Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Chromodomain-helicase-DNA-binding protein 8

Gene

Chd8

Organism
Rattus norvegicus (Rat)
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

GO - Biological processi

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

ReactomeiR-RNO-3769402. Deactivation of the beta-catenin transactivating complex.

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
Axis duplication inhibitor
Short name:
Duplin
Gene namesi
Name:Chd8UniRule annotation
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi620696. Chd8.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi457K → R: Does not affect sumoylation status. 1 Publication1
Mutagenesisi512K → R: Does not affect sumoylation status. 1 Publication1
Mutagenesisi609K → R: Induces a decrease in sumoylation status. 1 Publication1
Mutagenesisi654K → R: Does not affect sumoylation status. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003673111 – 2581Chromodomain-helicase-DNA-binding protein 8Add BLAST2581

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei432PhosphoserineBy similarity1
Modified residuei553PhosphoserineBy similarity1
Modified residuei562PhosphoserineBy similarity1
Cross-linki609Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)UniRule annotation
Modified residuei1420PhosphoserineCombined sources1
Modified residuei1424PhosphoserineCombined sources1
Modified residuei1976PhosphoserineBy similarity1
Modified residuei1978PhosphoserineBy similarity1
Modified residuei1993PhosphothreonineBy similarity1
Modified residuei1995PhosphoserineCombined sources1
Modified residuei1997PhosphoserineCombined sources1
Modified residuei2008PhosphoserineBy similarity1
Modified residuei2068PhosphoserineCombined sources1
Modified residuei2070PhosphoserineCombined sources1
Modified residuei2182PhosphoserineBy similarity1
Modified residuei2200PhosphoserineBy similarity1
Modified residuei2202PhosphoserineBy similarity1
Modified residuei2204PhosphothreonineBy similarity1
Modified residuei2211PhosphoserineBy similarity1
Modified residuei2215PhosphothreonineBy similarity1
Modified residuei2223PhosphoserineCombined sources1
Cross-linki2256Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei2519PhosphoserineBy similarity1

Post-translational modificationi

Sumoylated.UniRule annotation1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9JIX5.
PRIDEiQ9JIX5.

PTM databases

iPTMnetiQ9JIX5.
PhosphoSitePlusiQ9JIX5.

Expressioni

Gene expression databases

BgeeiENSRNOG00000025011.
GenevisibleiQ9JIX5. RN.

Interactioni

Subunit structurei

Interacts with p53/TP53, histone H1 and CTCF. 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 (By similarity). Interacts with CTNNB1 (PubMed:10921920). Interacts with PIAS3 (PubMed:16452319).UniRule annotation2 Publications

GO - Molecular functioni

  • armadillo repeat domain binding Source: RGD
  • beta-catenin binding Source: UniProtKB
  • histone binding Source: UniProtKB
  • methylated histone binding Source: UniProtKB
  • p53 binding Source: UniProtKB

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022593.

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 annotationAdd 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 biasi2068 – 2097Ser-richUniRule annotationAdd BLAST30
Compositional biasi2493 – 2508His-richUniRule annotationAdd BLAST16
Compositional biasi2538 – 2581Asp-richUniRule annotationAdd BLAST44

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.
HOGENOMiHOG000246942.
HOVERGENiHBG107676.
InParanoidiQ9JIX5.
KOiK04494.
OMAiFLAYMED.
PhylomeDBiQ9JIX5.
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: Q9JIX5-1) [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
QDGGSGDVGN SSASDLVPPP EETASTELPK ESTAPAPESL TLHDYTTQPT
110 120 130 140 150
SQEQPAQPVL QTSTPTSGLL QVSKSQEILS QGNPFMGVSA TAVSPSNTGG
160 170 180 190 200
QPSQSAPKIV ILKAPPNSSV TGAHVAQIQA QGITSTAQPL VAGTANGGKV
210 220 230 240 250
TFTKVLTGTP LRPGVSIVSG NTVLATKVPG NQAAVQRIVQ PSRPVKQLVL
260 270 280 290 300
QPVKGSAPAG NPGATGPPLK PAVTLTSTPA QGESKRITLV LQQPQSGGPQ
310 320 330 340 350
GHRHVVLGSL PGKIVLQGNQ LAALTQAKSA QGQPAKVVTI QLQVQQPQQK
360 370 380 390 400
IQIVPQPPSS QPQPQPPPSA QPLTLSSVQQ AQIMGPGQNP GQRLSVPLKM
410 420 430 440 450
VLQPQAGSSQ GASSGLSVVK VLSASEVAAL SSPASCAPHT AGKTGMEENR
460 470 480 490 500
RLEHQKKQEK ANRIVAEAIA RARARGEQNI PRVLNEDELP SVRPEEEGEK
510 520 530 540 550
KRRKKSSGER LKEEKPKKSK TAAASKTKGK SKLNTITPVV GKKRKRNTSS
560 570 580 590 600
DNSDVEVMPA QSPREDEESS IQKRRSNRQV KRKKYTEDLD IKITDDEEEE
610 620 630 640 650
EVDVTGPIKP EPILPEPVPE PDGETLPSMQ FFVENPSEED AAIVDKVLSM
660 670 680 690 700
RVVKKELPSG QYTEAEEFFV KYKNYSYLHC EWATISQLEK DKRIHQKLKR
710 720 730 740 750
FKTKMAQMRH FFHEDEEPFN PDYVEVDRIL DESHSVDKDN GEPVIYYLVK
760 770 780 790 800
WCSLPYEDST WELKEDVDEG KIREFKRIQS RHPELKRVNR PQANAWKKLE
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
INGAEEKILM EFREACHIIP QDFHLQAMVR 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 RSRRHDRHHT YGRTDCFRVE
1460 1470 1480 1490 1500
KHLLVYGWGR WRDILSHGRF KRRMTERDVE TICRAILVYC LLHYRGDENI
1510 1520 1530 1540 1550
KSFIWDLISP 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 LVEGIDFDKD CEDPEYKPLQ
1710 1720 1730 1740 1750
GPPKDPDDEG DPLMMMDEEI SVIDGDEAPV TQQPGHLFWP PGSALTARLR
1760 1770 1780 1790 1800
RLVTAYQRSY KREQMKIEAA ERGDRRRRRC EAAFKLKEIA RREKQQRWTR
1810 1820 1830 1840 1850
REQTDFYRVV STFGVEYDPD NMQFHWDRFR TFARLDKKTD ESLTKYFHGF
1860 1870 1880 1890 1900
VAMCRQVCRL PPAAGDEPPD PNLFIEPITE ERASRTLYRI ELLRRLREQV
1910 1920 1930 1940 1950
LCHPLLEDRL ALCQPPGLEL PKWWEPVRHD GELLRGAARH GVSQTDCNIM
1960 1970 1980 1990 2000
QDPDFSFLAA RMNYMQNHQA GASAASLSRC STPLLHQQCT SRTASPSPLR
2010 2020 2030 2040 2050
PDVPAEKSPE ENAVQVPSLD SLTLKLEDEV VARSRLTPQD YEIRVASSDT
2060 2070 2080 2090 2100
APLSRSVPPV KLEDDDDSDS ELDLSKLSPS SSSSSSSSSS SSSSDESEDE
2110 2120 2130 2140 2150
KEEKLTADRS RPKLYDEESL LSLTMSQDGF PNEDGEQMTP ELLLLQERQR
2160 2170 2180 2190 2200
ASEWPKDRVL INRIDLVCQA VLSGKWPSNR RSQEMTTGGI LGPGNHLLDS
2210 2220 2230 2240 2250
PSLTPGEYGD SPVPTPRSSS AASMVEEEAS AVTTAAAQFT KLRRGMDEKE
2260 2270 2280 2290 2300
FTVQIKDEEG LKLTFQKHRL MANGVMGDGH PLFHKKKGNR KKLVELEVEC
2310 2320 2330 2340 2350
MEEPNHLDVD LETRIPVINK VDGTLLVGDE APRRAELDMW LQGHPEFAVD
2360 2370 2380 2390 2400
PRFLAYMEER RKQKWQRCKK NNKTELNCLG MEPVQPANSR NGKKGHYAET
2410 2420 2430 2440 2450
AFNRVLPGPI APENSKKRVR RTRPDLSKMM ALMQGGSTGS LSLHNTFQHS
2460 2470 2480 2490 2500
SSNLQSVSSL GHSSATSASL PFMPFVMGGA AAPPHVDSST MLHHHHHHPH
2510 2520 2530 2540 2550
PHHHHHHHPG LRTTGYPSSP ATTTSGTALR LPTLQHEDDD EEEDEDDDDL
2560 2570 2580
SQGYDSSERD FSLIDDPMMP ANSDSSDDAD D
Length:2,581
Mass (Da):290,692
Last modified:March 24, 2009 - v2
Checksum:i4E2BBE55D7A2CD3D
GO
Isoform 2 (identifier: Q9JIX5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     743-749: PVIYYLV → VSWAQRV
     750-2581: Missing.

Show »
Length:749
Mass (Da):80,667
Checksum:i3CAE4FF0BCF89D05
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_036678743 – 749PVIYYLV → VSWAQRV in isoform 2. 1 Publication7
Alternative sequenceiVSP_036679750 – 2581Missing in isoform 2. 1 PublicationAdd BLAST1832

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF169825 mRNA. Translation: AAF89678.1.
CH474040 Genomic DNA. Translation: EDL88472.1.
RefSeqiNP_075222.2. NM_022933.2. [Q9JIX5-1]
XP_006251973.1. XM_006251911.3. [Q9JIX5-1]
UniGeneiRn.98337.

Genome annotation databases

EnsembliENSRNOT00000022593; ENSRNOP00000022593; ENSRNOG00000025011. [Q9JIX5-1]
ENSRNOT00000087722; ENSRNOP00000071948; ENSRNOG00000025011. [Q9JIX5-1]
GeneIDi65027.
KEGGirno:65027.
UCSCiRGD:620696. rat. [Q9JIX5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF169825 mRNA. Translation: AAF89678.1.
CH474040 Genomic DNA. Translation: EDL88472.1.
RefSeqiNP_075222.2. NM_022933.2. [Q9JIX5-1]
XP_006251973.1. XM_006251911.3. [Q9JIX5-1]
UniGeneiRn.98337.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022593.

PTM databases

iPTMnetiQ9JIX5.
PhosphoSitePlusiQ9JIX5.

Proteomic databases

PaxDbiQ9JIX5.
PRIDEiQ9JIX5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000022593; ENSRNOP00000022593; ENSRNOG00000025011. [Q9JIX5-1]
ENSRNOT00000087722; ENSRNOP00000071948; ENSRNOG00000025011. [Q9JIX5-1]
GeneIDi65027.
KEGGirno:65027.
UCSCiRGD:620696. rat. [Q9JIX5-1]

Organism-specific databases

CTDi57680.
RGDi620696. Chd8.

Phylogenomic databases

eggNOGiKOG0383. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00760000119067.
HOGENOMiHOG000246942.
HOVERGENiHBG107676.
InParanoidiQ9JIX5.
KOiK04494.
OMAiFLAYMED.
PhylomeDBiQ9JIX5.
TreeFamiTF313572.

Enzyme and pathway databases

ReactomeiR-RNO-3769402. Deactivation of the beta-catenin transactivating complex.

Miscellaneous databases

PROiQ9JIX5.

Gene expression databases

BgeeiENSRNOG00000025011.
GenevisibleiQ9JIX5. RN.

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_RAT
AccessioniPrimary (citable) accession number: Q9JIX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 24, 2009
Last modified: November 2, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.