ZNF3_HUMAN - dbPTM
ZNF3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNF3_HUMAN
UniProt AC P17036
Protein Name Zinc finger protein 3
Gene Name ZNF3
Organism Homo sapiens (Human).
Sequence Length 446
Subcellular Localization Nucleus .
Protein Description Involved in cell differentiation and/or proliferation..
Protein Sequence METQADLVSQEPQALLDSALPSKVPAFSDKDSLGDEMLAAALLKAKSQELVTFEDVAVYFIRKEWKRLEPAQRDLYRDVMLENYGNVFSLDRETRTENDQEISEDTRSHGVLLGRFQKDISQGLKFKEAYEREVSLKRPLGNSPGERLNRKMPDFGQVTVEEKLTPRGERSEKYNDFGNSFTVNSNLISHQRLPVGDRPHKCDECSKSFNRTSDLIQHQRIHTGEKPYECNECGKAFSQSSHLIQHQRIHTGEKPYECSDCGKTFSCSSALILHRRIHTGEKPYECNECGKTFSWSSTLTHHQRIHTGEKPYACNECGKAFSRSSTLIHHQRIHTGEKPYECNECGKAFSQSSHLYQHQRIHTGEKPYECMECGGKFTYSSGLIQHQRIHTGENPYECSECGKAFRYSSALVRHQRIHTGEKPLNGIGMSKSSLRVTTELNIREST
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
18PhosphorylationEPQALLDSALPSKVP
CHHHHHHHHCCCCCC		31.5129978859
22PhosphorylationLLDSALPSKVPAFSD
HHHHHCCCCCCCCCC		47.3224719451
23UbiquitinationLDSALPSKVPAFSDK
HHHHCCCCCCCCCCC		50.74-
28PhosphorylationPSKVPAFSDKDSLGD
CCCCCCCCCCCCCCH		45.9529449344
30UbiquitinationKVPAFSDKDSLGDEM
CCCCCCCCCCCCHHH		48.28-
32PhosphorylationPAFSDKDSLGDEMLA
CCCCCCCCCCHHHHH		39.7418491316
44UbiquitinationMLAAALLKAKSQELV
HHHHHHHHHHCCCCE		55.40-
76PhosphorylationEPAQRDLYRDVMLEN
CHHHHHHHHHHHHHH		14.73-
89PhosphorylationENYGNVFSLDRETRT
HHCCCEEEECCCCCC		25.6924719451
118SumoylationVLLGRFQKDISQGLK
CCHHHHHHHHHHCCC		55.08-
118UbiquitinationVLLGRFQKDISQGLK
CCHHHHHHHHHHCCC		55.08-
118SumoylationVLLGRFQKDISQGLK
CCHHHHHHHHHHCCC		55.08-
125SumoylationKDISQGLKFKEAYER
HHHHHCCCHHHHHHH		62.30-
125SumoylationKDISQGLKFKEAYER
HHHHHCCCHHHHHHH		62.3028112733
127SumoylationISQGLKFKEAYEREV
HHHCCCHHHHHHHHH		39.59-
127SumoylationISQGLKFKEAYEREV
HHHCCCHHHHHHHHH		39.59-
127UbiquitinationISQGLKFKEAYEREV
HHHCCCHHHHHHHHH		39.59-
130 (in isoform 2)Phosphorylation-19.33-
135PhosphorylationEAYEREVSLKRPLGN
HHHHHHHCCCCCCCC		24.3423917254
137UbiquitinationYEREVSLKRPLGNSP
HHHHHCCCCCCCCCH		44.45-
137SumoylationYEREVSLKRPLGNSP
HHHHHCCCCCCCCCH		44.45-
137SumoylationYEREVSLKRPLGNSP
HHHHHCCCCCCCCCH		44.45-
143PhosphorylationLKRPLGNSPGERLNR
CCCCCCCCHHHHHHC		32.2725159151
151SumoylationPGERLNRKMPDFGQV
HHHHHHCCCCCCCCE		54.4328112733
151SumoylationPGERLNRKMPDFGQV
HHHHHHCCCCCCCCE		54.43-
159PhosphorylationMPDFGQVTVEEKLTP
CCCCCCEEEEEECCC		17.8224719451
163SumoylationGQVTVEEKLTPRGER
CCEEEEEECCCCCCC		44.1228112733
165PhosphorylationVTVEEKLTPRGERSE
EEEEEECCCCCCCCC		23.2321712546
173UbiquitinationPRGERSEKYNDFGNS
CCCCCCCCCCCCCCC		51.07-
173SumoylationPRGERSEKYNDFGNS
CCCCCCCCCCCCCCC		51.0728112733
173SumoylationPRGERSEKYNDFGNS
CCCCCCCCCCCCCCC		51.07-
180PhosphorylationKYNDFGNSFTVNSNL
CCCCCCCCEEECCCC		23.7528555341
207SumoylationHKCDECSKSFNRTSD
CCCCHHHHHCCCHHH		71.39-
207SumoylationHKCDECSKSFNRTSD
CCCCHHHHHCCCHHH		71.39-
212PhosphorylationCSKSFNRTSDLIQHQ
HHHHCCCHHHHHHHC		27.9128555341
213PhosphorylationSKSFNRTSDLIQHQR
HHHCCCHHHHHHHCC		27.4728555341
223PhosphorylationIQHQRIHTGEKPYEC
HHHCCCCCCCCCCCC		44.6728152594
226UbiquitinationQRIHTGEKPYECNEC
CCCCCCCCCCCCCCH		55.00-
228PhosphorylationIHTGEKPYECNECGK
CCCCCCCCCCCCHHH		44.1528152594
238PhosphorylationNECGKAFSQSSHLIQ
CCHHHHHHCCHHHHC		33.7328555341
251PhosphorylationIQHQRIHTGEKPYEC
HCCCEECCCCCCEEC		44.6728985074
254UbiquitinationQRIHTGEKPYECSDC
CEECCCCCCEECCCC		55.00-
279PhosphorylationILHRRIHTGEKPYEC
HHCCCCCCCCCCEEC		44.6728152594
282UbiquitinationRRIHTGEKPYECNEC
CCCCCCCCCEECCCC		55.00-
284PhosphorylationIHTGEKPYECNECGK
CCCCCCCEECCCCCC		44.1528152594
307PhosphorylationTHHQRIHTGEKPYAC
CCCCCCCCCCCCCCC		44.6721712546
310UbiquitinationQRIHTGEKPYACNEC
CCCCCCCCCCCCCCC		44.68-
319UbiquitinationYACNECGKAFSRSST
CCCCCCCCCCCCCCC		58.90-
325PhosphorylationGKAFSRSSTLIHHQR
CCCCCCCCCEEEECE		26.5628555341
335PhosphorylationIHHQRIHTGEKPYEC
EEECEECCCCCCCCC		44.6728152594
338UbiquitinationQRIHTGEKPYECNEC
CEECCCCCCCCCCCC		55.00-
340PhosphorylationIHTGEKPYECNECGK
ECCCCCCCCCCCCHH		44.1528152594
350PhosphorylationNECGKAFSQSSHLYQ
CCCHHCHHCCHHHHC		33.7328555341
353PhosphorylationGKAFSQSSHLYQHQR
HHCHHCCHHHHCCCC		15.1828555341
363PhosphorylationYQHQRIHTGEKPYEC
HCCCCCCCCCCCCEE		44.6728985074
379PhosphorylationECGGKFTYSSGLIQH
ECCCEEEECCCCEEC		12.1728555341
380PhosphorylationCGGKFTYSSGLIQHQ
CCCEEEECCCCEECC		18.1828555341
391PhosphorylationIQHQRIHTGENPYEC
EECCEEECCCCCCCC		43.7628152594
396PhosphorylationIHTGENPYECSECGK
EECCCCCCCCCHHHH		40.9425839225
399PhosphorylationGENPYECSECGKAFR
CCCCCCCCHHHHHHH		24.7928152594
403UbiquitinationYECSECGKAFRYSSA
CCCCHHHHHHHHCHH		56.88-
407PhosphorylationECGKAFRYSSALVRH
HHHHHHHHCHHHHHH		10.6722817900
419PhosphorylationVRHQRIHTGEKPLNG
HHHCCCCCCCCCCCC		44.6728112733
422SumoylationQRIHTGEKPLNGIGM
CCCCCCCCCCCCCCC		57.0328112733
422SumoylationQRIHTGEKPLNGIGM
CCCCCCCCCCCCCCC		57.03-
431SumoylationLNGIGMSKSSLRVTT
CCCCCCCHHHCEEEE		34.8628112733
445PhosphorylationTELNIREST------
EEEECCCCC------		29.5725627689
446PhosphorylationELNIREST-------
EEECCCCC-------		37.5725627689
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 ZNF3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNF3_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 ZNF3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FHL2_HUMANFHL2physical
18255255
ID3_HUMANID3physical
18255255
ZN212_HUMANZNF212physical
18255255
ZNF3_HUMANZNF3physical
18255255
TRAF4_HUMANTRAF4physical
25416956
MTUS2_HUMANMTUS2physical
25416956
ADIP_HUMANSSX2IPphysical
25416956
SHCBP_HUMANSHCBP1physical
28514442
KBTB7_HUMANKBTBD7physical
28514442
PTPRK_HUMANPTPRKphysical
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 ZNF3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, AND MASSSPECTROMETRY.

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