Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q09XV5

- CHD8_MOUSE

UniProt

Q09XV5 - CHD8_MOUSE

Protein

Chromodomain-helicase-DNA-binding protein 8

Gene

Chd8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (17 Oct 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.2 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi838 – 8458ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. beta-catenin binding Source: UniProtKB
    3. DNA binding Source: UniProtKB
    4. DNA-dependent ATPase activity Source: UniProtKB
    5. DNA helicase activity Source: UniProtKB
    6. histone binding Source: UniProtKB
    7. methylated histone binding Source: UniProtKB
    8. p53 binding Source: UniProtKB
    9. protein binding Source: IntAct

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. ATP-dependent chromatin remodeling Source: UniProtKB
    3. canonical Wnt signaling pathway Source: UniProtKB
    4. in utero embryonic development Source: MGI
    5. negative regulation of apoptotic process Source: UniProtKB
    6. negative regulation of fibroblast apoptotic process Source: MGI
    7. negative regulation of transcription, DNA-templated Source: UniProtKB
    8. negative regulation of Wnt signaling pathway Source: UniProtKB
    9. positive regulation of transcription, DNA-templated Source: UniProtKB
    10. positive regulation of transcription from RNA polymerase III promoter Source: UniProtKB
    11. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    12. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Helicase, Hydrolase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation, Wnt signaling pathway

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromodomain-helicase-DNA-binding protein 8 (EC:3.6.4.12)
    Short name:
    CHD-8
    Alternative name(s):
    ATP-dependent helicase CHD8
    Axis duplication inhibitor
    Short name:
    Duplin
    Gene namesi
    Name:Chd8
    Synonyms:Kiaa1564
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:1915022. Chd8.

    Subcellular locationi

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

    GO - Cellular componenti

    1. MLL1 complex Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    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.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 25822582Chromodomain-helicase-DNA-binding protein 8PRO_0000367310Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei555 – 5551PhosphoserineBy similarity
    Modified residuei564 – 5641PhosphoserineBy similarity
    Cross-linki611 – 611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei1422 – 14221PhosphoserineBy similarity
    Modified residuei1426 – 14261PhosphoserineBy similarity
    Modified residuei1978 – 19781PhosphoserineBy similarity
    Modified residuei1995 – 19951PhosphothreonineBy similarity
    Modified residuei2010 – 20101PhosphoserineBy similarity
    Modified residuei2040 – 20401Phosphoserine1 Publication
    Modified residuei2070 – 20701PhosphoserineBy similarity
    Modified residuei2072 – 20721PhosphoserineBy similarity
    Modified residuei2184 – 21841PhosphoserineBy similarity
    Modified residuei2202 – 22021PhosphoserineBy similarity
    Modified residuei2213 – 22131PhosphoserineBy similarity
    Modified residuei2520 – 25201PhosphoserineBy similarity

    Post-translational modificationi

    Sumoylated.By similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ09XV5.
    PRIDEiQ09XV5.

    PTM databases

    PhosphoSiteiQ09XV5.

    Expressioni

    Developmental stagei

    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 E10.5.1 Publication

    Gene expression databases

    BgeeiQ09XV5.
    GenevestigatoriQ09XV5.

    Interactioni

    Subunit structurei

    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.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CtcfQ611643EBI-1169080,EBI-932785

    Protein-protein interaction databases

    BioGridi212432. 4 interactions.
    IntActiQ09XV5. 1 interaction.

    Structurei

    3D structure databases

    ProteinModelPortaliQ09XV5.
    SMRiQ09XV5. Positions 653-781, 790-1286, 2305-2374.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini644 – 71168Chromo 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini726 – 79267Chromo 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini825 – 999175Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1139 – 1290152Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi950 – 9534DEAH box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi292 – 412121Gln-richAdd
    BLAST
    Compositional biasi1777 – 17815Poly-Arg
    Compositional biasi2070 – 209930Ser-richAdd
    BLAST
    Compositional biasi2494 – 250916His-richAdd
    BLAST
    Compositional biasi2539 – 258244Asp-richAdd
    BLAST

    Sequence similaritiesi

    Contains 2 chromo domains.PROSITE-ProRule annotation
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0553.
    GeneTreeiENSGT00560000077077.
    HOGENOMiHOG000246942.
    HOVERGENiHBG107676.
    InParanoidiQ09XV5.
    KOiK04494.
    OMAiFLAYMED.
    OrthoDBiEOG7NSB1C.
    TreeFamiTF313572.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR006576. 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]
    PfamiPF07533. BRK. 2 hits.
    PF00385. Chromo. 2 hits.
    PF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view]
    SMARTiSM00592. BRK. 2 hits.
    SM00298. CHROMO. 2 hits.
    SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.
    SSF54160. SSF54160. 2 hits.
    PROSITEiPS50013. CHROMO_2. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q09XV5-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MADPIMDLFD DPNLFGLDSL TDDSFNQVTQ DPIEEALGLP SSLDSLDQMN     50
    QDGGGGDVGN SSASDLVPPP EETASTELPK ESTAPAPESL TLHDYTTQPT 100
    SQEQPAQPVL QTSTPTAGLL QVSKSQEILS QGNPFMGVSA TGVSPSNTGG 150
    QPSQSAPKIV ILKAPPNSSV TGTHVAQIQA QGITSTAQPL VAGTANGGKV 200
    TFTKVLTGTP LRPGVSIVSG NTVLATKVPG NQAAVQRIVQ PSRPVKQLVL 250
    QPVKGSAPAG NPGAAGPPLK PAVTLTSTPT QGESKRITLV LQQPQSGGPQ 300
    GHRHVVLGSL PGKIVLQGNQ LAALTQAKNA QGQPAKVVTI QLQVQQPQQK 350
    IQIVPQPPSS QPQPQPQPPP SAQPLTLSSV QQAQIMGPGQ NPGQRLSVPL 400
    KMVLQPQAGS SQGASSGLSV VKVLSASEVA ALSSPASCAP HTAGKTGMEE 450
    NRRLEHQKKQ EKANRIVAEA IARARARGEQ NIPRVLNEDE LPSVRPEEEG 500
    EKKRRKKSSG ERLKEEKPKK SKTAAASKTK GKSKLNTITP VVGKKRKRNT 550
    SSDNSDVEVM PAQSPREDEE SSIQKRRSNR QVKRKKYTED LDIKITDDEE 600
    EEEVDVTGPI KPEPILPEPV QEPDGETLPS MQFFVENPSE EDAAIVDKVL 650
    SMRVVKKELP SGQYTEAEEF FVKYKNYSYL HCEWATISQL EKDKRIHQKL 700
    KRFKTKMAQM RHFFHEDEEP FNPDYVEVDR ILDESHSVDK DNGEPVIYYL 750
    VKWCSLPYED STWELKEDVD EGKIREFKRI QSRHPELRRV NRPQANAWKK 800
    LELSHEYKNR NQLREYQLEG VNWLLFNWYN RQNCILADEM GLGKTIQSIA 850
    FLQEVYNVGI HGPFLVIAPL STITNWEREF NTWTEMNTIV YHGSLASRQM 900
    IQQYEMYCKD SRGRLIPGAY KFDALITTFE MILSDCPELR EIEWRCVIID 950
    EAHRLKNRNC KLLDSLKHMD LEHKVLLTGT PLQNTVEELF SLLHFLEPSQ 1000
    FPSESEFLKD FGDLKTEEQV QKLQAILKPM MLRRLKEDVE KNLAPKQETI 1050
    IEVELTNIQK KYYRAILEKN FSFLSKGAGH TNMPNLLNTM MELRKCCNHP 1100
    YLINGAEEKI LMEFREACHI IPQDFHLQAM VRSAGKLVLI DKLLPKLKAG 1150
    GHKVLIFSQM VRCLDILEDY LIQRRYLYER IDGRVRGNLR QAAIDRFSKP 1200
    DSDRFVFLLC TRAGGLGINL TAADTCIIFD SDWNPQNDLQ AQARCHRIGQ 1250
    SKAVKVYRLI TRNSYEREMF DKASLKLGLD KAVLQSMSGR DGNITGIQQF 1300
    SKKEIEDLLR KGAYAAIMEE DDEGSKFCEE DIDQILLRRT TTITIESEGK 1350
    GSTFAKASFV ASENRTDISL DDPNFWQKWA KKADLDMDLL NSKNNLVIDT 1400
    PRVRKQTRHF STLKDDDLVE FSDLESEDDE RPRSRRHDRH HTYGRTDCFR 1450
    VEKHLLVYGW GRWRDILSHG RFKRRMTERD VETICRAILV YCLLHYRGDE 1500
    NIKSFIWDLI SPAENGKTKE LQNHSGLSIP VPRGRKGKKV KSQSTFDIHK 1550
    ADWIRKYNPD TLFQDESYKK HLKHQCNKVL LRVRMLYYLR QEVIGDQAEK 1600
    VLGGAIASEI DIWFPVVDQL EVPTTWWDSE ADKSLLIGVF KHGYEKYNTM 1650
    RADPALCFLE KAGRPDDKAI AAEHRVLDNF SDLVEGIDFD KDCEDPEYKP 1700
    LQGPPKDPDD EGDPLMMMDE EISVIDGEEA QVTQQPGHLF WPPGSALTAR 1750
    LRRLVTAYQR SYKREQMKME AAERGDRRRR RCEAAFKLKE IARREKQQRW 1800
    TRREQTDFYR VVSTFGVEYD PDNMQFHWDR FRTFARLDKK TDESLTKYFH 1850
    GFVAMCRQVC RLPPAAGDEP PDPNLFIEPI TEERASRTLY RIELLRRLRE 1900
    QVLCHPLLED RLALCQPPGL ELPKWWEPVR HDGELLRGAA RHGVSQTDCN 1950
    IMQDPDFSFL AARMNYMQNH QAGASAASLS RCSTPLLHQQ CTSRTASPSP 2000
    LRPDAPVEKS PEESTVQVPN LESLTLKLED EVVARSRLTS QDYEVRVGSS 2050
    DTAPLSRSVP PVKLEDEDDS DSELDLSKLS PSSSSSSSSS SSSSSTDESE 2100
    DEKEEKLTAD RSRPKLYDEE SLLSLTMSQD GFPNEDGEQM TPELLLLQER 2150
    QRASEWPKDR VLINRIDLVC QAVLSGKWPS NRRSQEVTAG GILGPGNHLL 2200
    DSPSLTPGED GDSPVPTPRS GSAASMAEEE ASAVTTAAAQ FTKLRRGMDE 2250
    KEFTVQIKDE EGLKLTFQKH RLMANGVMGD GHPLFHKKKG NRKKLVELEV 2300
    ECMEEPNHLD LDLETRIPVI NKVDGTLLVG DEAPRRAELE MWLQGHPEFA 2350
    VDPRFLAYME ERRKQKWQRC KKNNKAELNC LGMEPVQPAN SRNGKKGHYA 2400
    ETAFNRVLPG PVAPENSKKR VRRTRPDLSK MMALMQGGST GSLSLHNTFQ 2450
    HSSSNLQSVS SLGHSSTTSA SLPFMPFVMG AAAPPHVDSS TMLHHHHHHP 2500
    HPHHHHHHHP GLRTTGYPSS PATTTSGTAL RLPTLQPEDD DEEEDEEDDD 2550
    LSQGYDSSER DFSLIDDPMM PANSDSSEDA DD 2582
    Length:2,582
    Mass (Da):290,847
    Last modified:October 17, 2006 - v1
    Checksum:iD9432500F6A8C329
    GO
    Isoform 2 (identifier: Q09XV5-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:751
    Mass (Da):80,950
    Checksum:i23F272C1595F2A90
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 211T → A in AAW56421. (PubMed:15367660)Curated
    Sequence conflicti2020 – 20201N → S in BAC98203. (PubMed:14621295)Curated
    Sequence conflicti2298 – 22981L → V in BAC98203. (PubMed:14621295)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei745 – 7517PVIYYLV → VSWARRT in isoform 2. 1 PublicationVSP_036676
    Alternative sequencei752 – 25821831Missing in isoform 2. 1 PublicationVSP_036677Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ190419 mRNA. Translation: ABB02259.1.
    AY863219 mRNA. Translation: AAW56421.1.
    AK129393 Transcribed RNA. Translation: BAC98203.2. Sequence problems.
    AK160299 mRNA. Translation: BAE35730.1.
    CCDSiCCDS36919.1. [Q09XV5-1]
    RefSeqiNP_963999.2. NM_201637.2. [Q09XV5-1]
    XP_006519539.1. XM_006519476.1. [Q09XV5-1]
    UniGeneiMm.289934.

    Genome annotation databases

    EnsembliENSMUST00000089752; ENSMUSP00000087184; ENSMUSG00000053754. [Q09XV5-1]
    GeneIDi67772.
    KEGGimmu:67772.
    UCSCiuc007tot.1. mouse. [Q09XV5-1]
    uc007tov.1. mouse. [Q09XV5-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ190419 mRNA. Translation: ABB02259.1 .
    AY863219 mRNA. Translation: AAW56421.1 .
    AK129393 Transcribed RNA. Translation: BAC98203.2 . Sequence problems.
    AK160299 mRNA. Translation: BAE35730.1 .
    CCDSi CCDS36919.1. [Q09XV5-1 ]
    RefSeqi NP_963999.2. NM_201637.2. [Q09XV5-1 ]
    XP_006519539.1. XM_006519476.1. [Q09XV5-1 ]
    UniGenei Mm.289934.

    3D structure databases

    ProteinModelPortali Q09XV5.
    SMRi Q09XV5. Positions 653-781, 790-1286, 2305-2374.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 212432. 4 interactions.
    IntActi Q09XV5. 1 interaction.

    PTM databases

    PhosphoSitei Q09XV5.

    Proteomic databases

    PaxDbi Q09XV5.
    PRIDEi Q09XV5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000089752 ; ENSMUSP00000087184 ; ENSMUSG00000053754 . [Q09XV5-1 ]
    GeneIDi 67772.
    KEGGi mmu:67772.
    UCSCi uc007tot.1. mouse. [Q09XV5-1 ]
    uc007tov.1. mouse. [Q09XV5-2 ]

    Organism-specific databases

    CTDi 57680.
    MGIi MGI:1915022. Chd8.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG0553.
    GeneTreei ENSGT00560000077077.
    HOGENOMi HOG000246942.
    HOVERGENi HBG107676.
    InParanoidi Q09XV5.
    KOi K04494.
    OMAi FLAYMED.
    OrthoDBi EOG7NSB1C.
    TreeFami TF313572.

    Miscellaneous databases

    ChiTaRSi CHD8. mouse.
    NextBioi 325525.
    PROi Q09XV5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q09XV5.
    Genevestigatori Q09XV5.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR006576. 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 ]
    Pfami PF07533. BRK. 2 hits.
    PF00385. Chromo. 2 hits.
    PF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view ]
    SMARTi SM00592. BRK. 2 hits.
    SM00298. CHROMO. 2 hits.
    SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    SSF54160. SSF54160. 2 hits.
    PROSITEi PS50013. CHROMO_2. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiCHD8_MOUSE
    AccessioniPrimary (citable) accession number: Q09XV5
    Secondary accession number(s): Q3TV89, Q5I1Z2, Q6ZPM8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 79 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3