ZN384_HUMAN - dbPTM
ZN384_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN384_HUMAN
UniProt AC Q8TF68
Protein Name Zinc finger protein 384
Gene Name ZNF384
Organism Homo sapiens (Human).
Sequence Length 577
Subcellular Localization Nucleus.
Protein Description Transcription factor that binds the consensus DNA sequence [GC]AAAAA. Seems to bind and regulate the promoters of MMP1, MMP3, MMP7 and COL1A1 (By similarity)..
Protein Sequence MEESHFNSNPYFWPSIPTVSGQIENTMFINKMKDQLLPEKGCGLAPPHYPTLLTVPASVSLPSGISMDTESKSDQLTPHSQASVTQNITVVPVPSTGLMTAGVSCSQRWRREGSQSRGPGLVITSPSGSLVTTASSAQTFPISAPMIVSALPPGSQALQVVPDLSKKVASTLTEEGGGGGGGGGSVAPKPPRGRKKKRMLESGLPEMNDPYVLSPEDDDDHQKDGKTYRCRMCSLTFYSKSEMQIHSKSHTETKPHKCPHCSKTFANSSYLAQHIRIHSGAKPYSCNFCEKSFRQLSHLQQHTRIHSKMHTETIKPHKCPHCSKTFANTSYLAQHLRIHSGAKPYNCSYCQKAFRQLSHLQQHTRIHTGDRPYKCAHPGCEKAFTQLSNLQSHRRQHNKDKPFKCHNCHRAYTDAASLEVHLSTHTVKHAKVYTCTICSRAYTSETYLMKHMRKHNPPDLQQQVQAAAAAAAVAQAQAQAQAQAQAQAQAQAQAQASQASQQQQQQQQQQQQQQQQPPPHFQSPGAAPQGGGGGDSNPNPPPQCSFDLTPYKTAEHHKDICLTVTTSTIQVEHLASS
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
11PhosphorylationSHFNSNPYFWPSIPT
CCCCCCCCCCCCCCC		23.64-
33UbiquitinationTMFINKMKDQLLPEK
CHHHHHHHHHCCCCC		43.8829967540
40UbiquitinationKDQLLPEKGCGLAPP
HHHCCCCCCCCCCCC		58.5229967540
58PhosphorylationTLLTVPASVSLPSGI
CEEEECCEEECCCCC		13.2327251275
58O-linked_GlycosylationTLLTVPASVSLPSGI
CEEEECCEEECCCCC		13.2323301498
60PhosphorylationLTVPASVSLPSGISM
EEECCEEECCCCCCC		31.8727251275
63PhosphorylationPASVSLPSGISMDTE
CCEEECCCCCCCCCC		54.7928348404
66PhosphorylationVSLPSGISMDTESKS
EECCCCCCCCCCCCC		17.7128348404
77O-linked_GlycosylationESKSDQLTPHSQASV
CCCCCCCCCCCCCCC		17.2123301498
80O-linked_GlycosylationSDQLTPHSQASVTQN
CCCCCCCCCCCCCCC		28.7523301498
83O-linked_GlycosylationLTPHSQASVTQNITV
CCCCCCCCCCCCEEE		20.3323301498
85O-linked_GlycosylationPHSQASVTQNITVVP
CCCCCCCCCCEEEEE		17.2523301498
89O-linked_GlycosylationASVTQNITVVPVPST
CCCCCCEEEEECCCC		24.0123301498
95O-linked_GlycosylationITVVPVPSTGLMTAG
EEEEECCCCCCCCCC		35.0323301498
112UbiquitinationCSQRWRREGSQSRGP
HHHHHHHCCCCCCCC		55.4029967540
167AcetylationVVPDLSKKVASTLTE
HCCCHHHHHHHCCCC		39.3926051181
167UbiquitinationVVPDLSKKVASTLTE
HCCCHHHHHHHCCCC		39.39-
170PhosphorylationDLSKKVASTLTEEGG
CHHHHHHHCCCCCCC		27.2622210691
171PhosphorylationLSKKVASTLTEEGGG
HHHHHHHCCCCCCCC		28.1422210691
173PhosphorylationKKVASTLTEEGGGGG
HHHHHCCCCCCCCCC		31.8928555341
185PhosphorylationGGGGGGGSVAPKPPR
CCCCCCCCCCCCCCC		20.5528555341
189AcetylationGGGSVAPKPPRGRKK
CCCCCCCCCCCCCCH		58.8926051181
202PhosphorylationKKKRMLESGLPEMND
CHHHHHHCCCCCCCC		41.4923403867
211PhosphorylationLPEMNDPYVLSPEDD
CCCCCCCCCCCCCCC		19.5230266825
214PhosphorylationMNDPYVLSPEDDDDH
CCCCCCCCCCCCCCC		19.0530266825
227PhosphorylationDHQKDGKTYRCRMCS
CCCCCCCEEEEEECE		23.0230631047
234PhosphorylationTYRCRMCSLTFYSKS
EEEEEECEEEEEECC		22.5422617229
236PhosphorylationRCRMCSLTFYSKSEM
EEEECEEEEEECCCE		12.3029978859
238PhosphorylationRMCSLTFYSKSEMQI
EECEEEEEECCCEEE		15.2328111955
251PhosphorylationQIHSKSHTETKPHKC
EEECCCCCCCCCCCC		53.06-
253PhosphorylationHSKSHTETKPHKCPH
ECCCCCCCCCCCCCC		51.54-
264PhosphorylationKCPHCSKTFANSSYL
CCCCCCCCCCCCHHH		16.2227080861
266UbiquitinationPHCSKTFANSSYLAQ
CCCCCCCCCCHHHHH		21.8929967540
268PhosphorylationCSKTFANSSYLAQHI
CCCCCCCCHHHHHHH		19.5525159151
269PhosphorylationSKTFANSSYLAQHIR
CCCCCCCHHHHHHHE		24.7925159151
270PhosphorylationKTFANSSYLAQHIRI
CCCCCCHHHHHHHEE		13.0821712546
279PhosphorylationAQHIRIHSGAKPYSC
HHHHEECCCCCCCCC		37.7724732914
282AcetylationIRIHSGAKPYSCNFC
HEECCCCCCCCCCCC		48.2726051181
284PhosphorylationIHSGAKPYSCNFCEK
ECCCCCCCCCCCCHH		25.7524732914
285PhosphorylationHSGAKPYSCNFCEKS
CCCCCCCCCCCCHHH		15.8824732914
291AcetylationYSCNFCEKSFRQLSH
CCCCCCHHHHHHHHH		56.9525825284
297PhosphorylationEKSFRQLSHLQQHTR
HHHHHHHHHHHHHHH		17.5120068231
303PhosphorylationLSHLQQHTRIHSKMH
HHHHHHHHHHHHHCC		27.2920068231
307PhosphorylationQQHTRIHSKMHTETI
HHHHHHHHHCCCCCC		29.3320068231
311PhosphorylationRIHSKMHTETIKPHK
HHHHHCCCCCCCCCC		31.1820068231
313PhosphorylationHSKMHTETIKPHKCP
HHHCCCCCCCCCCCC		35.1420068231
321UbiquitinationIKPHKCPHCSKTFAN
CCCCCCCCCCCCCCC		37.6429967540
340PhosphorylationAQHLRIHSGAKPYNC
HHHHHCCCCCCCCCC		37.7729214152
343AcetylationLRIHSGAKPYNCSYC
HHCCCCCCCCCCHHH		52.1126051181
358PhosphorylationQKAFRQLSHLQQHTR
HHHHHHHHHHHHHCC		17.51-
368PhosphorylationQQHTRIHTGDRPYKC
HHHCCCCCCCCCCCC		38.1026055452
382UbiquitinationCAHPGCEKAFTQLSN
CCCCCHHHHHHHHHH		53.5329967540
392PhosphorylationTQLSNLQSHRRQHNK
HHHHHHHHHHHHHCC		23.3328555341
433PhosphorylationTVKHAKVYTCTICSR
CCCCCEEEEEEECCC		8.7328152594
434PhosphorylationVKHAKVYTCTICSRA
CCCCEEEEEEECCCC		13.2228152594
442PhosphorylationCTICSRAYTSETYLM
EEECCCCCCCHHHHH		15.0821406692
443PhosphorylationTICSRAYTSETYLMK
EECCCCCCCHHHHHH		21.0721406692
444PhosphorylationICSRAYTSETYLMKH
ECCCCCCCHHHHHHH		18.4421406692
446PhosphorylationSRAYTSETYLMKHMR
CCCCCCHHHHHHHHH		23.0221406692
447PhosphorylationRAYTSETYLMKHMRK
CCCCCHHHHHHHHHH		10.7621406692
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 ZN384_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN384_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 ZN384_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TBA3C_HUMANTUBA3Cphysical
26186194
TRIP6_HUMANTRIP6physical
26186194
TBA3C_HUMANTUBA3Cphysical
28514442
TRIP6_HUMANTRIP6physical
28514442
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 ZN384_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-214, AND MASSSPECTROMETRY.

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