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Q9HCK8

- CHD8_HUMAN

UniProt

Q9HCK8 - CHD8_HUMAN

Protein

Chromodomain-helicase-DNA-binding protein 8

Gene

CHD8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 5 (11 Jan 2011)
      Previous versions | rss
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    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 bindingi836 – 8438ATPPROSITE-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. DNA duplex unwinding Source: GOC
    5. in utero embryonic development Source: Ensembl
    6. negative regulation of fibroblast apoptotic process Source: Ensembl
    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
    Helicase with SNF2 domain 1
    Gene namesi
    Name:CHD8
    Synonyms:HELSNF1, KIAA1564
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:20153. CHD8.

    Subcellular locationi

    Nucleus 2 Publications
    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
    3. protein complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Autism 18 (AUTS18) [MIM:615032]: A complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Most individuals with autism also manifest moderate mental retardation.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2498 – 24981Missing in AUTS18. 1 Publication
    VAR_069573

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi842 – 8421K → R: Abolishes ATPase activity. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi615032. phenotype.
    Orphaneti106. Autism.
    PharmGKBiPA134957052.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 25812581Chromodomain-helicase-DNA-binding protein 8PRO_0000080233Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei553 – 5531Phosphoserine1 Publication
    Modified residuei562 – 5621Phosphoserine1 Publication
    Cross-linki609 – 609Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei1420 – 14201Phosphoserine3 Publications
    Modified residuei1424 – 14241Phosphoserine3 Publications
    Modified residuei1976 – 19761Phosphoserine1 Publication
    Modified residuei1993 – 19931Phosphothreonine1 Publication
    Modified residuei2008 – 20081Phosphoserine3 Publications
    Modified residuei2046 – 20461Phosphoserine3 Publications
    Modified residuei2051 – 20511Phosphothreonine1 Publication
    Modified residuei2069 – 20691Phosphoserine1 Publication
    Modified residuei2071 – 20711Phosphoserine1 Publication
    Modified residuei2182 – 21821Phosphoserine1 Publication
    Modified residuei2200 – 22001Phosphoserine1 Publication
    Modified residuei2211 – 22111Phosphoserine1 Publication
    Modified residuei2519 – 25191Phosphoserine1 Publication

    Post-translational modificationi

    Sumoylated.By similarity

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9HCK8.
    PaxDbiQ9HCK8.
    PRIDEiQ9HCK8.

    PTM databases

    PhosphoSiteiQ9HCK8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9HCK8.
    BgeeiQ9HCK8.
    CleanExiHS_CHD8.
    GenevestigatoriQ9HCK8.

    Organism-specific databases

    HPAiHPA052186.

    Interactioni

    Subunit structurei

    Interacts with p53/TP53, histone H1, CTNNB1, CTCF and PIAS3. 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, KAT8/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with CHD7.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ASH2LQ9UBL32EBI-1169146,EBI-540797
    CHD7Q9P2D13EBI-4410319,EBI-3951683
    RBBP5Q152912EBI-1169146,EBI-592823
    WDR5P619643EBI-1169146,EBI-540834

    Protein-protein interaction databases

    BioGridi121709. 26 interactions.
    IntActiQ9HCK8. 21 interactions.
    MINTiMINT-7542705.

    Structurei

    Secondary structure

    1
    2581
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2311 – 23144
    Beta strandi2317 – 23193
    Turni2320 – 23223
    Helixi2328 – 23303
    Helixi2334 – 234310
    Beta strandi2347 – 23493
    Helixi2351 – 23599

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CKANMR-A2291-2364[»]
    2DL6NMR-A2303-2372[»]
    ProteinModelPortaliQ9HCK8.
    SMRiQ9HCK8. Positions 720-779, 2303-2372.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HCK8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini642 – 70968Chromo 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini724 – 79067Chromo 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini823 – 997175Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1137 – 1288152Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi948 – 9514DEAH box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi292 – 410119Gln-richAdd
    BLAST
    Compositional biasi2069 – 209830Ser-richAdd
    BLAST
    Compositional biasi2493 – 250816His-richAdd
    BLAST
    Compositional biasi2539 – 258143Asp-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.
    HOVERGENiHBG107676.
    KOiK04494.
    OMAiFLAYMED.
    OrthoDBiEOG7NSB1C.
    PhylomeDBiQ9HCK8.
    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. 1 hit.
    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: Q9HCK8-1) [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 SSASELVPPP EETAPTELSK ESTAPAPESI TLHDYTTQPA 100
    SQEQPAQPVL QTSTPTSGLL QVSKSQEILS QGNPFMGVSA TAVSSSSAGG 150
    QPPQSAPKIV ILKAPPSSSV TGAHVAQIQA QGITSTAQPL VAGTANGGKV 200
    TFTKVLTGTP LRPGVSIVSG NTVLAAKVPG NQAAVQRIVQ PSRPVKQLVL 250
    QPVKGSAPAG NPGATGPPLK PAVTLTSTPT QGESKRITLV LQQPQSGGPQ 300
    GHRHVVLGSL PGKIVLQGNQ LAALTQAKNA QGQPAKVVTI QLQVQQPQQK 350
    IQIVPQPPSS QPQPQQPPST QPVTLSSVQQ AQIMGPGQSP GQRLSVPVKV 400
    VLQPQAGSSQ GASSGLSVVK VLSASEVAAL SSPASSAPHS GGKTGMEENR 450
    RLEHQKKQEK ANRIVAEAIA RARARGEQNI PRVLNEDELP SVRPEEEGEK 500
    KRRKKSAGER LKEEKPKKSK TSGASKTKGK SKLNTITPVV GKKRKRNTSS 550
    DNSDVEVMPA QSPREDEESS IQKRRSNRQV KRKKYTEDLD IKITDDEEEE 600
    EVDVTGPIKP EPILPEPVQE PDGETLPSMQ FFVENPSEED AAIVDKVLSM 650
    RIVKKELPSG QYTEAEEFFV KYKNYSYLHC EWATISQLEK DKRIHQKLKR 700
    FKTKMAQMRH FFHEDEEPFN PDYVEVDRIL DESHSIDKDN GEPVIYYLVK 750
    WCSLPYEDST WELKEDVDEG KIREFKRIQS RHPELKRVNR PQASAWKKLE 800
    LSHEYKNRNQ LREYQLEGVN WLLFNWYNRQ NCILADEMGL GKTIQSIAFL 850
    QEVYNVGIHG PFLVIAPLST ITNWEREFNT WTEMNTIVYH GSLASRQMIQ 900
    QYEMYCKDSR GRLIPGAYKF DALITTFEMI LSDCPELREI EWRCVIIDEA 950
    HRLKNRNCKL LDSLKHMDLE HKVLLTGTPL QNTVEELFSL LHFLEPSQFP 1000
    SESEFLKDFG DLKTEEQVQK LQAILKPMML RRLKEDVEKN LAPKQETIIE 1050
    VELTNIQKKY YRAILEKNFS FLSKGAGHTN MPNLLNTMME LRKCCNHPYL 1100
    INGAEEKILT EFREACHIIP HDFHLQAMVR SAGKLVLIDK LLPKLKAGGH 1150
    KVLIFSQMVR CLDILEDYLI QRRYLYERID GRVRGNLRQA AIDRFSKPDS 1200
    DRFVFLLCTR AGGLGINLTA ADTCIIFDSD WNPQNDLQAQ ARCHRIGQSK 1250
    AVKVYRLITR NSYEREMFDK ASLKLGLDKA VLQSMSGRDG NITGIQQFSK 1300
    KEIEDLLRKG AYAAIMEEDD EGSKFCEEDI DQILLRRTTT ITIESEGKGS 1350
    TFAKASFVAS ENRTDISLDD PNFWQKWAKK ADLDMDLLNS KNNLVIDTPR 1400
    VRKQTRHFST LKDDDLVEFS DLESEDDERP RSRRHDRHHA YGRTDCFRVE 1450
    KHLLVYGWGR WRDILSHGRF KRRMTERDVE TICRAILVYC LLHYRGDENI 1500
    KGFIWDLISP AENGKTKELQ NHSGLSIPVP RGRKGKKVKS QSTFDIHKAD 1550
    WIRKYNPDTL FQDESYKKHL KHQCNKVLLR VRMLYYLRQE VIGDQAEKVL 1600
    GGAIASEIDI WFPVVDQLEV PTTWWDSEAD KSLLIGVFKH GYEKYNTMRA 1650
    DPALCFLEKA GRPDDKAIAA EHRVLDNFSD IVEGVDFDKD CEDPEYKPLQ 1700
    GPPKDQDDEG DPLMMMDEEI SVIDGDEAQV TQQPGHLFWP PGSALTARLR 1750
    RLVTAYQRSY KREQMKIEAA ERGDRRRRRC EAAFKLKEIA RREKQQRWTR 1800
    REQTDFYRVV STFGVEYDPD TMQFHWDRFR TFARLDKKTD ESLTKYFHGF 1850
    VAMCRQVCRL PPAAGDEPPD PNLFIEPITE ERASRTLYRI ELLRRLREQV 1900
    LCHPLLEDRL ALCQPPGPEL PKWWEPVRHD GELLRGAARH GVSQTDCNIM 1950
    QDPDFSFLAA RMNYMQNHQA GAPAPSLSRC STPLLHQQYT SRTASPLPLR 2000
    PDAPVEKSPE ETATQVPSLE SLTLKLEHEV VARSRPTPQD YEMRVSPSDT 2050
    TPLVSRSVPP VKLEDEDDSD SELDLSKLSP SSSSSSSSSS SSSSTDESED 2100
    EKEEKLTDQS RSKLYDEESL LSLTMSQDGF PNEDGEQMTP ELLLLQERQR 2150
    ASEWPKDRVL INRIDLVCQA VLSGKWPSSR RSQEMVTGGI LGPGNHLLDS 2200
    PSLTPGEYGD SPVPTPRSSS AASMAEEEAS AVSTAAAQFT KLRRGMDEKE 2250
    FTVQIKDEEG LKLTFQKHKL MANGVMGDGH PLFHKKKGNR KKLVELEVEC 2300
    MEEPNHLDVD LETRIPVINK VDGTLLVGED APRRAELEMW LQGHPEFAVD 2350
    PRFLAYMEDR RKQKWQRCKK NNKAELNCLG MEPVQTANSR NGKKGHHTET 2400
    VFNRVLPGPI APESSKKRAR RMRPDLSKMM ALMQGGSTGS LSLHNTFQHS 2450
    SSGLQSVSSL GHSSATSASL PFMPFVMGGA PSSPHVDSST MLHHHHHHPH 2500
    PHHHHHHHPG LRAPGYPSSP VTTASGTTLR LPPLQPEEDD DEDEEDDDDL 2550
    SQGYDSSERD FSLIDDPMMP ANSDSSEDAD D 2581
    Length:2,581
    Mass (Da):290,519
    Last modified:January 11, 2011 - v5
    Checksum:i379F09DC6F814851
    GO
    Isoform 2 (identifier: Q9HCK8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-281: MADPIMDLFD...AVTLTSTPTQ → MK

    Note: No experimental confirmation available.

    Show »
    Length:2,302
    Mass (Da):262,348
    Checksum:i3BA9FCDF2186AC0F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti594 – 5941T → A in CAH18170. (PubMed:17974005)Curated
    Sequence conflicti1008 – 10081D → N in CAH18170. (PubMed:17974005)Curated
    Sequence conflicti2481 – 24811P → Q in CAH18170. (PubMed:17974005)Curated
    Sequence conflicti2568 – 25681M → I in AAH36920. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2498 – 24981Missing in AUTS18. 1 Publication
    VAR_069573

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 281281MADPI…STPTQ → MK in isoform 2. 1 PublicationVSP_017270Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR749315 mRNA. Translation: CAH18170.1.
    AL834524 mRNA. Translation: CAD39180.1.
    AL135744 Genomic DNA. No translation available.
    AL161747 Genomic DNA. No translation available.
    CB043942 mRNA. No translation available.
    AB046784 mRNA. Translation: BAB13390.3.
    AK131077 mRNA. Translation: BAC85127.1.
    BC011695 mRNA. Translation: AAH11695.2.
    BC025964 mRNA. Translation: AAH25964.1.
    BC036920 mRNA. Translation: AAH36920.1.
    BC063693 mRNA. Translation: AAH63693.1.
    BC073903 mRNA. Translation: AAH73903.1.
    BC098452 mRNA. Translation: AAH98452.1.
    CCDSiCCDS45081.1. [Q9HCK8-2]
    CCDS53885.1. [Q9HCK8-1]
    RefSeqiNP_001164100.1. NM_001170629.1. [Q9HCK8-1]
    NP_065971.2. NM_020920.3. [Q9HCK8-2]
    UniGeneiHs.530698.

    Genome annotation databases

    EnsembliENST00000399982; ENSP00000382863; ENSG00000100888. [Q9HCK8-1]
    ENST00000430710; ENSP00000406288; ENSG00000100888. [Q9HCK8-2]
    ENST00000557364; ENSP00000451601; ENSG00000100888. [Q9HCK8-1]
    GeneIDi57680.
    KEGGihsa:57680.
    UCSCiuc001war.2. human. [Q9HCK8-1]
    uc001was.2. human. [Q9HCK8-2]

    Polymorphism databases

    DMDMi317373586.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR749315 mRNA. Translation: CAH18170.1 .
    AL834524 mRNA. Translation: CAD39180.1 .
    AL135744 Genomic DNA. No translation available.
    AL161747 Genomic DNA. No translation available.
    CB043942 mRNA. No translation available.
    AB046784 mRNA. Translation: BAB13390.3 .
    AK131077 mRNA. Translation: BAC85127.1 .
    BC011695 mRNA. Translation: AAH11695.2 .
    BC025964 mRNA. Translation: AAH25964.1 .
    BC036920 mRNA. Translation: AAH36920.1 .
    BC063693 mRNA. Translation: AAH63693.1 .
    BC073903 mRNA. Translation: AAH73903.1 .
    BC098452 mRNA. Translation: AAH98452.1 .
    CCDSi CCDS45081.1. [Q9HCK8-2 ]
    CCDS53885.1. [Q9HCK8-1 ]
    RefSeqi NP_001164100.1. NM_001170629.1. [Q9HCK8-1 ]
    NP_065971.2. NM_020920.3. [Q9HCK8-2 ]
    UniGenei Hs.530698.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CKA NMR - A 2291-2364 [» ]
    2DL6 NMR - A 2303-2372 [» ]
    ProteinModelPortali Q9HCK8.
    SMRi Q9HCK8. Positions 720-779, 2303-2372.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121709. 26 interactions.
    IntActi Q9HCK8. 21 interactions.
    MINTi MINT-7542705.

    PTM databases

    PhosphoSitei Q9HCK8.

    Polymorphism databases

    DMDMi 317373586.

    Proteomic databases

    MaxQBi Q9HCK8.
    PaxDbi Q9HCK8.
    PRIDEi Q9HCK8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000399982 ; ENSP00000382863 ; ENSG00000100888 . [Q9HCK8-1 ]
    ENST00000430710 ; ENSP00000406288 ; ENSG00000100888 . [Q9HCK8-2 ]
    ENST00000557364 ; ENSP00000451601 ; ENSG00000100888 . [Q9HCK8-1 ]
    GeneIDi 57680.
    KEGGi hsa:57680.
    UCSCi uc001war.2. human. [Q9HCK8-1 ]
    uc001was.2. human. [Q9HCK8-2 ]

    Organism-specific databases

    CTDi 57680.
    GeneCardsi GC14M021853.
    HGNCi HGNC:20153. CHD8.
    HPAi HPA052186.
    MIMi 610528. gene.
    615032. phenotype.
    neXtProti NX_Q9HCK8.
    Orphaneti 106. Autism.
    PharmGKBi PA134957052.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0553.
    HOVERGENi HBG107676.
    KOi K04494.
    OMAi FLAYMED.
    OrthoDBi EOG7NSB1C.
    PhylomeDBi Q9HCK8.
    TreeFami TF313572.

    Miscellaneous databases

    EvolutionaryTracei Q9HCK8.
    GeneWikii CHD8.
    GenomeRNAii 57680.
    NextBioi 64494.
    PROi Q9HCK8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HCK8.
    Bgeei Q9HCK8.
    CleanExi HS_CHD8.
    Genevestigatori Q9HCK8.

    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. 1 hit.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Lymph node and Uterine endothelium.
    2. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. The Cancer Genome Anatomy Project (CGAP) at the National Cancer Institute
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 28-176 (ISOFORM 1).
    4. "Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.
      DNA Res. 7:273-281(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 150-2581 (ISOFORM 1).
      Tissue: Brain.
    5. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    6. Ohara O., Nagase T., Kikuno R.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    7. "The nucleotide sequence of a long cDNA clone isolated from human spleen."
      Jikuya H., Takano J., Kikuno R., Nagase T., Ohara O.
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1038-2581.
      Tissue: Spleen.
    8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1674-2581.
      Tissue: Brain, Duodenum, Liver, Lung and Spleen.
    9. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
      Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
      Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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: INTERACTION WITH CTCF.
    12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2051, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "CHD8 associates with human Staf and contributes to efficient U6 RNA polymerase III transcription."
      Yuan C.-C., Zhao X., Florens L., Swanson S.K., Washburn M.P., Hernandez N.
      Mol. Cell. Biol. 27:8729-8738(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ZNF143.
    14. "Novel deletions of 14q11.2 associated with developmental delay, cognitive impairment and similar minor anomalies in three children."
      Zahir F., Firth H.V., Baross A., Delaney A.D., Eydoux P., Gibson W.T., Langlois S., Martin H., Willatt L., Marra M.A., Friedman J.M.
      J. Med. Genet. 44:556-561(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE ASSOCIATION WITH DEVELOPMENTAL DELAY.
    15. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2182 AND SER-2211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "CHD8 is an ATP-dependent chromatin remodeling factor that regulates beta-catenin target genes."
      Thompson B.A., Tremblay V., Lin G., Bochar D.A.
      Mol. Cell. Biol. 28:3894-3904(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1, IDENTIFICATION IN A COMPLEX WITH WDR5, MUTAGENESIS OF LYS-842.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562; SER-1976; SER-2008; SER-2046 AND SER-2519, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; SER-1420; SER-1424; THR-1993; SER-2008 AND SER-2200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    20. Cited for: INTERACTION WITH CHD7, SUBCELLULAR LOCATION.
    21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1420; SER-1424; SER-2008 AND SER-2046, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1420; SER-1424; SER-2046; SER-2069 AND SER-2071, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Solution structure of the first BRK domain from human chromodomain-helicase-DNA-binding protein 8."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 2291-2372.
    25. Cited for: VARIANT AUTS18 HIS-2498 DEL.

    Entry informationi

    Entry nameiCHD8_HUMAN
    AccessioniPrimary (citable) accession number: Q9HCK8
    Secondary accession number(s): Q4G0D8
    , Q68DQ0, Q6DKH9, Q6P440, Q6ZNL7, Q8N3Z9, Q8NCY4, Q8TBR9, Q96F26
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 19, 2002
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 140 of the entry and version 5 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Its gene is located in the 14q11.2 region of the genome which is associated with developmental delay, cognitive impairment and similar minor anomalies in some children, suggesting that it may be a good candidate for the phenotype.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3