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Reviewed, UniProtKB/Swiss-Prot Q9HCK8 (CHD8_HUMAN)

Last modified February 9, 2010. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Chromodomain-helicase-DNA-binding protein 8
      Short name=CHD-8
    EC=3.6.1.-
Alternative name(s):
    ATP-dependent helicase CHD8
    Helicase with SNF2 domain 1
Gene names
Name: CHD8
Synonyms: HELSNF1, KIAA1564
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length2581 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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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 to efficient U6 RNA polymerase III transcription. Ref.13 Ref.17

Subunit structure

Interacts with p53/TP53, histone H1, CTNNB1, CTCF and PIAS3. Component of some MLL1/MLL complex, at least composed of the core components MLL, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components C17orf49, CHD8, E2F6, HSP70, IN80C, KIAA1267, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Ref.13 Ref.17 Ref.11

Subcellular location

Nucleus. Note: Localizes to the promoter regions of several CTNNB1-responsive genes. Also present at known CTCF target sites. Ref.17

Post-translational modification

Sumoylated By similarity.

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.

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.

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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 term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processATP-dependent chromatin remodeling Ref.17

Inferred from mutant phenotype. Source: UniProtKB

Wnt receptor signaling pathway through beta-catenin Ref.17

Inferred from direct assay. Source: UniProtKB

chromatin assembly or disassembly

Inferred from electronic annotation. Source: InterPro

negative regulation of Wnt receptor signaling pathway Ref.17

Inferred from direct assay. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter Ref.13

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of transcription from RNA polymerase III promoter Ref.13

Inferred from mutant phenotype. Source: UniProtKB

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentMLL1 complex Ref.9

Inferred from direct assay. Source: UniProtKB

chromatin

Inferred from electronic annotation. Source: InterPro

   Molecular functionATP binding Ref.17

Inferred from direct assay. Source: UniProtKB

DNA binding Ref.17

Inferred from mutant phenotype. Source: UniProtKB

DNA helicase activity Ref.17

Inferred from mutant phenotype. Source: UniProtKB

DNA-dependent ATPase activity Ref.17

Inferred from direct assay. Source: UniProtKB

beta-catenin binding Ref.17

Inferred from direct assay. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: InterPro

methylated histone residue binding Ref.13

Inferred from direct assay. Source: UniProtKB

p53 binding

Inferred from sequence or structural similarity. Source: UniProtKB

transcription activator activity Ref.13

Inferred from direct assay. Source: UniProtKB

transcription repressor activity Ref.17

Inferred from mutant phenotype. Source: UniProtKB

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

CTCFP497111EBI-1169146,EBI-932887

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9HCK8-1)

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: Q9HCK8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-281: MADPIMDLFD...AVTLTSTPTQ → MK
Note: No experimental confirmation available.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25812581Chromodomain-helicase-DNA-binding protein 8
PRO_0000080233

Regions

Domain642 – 70968Chromo 1
Domain724 – 79067Chromo 2
Domain823 – 997175Helicase ATP-binding
Domain1137 – 1288152Helicase C-terminal
Nucleotide binding836 – 8438ATP Potential
Motif948 – 9514DEAH box
Compositional bias292 – 410119Gln-rich
Compositional bias2069 – 209830Ser-rich
Compositional bias2493 – 250816His-rich
Compositional bias2539 – 258143Asp-rich

Amino acid modifications

Modified residue5371Phosphothreonine Ref.12
Modified residue5501Phosphoserine Ref.18
Modified residue5531Phosphoserine Ref.18 Ref.21
Modified residue5621Phosphoserine Ref.18
Modified residue13981Phosphothreonine Ref.12
Modified residue14201Phosphoserine Ref.18 Ref.21 Ref.10
Modified residue14241Phosphoserine Ref.18 Ref.21 Ref.10
Modified residue19761Phosphoserine Ref.18
Modified residue19931Phosphothreonine Ref.21
Modified residue19951Phosphoserine Ref.18
Modified residue20081Phosphoserine Ref.18 Ref.21 Ref.20
Modified residue20461Phosphoserine Ref.18 Ref.21 Ref.15
Modified residue20691Phosphoserine Ref.10
Modified residue20711Phosphoserine Ref.10
Modified residue21821Phosphoserine Ref.16
Modified residue22001Phosphoserine Ref.21 Ref.16
Modified residue22021Phosphoserine Ref.16
Modified residue22111Phosphoserine Ref.16
Modified residue25181Phosphoserine Ref.18 Ref.20 Ref.16
Modified residue25191Phosphoserine Ref.21 Ref.20 Ref.15 Ref.16
Cross-link609Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence1 – 281281MADPI…STPTQ → MK in isoform 2.
VSP_017270

Experimental info

Mutagenesis8421K → R: Abolishes ATPase activity. Ref.17
Sequence conflict5941T → A in CAH18170. Ref.1
Sequence conflict10081N → D in BAB13390. Ref.4
Sequence conflict24811P → Q in CAH18170. Ref.1
Sequence conflict25681M → I in AAH36920. Ref.8

Secondary structure

1 ............ 2581
Helix Strand Turn

Details...

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Sequences

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

Last modified March 24, 2009. Version 4.
Checksum: 557DC2904F8D2F0A

FASTA2,581290,518
        10         20         30         40         50         60 
MADPIMDLFD DPNLFGLDSL TDDSFNQVTQ DPIEEALGLP SSLDSLDQMN QDGGGGDVGN 

        70         80         90        100        110        120 
SSASELVPPP EETAPTELSK ESTAPAPESI TLHDYTTQPA SQEQPAQPVL QTSTPTSGLL 

       130        140        150        160        170        180 
QVSKSQEILS QGNPFMGVSA TAVSSSSAGG QPPQSAPKIV ILKAPPSSSV TGAHVAQIQA 

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

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

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

       370        380        390        400        410        420 
QPQPQQPPST QPVTLSSVQQ AQIMGPGQSP GQRLSVPVKV VLQPQAGSSQ GASSGLSVVK 

       430        440        450        460        470        480 
VLSASEVAAL SSPASSAPHS GGKTGMEENR RLEHQKKQEK ANRIVAEAIA RARARGEQNI 

       490        500        510        520        530        540 
PRVLNEDELP SVRPEEEGEK KRRKKSAGER LKEEKPKKSK TSGASKTKGK SKLNTITPVV 

       550        560        570        580        590        600 
GKKRKRNTSS DNSDVEVMPA QSPREDEESS IQKRRSNRQV KRKKYTEDLD IKITDDEEEE 

       610        620        630        640        650        660 
EVDVTGPIKP EPILPEPVQE PDGETLPSMQ FFVENPSEED AAIVDKVLSM RIVKKELPSG 

       670        680        690        700        710        720 
QYTEAEEFFV KYKNYSYLHC EWATISQLEK DKRIHQKLKR FKTKMAQMRH FFHEDEEPFN 

       730        740        750        760        770        780 
PDYVEVDRIL DESHSIDKDN GEPVIYYLVK WCSLPYEDST WELKEDVDEG KIREFKRIQS 

       790        800        810        820        830        840 
RHPELKRVNR PQASAWKKLE LSHEYKNRNQ LREYQLEGVN WLLFNWYNRQ NCILADEMGL 

       850        860        870        880        890        900 
GKTIQSIAFL QEVYNVGIHG PFLVIAPLST ITNWEREFNT WTEMNTIVYH GSLASRQMIQ 

       910        920        930        940        950        960 
QYEMYCKDSR GRLIPGAYKF DALITTFEMI LSDCPELREI EWRCVIIDEA HRLKNRNCKL 

       970        980        990       1000       1010       1020 
LDSLKHMDLE HKVLLTGTPL QNTVEELFSL LHFLEPSQFP SESEFLKNFG DLKTEEQVQK 

      1030       1040       1050       1060       1070       1080 
LQAILKPMML RRLKEDVEKN LAPKQETIIE VELTNIQKKY YRAILEKNFS FLSKGAGHTN 

      1090       1100       1110       1120       1130       1140 
MPNLLNTMME LRKCCNHPYL INGAEEKILT EFREACHIIP HDFHLQAMVR SAGKLVLIDK 

      1150       1160       1170       1180       1190       1200 
LLPKLKAGGH KVLIFSQMVR CLDILEDYLI QRRYLYERID GRVRGNLRQA AIDRFSKPDS 

      1210       1220       1230       1240       1250       1260 
DRFVFLLCTR AGGLGINLTA ADTCIIFDSD WNPQNDLQAQ ARCHRIGQSK AVKVYRLITR 

      1270       1280       1290       1300       1310       1320 
NSYEREMFDK ASLKLGLDKA VLQSMSGRDG NITGIQQFSK KEIEDLLRKG AYAAIMEEDD 

      1330       1340       1350       1360       1370       1380 
EGSKFCEEDI DQILLRRTTT ITIESEGKGS TFAKASFVAS ENRTDISLDD PNFWQKWAKK 

      1390       1400       1410       1420       1430       1440 
ADLDMDLLNS KNNLVIDTPR VRKQTRHFST LKDDDLVEFS DLESEDDERP RSRRHDRHHA 

      1450       1460       1470       1480       1490       1500 
YGRTDCFRVE KHLLVYGWGR WRDILSHGRF KRRMTERDVE TICRAILVYC LLHYRGDENI 

      1510       1520       1530       1540       1550       1560 
KGFIWDLISP AENGKTKELQ NHSGLSIPVP RGRKGKKVKS QSTFDIHKAD WIRKYNPDTL 

      1570       1580       1590       1600       1610       1620 
FQDESYKKHL KHQCNKVLLR VRMLYYLRQE VIGDQAEKVL GGAIASEIDI WFPVVDQLEV 

      1630       1640       1650       1660       1670       1680 
PTTWWDSEAD KSLLIGVFKH GYEKYNTMRA DPALCFLEKA GRPDDKAIAA EHRVLDNFSD 

      1690       1700       1710       1720       1730       1740 
IVEGVDFDKD CEDPEYKPLQ GPPKDQDDEG DPLMMMDEEI SVIDGDEAQV TQQPGHLFWP 

      1750       1760       1770       1780       1790       1800 
PGSALTARLR RLVTAYQRSY KREQMKIEAA ERGDRRRRRC EAAFKLKEIA RREKQQRWTR 

      1810       1820       1830       1840       1850       1860 
REQTDFYRVV STFGVEYDPD TMQFHWDRFR TFARLDKKTD ESLTKYFHGF VAMCRQVCRL 

      1870       1880       1890       1900       1910       1920 
PPAAGDEPPD PNLFIEPITE ERASRTLYRI ELLRRLREQV LCHPLLEDRL ALCQPPGPEL 

      1930       1940       1950       1960       1970       1980 
PKWWEPVRHD GELLRGAARH GVSQTDCNIM QDPDFSFLAA RMNYMQNHQA GAPAPSLSRC 

      1990       2000       2010       2020       2030       2040 
STPLLHQQYT SRTASPLPLR PDAPVEKSPE ETATQVPSLE SLTLKLEHEV VARSRPTPQD 

      2050       2060       2070       2080       2090       2100 
YEMRVSPSDT TPLVSRSVPP VKLEDEDDSD SELDLSKLSP SSSSSSSSSS SSSSTDESED 

      2110       2120       2130       2140       2150       2160 
EKEEKLTDQS RSKLYDEESL LSLTMSQDGF PNEDGEQMTP ELLLLQERQR ASEWPKDRVL 

      2170       2180       2190       2200       2210       2220 
INRIDLVCQA VLSGKWPSSR RSQEMVTGGI LGPGNHLLDS PSLTPGEYGD SPVPTPRSSS 

      2230       2240       2250       2260       2270       2280 
AASMAEEEAS AVSTAAAQFT KLRRGMDEKE FTVQIKDEEG LKLTFQKHKL MANGVMGDGH 

      2290       2300       2310       2320       2330       2340 
PLFHKKKGNR KKLVELEVEC MEEPNHLDVD LETRIPVINK VDGTLLVGED APRRAELEMW 

      2350       2360       2370       2380       2390       2400 
LQGHPEFAVD PRFLAYMEDR RKQKWQRCKK NNKAELNCLG MEPVQTANSR NGKKGHHTET 

      2410       2420       2430       2440       2450       2460 
VFNRVLPGPI APESSKKRAR RMRPDLSKMM ALMQGGSTGS LSLHNTFQHS SSGLQSVSSL 

      2470       2480       2490       2500       2510       2520 
GHSSATSASL PFMPFVMGGA PSSPHVDSST MLHHHHHHPH PHHHHHHHPG LRAPGYPSSP 

      2530       2540       2550       2560       2570       2580 
VTTASGTTLR LPPLQPEEDD DEDEEDDDDL SQGYDSSERD FSLIDDPMMP ANSDSSEDAD 


D

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Isoform 2.

Checksum: 594B3793018ACB54
Show »

FASTA2,302262,347

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References

« Hide 'large scale' references
[1]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
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. expand/collapse author list , 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: 12508121] [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: 10997877] [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: 12168954] [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: 15489334] [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: 15960975] [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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1420; SER-1424; SER-2069 AND SER-2071, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"CTCF-dependent chromatin insulator is linked to epigenetic remodeling."
Ishihara K., Oshimura M., Nakao M.
Mol. Cell 23:733-742(2006) [PubMed: 16949368] [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: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-537 AND THR-1398, MASS SPECTROMETRY.
Tissue: Epithelium.
[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: 17938208] [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: 17545556] [Abstract]
Cited for: POSSIBLE ASSOCIATION WITH DEVELOPMENTAL DELAY.
[15]"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis."
Wang B., Malik R., Nigg E.A., Korner R.
Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2046 AND SER-2519, MASS SPECTROMETRY.
[16]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2182; SER-2200; SER-2202; SER-2211; SER-2518 AND SER-2519, MASS SPECTROMETRY.
[17]"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: 18378692] [Abstract]
Cited for: FUNCTION, DNA-BINDING, SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1, IDENTIFICATION IN A COMPLEX WITH WDR5, MUTAGENESIS OF LYS-842.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550; SER-553; SER-562; SER-1420; SER-1424; SER-1976; SER-1995; SER-2008; SER-2046 AND SER-2518, MASS SPECTROMETRY.
[19]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2008; SER-2518 AND SER-2519, MASS SPECTROMETRY.
[21]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-553; SER-1420; SER-1424; THR-1993; SER-2008; SER-2046; SER-2200 AND SER-2519, MASS SPECTROMETRY.
Tissue: T-cell.
[22]"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.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00398992.
IPI00719073.
RefSeqNP_065971.2.
UniGeneHs.530698

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CKANMR-A2291-2364[»]
2DL6NMR-A2303-2372[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ9HCK8. 3 interactions.
STRINGQ9HCK8.

PTM databases

PhosphoSiteQ9HCK8.

Proteomic databases

PRIDEQ9HCK8.

Genome annotation databases

EnsemblENST00000399982; ENSP00000382863; ENSG00000100888; Homo sapiens. [Genome view]
GeneID57680.
KEGGhsa:57680.
UCSCuc001was.1. human.

Organism-specific databases

CTD57680.
GeneCardsGC14M020923.
H-InvDBHIX0052994.
HGNCHGNC:20153. CHD8.
HPAHPA000849.
MIM610528. gene.
PharmGKBPA142672121.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG10258.
HOVERGENQ9HCK8.

Gene expression databases

ArrayExpressQ9HCK8.
BgeeQ9HCK8.
CleanExHS_CHD8.
GenevestigatorQ9HCK8.
GermOnlineENSG00000100888. Homo sapiens.

Family and domain databases

InterProIPR006576. BRK_domain.
IPR000953. Chromodomain.
IPR016197. Chromodomain-like.
IPR014001. DEAD-like_N.
IPR001650. DNA/RNA_helicase_C.
IPR014021. Helicase_SF1/SF2_ATP-bd.
IPR000330. SNF2_N.
[Graphical view]
PfamPF07533. BRK. 1 hit.
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]
PROSITEPS00598. CHROMO_1. False negative.
PS50013. CHROMO_2. 1 hit.
PS00690. DEAH_ATP_HELICASE. False negative.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio64494.
SOURCESearch...

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Entry information

Entry nameCHD8_HUMAN
AccessionPrimary (citable) accession number: Q9HCK8
Secondary accession number(s): Q4G0D8 expand/collapse secondary AC list , Q68DQ0, Q6DKH9, Q6P440, Q6ZNL7, Q8N3Z9, Q8NCY4, Q8TBR9, Q96F26
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: March 24, 2009
Last modified: February 9, 2010
This is version 93 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents