ZN227_HUMAN - dbPTM
ZN227_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN227_HUMAN
UniProt AC Q86WZ6
Protein Name Zinc finger protein 227
Gene Name ZNF227
Organism Homo sapiens (Human).
Sequence Length 799
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MPSQNYDLPQKKQEKMTKFQEAVTFKDVAVVFSREELRLLDLTQRKLYRDVMVENFKNLVAVGHLPFQPDMVSQLEAEEKLWMMETETQRSSKHQNKMETLQKFALKYLSNQELSCWQIWKQVASELTRCLQGKSSQLLQGDSIQVSENENNIMNPKGDSSIYIENQEFPFWRTQHSCGNTYLSESQIQSRGKQIDVKNNLQIHEDFMKKSPFHEHIKTDTEPKPCKGNEYGKIISDGSNQKLPLGEKPHPCGECGRGFSYSPRLPLHPNVHTGEKCFSQSSHLRTHQRIHPGEKLNRCHESGDCFNKSSFHSYQSNHTGEKSYRCDSCGKGFSSSTGLIIHYRTHTGEKPYKCEECGKCFSQSSNFQCHQRVHTEEKPYKCEECGKGFGWSVNLRVHQRVHRGEKPYKCEECGKGFTQAAHFHIHQRVHTGEKPYKCDVCGKGFSHNSPLICHRRVHTGEKPYKCEACGKGFTRNTDLHIHFRVHTGEKPYKCKECGKGFSQASNLQVHQNVHTGEKRFKCETCGKGFSQSSKLQTHQRVHTGEKPYRCDVCGKDFSYSSNLKLHQVIHTGEKPYKCEECGKGFSWRSNLHAHQRVHSGEKPYKCEQCDKSFSQAIDFRVHQRVHTGEKPYKCGVCGKGFSQSSGLQSHQRVHTGEKPYKCDVCGKGFRYSSQFIYHQRGHTGEKPYKCEECGKGFGRSLNLRHHQRVHTGEKPHICEECGKAFSLPSNLRVHLGVHTREKLFKCEECGKGFSQSARLEAHQRVHTGEKPYKCDICDKDFRHRSRLTYHQKVHTGKKL
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
6Phosphorylation--MPSQNYDLPQKKQ
--CCCCCCCCCHHHH		15.9527762562
17PhosphorylationQKKQEKMTKFQEAVT
HHHHHHCHHHHHCCC		39.5129514088
24PhosphorylationTKFQEAVTFKDVAVV
HHHHHCCCHHCEEEE		31.8329514088
160PhosphorylationIMNPKGDSSIYIENQ
CCCCCCCCCEEECCC		27.5728258704
161PhosphorylationMNPKGDSSIYIENQE
CCCCCCCCEEECCCC		24.9329759185
163PhosphorylationPKGDSSIYIENQEFP
CCCCCCEEECCCCCC		12.2529759185
174PhosphorylationQEFPFWRTQHSCGNT
CCCCCEECCCCCCCE		22.64-
190PhosphorylationLSESQIQSRGKQIDV
ECHHHHHHCCCEEEE		44.63-
198SumoylationRGKQIDVKNNLQIHE
CCCEEEECCCCEECH		36.05-
198SumoylationRGKQIDVKNNLQIHE
CCCEEEECCCCEECH		36.05-
209SumoylationQIHEDFMKKSPFHEH
EECHHHHHHCCCHHH		50.52-
209SumoylationQIHEDFMKKSPFHEH
EECHHHHHHCCCHHH		50.52-
211PhosphorylationHEDFMKKSPFHEHIK
CHHHHHHCCCHHHCC		27.5528555341
219PhosphorylationPFHEHIKTDTEPKPC
CCHHHCCCCCCCCCC		47.7729083192
221PhosphorylationHEHIKTDTEPKPCKG
HHHCCCCCCCCCCCC		60.4629083192
231PhosphorylationKPCKGNEYGKIISDG
CCCCCCCCCCEECCC		27.9329083192
233SumoylationCKGNEYGKIISDGSN
CCCCCCCCEECCCCC		35.64-
233SumoylationCKGNEYGKIISDGSN
CCCCCCCCEECCCCC		35.64-
236PhosphorylationNEYGKIISDGSNQKL
CCCCCEECCCCCCCC		39.1229083192
239PhosphorylationGKIISDGSNQKLPLG
CCEECCCCCCCCCCC		40.8729083192
242SumoylationISDGSNQKLPLGEKP
ECCCCCCCCCCCCCC		57.21-
242SumoylationISDGSNQKLPLGEKP
ECCCCCCCCCCCCCC		57.21-
248UbiquitinationQKLPLGEKPHPCGEC
CCCCCCCCCCCCCCC		46.99-
260PhosphorylationGECGRGFSYSPRLPL
CCCCCCCCCCCCCCC		27.7624719451
262PhosphorylationCGRGFSYSPRLPLHP
CCCCCCCCCCCCCCC		11.4424719451
264MethylationRGFSYSPRLPLHPNV
CCCCCCCCCCCCCCC		42.89115920405
279PhosphorylationHTGEKCFSQSSHLRT
CCCCCCCCCCHHHCC		38.3322210691
281PhosphorylationGEKCFSQSSHLRTHQ
CCCCCCCCHHHCCCC		20.6622210691
282PhosphorylationEKCFSQSSHLRTHQR
CCCCCCCHHHCCCCC		20.9222210691
295SumoylationQRIHPGEKLNRCHES
CCCCCCCHHHCCCCC		57.91-
295SumoylationQRIHPGEKLNRCHES
CCCCCCCHHHCCCCC		57.91-
324PhosphorylationNHTGEKSYRCDSCGK
CCCCCCEEECCCCCC		26.7430576142
343PhosphorylationSTGLIIHYRTHTGEK
CCCEEEEEEECCCCC		13.5430576142
345PhosphorylationGLIIHYRTHTGEKPY
CEEEEEEECCCCCCE		19.3428348404
347PhosphorylationIIHYRTHTGEKPYKC
EEEEEECCCCCCEEC		46.5626270265
350UbiquitinationYRTHTGEKPYKCEEC
EEECCCCCCEECCCC		55.80-
352PhosphorylationTHTGEKPYKCEECGK
ECCCCCCEECCCCCC		39.06-
353SumoylationHTGEKPYKCEECGKC
CCCCCCEECCCCCCE		43.63-
353SumoylationHTGEKPYKCEECGKC
CCCCCCEECCCCCCE		43.63-
353UbiquitinationHTGEKPYKCEECGKC
CCCCCCEECCCCCCE		43.63-
378SumoylationQRVHTEEKPYKCEEC
CCCCCCCCCEECCCC		47.63-
378SumoylationQRVHTEEKPYKCEEC
CCCCCCCCCEECCCC		47.63-
381SumoylationHTEEKPYKCEECGKG
CCCCCCEECCCCCCC		43.63-
381UbiquitinationHTEEKPYKCEECGKG
CCCCCCEECCCCCCC		43.63-
381SumoylationHTEEKPYKCEECGKG
CCCCCCEECCCCCCC		43.63-
409SumoylationHRGEKPYKCEECGKG
CCCCCCEECCCCCCC		43.63-
409UbiquitinationHRGEKPYKCEECGKG
CCCCCCEECCCCCCC		43.63-
409SumoylationHRGEKPYKCEECGKG
CCCCCCEECCCCCCC		43.63-
431PhosphorylationHIHQRVHTGEKPYKC
EEECCCCCCCCCEEC		44.1529496963
434SumoylationQRVHTGEKPYKCDVC
CCCCCCCCCEECCCC		55.80-
434UbiquitinationQRVHTGEKPYKCDVC
CCCCCCCCCEECCCC		55.80-
434SumoylationQRVHTGEKPYKCDVC
CCCCCCCCCEECCCC		55.80-
449PhosphorylationGKGFSHNSPLICHRR
CCCCCCCCCEEEECC		18.6923898821
459PhosphorylationICHRRVHTGEKPYKC
EEECCCCCCCCCEEC		44.1529496963
462UbiquitinationRRVHTGEKPYKCEAC
CCCCCCCCCEECCCC		55.80-
462SumoylationRRVHTGEKPYKCEAC
CCCCCCCCCEECCCC		55.80-
462SumoylationRRVHTGEKPYKCEAC
CCCCCCCCCEECCCC		55.80-
487PhosphorylationHIHFRVHTGEKPYKC
EEEEEEECCCCCEEC		44.1529496963
490SumoylationFRVHTGEKPYKCKEC
EEEECCCCCEECCCC		55.80-
490SumoylationFRVHTGEKPYKCKEC
EEEECCCCCEECCCC		55.80-
490UbiquitinationFRVHTGEKPYKCKEC
EEEECCCCCEECCCC		55.80-
515PhosphorylationQVHQNVHTGEKRFKC
EEECCCCCCCCEEEC		42.6328555341
530PhosphorylationETCGKGFSQSSKLQT
EECCCCCCCCCCCCC		37.5122210691
532PhosphorylationCGKGFSQSSKLQTHQ
CCCCCCCCCCCCCCC		28.3922210691
534SumoylationKGFSQSSKLQTHQRV
CCCCCCCCCCCCCCC		50.27-
534SumoylationKGFSQSSKLQTHQRV
CCCCCCCCCCCCCCC		50.27-
543PhosphorylationQTHQRVHTGEKPYRC
CCCCCCCCCCCCEEC		44.15-
546UbiquitinationQRVHTGEKPYRCDVC
CCCCCCCCCEECCCC		49.01-
560PhosphorylationCGKDFSYSSNLKLHQ
CCCCCCCCCCCEEEE		16.1428258704
571PhosphorylationKLHQVIHTGEKPYKC
EEEEEEECCCCCEEC		35.5929496963
574UbiquitinationQVIHTGEKPYKCEEC
EEEECCCCCEECCCC		55.80-
576PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECCCCCC		39.06-
577AcetylationHTGEKPYKCEECGKG
ECCCCCEECCCCCCC		43.6330593675
577SumoylationHTGEKPYKCEECGKG
ECCCCCEECCCCCCC		43.63-
577UbiquitinationHTGEKPYKCEECGKG
ECCCCCEECCCCCCC		43.63-
577SumoylationHTGEKPYKCEECGKG
ECCCCCEECCCCCCC		43.63-
612PhosphorylationKCEQCDKSFSQAIDF
CCCCCCCCHHHHHCE		19.5123403867
614PhosphorylationEQCDKSFSQAIDFRV
CCCCCCHHHHHCEEE		26.2823403867
627PhosphorylationRVHQRVHTGEKPYKC
EEECCCCCCCCCEEC		44.1529496963
630UbiquitinationQRVHTGEKPYKCGVC
CCCCCCCCCEECCCC		55.80-
630SumoylationQRVHTGEKPYKCGVC
CCCCCCCCCEECCCC		55.80-
630SumoylationQRVHTGEKPYKCGVC
CCCCCCCCCEECCCC		55.80-
655PhosphorylationQSHQRVHTGEKPYKC
CCCCEEECCCCCEEC		44.1529496963
658UbiquitinationQRVHTGEKPYKCDVC
CEEECCCCCEECCCC		55.80-
658SumoylationQRVHTGEKPYKCDVC
CEEECCCCCEECCCC		55.80-
658SumoylationQRVHTGEKPYKCDVC
CEEECCCCCEECCCC		55.80-
689UbiquitinationHTGEKPYKCEECGKG
CCCCCCEECCCCCCC		43.63-
689SumoylationHTGEKPYKCEECGKG
CCCCCCEECCCCCCC		43.63-
689SumoylationHTGEKPYKCEECGKG
CCCCCCEECCCCCCC		43.63-
745SumoylationHTREKLFKCEECGKG
CCHHHEEECHHHCCC		51.69-
745SumoylationHTREKLFKCEECGKG
CCHHHEEECHHHCCC		51.69-
767PhosphorylationEAHQRVHTGEKPYKC
HHHHHCCCCCCCCCC		44.1529496963
770SumoylationQRVHTGEKPYKCDIC
HHCCCCCCCCCCCCC		55.80-
770UbiquitinationQRVHTGEKPYKCDIC
HHCCCCCCCCCCCCC		55.80-
770SumoylationQRVHTGEKPYKCDIC
HHCCCCCCCCCCCCC		55.80-
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 ZN227_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN227_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 ZN227_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CEP70_HUMANCEP70physical
25416956
M3K20_HUMANZAKphysical
28514442
ZN664_HUMANZNF664physical
28514442
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN227_HUMAN

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Related Literatures of Post-Translational Modification

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