CHD8_MOUSE - dbPTM
CHD8_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHD8_MOUSE
UniProt AC Q09XV5
Protein Name Chromodomain-helicase-DNA-binding protein 8 {ECO:0000255|HAMAP-Rule:MF_03071}
Gene Name Chd8 {ECO:0000255|HAMAP-Rule:MF_03071}
Organism Mus musculus (Mouse).
Sequence Length 2582
Subcellular Localization Nucleus . Localizes to the promoter regions of several CTNNB1-responsive genes. Also present at known CTCF target sites.
Protein Description 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..
Protein Sequence MADPIMDLFDDPNLFGLDSLTDDSFNQVTQDPIEEALGLPSSLDSLDQMNQDGGGGDVGNSSASDLVPPPEETASTELPKESTAPAPESLTLHDYTTQPTSQEQPAQPVLQTSTPTAGLLQVSKSQEILSQGNPFMGVSATGVSPSNTGGQPSQSAPKIVILKAPPNSSVTGTHVAQIQAQGITSTAQPLVAGTANGGKVTFTKVLTGTPLRPGVSIVSGNTVLATKVPGNQAAVQRIVQPSRPVKQLVLQPVKGSAPAGNPGAAGPPLKPAVTLTSTPTQGESKRITLVLQQPQSGGPQGHRHVVLGSLPGKIVLQGNQLAALTQAKNAQGQPAKVVTIQLQVQQPQQKIQIVPQPPSSQPQPQPQPPPSAQPLTLSSVQQAQIMGPGQNPGQRLSVPLKMVLQPQAGSSQGASSGLSVVKVLSASEVAALSSPASCAPHTAGKTGMEENRRLEHQKKQEKANRIVAEAIARARARGEQNIPRVLNEDELPSVRPEEEGEKKRRKKSSGERLKEEKPKKSKTAAASKTKGKSKLNTITPVVGKKRKRNTSSDNSDVEVMPAQSPREDEESSIQKRRSNRQVKRKKYTEDLDIKITDDEEEEEVDVTGPIKPEPILPEPVQEPDGETLPSMQFFVENPSEEDAAIVDKVLSMRVVKKELPSGQYTEAEEFFVKYKNYSYLHCEWATISQLEKDKRIHQKLKRFKTKMAQMRHFFHEDEEPFNPDYVEVDRILDESHSVDKDNGEPVIYYLVKWCSLPYEDSTWELKEDVDEGKIREFKRIQSRHPELRRVNRPQANAWKKLELSHEYKNRNQLREYQLEGVNWLLFNWYNRQNCILADEMGLGKTIQSIAFLQEVYNVGIHGPFLVIAPLSTITNWEREFNTWTEMNTIVYHGSLASRQMIQQYEMYCKDSRGRLIPGAYKFDALITTFEMILSDCPELREIEWRCVIIDEAHRLKNRNCKLLDSLKHMDLEHKVLLTGTPLQNTVEELFSLLHFLEPSQFPSESEFLKDFGDLKTEEQVQKLQAILKPMMLRRLKEDVEKNLAPKQETIIEVELTNIQKKYYRAILEKNFSFLSKGAGHTNMPNLLNTMMELRKCCNHPYLINGAEEKILMEFREACHIIPQDFHLQAMVRSAGKLVLIDKLLPKLKAGGHKVLIFSQMVRCLDILEDYLIQRRYLYERIDGRVRGNLRQAAIDRFSKPDSDRFVFLLCTRAGGLGINLTAADTCIIFDSDWNPQNDLQAQARCHRIGQSKAVKVYRLITRNSYEREMFDKASLKLGLDKAVLQSMSGRDGNITGIQQFSKKEIEDLLRKGAYAAIMEEDDEGSKFCEEDIDQILLRRTTTITIESEGKGSTFAKASFVASENRTDISLDDPNFWQKWAKKADLDMDLLNSKNNLVIDTPRVRKQTRHFSTLKDDDLVEFSDLESEDDERPRSRRHDRHHTYGRTDCFRVEKHLLVYGWGRWRDILSHGRFKRRMTERDVETICRAILVYCLLHYRGDENIKSFIWDLISPAENGKTKELQNHSGLSIPVPRGRKGKKVKSQSTFDIHKADWIRKYNPDTLFQDESYKKHLKHQCNKVLLRVRMLYYLRQEVIGDQAEKVLGGAIASEIDIWFPVVDQLEVPTTWWDSEADKSLLIGVFKHGYEKYNTMRADPALCFLEKAGRPDDKAIAAEHRVLDNFSDLVEGIDFDKDCEDPEYKPLQGPPKDPDDEGDPLMMMDEEISVIDGEEAQVTQQPGHLFWPPGSALTARLRRLVTAYQRSYKREQMKMEAAERGDRRRRRCEAAFKLKEIARREKQQRWTRREQTDFYRVVSTFGVEYDPDNMQFHWDRFRTFARLDKKTDESLTKYFHGFVAMCRQVCRLPPAAGDEPPDPNLFIEPITEERASRTLYRIELLRRLREQVLCHPLLEDRLALCQPPGLELPKWWEPVRHDGELLRGAARHGVSQTDCNIMQDPDFSFLAARMNYMQNHQAGASAASLSRCSTPLLHQQCTSRTASPSPLRPDAPVEKSPEESTVQVPNLESLTLKLEDEVVARSRLTSQDYEVRVGSSDTAPLSRSVPPVKLEDEDDSDSELDLSKLSPSSSSSSSSSSSSSSTDESEDEKEEKLTADRSRPKLYDEESLLSLTMSQDGFPNEDGEQMTPELLLLQERQRASEWPKDRVLINRIDLVCQAVLSGKWPSNRRSQEVTAGGILGPGNHLLDSPSLTPGEDGDSPVPTPRSGSAASMAEEEASAVTTAAAQFTKLRRGMDEKEFTVQIKDEEGLKLTFQKHRLMANGVMGDGHPLFHKKKGNRKKLVELEVECMEEPNHLDLDLETRIPVINKVDGTLLVGDEAPRRAELEMWLQGHPEFAVDPRFLAYMEERRKQKWQRCKKNNKAELNCLGMEPVQPANSRNGKKGHYAETAFNRVLPGPVAPENSKKRVRRTRPDLSKMMALMQGGSTGSLSLHNTFQHSSSNLQSVSSLGHSSTTSASLPFMPFVMGAAAPPHVDSSTMLHHHHHHPHPHHHHHHHPGLRTTGYPSSPATTTSGTALRLPTLQPEDDDEEEDEEDDDLSQGYDSSERDFSLIDDPMMPANSDSSEDADD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
125PhosphorylationGLLQVSKSQEILSQG
CEEEECCHHHHHHCC		26.0722802335
153PhosphorylationSNTGGQPSQSAPKIV
CCCCCCCCCCCCEEE		28.9522802335
155PhosphorylationTGGQPSQSAPKIVIL
CCCCCCCCCCEEEEE		51.3722802335
207PhosphorylationVTFTKVLTGTPLRPG
EEEEEEEECCCCCCC		41.8326643407
209PhosphorylationFTKVLTGTPLRPGVS
EEEEEECCCCCCCEE		17.5726643407
256PhosphorylationVLQPVKGSAPAGNPG
EEEECCCCCCCCCCC		25.9222802335
274PhosphorylationPPLKPAVTLTSTPTQ
CCCCCCEEEEECCCC		26.8222802335
284PhosphorylationSTPTQGESKRITLVL
ECCCCCCCCEEEEEE		33.7722802335
296PhosphorylationLVLQQPQSGGPQGHR
EEEECCCCCCCCCCC		53.02-
434PhosphorylationSEVAALSSPASCAPH
HHHHHHCCCCCCCCC		25.90-
462AcetylationEHQKKQEKANRIVAE
HHHHHHHHHHHHHHH		48.767612799
521PhosphorylationKEEKPKKSKTAAASK
HHHCCCCCCCCHHHC		41.1719854140
523PhosphorylationEKPKKSKTAAASKTK
HCCCCCCCCHHHCCC		28.7219854140
527PhosphorylationKSKTAAASKTKGKSK
CCCCCHHHCCCCCHH		35.8119854140
537PhosphorylationKGKSKLNTITPVVGK
CCCHHCCCCCCCCCC		36.3428066266
539PhosphorylationKSKLNTITPVVGKKR
CHHCCCCCCCCCCCC		14.1628066266
550PhosphorylationGKKRKRNTSSDNSDV
CCCCCCCCCCCCCCC		33.3725521595
551PhosphorylationKKRKRNTSSDNSDVE
CCCCCCCCCCCCCCE		38.9623429704
552PhosphorylationKRKRNTSSDNSDVEV
CCCCCCCCCCCCCEE		38.4823375375
555PhosphorylationRNTSSDNSDVEVMPA
CCCCCCCCCCEECCC		48.2825521595
564PhosphorylationVEVMPAQSPREDEES
CEECCCCCCCCCHHH		28.2025521595
571PhosphorylationSPREDEESSIQKRRS
CCCCCHHHHHHHHHH		30.6023375375
572PhosphorylationPREDEESSIQKRRSN
CCCCHHHHHHHHHHH		32.1129899451
773AcetylationKEDVDEGKIREFKRI
CCCCCHHHHHHHHHH		36.227630785
1009SumoylationPSESEFLKDFGDLKT
CCHHHHHHHHCCCCC		57.2228289178
1015SumoylationLKDFGDLKTEEQVQK
HHHHCCCCCHHHHHH		59.6428289178
1069UbiquitinationYYRAILEKNFSFLSK
HHHHHHHHCCCHHHC		60.9022790023
1272AcetylationYEREMFDKASLKLGL
HHHHCCCHHHHHHCC		28.7215618183
1302AcetylationTGIQQFSKKEIEDLL
CHHHHCCHHHHHHHH		56.5715618195
1400PhosphorylationKNNLVIDTPRVRKQT
CCCEEECCHHHHHHC		11.2322006019
1411PhosphorylationRKQTRHFSTLKDDDL
HHHCCCCCCCCCCCC		27.0625367039
1412PhosphorylationKQTRHFSTLKDDDLV
HHCCCCCCCCCCCCE		36.5625367039
1422PhosphorylationDDDLVEFSDLESEDD
CCCCEEHHHCCCCCC		27.9927087446
1426PhosphorylationVEFSDLESEDDERPR
EEHHHCCCCCCCCCC		54.3327087446
1468PhosphorylationGRWRDILSHGRFKRR
CHHHHHHHCCCHHHC		24.99-
1525PhosphorylationTKELQNHSGLSIPVP
CCCCCCCCCCCCCCC		49.32-
1542PhosphorylationRKGKKVKSQSTFDIH
CCCCCCCCCCCEEHH		32.1425338131
1681PhosphorylationHRVLDNFSDLVEGID
HHHHHCHHHHHCCCC		35.9723608596
1698PhosphorylationKDCEDPEYKPLQGPP
CCCCCCCCCCCCCCC		24.24-
1733PhosphorylationDGEEAQVTQQPGHLF
CCCCCEEECCCCCCC		14.9224704852
1966PhosphorylationFLAARMNYMQNHQAG
HHHHHHHHHHHCCCC		7.2525777480
1975PhosphorylationQNHQAGASAASLSRC
HHCCCCCCHHHHHHC		24.3726643407
1978PhosphorylationQAGASAASLSRCSTP
CCCCCHHHHHHCCCH		26.9626643407
1980PhosphorylationGASAASLSRCSTPLL
CCCHHHHHHCCCHHH		28.8421082442
1983PhosphorylationAASLSRCSTPLLHQQ
HHHHHHCCCHHHHHH		31.7621082442
1984PhosphorylationASLSRCSTPLLHQQC
HHHHHCCCHHHHHHH		22.9126745281
1992PhosphorylationPLLHQQCTSRTASPS
HHHHHHHCCCCCCCC		19.5321082442
1993PhosphorylationLLHQQCTSRTASPSP
HHHHHHCCCCCCCCC		34.9519060867
1995PhosphorylationHQQCTSRTASPSPLR
HHHHCCCCCCCCCCC		31.1125521595
1997PhosphorylationQCTSRTASPSPLRPD
HHCCCCCCCCCCCCC		25.8725521595
1999PhosphorylationTSRTASPSPLRPDAP
CCCCCCCCCCCCCCC		33.7925521595
2010PhosphorylationPDAPVEKSPEESTVQ
CCCCCCCCCCCCCEE		24.8426824392
2014PhosphorylationVEKSPEESTVQVPNL
CCCCCCCCCEECCCH		32.0126643407
2015PhosphorylationEKSPEESTVQVPNLE
CCCCCCCCEECCCHH		20.4525521595
2036PhosphorylationEDEVVARSRLTSQDY
CCHHHHHHHCCCCCE		23.1525777480
2039PhosphorylationVVARSRLTSQDYEVR
HHHHHHCCCCCEEEE		24.1927149854
2040PhosphorylationVARSRLTSQDYEVRV
HHHHHCCCCCEEEEE		26.1626824392
2043PhosphorylationSRLTSQDYEVRVGSS
HHCCCCCEEEEECCC		14.5328833060
2070PhosphorylationKLEDEDDSDSELDLS
CCCCCCCCCCCCCHH		56.1925521595
2072PhosphorylationEDEDDSDSELDLSKL
CCCCCCCCCCCHHHC		43.9725521595
2077PhosphorylationSDSELDLSKLSPSSS
CCCCCCHHHCCCCCC		31.0823737553
2184PhosphorylationKWPSNRRSQEVTAGG
CCCCCCCCCEEECCC		27.7025619855
2188PhosphorylationNRRSQEVTAGGILGP
CCCCCEEECCCCCCC		20.8725619855
2202PhosphorylationPGNHLLDSPSLTPGE
CCCCCCCCCCCCCCC		19.1621082442
2204PhosphorylationNHLLDSPSLTPGEDG
CCCCCCCCCCCCCCC		49.1522942356
2206PhosphorylationLLDSPSLTPGEDGDS
CCCCCCCCCCCCCCC		33.3221082442
2213PhosphorylationTPGEDGDSPVPTPRS
CCCCCCCCCCCCCCC		33.0726824392
2217PhosphorylationDGDSPVPTPRSGSAA
CCCCCCCCCCCCCHH		31.4125619855
2220PhosphorylationSPVPTPRSGSAASMA
CCCCCCCCCCHHHHH		38.0028833060
2222PhosphorylationVPTPRSGSAASMAEE
CCCCCCCCHHHHHHH		23.1628833060
2225PhosphorylationPRSGSAASMAEEEAS
CCCCCHHHHHHHHHH		20.4528833060
2232PhosphorylationSMAEEEASAVTTAAA
HHHHHHHHHHHHHHH		26.9328833060
2235PhosphorylationEEEASAVTTAAAQFT
HHHHHHHHHHHHHHH		15.5028833060
2242PhosphorylationTTAAAQFTKLRRGMD
HHHHHHHHHHHCCCC		19.6528833060
2326PhosphorylationVINKVDGTLLVGDEA
EEEEECCEEEECCCC		16.6828059163
2391PhosphorylationEPVQPANSRNGKKGH
CCCCCCCCCCCCCCC		29.2721183079
2439PhosphorylationMALMQGGSTGSLSLH
HHHHHCCCCCCEECH		36.10-
2440PhosphorylationALMQGGSTGSLSLHN
HHHHCCCCCCEECHH		33.78-
2442PhosphorylationMQGGSTGSLSLHNTF
HHCCCCCCEECHHHC		18.18-
2514PhosphorylationHHHPGLRTTGYPSSP
CCCCCCCCCCCCCCC		29.6125777480
2515PhosphorylationHHPGLRTTGYPSSPA
CCCCCCCCCCCCCCC		28.4325777480
2517PhosphorylationPGLRTTGYPSSPATT
CCCCCCCCCCCCCCC		9.6125777480
2519PhosphorylationLRTTGYPSSPATTTS
CCCCCCCCCCCCCCC		40.2326239621
2520PhosphorylationRTTGYPSSPATTTSG
CCCCCCCCCCCCCCC		17.6627149854
2523PhosphorylationGYPSSPATTTSGTAL
CCCCCCCCCCCCCEE		33.7128066266
2524PhosphorylationYPSSPATTTSGTALR
CCCCCCCCCCCCEEE		22.5228066266
2525PhosphorylationPSSPATTTSGTALRL
CCCCCCCCCCCEEEC		22.3228066266
2552PhosphorylationDEEDDDLSQGYDSSE
CCCCCCCCCCCCCCH		28.6726370283
2557PhosphorylationDLSQGYDSSERDFSL
CCCCCCCCCHHCCCC		26.1426370283
2574PhosphorylationDPMMPANSDSSEDAD
CCCCCCCCCCCCCCC		40.7619854140
2576PhosphorylationMMPANSDSSEDADD-
CCCCCCCCCCCCCC-		35.1319854140
2577PhosphorylationMPANSDSSEDADD--
CCCCCCCCCCCCC--		44.4819854140
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CHD8_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHD8_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CHD8_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IMA4_MOUSEKpna3physical
11744694
IMA5_MOUSEKpna1physical
11744694
IMA1_MOUSEKpna2physical
11744694
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CHD8_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1422 AND SER-1426, ANDMASS SPECTROMETRY.

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