ZBTB4_HUMAN - dbPTM
ZBTB4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZBTB4_HUMAN
UniProt AC Q9P1Z0
Protein Name Zinc finger and BTB domain-containing protein 4
Gene Name ZBTB4
Organism Homo sapiens (Human).
Sequence Length 1013
Subcellular Localization Nucleus . Chromosome . Localizes to chromocenters.
Protein Description Transcriptional repressor with bimodal DNA-binding specificity. Represses transcription in a methyl-CpG-dependent manner. Binds with a higher affinity to methylated CpG dinucleotides in the consensus sequence 5'-CGCG-3' but can also bind to the non-methylated consensus sequence 5'-CTGCNA-3' also known as the consensus kaiso binding site (KBS). Can also bind specifically to a single methyl-CpG pair and can bind hemimethylated DNA but with a lower affinity compared to methylated DNA. [PubMed: 16354688 Plays a role in postnatal myogenesis, may be involved in the regulation of satellite cells self-renewal (By similarity]
Protein Sequence MPPPAEVTDPSHAPAVLRQLNEQRLRGLFCDVTLIAGDTKFPAHRSVLAASSPFFREALLTSAPLPLPPATGGAAPNPATTTAASSSSSSSSSSSSSSSSASSSSSSSSSSPPPASPPASSPPRVLELPGVPAAAFSDVLNFIYSARLALPGGGGDGAAVAEIGALGRRLGISRLQGLGEGGDAWVPPTPAPMATSQPEEDSFGPGPRPAGEWEGDRAEAQAPDLQCSLPRRPLPCPQCGKSFIHPKRLQTHEAQCRRGASTRGSTGLGAGGAGPGGPAGVDASALPPPVGFRGGPEHVVKVVGGHVLYVCAACERSYVTLSSLKRHSNVHSWRRKYPCRYCEKVFALAEYRTKHEVWHTGERRYQCIFCWETFVTYYNLKTHQRAFHGISPGLLASEKTPNGGYKPKLNTLKLYRLLPMRAAKRPYKTYSQGAPEAPLSPTLNTPAPVAMPASPPPGPPPAPEPGPPPSVITFAHPAPSVIVHGGSSSGGGGSGTASTGGSQAASVITYTAPPRPPKKREYPPPPPEPAATPTSPATAVSPATAAGPAMATTTEEAKGRNPRAGRTLTYTAKPVGGIGGGGGPPTGAGRGPSQLQAPPPLCQITVRIGEEAIVKRRISETDLRPGELSGEEMEESEEDEEEEDEEEEEEDEEESKAGGEDQLWRPYYSYKPKRKAGAAGGASVGGSGLPRGRRPPRWRQKLERRSWEETPAAESPAGRARTERRHRCGDCAQTFTTLRKLRKHQEAHGGGSHSSRAGRRPSTRFTCPHCAKVCKTAAALSRHGQRHAAERPGGTPTPVIAYSKGSAGTRPGDVKEEAPQEMQVSSSSGEAGGGSTAAEEASETASLQDPIISGGEEPPVVASGGSYVYPPVQEFPLALIGGGREPGGGRGKSGSEGPVGAGEGDRMEGIGAAKVTFYPEPYPLVYGPQLLAAYPYNFSNLAALPVALNMVLPDEKGAGALPFLPGVFGYAVNPQAAPPAPPTPPPPTLPPPIPPKGEGERAGVERTQKGDVG
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
40SumoylationTLIAGDTKFPAHRSV
EEEECCCCCHHHHHH		54.8328112733
87PhosphorylationTTTAASSSSSSSSSS
CCCCCCCCCCCCCCC		31.57-
88PhosphorylationTTAASSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
89PhosphorylationTAASSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
90PhosphorylationAASSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
91PhosphorylationASSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
92PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
93PhosphorylationSSSSSSSSSSSSSSS
CCCCCCCCCCCCCCC		35.87-
104PhosphorylationSSSSASSSSSSSSSS
CCCCCCCCCCCCCCC		31.57-
105PhosphorylationSSSASSSSSSSSSSP
CCCCCCCCCCCCCCC		35.87-
106PhosphorylationSSASSSSSSSSSSPP
CCCCCCCCCCCCCCC		35.87-
107PhosphorylationSASSSSSSSSSSPPP
CCCCCCCCCCCCCCC		35.87-
265PhosphorylationRGASTRGSTGLGAGG
CCCCCCCCCCCCCCC		18.93-
266PhosphorylationGASTRGSTGLGAGGA
CCCCCCCCCCCCCCC		38.97-
284PhosphorylationGPAGVDASALPPPVG
CCCCCCHHHCCCCCC		26.3519690332
322PhosphorylationERSYVTLSSLKRHSN
CCCEEEHHHHHHCCC		25.0226699800
323PhosphorylationRSYVTLSSLKRHSNV
CCEEEHHHHHHCCCC		40.8126699800
391PhosphorylationQRAFHGISPGLLASE
HHHHCCCCCCCCCCC		19.9430266825
397PhosphorylationISPGLLASEKTPNGG
CCCCCCCCCCCCCCC		39.3323186163
406AcetylationKTPNGGYKPKLNTLK
CCCCCCCCCCCCHHH		38.6626051181
415PhosphorylationKLNTLKLYRLLPMRA
CCCHHHHHHHHHHHH		9.53-
532PhosphorylationPPPEPAATPTSPATA
CCCCCCCCCCCCCCC		29.2528348404
534PhosphorylationPEPAATPTSPATAVS
CCCCCCCCCCCCCCC		42.8828348404
535PhosphorylationEPAATPTSPATAVSP
CCCCCCCCCCCCCCC		17.4628348404
538PhosphorylationATPTSPATAVSPATA
CCCCCCCCCCCCCCC		30.8628348404
541PhosphorylationTSPATAVSPATAAGP
CCCCCCCCCCCCCCC		13.3228348404
544PhosphorylationATAVSPATAAGPAMA
CCCCCCCCCCCCCCC		22.0328348404
552PhosphorylationAAGPAMATTTEEAKG
CCCCCCCCCCHHHCC		22.5924275569
573AcetylationRTLTYTAKPVGGIGG
CEEEEECEECCCCCC		32.2226051181
573SumoylationRTLTYTAKPVGGIGG
CEEEEECEECCCCCC		32.2228112733
605PhosphorylationPPPLCQITVRIGEEA
CCCEEEEEEEECCHH		4.2823312004
615SumoylationIGEEAIVKRRISETD
ECCHHHHEEECCCCC		29.8228112733
615SumoylationIGEEAIVKRRISETD
ECCHHHHEEECCCCC		29.82-
629PhosphorylationDLRPGELSGEEMEES
CCCCCCCCCCCCCCC		39.6028348404
636PhosphorylationSGEEMEESEEDEEEE
CCCCCCCCCCCHHHH		32.7428348404
675AcetylationYSYKPKRKAGAAGGA
CCCCCCCCCCCCCCC		58.2522368461
683PhosphorylationAGAAGGASVGGSGLP
CCCCCCCCCCCCCCC		25.2724247654
687PhosphorylationGGASVGGSGLPRGRR
CCCCCCCCCCCCCCC		31.0924247654
691MethylationVGGSGLPRGRRPPRW
CCCCCCCCCCCCCHH		57.1880701747
706PhosphorylationRQKLERRSWEETPAA
HHHHHHCCCCCCCCC		45.0930108239
710PhosphorylationERRSWEETPAAESPA
HHCCCCCCCCCCCCC		13.5021712546
715PhosphorylationEETPAAESPAGRART
CCCCCCCCCCHHHHH		18.4721815630
795PhosphorylationAAERPGGTPTPVIAY
HHCCCCCCCCCEEEE		29.8823401153
797PhosphorylationERPGGTPTPVIAYSK
CCCCCCCCCEEEEEC		29.9923403867
802PhosphorylationTPTPVIAYSKGSAGT
CCCCEEEEECCCCCC		10.3723403867
803PhosphorylationPTPVIAYSKGSAGTR
CCCEEEEECCCCCCC		22.8623403867
815SumoylationGTRPGDVKEEAPQEM
CCCCCCCCCCCCCCE		55.36-
895PhosphorylationGGRGKSGSEGPVGAG
CCCCCCCCCCCCCCC		46.6121815630
970PhosphorylationFLPGVFGYAVNPQAA
CCCCCCEEEECCCCC		8.9128348404
983PhosphorylationAAPPAPPTPPPPTLP
CCCCCCCCCCCCCCC		47.5728112733
988PhosphorylationPPTPPPPTLPPPIPP
CCCCCCCCCCCCCCC		58.6423879269
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
795TPhosphorylationKinaseHIPK2Q9H2X6
Uniprot
797TPhosphorylationKinaseHIPK2Q9H2X6
Uniprot
983TPhosphorylationKinaseHIPK2Q9H2X6
Uniprot
-KUbiquitinationE3 ubiquitin ligaseICP0P08393
PMID:32416261
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZBTB4_HUMAN !!
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 ZBTB4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIN3A_HUMANSIN3Aphysical
18451802
SIN3B_HUMANSIN3Bphysical
18451802
HIPK2_HUMANHIPK2physical
19448668
ZBT17_HUMANZBTB17physical
18451802
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZBTB4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The human protein kinase HIPK2 phosphorylates and downregulates themethyl-binding transcription factor ZBTB4.";
Yamada D., Perez-Torrado R., Filion G., Caly M., Jammart B.,Devignot V., Sasai N., Ravassard P., Mallet J., Sastre-Garau X.,Schmitz M.L., Defossez P.A.;
Oncogene 28:2535-2544(2009).
Cited for: PHOSPHORYLATION AT THR-795; THR-797 AND THR-983 BY HIPK2, MUTAGENESISOF THR-795; THR-797 AND THR-983, AND INTERACTION WITH HIPK2.

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