ZNF12_HUMAN - dbPTM
ZNF12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNF12_HUMAN
UniProt AC P17014
Protein Name Zinc finger protein 12
Gene Name ZNF12
Organism Homo sapiens (Human).
Sequence Length 697
Subcellular Localization Nucleus .
Protein Description Transcriptional repressor which suppresses activation protein 1 (AP-1)- and serum response element (SRE)-mediated transcriptional activity..
Protein Sequence MNKSLGPVSFKDVAVDFTQEEWQQLDPEQKITYRDVMLENYSNLVSVGYHIIKPDVISKLEQGEEPWIVEGEFLLQSYPDEVWQTDDLIERIQEEENKPSRQTVFIETLIEERGNVPGKTFDVETNPVPSRKIAYKNSLCDSCEKCLTSVSEYISSDGSYARMKADECSGCGKSLLHIKLEKTHPGDQAYEFNQNGEPYTLNEESLYQKIRILEKPFEYIECQKAFQKDTVFVNHMEEKPYKWNGSEIAFLQMSDLTVHQTSHMEMKPYECSECGKSFCKKSKFIIHQRTHTGEKPYECNQCGKSFCQKGTLTVHQRTHTGEKPYECNECGKNFYQKLHLIQHQRTHSGEKPYECSYCGKSFCQKTHLTQHQRTHSGERPYVCHDCGKTFSQKSALNDHQKIHTGVKLYKCSECGKCFCRKSTLTTHLRTHTGEKPYECNECGKFFSRLSYLTVHYRTHSGEKPYECNECGKTFYLNSALMRHQRVHTGEKPYECNECGKLFSQLSYLTIHHRTHSGVKPYECSECGKTFYQNSALCRHRRIHKGEKPYECYICGKFFSQMSYLTIHHRIHSGEKPYECSECGKTFCQNSALNRHQRTHTGEKAYECYECGKCFSQMSYLTIHHRIHSGEKPFECNECGKAFSRMSYLTVHYRTHSGEKPYECTECGKKFYHKSAFNSHQRIHRRGNMNVIDVGRLL
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
3Sumoylation-----MNKSLGPVSF
-----CCCCCCCCCH		45.8428112733
4Phosphorylation----MNKSLGPVSFK
----CCCCCCCCCHH		33.2923532336
9PhosphorylationNKSLGPVSFKDVAVD
CCCCCCCCHHHEEEE		29.7023532336
64 (in isoform 4)Phosphorylation-61.6627251275
67 (in isoform 4)Phosphorylation-15.5627251275
72 (in isoform 4)Phosphorylation-21.4427251275
98SumoylationRIQEEENKPSRQTVF
HHHHHCCCCCCEEEE		47.88-
98SumoylationRIQEEENKPSRQTVF
HHHHHCCCCCCEEEE		47.8828112733
98UbiquitinationRIQEEENKPSRQTVF
HHHHHCCCCCCEEEE		47.8824816145
100 (in isoform 5)Phosphorylation-38.3327251275
102UbiquitinationEENKPSRQTVFIETL
HCCCCCCEEEEEHHH		46.4821890473
102UbiquitinationEENKPSRQTVFIETL
HCCCCCCEEEEEHHH		46.4821890473
103 (in isoform 5)Phosphorylation-19.1027251275
108 (in isoform 5)Phosphorylation-28.3727251275
136UbiquitinationPSRKIAYKNSLCDSC
CCCHHHHCCCCCHHH		30.9129967540
144UbiquitinationNSLCDSCEKCLTSVS
CCCCHHHHHHHHHHH		51.2429967540
153PhosphorylationCLTSVSEYISSDGSY
HHHHHHHHHHCCCCC		9.90-
160PhosphorylationYISSDGSYARMKADE
HHHCCCCCEEEECHH		12.07-
171UbiquitinationKADECSGCGKSLLHI
ECHHCCCCCCEEEEE		3.4029967540
177UbiquitinationGCGKSLLHIKLEKTH
CCCCEEEEEEEEECC		22.0429967540
179SumoylationGKSLLHIKLEKTHPG
CCEEEEEEEEECCCC		39.59-
179SumoylationGKSLLHIKLEKTHPG
CCEEEEEEEEECCCC		39.5928112733
182SumoylationLLHIKLEKTHPGDQA
EEEEEEEECCCCCCC		63.6728112733
182UbiquitinationLLHIKLEKTHPGDQA
EEEEEEEECCCCCCC		63.6729967540
183PhosphorylationLHIKLEKTHPGDQAY
EEEEEEECCCCCCCE		24.75-
186UbiquitinationKLEKTHPGDQAYEFN
EEEECCCCCCCEEEC		31.8729967540
201UbiquitinationQNGEPYTLNEESLYQ
CCCCCCCCCHHHHHH		6.6529967540
209SumoylationNEESLYQKIRILEKP
CHHHHHHHHHHHHCC		22.0128112733
209UbiquitinationNEESLYQKIRILEKP
CHHHHHHHHHHHHCC		22.0129967540
215UbiquitinationQKIRILEKPFEYIEC
HHHHHHHCCCCHHHH		52.1129967540
215SumoylationQKIRILEKPFEYIEC
HHHHHHHCCCCHHHH		52.1128112733
224SumoylationFEYIECQKAFQKDTV
CCHHHHHHHHHCCCE		63.93-
224UbiquitinationFEYIECQKAFQKDTV
CCHHHHHHHHHCCCE		63.9329967540
224SumoylationFEYIECQKAFQKDTV
CCHHHHHHHHHCCCE		63.9328112733
239SumoylationFVNHMEEKPYKWNGS
EEECCCCCCCCCCCC		40.1028112733
239UbiquitinationFVNHMEEKPYKWNGS
EEECCCCCCCCCCCC		40.1029967540
239SumoylationFVNHMEEKPYKWNGS
EEECCCCCCCCCCCC		40.10-
263UbiquitinationLTVHQTSHMEMKPYE
CEEECCCCCCCCCEE		21.4321890473
283SumoylationKSFCKKSKFIIHQRT
HHHHHCCCEEEEECC		49.84-
283SumoylationKSFCKKSKFIIHQRT
HHHHHCCCEEEEECC		49.84-
283AcetylationKSFCKKSKFIIHQRT
HHHHHCCCEEEEECC		49.8425953088
290PhosphorylationKFIIHQRTHTGEKPY
CEEEEECCCCCCCCE		19.74-
292PhosphorylationIIHQRTHTGEKPYEC
EEEECCCCCCCCEEC		46.56-
295SumoylationQRTHTGEKPYECNQC
ECCCCCCCCEECCCC		55.00-
295SumoylationQRTHTGEKPYECNQC
ECCCCCCCCEECCCC		55.00-
295UbiquitinationQRTHTGEKPYECNQC
ECCCCCCCCEECCCC		55.00-
295AcetylationQRTHTGEKPYECNQC
ECCCCCCCCEECCCC		55.007428711
299UbiquitinationTGEKPYECNQCGKSF
CCCCCEECCCCCCCH		3.3421890473
309SumoylationCGKSFCQKGTLTVHQ
CCCCHHCCCCEEEEE		55.85-
309SumoylationCGKSFCQKGTLTVHQ
CCCCHHCCCCEEEEE		55.8528112733
318PhosphorylationTLTVHQRTHTGEKPY
CEEEEECCCCCCCCE		19.7428348404
320PhosphorylationTVHQRTHTGEKPYEC
EEEECCCCCCCCEEC		46.5629496963
323UbiquitinationQRTHTGEKPYECNEC
ECCCCCCCCEECCCC		55.00-
327UbiquitinationTGEKPYECNECGKNF
CCCCCEECCCCCHHH		4.2429967540
337SumoylationCGKNFYQKLHLIQHQ
CCHHHHHHHHHHEEC		26.8828112733
337UbiquitinationCGKNFYQKLHLIQHQ
CCHHHHHHHHHHEEC		26.8821890473
346PhosphorylationHLIQHQRTHSGEKPY
HHHEECCCCCCCCCE		17.52-
348PhosphorylationIQHQRTHSGEKPYEC
HEECCCCCCCCCEEC		48.29-
353PhosphorylationTHSGEKPYECSYCGK
CCCCCCCEECCCCCC		40.41-
356PhosphorylationGEKPYECSYCGKSFC
CCCCEECCCCCCCHH		16.12-
365UbiquitinationCGKSFCQKTHLTQHQ
CCCCHHHHHCCCCCC		38.8129967540
366PhosphorylationGKSFCQKTHLTQHQR
CCCHHHHHCCCCCCC		9.02-
393UbiquitinationCGKTFSQKSALNDHQ
CCCCCCHHHHCCCCC		36.18-
395UbiquitinationKTFSQKSALNDHQKI
CCCCHHHHCCCCCHH		19.8821890473
395UbiquitinationKTFSQKSALNDHQKI
CCCCHHHHCCCCCHH		19.8821890473
395UbiquitinationKTFSQKSALNDHQKI
CCCCHHHHCCCCCHH		19.8821890473
422PhosphorylationGKCFCRKSTLTTHLR
CCEEEECCCCEEECC		14.86-
430PhosphorylationTLTTHLRTHTGEKPY
CCEEECCCCCCCCCE		30.1028348404
432PhosphorylationTTHLRTHTGEKPYEC
EEECCCCCCCCCEEC		46.5629496963
435UbiquitinationLRTHTGEKPYECNEC
CCCCCCCCCEECCCC		55.00-
447PhosphorylationNECGKFFSRLSYLTV
CCCHHHHHHHEEEEE		35.1325394399
450PhosphorylationGKFFSRLSYLTVHYR
HHHHHHHEEEEEEEE		19.5829743597
451PhosphorylationKFFSRLSYLTVHYRT
HHHHHHEEEEEEEEC		15.8124260401
456PhosphorylationLSYLTVHYRTHSGEK
HEEEEEEEECCCCCC		16.9324260401
460PhosphorylationTVHYRTHSGEKPYEC
EEEEECCCCCCCEEE		48.2923898821
463UbiquitinationYRTHSGEKPYECNEC
EECCCCCCCEEECCC		57.32-
488PhosphorylationMRHQRVHTGEKPYEC
HHCCCCCCCCCCCCC		44.1523898821
491UbiquitinationQRVHTGEKPYECNEC
CCCCCCCCCCCCCHH		55.00-
572PhosphorylationTIHHRIHSGEKPYEC
EEEEECCCCCCCEEC		46.4028348404
575UbiquitinationHRIHSGEKPYECSEC
EECCCCCCCEECCCC		57.32-
598PhosphorylationALNRHQRTHTGEKAY
HCCCCCCCCCCCCCE		19.74-
600PhosphorylationNRHQRTHTGEKAYEC
CCCCCCCCCCCCEEH		46.56-
603UbiquitinationQRTHTGEKAYECYEC
CCCCCCCCCEEHHHC		58.58-
631UbiquitinationHRIHSGEKPFECNEC
CCCCCCCCCEECCCC		59.54-
661PhosphorylationTHSGEKPYECTECGK
CCCCCCCEEECCCCC		34.40-
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 ZNF12_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNF12_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 ZNF12_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZNF12_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 ZNF12_HUMAN

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Related Literatures of Post-Translational Modification

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