Q09XV5 · CHD8_MOUSE
- ProteinChromodomain-helicase-DNA-binding protein 8
- GeneChd8
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2582 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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. Regulates alternative splicing of a core group of genes involved in neuronal differentiation, cell cycle and DNA repair. Enables H3K36me3-coupled transcription elongation and co-transcriptional RNA processing likely via interaction with HNRNPL.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Features
Showing features for binding site.
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameChromodomain-helicase-DNA-binding protein 8
- EC number
- Short namesCHD-8
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ09XV5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to the promoter regions of several CTNNB1-responsive genes. Also present at known CTCF target sites.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Death during early embryogenesis due to widespread apoptosis. Embryos manifest growth retardation from 5.5 dpc and developmental arrest accompanied by massive apoptosis at 7.5 dpc. 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.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 99 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000367310 | 1-2582 | Chromodomain-helicase-DNA-binding protein 8 | |||
Sequence: MADPIMDLFDDPNLFGLDSLTDDSFNQVTQDPIEEALGLPSSLDSLDQMNQDGGGGDVGNSSASDLVPPPEETASTELPKESTAPAPESLTLHDYTTQPTSQEQPAQPVLQTSTPTAGLLQVSKSQEILSQGNPFMGVSATGVSPSNTGGQPSQSAPKIVILKAPPNSSVTGTHVAQIQAQGITSTAQPLVAGTANGGKVTFTKVLTGTPLRPGVSIVSGNTVLATKVPGNQAAVQRIVQPSRPVKQLVLQPVKGSAPAGNPGAAGPPLKPAVTLTSTPTQGESKRITLVLQQPQSGGPQGHRHVVLGSLPGKIVLQGNQLAALTQAKNAQGQPAKVVTIQLQVQQPQQKIQIVPQPPSSQPQPQPQPPPSAQPLTLSSVQQAQIMGPGQNPGQRLSVPLKMVLQPQAGSSQGASSGLSVVKVLSASEVAALSSPASCAPHTAGKTGMEENRRLEHQKKQEKANRIVAEAIARARARGEQNIPRVLNEDELPSVRPEEEGEKKRRKKSSGERLKEEKPKKSKTAAASKTKGKSKLNTITPVVGKKRKRNTSSDNSDVEVMPAQSPREDEESSIQKRRSNRQVKRKKYTEDLDIKITDDEEEEEVDVTGPIKPEPILPEPVQEPDGETLPSMQFFVENPSEEDAAIVDKVLSMRVVKKELPSGQYTEAEEFFVKYKNYSYLHCEWATISQLEKDKRIHQKLKRFKTKMAQMRHFFHEDEEPFNPDYVEVDRILDESHSVDKDNGEPVIYYLVKWCSLPYEDSTWELKEDVDEGKIREFKRIQSRHPELRRVNRPQANAWKKLELSHEYKNRNQLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYHGSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAPKQETIIEVELTNIQKKYYRAILEKNFSFLSKGAGHTNMPNLLNTMMELRKCCNHPYLINGAEEKILMEFREACHIIPQDFHLQAMVRSAGKLVLIDKLLPKLKAGGHKVLIFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQSMSGRDGNITGIQQFSKKEIEDLLRKGAYAAIMEEDDEGSKFCEEDIDQILLRRTTTITIESEGKGSTFAKASFVASENRTDISLDDPNFWQKWAKKADLDMDLLNSKNNLVIDTPRVRKQTRHFSTLKDDDLVEFSDLESEDDERPRSRRHDRHHTYGRTDCFRVEKHLLVYGWGRWRDILSHGRFKRRMTERDVETICRAILVYCLLHYRGDENIKSFIWDLISPAENGKTKELQNHSGLSIPVPRGRKGKKVKSQSTFDIHKADWIRKYNPDTLFQDESYKKHLKHQCNKVLLRVRMLYYLRQEVIGDQAEKVLGGAIASEIDIWFPVVDQLEVPTTWWDSEADKSLLIGVFKHGYEKYNTMRADPALCFLEKAGRPDDKAIAAEHRVLDNFSDLVEGIDFDKDCEDPEYKPLQGPPKDPDDEGDPLMMMDEEISVIDGEEAQVTQQPGHLFWPPGSALTARLRRLVTAYQRSYKREQMKMEAAERGDRRRRRCEAAFKLKEIARREKQQRWTRREQTDFYRVVSTFGVEYDPDNMQFHWDRFRTFARLDKKTDESLTKYFHGFVAMCRQVCRLPPAAGDEPPDPNLFIEPITEERASRTLYRIELLRRLREQVLCHPLLEDRLALCQPPGLELPKWWEPVRHDGELLRGAARHGVSQTDCNIMQDPDFSFLAARMNYMQNHQAGASAASLSRCSTPLLHQQCTSRTASPSPLRPDAPVEKSPEESTVQVPNLESLTLKLEDEVVARSRLTSQDYEVRVGSSDTAPLSRSVPPVKLEDEDDSDSELDLSKLSPSSSSSSSSSSSSSSTDESEDEKEEKLTADRSRPKLYDEESLLSLTMSQDGFPNEDGEQMTPELLLLQERQRASEWPKDRVLINRIDLVCQAVLSGKWPSNRRSQEVTAGGILGPGNHLLDSPSLTPGEDGDSPVPTPRSGSAASMAEEEASAVTTAAAQFTKLRRGMDEKEFTVQIKDEEGLKLTFQKHRLMANGVMGDGHPLFHKKKGNRKKLVELEVECMEEPNHLDLDLETRIPVINKVDGTLLVGDEAPRRAELEMWLQGHPEFAVDPRFLAYMEERRKQKWQRCKKNNKAELNCLGMEPVQPANSRNGKKGHYAETAFNRVLPGPVAPENSKKRVRRTRPDLSKMMALMQGGSTGSLSLHNTFQHSSSNLQSVSSLGHSSTTSASLPFMPFVMGAAAPPHVDSSTMLHHHHHHPHPHHHHHHHPGLRTTGYPSSPATTTSGTALRLPTLQPEDDDEEEDEEDDDLSQGYDSSERDFSLIDDPMMPANSDSSEDADD | ||||||
Modified residue | 434 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 555 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 564 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 611 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K | ||||||
Modified residue | 1422 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1426 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1978 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1980 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1995 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 1997 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1999 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2010 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 2027 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 2040 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2070 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2072 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2184 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2202 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2204 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2206 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 2213 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 2217 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 2225 | Phosphoserine | ||||
Sequence: S | ||||||
Cross-link | 2258 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | ||||||
Modified residue | 2520 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Sumoylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
Expressed predominantly from early- to mid-stage mouse embryogenesis. Detected throughout embryos from 7.5 to 9.5 dpc but localizes predominantly in the brain, faces, branchial arches, limb buds, and tail buds of embryos at 10.5 dpc.
Gene expression databases
Interaction
Subunit
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).
Interacts with TLK2 (By similarity).
Interacts with HNRNPL in an RNA-dependent manner
Interacts with p53/TP53 and histone H1 (PubMed:19151705).
Interacts with CTCF (PubMed:16949368).
Interacts with TLK2 (By similarity).
Interacts with HNRNPL in an RNA-dependent manner
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q09XV5 | Cebpb P28033 | 2 | EBI-1169080, EBI-1029979 | |
BINARY | Q09XV5 | Ctcf Q61164 | 3 | EBI-1169080, EBI-932785 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 22-111 | Disordered | ||||
Sequence: DDSFNQVTQDPIEEALGLPSSLDSLDQMNQDGGGGDVGNSSASDLVPPPEETASTELPKESTAPAPESLTLHDYTTQPTSQEQPAQPVLQ | ||||||
Compositional bias | 43-58 | Polar residues | ||||
Sequence: LDSLDQMNQDGGGGDV | ||||||
Compositional bias | 89-111 | Polar residues | ||||
Sequence: SLTLHDYTTQPTSQEQPAQPVLQ | ||||||
Region | 136-155 | Disordered | ||||
Sequence: MGVSATGVSPSNTGGQPSQS | ||||||
Region | 253-283 | Disordered | ||||
Sequence: VKGSAPAGNPGAAGPPLKPAVTLTSTPTQGE | ||||||
Region | 349-377 | Disordered | ||||
Sequence: QKIQIVPQPPSSQPQPQPQPPPSAQPLTL | ||||||
Compositional bias | 357-373 | Pro residues | ||||
Sequence: PPSSQPQPQPQPPPSAQ | ||||||
Region | 475-585 | Disordered | ||||
Sequence: RARGEQNIPRVLNEDELPSVRPEEEGEKKRRKKSSGERLKEEKPKKSKTAAASKTKGKSKLNTITPVVGKKRKRNTSSDNSDVEVMPAQSPREDEESSIQKRRSNRQVKRK | ||||||
Compositional bias | 490-523 | Basic and acidic residues | ||||
Sequence: ELPSVRPEEEGEKKRRKKSSGERLKEEKPKKSKT | ||||||
Compositional bias | 562-585 | Basic and acidic residues | ||||
Sequence: AQSPREDEESSIQKRRSNRQVKRK | ||||||
Region | 598-617 | Disordered | ||||
Sequence: DEEEEEVDVTGPIKPEPILP | ||||||
Domain | 644-711 | Chromo 1 | ||||
Sequence: AIVDKVLSMRVVKKELPSGQYTEAEEFFVKYKNYSYLHCEWATISQLEKDKRIHQKLKRFKTKMAQMR | ||||||
Domain | 726-792 | Chromo 2 | ||||
Sequence: VEVDRILDESHSVDKDNGEPVIYYLVKWCSLPYEDSTWELKEDVDEGKIREFKRIQSRHPELRRVNR | ||||||
Domain | 825-999 | Helicase ATP-binding | ||||
Sequence: LFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYHGSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPS | ||||||
Motif | 950-953 | DEAH box | ||||
Sequence: DEAH | ||||||
Domain | 1139-1290 | Helicase C-terminal | ||||
Sequence: LIDKLLPKLKAGGHKVLIFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQSMSGR | ||||||
Compositional bias | 1694-1712 | Basic and acidic residues | ||||
Sequence: EDPEYKPLQGPPKDPDDEG | ||||||
Region | 1694-1715 | Disordered | ||||
Sequence: EDPEYKPLQGPPKDPDDEGDPL | ||||||
Region | 1791-2304 | Interaction with FAM124B | ||||
Sequence: IARREKQQRWTRREQTDFYRVVSTFGVEYDPDNMQFHWDRFRTFARLDKKTDESLTKYFHGFVAMCRQVCRLPPAAGDEPPDPNLFIEPITEERASRTLYRIELLRRLREQVLCHPLLEDRLALCQPPGLELPKWWEPVRHDGELLRGAARHGVSQTDCNIMQDPDFSFLAARMNYMQNHQAGASAASLSRCSTPLLHQQCTSRTASPSPLRPDAPVEKSPEESTVQVPNLESLTLKLEDEVVARSRLTSQDYEVRVGSSDTAPLSRSVPPVKLEDEDDSDSELDLSKLSPSSSSSSSSSSSSSSTDESEDEKEEKLTADRSRPKLYDEESLLSLTMSQDGFPNEDGEQMTPELLLLQERQRASEWPKDRVLINRIDLVCQAVLSGKWPSNRRSQEVTAGGILGPGNHLLDSPSLTPGEDGDSPVPTPRSGSAASMAEEEASAVTTAAAQFTKLRRGMDEKEFTVQIKDEEGLKLTFQKHRLMANGVMGDGHPLFHKKKGNRKKLVELEVECME | ||||||
Region | 1990-2019 | Disordered | ||||
Sequence: QCTSRTASPSPLRPDAPVEKSPEESTVQVP | ||||||
Region | 2045-2120 | Disordered | ||||
Sequence: VRVGSSDTAPLSRSVPPVKLEDEDDSDSELDLSKLSPSSSSSSSSSSSSSSTDESEDEKEEKLTADRSRPKLYDEE | ||||||
Compositional bias | 2076-2095 | Polar residues | ||||
Sequence: LSKLSPSSSSSSSSSSSSSS | ||||||
Compositional bias | 2096-2118 | Basic and acidic residues | ||||
Sequence: TDESEDEKEEKLTADRSRPKLYD | ||||||
Region | 2187-2233 | Disordered | ||||
Sequence: VTAGGILGPGNHLLDSPSLTPGEDGDSPVPTPRSGSAASMAEEEASA | ||||||
Region | 2486-2582 | Disordered | ||||
Sequence: HVDSSTMLHHHHHHPHPHHHHHHHPGLRTTGYPSSPATTTSGTALRLPTLQPEDDDEEEDEEDDDLSQGYDSSERDFSLIDDPMMPANSDSSEDADD | ||||||
Compositional bias | 2492-2512 | Basic residues | ||||
Sequence: MLHHHHHHPHPHHHHHHHPGL | ||||||
Compositional bias | 2516-2532 | Polar residues | ||||
Sequence: GYPSSPATTTSGTALRL | ||||||
Compositional bias | 2537-2554 | Acidic residues | ||||
Sequence: PEDDDEEEDEEDDDLSQG |
Sequence similarities
Belongs to the SNF2/RAD54 helicase family. CHD8 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q09XV5-1
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.
- Name1
- Length2,582
- Mass (Da)290,847
- Last updated2006-10-17 v1
- ChecksumD9432500F6A8C329
Q09XV5-2
- Name2
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2I3BR97 | A0A2I3BR97_MOUSE | Chd8 | 22 | ||
A0A2I3BRI1 | A0A2I3BRI1_MOUSE | Chd8 | 138 | ||
F7AL76 | F7AL76_MOUSE | Chd8 | 1031 |
Sequence caution
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 21 | in Ref. 2; AAW56421 | ||||
Sequence: T → A | ||||||
Compositional bias | 43-58 | Polar residues | ||||
Sequence: LDSLDQMNQDGGGGDV | ||||||
Compositional bias | 89-111 | Polar residues | ||||
Sequence: SLTLHDYTTQPTSQEQPAQPVLQ | ||||||
Compositional bias | 357-373 | Pro residues | ||||
Sequence: PPSSQPQPQPQPPPSAQ | ||||||
Compositional bias | 490-523 | Basic and acidic residues | ||||
Sequence: ELPSVRPEEEGEKKRRKKSSGERLKEEKPKKSKT | ||||||
Compositional bias | 562-585 | Basic and acidic residues | ||||
Sequence: AQSPREDEESSIQKRRSNRQVKRK | ||||||
Alternative sequence | VSP_036676 | 745-751 | in isoform 2 | |||
Sequence: PVIYYLV → VSWARRT | ||||||
Alternative sequence | VSP_036677 | 752-2582 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 1694-1712 | Basic and acidic residues | ||||
Sequence: EDPEYKPLQGPPKDPDDEG | ||||||
Sequence conflict | 2020 | in Ref. 3; BAC98203 | ||||
Sequence: N → S | ||||||
Compositional bias | 2076-2095 | Polar residues | ||||
Sequence: LSKLSPSSSSSSSSSSSSSS | ||||||
Compositional bias | 2096-2118 | Basic and acidic residues | ||||
Sequence: TDESEDEKEEKLTADRSRPKLYD | ||||||
Sequence conflict | 2298 | in Ref. 3; BAC98203 | ||||
Sequence: L → V | ||||||
Compositional bias | 2492-2512 | Basic residues | ||||
Sequence: MLHHHHHHPHPHHHHHHHPGL | ||||||
Compositional bias | 2516-2532 | Polar residues | ||||
Sequence: GYPSSPATTTSGTALRL | ||||||
Compositional bias | 2537-2554 | Acidic residues | ||||
Sequence: PEDDDEEEDEEDDDLSQG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ190419 EMBL· GenBank· DDBJ | ABB02259.1 EMBL· GenBank· DDBJ | mRNA | ||
AY863219 EMBL· GenBank· DDBJ | AAW56421.1 EMBL· GenBank· DDBJ | mRNA | ||
AK129393 EMBL· GenBank· DDBJ | BAC98203.2 EMBL· GenBank· DDBJ | Transcribed RNA | Sequence problems. | |
AK160299 EMBL· GenBank· DDBJ | BAE35730.1 EMBL· GenBank· DDBJ | mRNA |