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Protein

Chromodomain-helicase-DNA-binding protein 8

Gene

CHD8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.UniRule annotation2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi836 – 843ATPUniRule annotation8

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • beta-catenin binding Source: UniProtKB
  • chromatin binding Source: MGI
  • DNA binding Source: UniProtKB
  • DNA-dependent ATPase activity Source: UniProtKB
  • DNA helicase activity Source: UniProtKB
  • histone binding Source: UniProtKB
  • methylated histone binding Source: UniProtKB
  • p53 binding Source: UniProtKB

GO - Biological processi

  • ATP-dependent chromatin remodeling Source: UniProtKB
  • brain development Source: GO_Central
  • canonical Wnt signaling pathway Source: UniProtKB
  • chromatin modification Source: UniProtKB-KW
  • digestive tract development Source: GO_Central
  • in utero embryonic development Source: Ensembl
  • negative regulation of canonical Wnt signaling pathway Source: MGI
  • negative regulation of fibroblast apoptotic process Source: Ensembl
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: GO_Central
  • negative regulation of Wnt signaling pathway Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase III promoter Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000100888-MONOMER.
ReactomeiR-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
SIGNORiQ9HCK8.

Names & Taxonomyi

Protein namesi
Recommended name:
Chromodomain-helicase-DNA-binding protein 8UniRule annotation (EC:3.6.4.12UniRule annotation)
Short name:
CHD-8UniRule annotation
Alternative name(s):
ATP-dependent helicase CHD8UniRule annotation
Helicase with SNF2 domain 1
Gene namesi
Name:CHD8UniRule annotation
Synonyms:HELSNF1, KIAA1564
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:20153. CHD8.

Subcellular locationi

GO - Cellular componenti

  • MLL1 complex Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Autism 18 (AUTS18)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:615032
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0695732498Missing in AUTS18. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi842K → R: Abolishes ATPase activity. 1 Publication1

Keywords - Diseasei

Autism, Autism spectrum disorder, Disease mutation

Organism-specific databases

DisGeNETi57680.
MalaCardsiCHD8.
MIMi615032. phenotype.
OpenTargetsiENSG00000100888.
Orphaneti106. Autism.
PharmGKBiPA134957052.

Polymorphism and mutation databases

BioMutaiCHD8.
DMDMi317373586.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000802331 – 2581Chromodomain-helicase-DNA-binding protein 8Add BLAST2581

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei432PhosphoserineCombined sources1
Modified residuei553PhosphoserineCombined sources1
Modified residuei562PhosphoserineCombined sources1
Cross-linki609Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)UniRule annotation
Modified residuei1420PhosphoserineCombined sources1
Modified residuei1424PhosphoserineCombined sources1
Modified residuei1976PhosphoserineCombined sources1
Modified residuei1978PhosphoserineCombined sources1
Modified residuei1993PhosphothreonineCombined sources1
Modified residuei1995PhosphoserineBy similarity1
Modified residuei2008PhosphoserineCombined sources1
Modified residuei2046PhosphoserineCombined sources1
Modified residuei2051PhosphothreonineCombined sources1
Modified residuei2069PhosphoserineCombined sources1
Modified residuei2071PhosphoserineCombined sources1
Modified residuei2182PhosphoserineCombined sources1
Modified residuei2200PhosphoserineCombined sources1
Modified residuei2202PhosphoserineBy similarity1
Modified residuei2204PhosphothreonineBy similarity1
Modified residuei2211PhosphoserineCombined sources1
Modified residuei2215PhosphothreonineBy similarity1
Modified residuei2223PhosphoserineBy similarity1
Cross-linki2256Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei2519PhosphoserineCombined sources1

Post-translational modificationi

Sumoylated.UniRule annotation

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ9HCK8.
MaxQBiQ9HCK8.
PaxDbiQ9HCK8.
PeptideAtlasiQ9HCK8.
PRIDEiQ9HCK8.

PTM databases

iPTMnetiQ9HCK8.
PhosphoSitePlusiQ9HCK8.

Expressioni

Gene expression databases

BgeeiENSG00000100888.
CleanExiHS_CHD8.
ExpressionAtlasiQ9HCK8. baseline and differential.
GenevisibleiQ9HCK8. HS.

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. Interacts with FAM124B (PubMed:23285124).UniRule annotation6 Publications

Binary interactionsi

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

GO - Molecular functioni

  • beta-catenin binding Source: UniProtKB
  • histone binding Source: UniProtKB
  • methylated histone binding Source: UniProtKB
  • p53 binding Source: UniProtKB

Protein-protein interaction databases

BioGridi121709. 60 interactors.
DIPiDIP-38021N.
IntActiQ9HCK8. 36 interactors.
MINTiMINT-7542705.
STRINGi9606.ENSP00000382863.

Structurei

Secondary structure

12581
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2311 – 2314Combined sources4
Beta strandi2317 – 2319Combined sources3
Turni2320 – 2322Combined sources3
Helixi2328 – 2330Combined sources3
Helixi2334 – 2343Combined sources10
Beta strandi2347 – 2349Combined sources3
Helixi2351 – 2359Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CKANMR-A2291-2364[»]
2DL6NMR-A2303-2372[»]
ProteinModelPortaliQ9HCK8.
SMRiQ9HCK8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HCK8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini642 – 709Chromo 1UniRule annotationAdd BLAST68
Domaini724 – 790Chromo 2UniRule annotationAdd BLAST67
Domaini823 – 997Helicase ATP-bindingUniRule annotationAdd BLAST175
Domaini1137 – 1288Helicase C-terminalUniRule annotationAdd BLAST152

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1789 – 2302Interaction with FAM124BUniRule annotation1 PublicationAdd BLAST514

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi948 – 951DEAH boxUniRule annotation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi292 – 410Gln-richUniRule annotationAdd BLAST119
Compositional biasi2069 – 2098Ser-richUniRule annotationAdd BLAST30
Compositional biasi2493 – 2508His-richUniRule annotationAdd BLAST16
Compositional biasi2539 – 2581Asp-richUniRule annotationAdd BLAST43

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family. CHD8 subfamily.UniRule annotation
Contains 2 chromo domains.UniRule annotation
Contains 1 helicase ATP-binding domain.UniRule annotation
Contains 1 helicase C-terminal domain.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0383. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00760000119067.
HOVERGENiHBG107676.
InParanoidiQ9HCK8.
KOiK04494.
OMAiFLAYMED.
OrthoDBiEOG091G0022.
PhylomeDBiQ9HCK8.
TreeFamiTF313572.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_03071. CHD8. 1 hit.
InterProiIPR006576. BRK_domain.
IPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
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. AlignAdd to basket

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

        10         20         30         40         50
MADPIMDLFD DPNLFGLDSL TDDSFNQVTQ DPIEEALGLP SSLDSLDQMN
60 70 80 90 100
QDGGGGDVGN SSASELVPPP EETAPTELSK ESTAPAPESI TLHDYTTQPA
110 120 130 140 150
SQEQPAQPVL QTSTPTSGLL QVSKSQEILS QGNPFMGVSA TAVSSSSAGG
160 170 180 190 200
QPPQSAPKIV ILKAPPSSSV TGAHVAQIQA QGITSTAQPL VAGTANGGKV
210 220 230 240 250
TFTKVLTGTP LRPGVSIVSG NTVLAAKVPG NQAAVQRIVQ PSRPVKQLVL
260 270 280 290 300
QPVKGSAPAG NPGATGPPLK PAVTLTSTPT QGESKRITLV LQQPQSGGPQ
310 320 330 340 350
GHRHVVLGSL PGKIVLQGNQ LAALTQAKNA QGQPAKVVTI QLQVQQPQQK
360 370 380 390 400
IQIVPQPPSS QPQPQQPPST QPVTLSSVQQ AQIMGPGQSP GQRLSVPVKV
410 420 430 440 450
VLQPQAGSSQ GASSGLSVVK VLSASEVAAL SSPASSAPHS GGKTGMEENR
460 470 480 490 500
RLEHQKKQEK ANRIVAEAIA RARARGEQNI PRVLNEDELP SVRPEEEGEK
510 520 530 540 550
KRRKKSAGER LKEEKPKKSK TSGASKTKGK SKLNTITPVV GKKRKRNTSS
560 570 580 590 600
DNSDVEVMPA QSPREDEESS IQKRRSNRQV KRKKYTEDLD IKITDDEEEE
610 620 630 640 650
EVDVTGPIKP EPILPEPVQE PDGETLPSMQ FFVENPSEED AAIVDKVLSM
660 670 680 690 700
RIVKKELPSG QYTEAEEFFV KYKNYSYLHC EWATISQLEK DKRIHQKLKR
710 720 730 740 750
FKTKMAQMRH FFHEDEEPFN PDYVEVDRIL DESHSIDKDN GEPVIYYLVK
760 770 780 790 800
WCSLPYEDST WELKEDVDEG KIREFKRIQS RHPELKRVNR PQASAWKKLE
810 820 830 840 850
LSHEYKNRNQ LREYQLEGVN WLLFNWYNRQ NCILADEMGL GKTIQSIAFL
860 870 880 890 900
QEVYNVGIHG PFLVIAPLST ITNWEREFNT WTEMNTIVYH GSLASRQMIQ
910 920 930 940 950
QYEMYCKDSR GRLIPGAYKF DALITTFEMI LSDCPELREI EWRCVIIDEA
960 970 980 990 1000
HRLKNRNCKL LDSLKHMDLE HKVLLTGTPL QNTVEELFSL LHFLEPSQFP
1010 1020 1030 1040 1050
SESEFLKDFG DLKTEEQVQK LQAILKPMML RRLKEDVEKN LAPKQETIIE
1060 1070 1080 1090 1100
VELTNIQKKY YRAILEKNFS FLSKGAGHTN MPNLLNTMME LRKCCNHPYL
1110 1120 1130 1140 1150
INGAEEKILT EFREACHIIP HDFHLQAMVR SAGKLVLIDK LLPKLKAGGH
1160 1170 1180 1190 1200
KVLIFSQMVR CLDILEDYLI QRRYLYERID GRVRGNLRQA AIDRFSKPDS
1210 1220 1230 1240 1250
DRFVFLLCTR AGGLGINLTA ADTCIIFDSD WNPQNDLQAQ ARCHRIGQSK
1260 1270 1280 1290 1300
AVKVYRLITR NSYEREMFDK ASLKLGLDKA VLQSMSGRDG NITGIQQFSK
1310 1320 1330 1340 1350
KEIEDLLRKG AYAAIMEEDD EGSKFCEEDI DQILLRRTTT ITIESEGKGS
1360 1370 1380 1390 1400
TFAKASFVAS ENRTDISLDD PNFWQKWAKK ADLDMDLLNS KNNLVIDTPR
1410 1420 1430 1440 1450
VRKQTRHFST LKDDDLVEFS DLESEDDERP RSRRHDRHHA YGRTDCFRVE
1460 1470 1480 1490 1500
KHLLVYGWGR WRDILSHGRF KRRMTERDVE TICRAILVYC LLHYRGDENI
1510 1520 1530 1540 1550
KGFIWDLISP AENGKTKELQ NHSGLSIPVP RGRKGKKVKS QSTFDIHKAD
1560 1570 1580 1590 1600
WIRKYNPDTL FQDESYKKHL KHQCNKVLLR VRMLYYLRQE VIGDQAEKVL
1610 1620 1630 1640 1650
GGAIASEIDI WFPVVDQLEV PTTWWDSEAD KSLLIGVFKH GYEKYNTMRA
1660 1670 1680 1690 1700
DPALCFLEKA GRPDDKAIAA EHRVLDNFSD IVEGVDFDKD CEDPEYKPLQ
1710 1720 1730 1740 1750
GPPKDQDDEG DPLMMMDEEI SVIDGDEAQV TQQPGHLFWP PGSALTARLR
1760 1770 1780 1790 1800
RLVTAYQRSY KREQMKIEAA ERGDRRRRRC EAAFKLKEIA RREKQQRWTR
1810 1820 1830 1840 1850
REQTDFYRVV STFGVEYDPD TMQFHWDRFR TFARLDKKTD ESLTKYFHGF
1860 1870 1880 1890 1900
VAMCRQVCRL PPAAGDEPPD PNLFIEPITE ERASRTLYRI ELLRRLREQV
1910 1920 1930 1940 1950
LCHPLLEDRL ALCQPPGPEL PKWWEPVRHD GELLRGAARH GVSQTDCNIM
1960 1970 1980 1990 2000
QDPDFSFLAA RMNYMQNHQA GAPAPSLSRC STPLLHQQYT SRTASPLPLR
2010 2020 2030 2040 2050
PDAPVEKSPE ETATQVPSLE SLTLKLEHEV VARSRPTPQD YEMRVSPSDT
2060 2070 2080 2090 2100
TPLVSRSVPP VKLEDEDDSD SELDLSKLSP SSSSSSSSSS SSSSTDESED
2110 2120 2130 2140 2150
EKEEKLTDQS RSKLYDEESL LSLTMSQDGF PNEDGEQMTP ELLLLQERQR
2160 2170 2180 2190 2200
ASEWPKDRVL INRIDLVCQA VLSGKWPSSR RSQEMVTGGI LGPGNHLLDS
2210 2220 2230 2240 2250
PSLTPGEYGD SPVPTPRSSS AASMAEEEAS AVSTAAAQFT KLRRGMDEKE
2260 2270 2280 2290 2300
FTVQIKDEEG LKLTFQKHKL MANGVMGDGH PLFHKKKGNR KKLVELEVEC
2310 2320 2330 2340 2350
MEEPNHLDVD LETRIPVINK VDGTLLVGED APRRAELEMW LQGHPEFAVD
2360 2370 2380 2390 2400
PRFLAYMEDR RKQKWQRCKK NNKAELNCLG MEPVQTANSR NGKKGHHTET
2410 2420 2430 2440 2450
VFNRVLPGPI APESSKKRAR RMRPDLSKMM ALMQGGSTGS LSLHNTFQHS
2460 2470 2480 2490 2500
SSGLQSVSSL GHSSATSASL PFMPFVMGGA PSSPHVDSST MLHHHHHHPH
2510 2520 2530 2540 2550
PHHHHHHHPG LRAPGYPSSP VTTASGTTLR LPPLQPEEDD DEDEEDDDDL
2560 2570 2580
SQGYDSSERD FSLIDDPMMP ANSDSSEDAD D
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)DescriptionActionsGraphical viewLength
Sequence conflicti594T → A in CAH18170 (PubMed:17974005).Curated1
Sequence conflicti1008D → N in CAH18170 (PubMed:17974005).Curated1
Sequence conflicti2481P → Q in CAH18170 (PubMed:17974005).Curated1
Sequence conflicti2568M → I in AAH36920 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0695732498Missing in AUTS18. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0172701 – 281MADPI…STPTQ → MK in isoform 2. 1 PublicationAdd BLAST281

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.3. human. [Q9HCK8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CKANMR-A2291-2364[»]
2DL6NMR-A2303-2372[»]
ProteinModelPortaliQ9HCK8.
SMRiQ9HCK8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121709. 60 interactors.
DIPiDIP-38021N.
IntActiQ9HCK8. 36 interactors.
MINTiMINT-7542705.
STRINGi9606.ENSP00000382863.

PTM databases

iPTMnetiQ9HCK8.
PhosphoSitePlusiQ9HCK8.

Polymorphism and mutation databases

BioMutaiCHD8.
DMDMi317373586.

Proteomic databases

EPDiQ9HCK8.
MaxQBiQ9HCK8.
PaxDbiQ9HCK8.
PeptideAtlasiQ9HCK8.
PRIDEiQ9HCK8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000399982; ENSP00000382863; ENSG00000100888. [Q9HCK8-1]
ENST00000430710; ENSP00000406288; ENSG00000100888. [Q9HCK8-2]
ENST00000557364; ENSP00000451601; ENSG00000100888. [Q9HCK8-1]
GeneIDi57680.
KEGGihsa:57680.
UCSCiuc001war.3. human. [Q9HCK8-1]

Organism-specific databases

CTDi57680.
DisGeNETi57680.
GeneCardsiCHD8.
HGNCiHGNC:20153. CHD8.
HPAiHPA052186.
MalaCardsiCHD8.
MIMi610528. gene.
615032. phenotype.
neXtProtiNX_Q9HCK8.
OpenTargetsiENSG00000100888.
Orphaneti106. Autism.
PharmGKBiPA134957052.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0383. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00760000119067.
HOVERGENiHBG107676.
InParanoidiQ9HCK8.
KOiK04494.
OMAiFLAYMED.
OrthoDBiEOG091G0022.
PhylomeDBiQ9HCK8.
TreeFamiTF313572.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000100888-MONOMER.
ReactomeiR-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
SIGNORiQ9HCK8.

Miscellaneous databases

ChiTaRSiCHD8. human.
EvolutionaryTraceiQ9HCK8.
GeneWikiiCHD8.
GenomeRNAii57680.
PROiQ9HCK8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100888.
CleanExiHS_CHD8.
ExpressionAtlasiQ9HCK8. baseline and differential.
GenevisibleiQ9HCK8. HS.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_03071. CHD8. 1 hit.
InterProiIPR006576. BRK_domain.
IPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 162 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.