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Q09XV5

- CHD8_MOUSE

UniProt

Q09XV5 - CHD8_MOUSE

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Protein

Chromodomain-helicase-DNA-binding protein 8

Gene

Chd8

Organism
Mus musculus (Mouse)
Status
Reviewed - 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.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi838 – 8458ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB
  2. beta-catenin binding Source: UniProtKB
  3. DNA binding Source: UniProtKB
  4. DNA-dependent ATPase activity Source: UniProtKB
  5. DNA helicase activity Source: UniProtKB
  6. histone binding Source: UniProtKB
  7. methylated histone binding Source: UniProtKB
  8. p53 binding Source: UniProtKB

GO - Biological processi

  1. ATP-dependent chromatin remodeling Source: UniProtKB
  2. canonical Wnt signaling pathway Source: UniProtKB
  3. in utero embryonic development Source: MGI
  4. negative regulation of apoptotic process Source: UniProtKB
  5. negative regulation of fibroblast apoptotic process Source: MGI
  6. negative regulation of transcription, DNA-templated Source: UniProtKB
  7. negative regulation of Wnt signaling pathway Source: UniProtKB
  8. positive regulation of transcription, DNA-templated Source: UniProtKB
  9. positive regulation of transcription from RNA polymerase III promoter Source: UniProtKB
  10. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  11. 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

Names & Taxonomyi

Protein namesi
Recommended name:
Chromodomain-helicase-DNA-binding protein 8 (EC:3.6.4.12)
Short name:
CHD-8
Alternative name(s):
ATP-dependent helicase CHD8
Axis duplication inhibitor
Short name:
Duplin
Gene namesi
Name:Chd8
Synonyms:Kiaa1564
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1915022. Chd8.

Subcellular locationi

Nucleus 1 Publication
Note: Localizes to the promoter regions of several CTNNB1-responsive genes. Also present at known CTCF target sites.

GO - Cellular componenti

  1. MLL1 complex Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 25822582Chromodomain-helicase-DNA-binding protein 8PRO_0000367310Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei555 – 5551PhosphoserineBy similarity
Modified residuei564 – 5641PhosphoserineBy similarity
Cross-linki611 – 611Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei1422 – 14221PhosphoserineBy similarity
Modified residuei1426 – 14261PhosphoserineBy similarity
Modified residuei1978 – 19781PhosphoserineBy similarity
Modified residuei1995 – 19951PhosphothreonineBy similarity
Modified residuei2010 – 20101PhosphoserineBy similarity
Modified residuei2040 – 20401Phosphoserine1 Publication
Modified residuei2070 – 20701PhosphoserineBy similarity
Modified residuei2072 – 20721PhosphoserineBy similarity
Modified residuei2184 – 21841PhosphoserineBy similarity
Modified residuei2202 – 22021PhosphoserineBy similarity
Modified residuei2213 – 22131PhosphoserineBy similarity
Modified residuei2520 – 25201PhosphoserineBy similarity

Post-translational modificationi

Sumoylated.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ09XV5.
PaxDbiQ09XV5.
PRIDEiQ09XV5.

PTM databases

PhosphoSiteiQ09XV5.

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

BgeeiQ09XV5.
GenevestigatoriQ09XV5.

Interactioni

Subunit structurei

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, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with CHD7 (By similarity). Interacts with p53/TP53, histone H1, CTNNB1, CTCF and PIAS3. Component of a multiprotein complex of 900 kDa containing WDR5.By similarity2 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi212432. 4 interactions.
IntActiQ09XV5. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ09XV5.
SMRiQ09XV5. Positions 653-781, 790-1286, 2305-2374.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini644 – 71168Chromo 1PROSITE-ProRule annotationAdd
BLAST
Domaini726 – 79267Chromo 2PROSITE-ProRule annotationAdd
BLAST
Domaini825 – 999175Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1139 – 1290152Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi950 – 9534DEAH box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi292 – 412121Gln-richAdd
BLAST
Compositional biasi1777 – 17815Poly-Arg
Compositional biasi2070 – 209930Ser-richAdd
BLAST
Compositional biasi2494 – 250916His-richAdd
BLAST
Compositional biasi2539 – 258244Asp-richAdd
BLAST

Sequence similaritiesi

Contains 2 chromo domains.PROSITE-ProRule annotation
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0553.
GeneTreeiENSGT00760000119067.
HOGENOMiHOG000246942.
HOVERGENiHBG107676.
InParanoidiQ09XV5.
KOiK04494.
OMAiFLAYMED.
OrthoDBiEOG7NSB1C.
TreeFamiTF313572.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR006576. BRK_domain.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PfamiPF07533. BRK. 2 hits.
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. Align

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 BAC98203.2 differs from that shown. Reason: Partially unspliced pre-RNA.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211T → A in AAW56421. (PubMed:15367660)Curated
Sequence conflicti2020 – 20201N → S in BAC98203. (PubMed:14621295)Curated
Sequence conflicti2298 – 22981L → V in BAC98203. (PubMed:14621295)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei745 – 7517PVIYYLV → VSWARRT in isoform 2. 1 PublicationVSP_036676
Alternative sequencei752 – 25821831Missing in isoform 2. 1 PublicationVSP_036677Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006519476.1. [Q09XV5-1]
UniGeneiMm.289934.

Genome annotation databases

EnsembliENSMUST00000089752; ENSMUSP00000087184; 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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS36919.1. [Q09XV5-1 ]
RefSeqi NP_963999.2. NM_201637.2. [Q09XV5-1 ]
XP_006519539.1. XM_006519476.1. [Q09XV5-1 ]
UniGenei Mm.289934.

3D structure databases

ProteinModelPortali Q09XV5.
SMRi Q09XV5. Positions 653-781, 790-1286, 2305-2374.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 212432. 4 interactions.
IntActi Q09XV5. 1 interaction.

PTM databases

PhosphoSitei Q09XV5.

Proteomic databases

MaxQBi Q09XV5.
PaxDbi Q09XV5.
PRIDEi Q09XV5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000089752 ; ENSMUSP00000087184 ; ENSMUSG00000053754 . [Q09XV5-1 ]
GeneIDi 67772.
KEGGi mmu:67772.
UCSCi uc007tot.1. mouse. [Q09XV5-1 ]
uc007tov.1. mouse. [Q09XV5-2 ]

Organism-specific databases

CTDi 57680.
MGIi MGI:1915022. Chd8.
Rougei Search...

Phylogenomic databases

eggNOGi COG0553.
GeneTreei ENSGT00760000119067.
HOGENOMi HOG000246942.
HOVERGENi HBG107676.
InParanoidi Q09XV5.
KOi K04494.
OMAi FLAYMED.
OrthoDBi EOG7NSB1C.
TreeFami TF313572.

Miscellaneous databases

ChiTaRSi CHD8. mouse.
NextBioi 325525.
PROi Q09XV5.
SOURCEi Search...

Gene expression databases

Bgeei Q09XV5.
Genevestigatori Q09XV5.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR006576. BRK_domain.
IPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view ]
Pfami PF07533. BRK. 2 hits.
PF00385. Chromo. 2 hits.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view ]
SMARTi SM00592. BRK. 2 hits.
SM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 2 hits.
PROSITEi PS50013. CHROMO_2. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CTCF, SUBCELLULAR LOCATION.
    Tissue: Embryo.
  2. "Early embryonic death in mice lacking the beta-catenin-binding protein Duplin."
    Nishiyama M., Nakayama K., Tsunematsu R., Tsukiyama T., Kikuchi A., Nakayama K.I.
    Mol. Cell. Biol. 24:8386-8394(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1730-2582.
    Tissue: Brain.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2020-2582.
    Strain: C57BL/6J.
    Tissue: Thymus.
  5. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2040, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "CHD8 suppresses p53-mediated apoptosis through histone H1 recruitment during early embryogenesis."
    Nishiyama M., Oshikawa K., Tsukada Y.I., Nakagawa T., Iemura S., Natsume T., Fan Y., Kikuchi A., Skoultchi A.I., Nakayama K.I.
    Nat. Cell Biol. 11:172-182(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH TP53 AND HISTONE H1.

Entry informationi

Entry nameiCHD8_MOUSE
AccessioniPrimary (citable) accession number: Q09XV5
Secondary accession number(s): Q3TV89, Q5I1Z2, Q6ZPM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 17, 2006
Last modified: October 29, 2014
This is version 80 of the entry and version 1 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3