ZN496_HUMAN - dbPTM
ZN496_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN496_HUMAN
UniProt AC Q96IT1
Protein Name Zinc finger protein 496
Gene Name ZNF496
Organism Homo sapiens (Human).
Sequence Length 587
Subcellular Localization Nucleus .
Protein Description DNA-binding transcription factor that can both act as an activator and a repressor..
Protein Sequence MPTALCPRVLAPKESEEPRKMRSPPGENPSPQGELPSPESSRRLFRRFRYQEAAGPREALQRLWDLCGGWLRPERHTKEQILELLVLEQFLAILPREIQSWVRAQEPESGEQAVAAVEALEREPGRPWQWLKHCEDPVVIDDGDSPLDQEQEQLPVEPHSDLAKNQDAQPITLAQCLGLPSRPPSQLSGDPVLQDAFLLQEENVRDTQQVTTLQLPPSRVSPFKDMILCFSEEDWSLLDPAQTGFYGEFIIGEDYGVSMPPNDLAAQPDLSQGEENEPRVPELQDLQGKEVPQVSYLDSPSLQPFQVEERRKREELQVPEFQACPQTVVPQNTYPAGGNPRSLENSLDEEVTIEIVLSSSGDEDSQHGPYCTEELGSPTEKQRSLPASHRSSTEAGGEVQTSKKSYVCPNCGKIFRWRVNFIRHLRSRREQEKPHECSVCGELFSDSEDLDGHLESHEAQKPYRCGACGKSFRLNSHLLSHRRIHLQPDRLQPVEKREQAASEDADKGPKEPLENGKAKLSFQCCECGKAFQRHDHLARHRSHFHLKDKARPFQCRYCVKSFTQNYDLLRHERLHMKRRSKQALNSY
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
13SumoylationCPRVLAPKESEEPRK
CCCCCCCCCCCCCCC		69.1628112733
13 (in isoform 2)Ubiquitination-69.16-
13UbiquitinationCPRVLAPKESEEPRK
CCCCCCCCCCCCCCC		69.16-
23PhosphorylationEEPRKMRSPPGENPS
CCCCCCCCCCCCCCC		31.7630266825
30PhosphorylationSPPGENPSPQGELPS
CCCCCCCCCCCCCCC		41.2430266825
37PhosphorylationSPQGELPSPESSRRL
CCCCCCCCHHHHHHH		54.6630266825
50PhosphorylationRLFRRFRYQEAAGPR
HHHHHHHHHHHHCHH		14.1630622161
181PhosphorylationAQCLGLPSRPPSQLS
HHHHCCCCCCHHHHC		63.5626074081
185PhosphorylationGLPSRPPSQLSGDPV
CCCCCCHHHHCCCCH		46.5720044836
188PhosphorylationSRPPSQLSGDPVLQD
CCCHHHHCCCCHHHH		33.2528387310
218PhosphorylationTTLQLPPSRVSPFKD
EEEECCHHHCCCCCC		43.2926074081
221PhosphorylationQLPPSRVSPFKDMIL
ECCHHHCCCCCCEEE		24.4130266825
269UbiquitinationNDLAAQPDLSQGEEN
HHCCCCCCCCCCCCC		47.0421963094
289UbiquitinationELQDLQGKEVPQVSY
HHHHHCCCCCCCCEE		42.4521906983
295PhosphorylationGKEVPQVSYLDSPSL
CCCCCCCEECCCCCC		18.0926074081
296PhosphorylationKEVPQVSYLDSPSLQ
CCCCCCEECCCCCCC		18.7026074081
299PhosphorylationPQVSYLDSPSLQPFQ
CCCEECCCCCCCCCC		17.5028112733
301PhosphorylationVSYLDSPSLQPFQVE
CEECCCCCCCCCCHH		43.5226074081
325UbiquitinationVPEFQACPQTVVPQN
CCCCCCCCCCCCCCC		35.5721963094
325 (in isoform 2)Ubiquitination-35.57-
388PhosphorylationKQRSLPASHRSSTEA
HHHCCCCCCCCCCCC		19.9325627689
391PhosphorylationSLPASHRSSTEAGGE
CCCCCCCCCCCCCCC		35.8727251275
392PhosphorylationLPASHRSSTEAGGEV
CCCCCCCCCCCCCCE		30.1725159151
393PhosphorylationPASHRSSTEAGGEVQ
CCCCCCCCCCCCCEE		30.9725627689
403SumoylationGGEVQTSKKSYVCPN
CCCEECCCCCEECCC		49.4828112733
403SumoylationGGEVQTSKKSYVCPN
CCCEECCCCCEECCC		49.48-
404SumoylationGEVQTSKKSYVCPNC
CCEECCCCCEECCCC		46.95-
404SumoylationGEVQTSKKSYVCPNC
CCEECCCCCEECCCC		46.95-
445PhosphorylationSVCGELFSDSEDLDG
CCCHHHCCCCCCCCC		53.5030576142
447PhosphorylationCGELFSDSEDLDGHL
CHHHCCCCCCCCCCH		31.63-
496SumoylationDRLQPVEKREQAASE
CCCCCHHHHHHHHHC		62.5628112733
496SumoylationDRLQPVEKREQAASE
CCCCCHHHHHHHHHC		62.56-
519SumoylationPLENGKAKLSFQCCE
CCCCCCEEEEEEECC		48.42-
519SumoylationPLENGKAKLSFQCCE
CCCCCCEEEEEEECC		48.42-
561PhosphorylationQCRYCVKSFTQNYDL
CCHHHHHHHHHCHHH		17.0926503514
580PhosphorylationRLHMKRRSKQALNSY
HHHHHHHHHHHHHCC		32.9029083192
586PhosphorylationRSKQALNSY------
HHHHHHHCC------		32.8229083192
587PhosphorylationSKQALNSY-------
HHHHHHCC-------		22.8529083192
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 ZN496_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN496_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 ZN496_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NSD1_HUMANNSD1physical
15169884
TIF1B_HUMANTRIM28physical
20176155
CBX3_HUMANCBX3physical
20176155
ZN483_HUMANZNF483physical
25416956
ZSC22_HUMANZSCAN22physical
25416956
ZKSC4_HUMANZKSCAN4physical
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 ZN496_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-299, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185, AND MASSSPECTROMETRY.

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