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Protein

Chromodomain-helicase-DNA-binding protein 8

Gene

Chd8

Organism
Mus musculus (Mouse)
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 bindingi838 – 845ATPUniRule 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

Complete GO annotation...

Keywordsi

Molecular functionActivator, Chromatin regulator, DNA-binding, Helicase, Hydrolase, Repressor
Biological processTranscription, Transcription regulation, Wnt signaling pathway
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-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
Synonyms:Kiaa1564
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1915022. Chd8.

Subcellular locationi

  • Nucleus UniRule annotation1 Publication

  • Note: Localizes to the promoter regions of several CTNNB1-responsive genes. Also present at known CTCF target sites.UniRule annotation

GO - Cellular componenti

  • MLL1 complex Source: UniProtKB
  • nucleoplasm Source: MGI
  • nucleus Source: UniProtKB
  • protein complex Source: MGI

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Death during early embryogenesis due to widespread apoptosis. Embryos manifest growth retardation from E5.5 and developmental arrest accompanied by massive apoptosis at E7.5. They develop into an egg cylinder but do not form a primitive streak or mesoderm. Mice lacking both Tp53 and Chd8 ameliorate this developmental arrest.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003673101 – 2582Chromodomain-helicase-DNA-binding protein 8Add BLAST2582

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei434PhosphoserineBy similarity1
Modified residuei555PhosphoserineCombined sources1
Modified residuei564PhosphoserineBy similarity1
Cross-linki611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)UniRule annotation
Modified residuei1422PhosphoserineCombined sources1
Modified residuei1426PhosphoserineCombined sources1
Modified residuei1978PhosphoserineBy similarity1
Modified residuei1980PhosphoserineBy similarity1
Modified residuei1995PhosphothreonineBy similarity1
Modified residuei1997PhosphoserineBy similarity1
Modified residuei1999PhosphoserineCombined sources1
Modified residuei2010PhosphoserineBy similarity1
Modified residuei2040PhosphoserineCombined sources1
Modified residuei2070PhosphoserineBy similarity1
Modified residuei2072PhosphoserineBy similarity1
Modified residuei2184PhosphoserineBy similarity1
Modified residuei2202PhosphoserineCombined sources1
Modified residuei2204PhosphoserineCombined sources1
Modified residuei2206PhosphothreonineCombined sources1
Modified residuei2213PhosphoserineCombined sources1
Modified residuei2217PhosphothreonineCombined sources1
Modified residuei2225PhosphoserineBy similarity1
Cross-linki2258Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei2520PhosphoserineBy similarity1

Post-translational modificationi

Sumoylated.UniRule annotation

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ09XV5.
MaxQBiQ09XV5.
PaxDbiQ09XV5.
PeptideAtlasiQ09XV5.
PRIDEiQ09XV5.

PTM databases

iPTMnetiQ09XV5.
PhosphoSitePlusiQ09XV5.

Expressioni

Developmental stagei

Expressed predominantly from early- to mid-stage mouse embryogenesis. Detected throughout embryos from E7.5 to E9.5 but localizes predominantly in the brain, faces, branchial arches, limb buds, and tail buds of embryos at E10.5.1 Publication

Gene expression databases

BgeeiENSMUSG00000053754.
ExpressionAtlasiQ09XV5. baseline and differential.
GenevisibleiQ09XV5. MM.

Interactioni

Subunit structurei

Interacts with CTNNB1 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 (By similarity). Interacts with p53/TP53 and histone H1 (PubMed:19151705). Interacts with CTCF (PubMed:16949368).UniRule annotation2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CtcfQ611643EBI-1169080,EBI-932785

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

BioGridi212432. 4 interactors.
IntActiQ09XV5. 1 interactor.
STRINGi10090.ENSMUSP00000087184.

Structurei

3D structure databases

ProteinModelPortaliQ09XV5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini644 – 711Chromo 1UniRule annotationAdd BLAST68
Domaini726 – 792Chromo 2UniRule annotationAdd BLAST67
Domaini825 – 999Helicase ATP-bindingUniRule annotationAdd BLAST175
Domaini1139 – 1290Helicase C-terminalUniRule annotationAdd BLAST152

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1791 – 2304Interaction with FAM124BUniRule annotationAdd BLAST514

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi950 – 953DEAH boxUniRule annotation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi292 – 412Gln-richUniRule annotationAdd BLAST121
Compositional biasi2070 – 2099Ser-richUniRule annotationAdd BLAST30
Compositional biasi2494 – 2509His-richUniRule annotationAdd BLAST16
Compositional biasi2539 – 2582Asp-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.
InParanoidiQ09XV5.
KOiK04494.
OMAiFLAYMED.
OrthoDBiEOG091G0022.
TreeFamiTF313572.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_03071. CHD8. 1 hit.
InterProiIPR006576. BRK_domain.
IPR000953. Chromo/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: Q09XV5-1) [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 SSASDLVPPP EETASTELPK ESTAPAPESL TLHDYTTQPT
110 120 130 140 150
SQEQPAQPVL QTSTPTAGLL QVSKSQEILS QGNPFMGVSA TGVSPSNTGG
160 170 180 190 200
QPSQSAPKIV ILKAPPNSSV TGTHVAQIQA QGITSTAQPL VAGTANGGKV
210 220 230 240 250
TFTKVLTGTP LRPGVSIVSG NTVLATKVPG NQAAVQRIVQ PSRPVKQLVL
260 270 280 290 300
QPVKGSAPAG NPGAAGPPLK PAVTLTSTPT QGESKRITLV LQQPQSGGPQ
310 320 330 340 350
GHRHVVLGSL PGKIVLQGNQ LAALTQAKNA QGQPAKVVTI QLQVQQPQQK
360 370 380 390 400
IQIVPQPPSS QPQPQPQPPP SAQPLTLSSV QQAQIMGPGQ NPGQRLSVPL
410 420 430 440 450
KMVLQPQAGS SQGASSGLSV VKVLSASEVA ALSSPASCAP HTAGKTGMEE
460 470 480 490 500
NRRLEHQKKQ EKANRIVAEA IARARARGEQ NIPRVLNEDE LPSVRPEEEG
510 520 530 540 550
EKKRRKKSSG ERLKEEKPKK SKTAAASKTK GKSKLNTITP VVGKKRKRNT
560 570 580 590 600
SSDNSDVEVM PAQSPREDEE SSIQKRRSNR QVKRKKYTED LDIKITDDEE
610 620 630 640 650
EEEVDVTGPI KPEPILPEPV QEPDGETLPS MQFFVENPSE EDAAIVDKVL
660 670 680 690 700
SMRVVKKELP SGQYTEAEEF FVKYKNYSYL HCEWATISQL EKDKRIHQKL
710 720 730 740 750
KRFKTKMAQM RHFFHEDEEP FNPDYVEVDR ILDESHSVDK DNGEPVIYYL
760 770 780 790 800
VKWCSLPYED STWELKEDVD EGKIREFKRI QSRHPELRRV NRPQANAWKK
810 820 830 840 850
LELSHEYKNR NQLREYQLEG VNWLLFNWYN RQNCILADEM GLGKTIQSIA
860 870 880 890 900
FLQEVYNVGI HGPFLVIAPL STITNWEREF NTWTEMNTIV YHGSLASRQM
910 920 930 940 950
IQQYEMYCKD SRGRLIPGAY KFDALITTFE MILSDCPELR EIEWRCVIID
960 970 980 990 1000
EAHRLKNRNC KLLDSLKHMD LEHKVLLTGT PLQNTVEELF SLLHFLEPSQ
1010 1020 1030 1040 1050
FPSESEFLKD FGDLKTEEQV QKLQAILKPM MLRRLKEDVE KNLAPKQETI
1060 1070 1080 1090 1100
IEVELTNIQK KYYRAILEKN FSFLSKGAGH TNMPNLLNTM MELRKCCNHP
1110 1120 1130 1140 1150
YLINGAEEKI LMEFREACHI IPQDFHLQAM VRSAGKLVLI DKLLPKLKAG
1160 1170 1180 1190 1200
GHKVLIFSQM VRCLDILEDY LIQRRYLYER IDGRVRGNLR QAAIDRFSKP
1210 1220 1230 1240 1250
DSDRFVFLLC TRAGGLGINL TAADTCIIFD SDWNPQNDLQ AQARCHRIGQ
1260 1270 1280 1290 1300
SKAVKVYRLI TRNSYEREMF DKASLKLGLD KAVLQSMSGR DGNITGIQQF
1310 1320 1330 1340 1350
SKKEIEDLLR KGAYAAIMEE DDEGSKFCEE DIDQILLRRT TTITIESEGK
1360 1370 1380 1390 1400
GSTFAKASFV ASENRTDISL DDPNFWQKWA KKADLDMDLL NSKNNLVIDT
1410 1420 1430 1440 1450
PRVRKQTRHF STLKDDDLVE FSDLESEDDE RPRSRRHDRH HTYGRTDCFR
1460 1470 1480 1490 1500
VEKHLLVYGW GRWRDILSHG RFKRRMTERD VETICRAILV YCLLHYRGDE
1510 1520 1530 1540 1550
NIKSFIWDLI SPAENGKTKE LQNHSGLSIP VPRGRKGKKV KSQSTFDIHK
1560 1570 1580 1590 1600
ADWIRKYNPD TLFQDESYKK HLKHQCNKVL LRVRMLYYLR QEVIGDQAEK
1610 1620 1630 1640 1650
VLGGAIASEI DIWFPVVDQL EVPTTWWDSE ADKSLLIGVF KHGYEKYNTM
1660 1670 1680 1690 1700
RADPALCFLE KAGRPDDKAI AAEHRVLDNF SDLVEGIDFD KDCEDPEYKP
1710 1720 1730 1740 1750
LQGPPKDPDD EGDPLMMMDE EISVIDGEEA QVTQQPGHLF WPPGSALTAR
1760 1770 1780 1790 1800
LRRLVTAYQR SYKREQMKME AAERGDRRRR RCEAAFKLKE IARREKQQRW
1810 1820 1830 1840 1850
TRREQTDFYR VVSTFGVEYD PDNMQFHWDR FRTFARLDKK TDESLTKYFH
1860 1870 1880 1890 1900
GFVAMCRQVC RLPPAAGDEP PDPNLFIEPI TEERASRTLY RIELLRRLRE
1910 1920 1930 1940 1950
QVLCHPLLED RLALCQPPGL ELPKWWEPVR HDGELLRGAA RHGVSQTDCN
1960 1970 1980 1990 2000
IMQDPDFSFL AARMNYMQNH QAGASAASLS RCSTPLLHQQ CTSRTASPSP
2010 2020 2030 2040 2050
LRPDAPVEKS PEESTVQVPN LESLTLKLED EVVARSRLTS QDYEVRVGSS
2060 2070 2080 2090 2100
DTAPLSRSVP PVKLEDEDDS DSELDLSKLS PSSSSSSSSS SSSSSTDESE
2110 2120 2130 2140 2150
DEKEEKLTAD RSRPKLYDEE SLLSLTMSQD GFPNEDGEQM TPELLLLQER
2160 2170 2180 2190 2200
QRASEWPKDR VLINRIDLVC QAVLSGKWPS NRRSQEVTAG GILGPGNHLL
2210 2220 2230 2240 2250
DSPSLTPGED GDSPVPTPRS GSAASMAEEE ASAVTTAAAQ FTKLRRGMDE
2260 2270 2280 2290 2300
KEFTVQIKDE EGLKLTFQKH RLMANGVMGD GHPLFHKKKG NRKKLVELEV
2310 2320 2330 2340 2350
ECMEEPNHLD LDLETRIPVI NKVDGTLLVG DEAPRRAELE MWLQGHPEFA
2360 2370 2380 2390 2400
VDPRFLAYME ERRKQKWQRC KKNNKAELNC LGMEPVQPAN SRNGKKGHYA
2410 2420 2430 2440 2450
ETAFNRVLPG PVAPENSKKR VRRTRPDLSK MMALMQGGST GSLSLHNTFQ
2460 2470 2480 2490 2500
HSSSNLQSVS SLGHSSTTSA SLPFMPFVMG AAAPPHVDSS TMLHHHHHHP
2510 2520 2530 2540 2550
HPHHHHHHHP GLRTTGYPSS PATTTSGTAL RLPTLQPEDD DEEEDEEDDD
2560 2570 2580
LSQGYDSSER DFSLIDDPMM PANSDSSEDA DD
Length:2,582
Mass (Da):290,847
Last modified:October 17, 2006 - v1
Checksum:iD9432500F6A8C329
GO
Isoform 2 (identifier: Q09XV5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     745-751: PVIYYLV → VSWARRT
     752-2582: Missing.

Show »
Length:751
Mass (Da):80,950
Checksum:i23F272C1595F2A90
GO

Sequence cautioni

The sequence BAC98203 differs from that shown. Partially unspliced pre-RNA.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti21T → A in AAW56421 (PubMed:15367660).Curated1
Sequence conflicti2020N → S in BAC98203 (PubMed:14621295).Curated1
Sequence conflicti2298L → V in BAC98203 (PubMed:14621295).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_036676745 – 751PVIYYLV → VSWARRT in isoform 2. 1 Publication7
Alternative sequenceiVSP_036677752 – 2582Missing in isoform 2. 1 PublicationAdd BLAST1831

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ190419 mRNA. Translation: ABB02259.1.
AY863219 mRNA. Translation: AAW56421.1.
AK129393 Transcribed RNA. Translation: BAC98203.2. Sequence problems.
AK160299 mRNA. Translation: BAE35730.1.
CCDSiCCDS36919.1. [Q09XV5-1]
RefSeqiNP_963999.2. NM_201637.2. [Q09XV5-1]
XP_006519539.1. XM_006519476.3. [Q09XV5-1]
UniGeneiMm.289934.

Genome annotation databases

EnsembliENSMUST00000089752; ENSMUSP00000087184; ENSMUSG00000053754. [Q09XV5-1]
ENSMUST00000200169; ENSMUSP00000142890; ENSMUSG00000053754. [Q09XV5-1]
GeneIDi67772.
KEGGimmu:67772.
UCSCiuc007tot.1. mouse. [Q09XV5-1]
uc007tov.1. mouse. [Q09XV5-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ190419 mRNA. Translation: ABB02259.1.
AY863219 mRNA. Translation: AAW56421.1.
AK129393 Transcribed RNA. Translation: BAC98203.2. Sequence problems.
AK160299 mRNA. Translation: BAE35730.1.
CCDSiCCDS36919.1. [Q09XV5-1]
RefSeqiNP_963999.2. NM_201637.2. [Q09XV5-1]
XP_006519539.1. XM_006519476.3. [Q09XV5-1]
UniGeneiMm.289934.

3D structure databases

ProteinModelPortaliQ09XV5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212432. 4 interactors.
IntActiQ09XV5. 1 interactor.
STRINGi10090.ENSMUSP00000087184.

PTM databases

iPTMnetiQ09XV5.
PhosphoSitePlusiQ09XV5.

Proteomic databases

EPDiQ09XV5.
MaxQBiQ09XV5.
PaxDbiQ09XV5.
PeptideAtlasiQ09XV5.
PRIDEiQ09XV5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000089752; ENSMUSP00000087184; ENSMUSG00000053754. [Q09XV5-1]
ENSMUST00000200169; ENSMUSP00000142890; ENSMUSG00000053754. [Q09XV5-1]
GeneIDi67772.
KEGGimmu:67772.
UCSCiuc007tot.1. mouse. [Q09XV5-1]
uc007tov.1. mouse. [Q09XV5-2]

Organism-specific databases

CTDi57680.
MGIiMGI:1915022. Chd8.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0383. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00760000119067.
HOGENOMiHOG000246942.
HOVERGENiHBG107676.
InParanoidiQ09XV5.
KOiK04494.
OMAiFLAYMED.
OrthoDBiEOG091G0022.
TreeFamiTF313572.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiChd8. mouse.
PROiQ09XV5.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000053754.
ExpressionAtlasiQ09XV5. baseline and differential.
GenevisibleiQ09XV5. MM.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_03071. CHD8. 1 hit.
InterProiIPR006576. BRK_domain.
IPR000953. Chromo/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_MOUSE
AccessioniPrimary (citable) accession number: Q09XV5
Secondary accession number(s): Q3TV89, Q5I1Z2, Q6ZPM8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 17, 2006
Last modified: January 18, 2017
This is version 100 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.