Q9HCK8 (CHD8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chromodomain-helicase-DNA-binding protein 8
Short name=CHD-8
EC=3.6.4.12

Alternative name(s):
ATP-dependent helicase CHD8
Helicase with SNF2 domain 1

Gene names

Name:	CHD8
Synonyms:	HELSNF1, KIAA1564

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2581 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA helicase that acts as a chromatin remodeling factor and regulates transcription. Acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. Suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity. Acts as a negative regulator of Wnt signaling pathway by regulating beta-catenin (CTNNB1) activity. Negatively regulates CTNNB1-targeted gene expression by being recruited specifically to the promoter regions of several CTNNB1 responsive genes. Involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. Acts as a suppressor of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. Also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. Ref.13 Ref.16
Catalytic activity	ATP + H2O = ADP + phosphate.
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 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. Ref.9 Ref.11 Ref.13 Ref.16 Ref.19
Subcellular location	Nucleus. Note: Localizes to the promoter regions of several CTNNB1-responsive genes. Also present at known CTCF target sites. Ref.16 Ref.19
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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation Wnt signaling pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Activator Chromatin regulator Helicase Hydrolase Repressor
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP-dependent chromatin remodeling Inferred from mutant phenotype Ref.16. Source: UniProtKB canonical Wnt receptor signaling pathway Inferred from direct assay Ref.16. Source: UniProtKB in utero embryonic development Inferred from electronic annotation. Source: Compara negative regulation of Wnt receptor signaling pathway Inferred from direct assay Ref.16. Source: UniProtKB negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from mutant phenotype Ref.16. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype Ref.13. Source: UniProtKB positive regulation of transcription from RNA polymerase III promoter Inferred from mutant phenotype Ref.13. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	MLL1 complex Inferred from direct assay Ref.9. Source: UniProtKB
Molecular_function	ATP binding Inferred from direct assay Ref.16. Source: UniProtKB DNA binding Inferred from mutant phenotype Ref.16. Source: UniProtKB DNA helicase activity Inferred from mutant phenotype Ref.16. Source: UniProtKB DNA-dependent ATPase activity Inferred from direct assay Ref.16. Source: UniProtKB beta-catenin binding Inferred from direct assay Ref.16. Source: UniProtKB methylated histone residue binding Inferred from direct assay Ref.13. Source: UniProtKB p53 binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CHD7	Q9P2D1	3	EBI-4410319,EBI-3951683

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2581

2581

Chromodomain-helicase-DNA-binding protein 8

PRO_0000080233

Regions

Domain

642 – 709

68

Chromo 1

Domain

724 – 790

67

Chromo 2

Domain

823 – 997

175

Helicase ATP-binding

Domain

1137 – 1288

152

Helicase C-terminal

Nucleotide binding

836 – 843

8

ATP Potential

Motif

948 – 951

4

DEAH box

Compositional bias

292 – 410

119

Gln-rich

Compositional bias

2069 – 2098

30

Ser-rich

Compositional bias

2493 – 2508

16

His-rich

Compositional bias

2539 – 2581

43

Asp-rich

Amino acid modifications

Modified residue

553

1

Phosphoserine Ref.18

Modified residue

562

1

Phosphoserine Ref.17

Modified residue

1420

1

Phosphoserine Ref.18 Ref.20 Ref.22

Modified residue

1424

1

Phosphoserine Ref.18 Ref.20 Ref.22

Modified residue

1976

1

Phosphoserine Ref.17

Modified residue

1993

1

Phosphothreonine Ref.18

Modified residue

2008

1

Phosphoserine Ref.17 Ref.18 Ref.20

Modified residue

2046

1

Phosphoserine Ref.17 Ref.20 Ref.22

Modified residue

2051

1

Phosphothreonine Ref.12

Modified residue

2069

1

Phosphoserine Ref.22

Modified residue

2071

1

Phosphoserine Ref.22

Modified residue

2182

1

Phosphoserine Ref.15

Modified residue

2200

1

Phosphoserine Ref.18

Modified residue

2211

1

Phosphoserine Ref.15

Modified residue

2519

1

Phosphoserine Ref.17

Cross-link

609

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence

1 – 281

281

MADPI…STPTQ → MK in isoform 2.

VSP_017270

Experimental info

Mutagenesis

842

1

K → R: Abolishes ATPase activity. Ref.16

Sequence conflict

594

1

T → A in CAH18170. Ref.1

Sequence conflict

1008

1

D → N in CAH18170. Ref.1

Sequence conflict

2481

1

P → Q in CAH18170. Ref.1

Sequence conflict

2568

1

M → I in AAH36920. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

2581

Helix Strand Turn

Details...

Beta strand

2311 – 2314

4

Beta strand

2317 – 2319

3

Turn

2320 – 2322

3

Helix

2328 – 2330

3

Helix

2334 – 2343

10

Beta strand

2347 – 2349

3

Helix

2351 – 2359

9

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 11, 2011. Version 5. Checksum: 379F09DC6F814851	FASTA	2,581	290,519
	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 SESEFLKDFG 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
	Isoform 2 [UniParc]. Checksum: 3BA9FCDF2186AC0F	FASTA	2,302	262,348
	10 20 30 40 50 60 MKGESKRITL VLQQPQSGGP QGHRHVVLGS LPGKIVLQGN QLAALTQAKN AQGQPAKVVT 70 80 90 100 110 120 IQLQVQQPQQ KIQIVPQPPS SQPQPQQPPS TQPVTLSSVQ QAQIMGPGQS PGQRLSVPVK 130 140 150 160 170 180 VVLQPQAGSS QGASSGLSVV KVLSASEVAA LSSPASSAPH SGGKTGMEEN RRLEHQKKQE 190 200 210 220 230 240 KANRIVAEAI ARARARGEQN IPRVLNEDEL PSVRPEEEGE KKRRKKSAGE RLKEEKPKKS 250 260 270 280 290 300 KTSGASKTKG KSKLNTITPV VGKKRKRNTS SDNSDVEVMP AQSPREDEES SIQKRRSNRQ 310 320 330 340 350 360 VKRKKYTEDL DIKITDDEEE EEVDVTGPIK PEPILPEPVQ EPDGETLPSM QFFVENPSEE 370 380 390 400 410 420 DAAIVDKVLS MRIVKKELPS GQYTEAEEFF VKYKNYSYLH CEWATISQLE KDKRIHQKLK 430 440 450 460 470 480 RFKTKMAQMR HFFHEDEEPF NPDYVEVDRI LDESHSIDKD NGEPVIYYLV KWCSLPYEDS 490 500 510 520 530 540 TWELKEDVDE GKIREFKRIQ SRHPELKRVN RPQASAWKKL ELSHEYKNRN QLREYQLEGV 550 560 570 580 590 600 NWLLFNWYNR QNCILADEMG LGKTIQSIAF LQEVYNVGIH GPFLVIAPLS TITNWEREFN 610 620 630 640 650 660 TWTEMNTIVY HGSLASRQMI QQYEMYCKDS RGRLIPGAYK FDALITTFEM ILSDCPELRE 670 680 690 700 710 720 IEWRCVIIDE AHRLKNRNCK LLDSLKHMDL EHKVLLTGTP LQNTVEELFS LLHFLEPSQF 730 740 750 760 770 780 PSESEFLKDF GDLKTEEQVQ KLQAILKPMM LRRLKEDVEK NLAPKQETII EVELTNIQKK 790 800 810 820 830 840 YYRAILEKNF SFLSKGAGHT NMPNLLNTMM ELRKCCNHPY LINGAEEKIL TEFREACHII 850 860 870 880 890 900 PHDFHLQAMV RSAGKLVLID KLLPKLKAGG HKVLIFSQMV RCLDILEDYL IQRRYLYERI 910 920 930 940 950 960 DGRVRGNLRQ AAIDRFSKPD SDRFVFLLCT RAGGLGINLT AADTCIIFDS DWNPQNDLQA 970 980 990 1000 1010 1020 QARCHRIGQS KAVKVYRLIT RNSYEREMFD KASLKLGLDK AVLQSMSGRD GNITGIQQFS 1030 1040 1050 1060 1070 1080 KKEIEDLLRK GAYAAIMEED DEGSKFCEED IDQILLRRTT TITIESEGKG STFAKASFVA 1090 1100 1110 1120 1130 1140 SENRTDISLD DPNFWQKWAK KADLDMDLLN SKNNLVIDTP RVRKQTRHFS TLKDDDLVEF 1150 1160 1170 1180 1190 1200 SDLESEDDER PRSRRHDRHH AYGRTDCFRV EKHLLVYGWG RWRDILSHGR FKRRMTERDV 1210 1220 1230 1240 1250 1260 ETICRAILVY CLLHYRGDEN IKGFIWDLIS PAENGKTKEL QNHSGLSIPV PRGRKGKKVK 1270 1280 1290 1300 1310 1320 SQSTFDIHKA DWIRKYNPDT LFQDESYKKH LKHQCNKVLL RVRMLYYLRQ EVIGDQAEKV 1330 1340 1350 1360 1370 1380 LGGAIASEID IWFPVVDQLE VPTTWWDSEA DKSLLIGVFK HGYEKYNTMR ADPALCFLEK 1390 1400 1410 1420 1430 1440 AGRPDDKAIA AEHRVLDNFS DIVEGVDFDK DCEDPEYKPL QGPPKDQDDE GDPLMMMDEE 1450 1460 1470 1480 1490 1500 ISVIDGDEAQ VTQQPGHLFW PPGSALTARL RRLVTAYQRS YKREQMKIEA AERGDRRRRR 1510 1520 1530 1540 1550 1560 CEAAFKLKEI ARREKQQRWT RREQTDFYRV VSTFGVEYDP DTMQFHWDRF RTFARLDKKT 1570 1580 1590 1600 1610 1620 DESLTKYFHG FVAMCRQVCR LPPAAGDEPP DPNLFIEPIT EERASRTLYR IELLRRLREQ 1630 1640 1650 1660 1670 1680 VLCHPLLEDR LALCQPPGPE LPKWWEPVRH DGELLRGAAR HGVSQTDCNI MQDPDFSFLA 1690 1700 1710 1720 1730 1740 ARMNYMQNHQ AGAPAPSLSR CSTPLLHQQY TSRTASPLPL RPDAPVEKSP EETATQVPSL 1750 1760 1770 1780 1790 1800 ESLTLKLEHE VVARSRPTPQ DYEMRVSPSD TTPLVSRSVP PVKLEDEDDS DSELDLSKLS 1810 1820 1830 1840 1850 1860 PSSSSSSSSS SSSSSTDESE DEKEEKLTDQ SRSKLYDEES LLSLTMSQDG FPNEDGEQMT 1870 1880 1890 1900 1910 1920 PELLLLQERQ RASEWPKDRV LINRIDLVCQ AVLSGKWPSS RRSQEMVTGG ILGPGNHLLD 1930 1940 1950 1960 1970 1980 SPSLTPGEYG DSPVPTPRSS SAASMAEEEA SAVSTAAAQF TKLRRGMDEK EFTVQIKDEE 1990 2000 2010 2020 2030 2040 GLKLTFQKHK LMANGVMGDG HPLFHKKKGN RKKLVELEVE CMEEPNHLDV DLETRIPVIN 2050 2060 2070 2080 2090 2100 KVDGTLLVGE DAPRRAELEM WLQGHPEFAV DPRFLAYMED RRKQKWQRCK KNNKAELNCL 2110 2120 2130 2140 2150 2160 GMEPVQTANS RNGKKGHHTE TVFNRVLPGP IAPESSKKRA RRMRPDLSKM MALMQGGSTG 2170 2180 2190 2200 2210 2220 SLSLHNTFQH SSSGLQSVSS LGHSSATSAS LPFMPFVMGG APSSPHVDSS TMLHHHHHHP 2230 2240 2250 2260 2270 2280 HPHHHHHHHP GLRAPGYPSS PVTTASGTTL RLPPLQPEED DDEDEEDDDD LSQGYDSSER 2290 2300 DFSLIDDPMM PANSDSSEDA DD

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-562; SER-1976; SER-2008; SER-2046 AND SER-2519, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"CHD8 interacts with CHD7, a protein which is mutated in CHARGE syndrome." Batsukh T., Pieper L., Koszucka A.M., von Velsen N., Hoyer-Fender S., Elbracht M., Bergman J.E., Hoefsloot L.H., Pauli S. Hum. Mol. Genet. 19:2858-2866(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CHD7, SUBCELLULAR LOCATION.
[20]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]	"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, MASS SPECTROMETRY.
[23]	"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.

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.

IPI

IPI00398992.
IPI00719073.

RefSeq

NP_001164100.1. NM_001170629.1.
NP_065971.2. NM_020920.3.

UniGene

Hs.530698.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CKA	NMR	-	A	2291-2364	[»]
2DL6	NMR	-	A	2303-2372	[»]

ProteinModelPortal

Q9HCK8.

SMR

Q9HCK8. Positions 720-779, 2303-2372.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9HCK8. 17 interactions.

PTM databases

PhosphoSite

Q9HCK8.

Polymorphism databases

DMDM

226706293.

Proteomic databases

PaxDb

Q9HCK8.

PRIDE

Q9HCK8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000399982; ENSP00000382863; ENSG00000100888.
ENST00000430710; ENSP00000406288; ENSG00000100888.
ENST00000557364; ENSP00000451601; ENSG00000100888.

GeneID

57680.

KEGG

hsa:57680.

UCSC

uc001war.2. human.
uc001was.2. human.

Organism-specific databases

CTD

57680.

GeneCards

GC14M021853.

HGNC

HGNC:20153. CHD8.

HPA

HPA000849.

MIM

610528. gene.

neXtProt

NX_Q9HCK8.

PharmGKB

PA134957052.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0553.

HOVERGEN

HBG107676.

KO

K04494.

OMA

FLAYMED.

Gene expression databases

ArrayExpress

Q9HCK8.

Bgee

Q9HCK8.

CleanEx

HS_CHD8.

Genevestigator

Q9HCK8.

GermOnline

ENSG00000100888. Homo sapiens.

Family and domain databases

InterPro

IPR006576. BRK_domain.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR000330. SNF2_N.
[Graphical view]

Pfam

PF07533. BRK. 1 hit.
PF00385. Chromo. 2 hits.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]

SMART

SM00592. BRK. 2 hits.
SM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

SUPFAM

SSF54160. Chromodomain-like. 2 hits.

PROSITE

PS00598. 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]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9HCK8.

GenomeRNAi

57680.

NextBio

64494.

SOURCE

Search...

Entry information

Entry name

CHD8_HUMAN

Accession

Primary (citable) accession number: Q9HCK8
Secondary accession number(s): Q4G0D8 , Q68DQ0, Q6DKH9, Q6P440, Q6ZNL7, Q8N3Z9, Q8NCY4, Q8TBR9, Q96F26

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	January 11, 2011
Last modified:	April 3, 2013
This is version 128 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.