ZBT10_HUMAN - dbPTM
ZBT10_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZBT10_HUMAN
UniProt AC Q96DT7
Protein Name Zinc finger and BTB domain-containing protein 10
Gene Name ZBTB10
Organism Homo sapiens (Human).
Sequence Length 871
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MSFSEMNRRTLAFRGGGLVTASGGGSTNNNAGGEASAWPPQPQPRQPPPPAPPALQPPNGRGADEEVELEGLEPQDLEASAGPAAGAAEEAKELLLPQDAGGPTSLGGGAGGPLLAERNRRTLAFRGGGGGGLGNNGSSRGRPETSVWPLRHFNGRGPATVDLELDALEGKELMQDGASLSDSTEDEEEGASLGDGSGAEGGSCSSSRRSGGDGGDEVEGSGVGAGEGETVQHFPLARPKSLMQKLQCSFQTSWLKDFPWLRYSKDTGLMSCGWCQKTPADGGSVDLPPVGHDELSRGTRNYKKTLLLRHHVSTEHKLHEANAQESEIPSEEGYCDFNSRPNENSYCYQLLRQLNEQRKKGILCDVSIVVSGKIFKAHKNILVAGSRFFKTLYCFSNKESPNQNNTTHLDIAAVQGFSVILDFLYSGNLVLTSQNAIEVMTVASYLQMSEVVQTCRNFIKDALNISIKSEAPESVVVDYNNRKPVNRDGLSSSRDQKIASFWATRNLTNLASNVKIENDGCNVDEGQIENYQMNDSSWVQDGSPEMAENESEGQTKVFIWNNMGSQGIQETGKTRRKNQTTKRFIYNIPPNNETNLEDCSVMQPPVAYPEENTLLIKEEPDLDGALLSGPDGDRNVNANLLAEAGTSQDGGDAGTSHDFKYGLMPGPSNDFKYGLIPGTSNDFKYGLIPGASNDFKYGLLPESWPKQETWENGESSLIMNKLKCPHCSYVAKYRRTLKRHLLIHTGVRSFSCDICGKLFTRREHVKRHSLVHKKDKKYKCMVCKKIFMLAASVGIRHGSRRYGVCVDCADKSQPGGQEGVDQGQDTEFPRDEEYEENEVGEADEELVDDGEDQNDPSRWDESGEVCMSLDD
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
2Phosphorylation------MSFSEMNRR
------CCHHHHHCC		37.1623401153
4Phosphorylation----MSFSEMNRRTL
----CCHHHHHCCCE		28.7323401153
80PhosphorylationEPQDLEASAGPAAGA
CHHHHHHCCCCCCCH		25.1227499020
104PhosphorylationPQDAGGPTSLGGGAG
CCCCCCCCCCCCCCC		39.6028348404
105PhosphorylationQDAGGPTSLGGGAGG
CCCCCCCCCCCCCCC		28.3124173317
126MethylationNRRTLAFRGGGGGGL
CCCCEEECCCCCCCC		36.9224129315
140MethylationLGNNGSSRGRPETSV
CCCCCCCCCCCCCCE		47.0030761589
160PhosphorylationFNGRGPATVDLELDA
CCCCCCCEEEEEEHH		20.0728348404
168 (in isoform 2)Ubiquitination-9.9621890473
210PhosphorylationSCSSSRRSGGDGGDE
CCCCCCCCCCCCCCC		46.1223401153
221PhosphorylationGGDEVEGSGVGAGEG
CCCCCCCCCCCCCCC		19.4629214152
230PhosphorylationVGAGEGETVQHFPLA
CCCCCCCEEEECCCC		36.0027251275
241PhosphorylationFPLARPKSLMQKLQC
CCCCCCHHHHHHHCC		31.5822210691
245SumoylationRPKSLMQKLQCSFQT
CCHHHHHHHCCHHCC		26.9328112733
267PhosphorylationWLRYSKDTGLMSCGW
CCEECCCCCCCCCCC		35.63-
278PhosphorylationSCGWCQKTPADGGSV
CCCCCCCCCCCCCCC		9.6026714015
284PhosphorylationKTPADGGSVDLPPVG
CCCCCCCCCCCCCCC		20.2830624053
367PhosphorylationKGILCDVSIVVSGKI
CCCCCEEEEEECCCH		9.0922210691
418PhosphorylationIAAVQGFSVILDFLY
HHHHCCCHHHHHHHH		18.31-
460UbiquitinationQTCRNFIKDALNISI
HHHHHHHHHHHCCCC		32.5821890473
460 (in isoform 1)Ubiquitination-32.5821890473
460UbiquitinationQTCRNFIKDALNISI
HHHHHHHHHHHCCCC		32.582189047
466PhosphorylationIKDALNISIKSEAPE
HHHHHCCCCCCCCCC		23.9229978859
468SumoylationDALNISIKSEAPESV
HHHCCCCCCCCCCCE		35.14-
468SumoylationDALNISIKSEAPESV
HHHCCCCCCCCCCCE		35.1428112733
474PhosphorylationIKSEAPESVVVDYNN
CCCCCCCCEEEECCC		21.1028355574
479PhosphorylationPESVVVDYNNRKPVN
CCCEEEECCCCCCCC		11.6125003641
483SumoylationVVDYNNRKPVNRDGL
EEECCCCCCCCCCCC		56.2828112733
497SumoylationLSSSRDQKIASFWAT
CCCCHHHHHHHHHHH		44.5228112733
508PhosphorylationFWATRNLTNLASNVK
HHHHCCHHHHHHCCE		31.5628555341
512PhosphorylationRNLTNLASNVKIEND
CCHHHHHHCCEEECC		45.3727499020
515SumoylationTNLASNVKIENDGCN
HHHHHCCEEECCCCC		48.86-
536PhosphorylationENYQMNDSSWVQDGS
EEEECCCCCCCCCCC		22.5428348404
537PhosphorylationNYQMNDSSWVQDGSP
EEECCCCCCCCCCCH		33.8428348404
543PhosphorylationSSWVQDGSPEMAENE
CCCCCCCCHHHHCCC		26.4422210691
565PhosphorylationFIWNNMGSQGIQETG
EEEECCCCCCCHHCC		17.9217525332
573SumoylationQGIQETGKTRRKNQT
CCCHHCCCCCCCCCC		46.4028112733
573AcetylationQGIQETGKTRRKNQT
CCCHHCCCCCCCCCC		46.4025953088
617SumoylationEENTLLIKEEPDLDG
CCCEEEEECCCCCCC		56.87-
628PhosphorylationDLDGALLSGPDGDRN
CCCCCEECCCCCCCC		49.4830266825
646PhosphorylationNLLAEAGTSQDGGDA
HHHHCCCCCCCCCCC		30.2029978859
647PhosphorylationLLAEAGTSQDGGDAG
HHHCCCCCCCCCCCC		25.9217525332
655PhosphorylationQDGGDAGTSHDFKYG
CCCCCCCCCCCCCCC		25.3029978859
656PhosphorylationDGGDAGTSHDFKYGL
CCCCCCCCCCCCCCC		21.8229978859
661 (in isoform 2)Phosphorylation-18.58-
668 (in isoform 2)Phosphorylation-55.75-
672SumoylationPGPSNDFKYGLIPGT
CCCCCCCCCCCCCCC		41.0728112733
679PhosphorylationKYGLIPGTSNDFKYG
CCCCCCCCCCCCCCC		20.9927251275
680PhosphorylationYGLIPGTSNDFKYGL
CCCCCCCCCCCCCCC		40.0726714015
684SumoylationPGTSNDFKYGLIPGA
CCCCCCCCCCCCCCC		41.0728112733
692PhosphorylationYGLIPGASNDFKYGL
CCCCCCCCCCCCCCC		42.7327499020
696SumoylationPGASNDFKYGLLPES
CCCCCCCCCCCCCCC		41.0728112733
706SumoylationLLPESWPKQETWENG
CCCCCCCCHHHCCCC		55.2828112733
709PhosphorylationESWPKQETWENGESS
CCCCCHHHCCCCCCC		35.27-
715PhosphorylationETWENGESSLIMNKL
HHCCCCCCCCHHHCC		31.66-
721PhosphorylationESSLIMNKLKCPHCS
CCCCHHHCCCCCCCH		31.7618669648
745PhosphorylationKRHLLIHTGVRSFSC
HHHHHEECCCCCEEC		30.3118669648
792PhosphorylationKIFMLAASVGIRHGS
HHHHHHHHHCCCCCC		18.4423898821
799PhosphorylationSVGIRHGSRRYGVCV
HHCCCCCCCCEEEEE		13.8823898821
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
-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 ZBT10_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 ZBT10_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN417_HUMANZNF417physical
25416956
MOB3C_HUMANMOB3Cphysical
25416956
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 ZBT10_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210 AND THR-745, ANDMASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-565 AND SER-647, ANDMASS SPECTROMETRY.

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