mRNA. Translation: BAE35730.1.
CCDSCCDS36919.1. [Q09XV5-1]
RefSeqNP_963999.2. NM_201637.2. [Q09XV5-1]
XP_006519539.1. XM_006519476.1. [Q09XV5-1]
UniGeneMm.289934.

3D structure databases

ProteinModelPortalQ09XV5.
SMRQ09XV5. Positions 653-781, 790-1286, 2305-2374.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid212432. 4 interactions.
IntActQ09XV5. 1 interaction.

PTM databases

PhosphoSiteQ09XV5.

Proteomic databases

PaxDbQ09XV5.
PRIDEQ09XV5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000089752; ENSMUSP00000087184; ENSMUSG00000053754. [Q09XV5-1]
GeneID67772.
KEGGmmu:67772.
UCSCuc007tot.1. mouse. [Q09XV5-1]
uc007tov.1. mouse. [Q09XV5-2]

Organism-specific databases

CTD57680.
MGIMGI:1915022. Chd8.
RougeSearch...

Phylogenomic databases

eggNOGCOG0553.
GeneTreeENSGT00560000077077.
HOGENOMHOG000246942.
HOVERGENHBG107676.
InParanoidQ09XV5.
KOK04494.
OMAFLAYMED.
OrthoDBEOG7NSB1C.
TreeFamTF313572.

Gene expression databases

BgeeQ09XV5.
GenevestigatorQ09XV5.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR006576. BRK_domain.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PfamPF07533. BRK. 2 hits.
PF00385. Chromo. 2 hits.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00592. BRK. 2 hits.
SM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 2 hits.
PROSITEPS50013. CHROMO_2. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCHD8. mouse.
NextBio325525.
PROQ09XV5.
SOURCESearch...

Entry information

Entry nameCHD8_MOUSE
AccessionPrimary (citable) accession number: Q09XV5
Secondary accession number(s): Q3TV89, Q5I1Z2, Q6ZPM8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot