ZN503_HUMAN - dbPTM
ZN503_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN503_HUMAN
UniProt AC Q96F45
Protein Name Zinc finger protein 503
Gene Name ZNF503
Organism Homo sapiens (Human).
Sequence Length 646
Subcellular Localization Nucleus.
Protein Description May function as a transcriptional repressor..
Protein Sequence MSTAPSLSALRSSKHSGGGGGGGGGGGADPAWTSALSGNSSGPGPGSSPAGSTKPFVHAVPPSDPLRQANRLPIKVLKMLTARTGHILHPEYLQPLPSTPVSPIELDAKKSPLALLAQTCSQIGKPDPSPSSKLSSVASNGGGAGGAGGGAAGDKDTKSGPLKLSDIGVEDKSSFKPYSKPGSDKKEPGGGGGGGGGGGGGGGGVSSEKSGFRVPSATCQPFTPRTGSPSSSASACSPGGMLSSAGGAPEGKDDKKDTDVGGGGKGTGGASAEGGPTGLAHGRISCGGGINVDVNQHPDGGPGGKALGSDCGGSSGSSSGSGPSAPTSSSVLGSGLVAPVSPYKPGQTVFPLPPAGMTYPGSLAGAYAGYPPQFLPHGVALDPTKPGSLVGAQLAAAAAGSLGCSKPAGSSPLAGASPPSVMTASLCRDPYCLSYHCASHLAGAAAASASCAHDPAAAAAALKSGYPLVYPTHPLHGVHSSLTAAAAAGATPPSLAGHPLYPYGFMLPNDPLPHICNWVSANGPCDKRFATSEELLSHLRTHTAFPGTDKLLSGYPSSSSLASAAAAAMACHMHIPTSGAPGSPGTLALRSPHHALGLSSRYHPYSKSPLPTPGAPVPVPAATGPYYSPYALYGQRLTTASALGYQ
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
12PhosphorylationPSLSALRSSKHSGGG
CCHHHHHCCCCCCCC		44.5922210691
13PhosphorylationSLSALRSSKHSGGGG
CHHHHHCCCCCCCCC		28.1422210691
16PhosphorylationALRSSKHSGGGGGGG
HHHCCCCCCCCCCCC		42.7528961369
33PhosphorylationGGADPAWTSALSGNS
CCCCHHHHHHCCCCC		13.2628961369
34PhosphorylationGADPAWTSALSGNSS
CCCHHHHHHCCCCCC		19.2628961369
37PhosphorylationPAWTSALSGNSSGPG
HHHHHHCCCCCCCCC		35.3328961369
40PhosphorylationTSALSGNSSGPGPGS
HHHCCCCCCCCCCCC		39.9528961369
41PhosphorylationSALSGNSSGPGPGSS
HHCCCCCCCCCCCCC		53.6728961369
47PhosphorylationSSGPGPGSSPAGSTK
CCCCCCCCCCCCCCC		35.9628961369
48PhosphorylationSGPGPGSSPAGSTKP
CCCCCCCCCCCCCCC		25.3728961369
75UbiquitinationQANRLPIKVLKMLTA
HHCCCCHHHHHHHHH		39.3129967540
92PhosphorylationGHILHPEYLQPLPST
CCCCCHHHCCCCCCC		18.3223312004
98PhosphorylationEYLQPLPSTPVSPIE
HHCCCCCCCCCCCCC		53.6923898821
99PhosphorylationYLQPLPSTPVSPIEL
HCCCCCCCCCCCCCC		26.2721712546
102PhosphorylationPLPSTPVSPIELDAK
CCCCCCCCCCCCCCC		22.7425159151
111PhosphorylationIELDAKKSPLALLAQ
CCCCCCCCHHHHHHH		25.1725849741
119PhosphorylationPLALLAQTCSQIGKP
HHHHHHHHHHHHCCC		14.4422210691
121PhosphorylationALLAQTCSQIGKPDP
HHHHHHHHHHCCCCC		28.3722210691
129PhosphorylationQIGKPDPSPSSKLSS
HHCCCCCCCCHHHHH		44.8121712546
132PhosphorylationKPDPSPSSKLSSVAS
CCCCCCCHHHHHHHH		40.7921712546
135PhosphorylationPSPSSKLSSVASNGG
CCCCHHHHHHHHCCC		26.8822210691
136PhosphorylationSPSSKLSSVASNGGG
CCCHHHHHHHHCCCC		31.9428857561
139PhosphorylationSKLSSVASNGGGAGG
HHHHHHHHCCCCCCC		33.5728857561
165PhosphorylationKSGPLKLSDIGVEDK
CCCCCCHHHCCCCCC		26.1227134283
172AcetylationSDIGVEDKSSFKPYS
HHCCCCCCCCCCCCC		34.2023954790
179PhosphorylationKSSFKPYSKPGSDKK
CCCCCCCCCCCCCCC		40.68-
183PhosphorylationKPYSKPGSDKKEPGG
CCCCCCCCCCCCCCC		55.58-
206PhosphorylationGGGGGGVSSEKSGFR
CCCCCCCCCCCCCCC		35.73-
209AcetylationGGGVSSEKSGFRVPS
CCCCCCCCCCCCCCC		58.80-
210PhosphorylationGGVSSEKSGFRVPSA
CCCCCCCCCCCCCCC		38.8318452278
216PhosphorylationKSGFRVPSATCQPFT
CCCCCCCCCCCCCCC		33.0927732954
218PhosphorylationGFRVPSATCQPFTPR
CCCCCCCCCCCCCCC		18.9327732954
223PhosphorylationSATCQPFTPRTGSPS
CCCCCCCCCCCCCCC		20.6727273156
226PhosphorylationCQPFTPRTGSPSSSA
CCCCCCCCCCCCCCC		43.1222617229
228PhosphorylationPFTPRTGSPSSSASA
CCCCCCCCCCCCCCC		22.4625159151
230PhosphorylationTPRTGSPSSSASACS
CCCCCCCCCCCCCCC		38.3329116813
231PhosphorylationPRTGSPSSSASACSP
CCCCCCCCCCCCCCC		33.0526657352
232PhosphorylationRTGSPSSSASACSPG
CCCCCCCCCCCCCCC		30.4926657352
234PhosphorylationGSPSSSASACSPGGM
CCCCCCCCCCCCCCC		31.5819413330
237PhosphorylationSSSASACSPGGMLSS
CCCCCCCCCCCCCCC		26.7125159151
243PhosphorylationCSPGGMLSSAGGAPE
CCCCCCCCCCCCCCC		14.8429978859
244PhosphorylationSPGGMLSSAGGAPEG
CCCCCCCCCCCCCCC		27.2930576142
258PhosphorylationGKDDKKDTDVGGGGK
CCCCCCCCCCCCCCC		41.2728857561
265AcetylationTDVGGGGKGTGGASA
CCCCCCCCCCCCCCC		57.4826051181
285PhosphorylationGLAHGRISCGGGINV
CCCCCEEEECCCEEE		12.8328985074
401PhosphorylationLAAAAAGSLGCSKPA
HHHHHHHHCCCCCCC		19.5022210691
405PhosphorylationAAGSLGCSKPAGSSP
HHHHCCCCCCCCCCC		39.6222210691
410PhosphorylationGCSKPAGSSPLAGAS
CCCCCCCCCCCCCCC		30.7829449344
411PhosphorylationCSKPAGSSPLAGASP
CCCCCCCCCCCCCCC		24.0229449344
417PhosphorylationSSPLAGASPPSVMTA
CCCCCCCCCCCCHHH		36.1029449344
420PhosphorylationLAGASPPSVMTASLC
CCCCCCCCCHHHHHC		28.0929449344
528MethylationANGPCDKRFATSEEL
CCCCCCHHCCCHHHH		17.12-
591PhosphorylationPGTLALRSPHHALGL
CCEEEECCCCHHCCC		29.4528555341
601MethylationHALGLSSRYHPYSKS
HHCCCCCCCCCCCCC		30.33115920509
608PhosphorylationRYHPYSKSPLPTPGA
CCCCCCCCCCCCCCC		26.2324719451
636MethylationPYALYGQRLTTASAL
CCCCCCCCHHHHHHH		29.6454560867
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 ZN503_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN503_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 ZN503_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN503_HUMAN !!
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 ZN503_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-226; SER-234; SER-237AND SER-244, AND MASS SPECTROMETRY.

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