ZN254_HUMAN - dbPTM
ZN254_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN254_HUMAN
UniProt AC O75437
Protein Name Zinc finger protein 254
Gene Name ZNF254
Organism Homo sapiens (Human).
Sequence Length 659
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MPGPPRSLEMGLLTFRDVAIEFSLEEWQHLDIAQQNLYRNVMLENYRNLAFLGIAVSKPDLITCLEQGKEPWNMKRHEMVDEPPGMCPHFAQDLWPEQGMEDSFQKAILRRYGKYGHENLQLRKGCKSVDEYKVNKEGYNGLNQCFTTAQSKVFQCDKYLKVFYKFLNSNRPKIRHTEKKSFKCKKRVKLFCMLSHKTQHKSIYHREKSYKCKECGKTFNWSSTLTNHRKIYTEEKPYKCEEYNKSPKQLSTLTTHEIIHAGEKLYKCEECGEAFNRSSNLTTHKIIHTGEKPYKCEECGKAFIWSSTLTEHKKIHTRKKPYKCEECGKAFIWSSTLTRHKRMHTGEKPYKCEECGKAFSQSSTLTTHKIIHTGEKRYKCLECGKAFKQLSTLTTHKIIHVGEKLYKCEECGKGFNRSSNLTTHKIIHTGEKPYKCEECGKAFIWSSTLTKHKRIHTREKPYKCEECGKAFIWSSTLTRHKRMHTGEKPYKCEECGKSFSQSSTLTTHKIIHTGEKPYKCEECGKAFNWSSTLTKHKIIHTEEKPYKCEKCGKAFKQSSILTNHKRIHTGEKPYKCEECGKSFNRSSTFTKHKVIHTGVKPYKCEECGKAFFWSSTLTKHKRIHTGEQPYKWEKFGKAFNRSSHLTTDKITHWREILQV
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
195PhosphorylationVKLFCMLSHKTQHKS
HHHHHHHCCCCCCCH		8.96-
198PhosphorylationFCMLSHKTQHKSIYH
HHHHCCCCCCCHHHH		30.40-
202PhosphorylationSHKTQHKSIYHREKS
CCCCCCCHHHHCCCC		26.6724719451
204PhosphorylationKTQHKSIYHREKSYK
CCCCCHHHHCCCCEE		11.25-
232PhosphorylationLTNHRKIYTEEKPYK
HCCCCCEECCCCCCC		15.90-
233PhosphorylationTNHRKIYTEEKPYKC
CCCCCEECCCCCCCH		40.93-
238PhosphorylationIYTEEKPYKCEEYNK
EECCCCCCCHHHHCC		39.06-
243PhosphorylationKPYKCEEYNKSPKQL
CCCCHHHHCCCHHHH		12.95-
278PhosphorylationCGEAFNRSSNLTTHK
HHHHCCCCCCCCCCE		25.3627732954
279PhosphorylationGEAFNRSSNLTTHKI
HHHCCCCCCCCCCEE		32.4027732954
282PhosphorylationFNRSSNLTTHKIIHT
CCCCCCCCCCEEEEC		30.9827732954
283PhosphorylationNRSSNLTTHKIIHTG
CCCCCCCCCEEEECC		25.0827732954
285UbiquitinationSSNLTTHKIIHTGEK
CCCCCCCEEEECCCC		41.06-
289PhosphorylationTTHKIIHTGEKPYKC
CCCEEEECCCCCEEC		36.3129496963
292UbiquitinationKIIHTGEKPYKCEEC
EEEECCCCCEECCCC		55.80-
294PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECCCCCC		39.06-
295AcetylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCE		43.6319825523
295SumoylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCE		43.63-
295UbiquitinationHTGEKPYKCEECGKA
ECCCCCEECCCCCCE		43.63-
295SumoylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCE		43.63-
306PhosphorylationCGKAFIWSSTLTEHK
CCCEEEEECCCCCCC		14.50-
307PhosphorylationGKAFIWSSTLTEHKK
CCEEEEECCCCCCCC		16.67-
317PhosphorylationTEHKKIHTRKKPYKC
CCCCCCCCCCCCCCC		47.8917924679
323SumoylationHTRKKPYKCEECGKA
CCCCCCCCCCHHCCE		43.63-
323UbiquitinationHTRKKPYKCEECGKA
CCCCCCCCCCHHCCE		43.63-
323SumoylationHTRKKPYKCEECGKA
CCCCCCCCCCHHCCE		43.63-
351SumoylationHTGEKPYKCEECGKA
CCCCCCEECHHHHHC		43.63-
351SumoylationHTGEKPYKCEECGKA
CCCCCCEECHHHHHC		43.63-
351UbiquitinationHTGEKPYKCEECGKA
CCCCCCEECHHHHHC		43.63-
360PhosphorylationEECGKAFSQSSTLTT
HHHHHCCCCCCCCCC		33.7328270605
362PhosphorylationCGKAFSQSSTLTTHK
HHHCCCCCCCCCCEE		24.8828270605
363PhosphorylationGKAFSQSSTLTTHKI
HHCCCCCCCCCCEEE		21.5728270605
364PhosphorylationKAFSQSSTLTTHKII
HCCCCCCCCCCEEEE		33.1128270605
366PhosphorylationFSQSSTLTTHKIIHT
CCCCCCCCCEEEEEC		27.2628270605
367PhosphorylationSQSSTLTTHKIIHTG
CCCCCCCCEEEEECC		25.0428270605
369SumoylationSSTLTTHKIIHTGEK
CCCCCCEEEEECCCH		41.06-
369UbiquitinationSSTLTTHKIIHTGEK
CCCCCCEEEEECCCH		41.06-
369SumoylationSSTLTTHKIIHTGEK
CCCCCCEEEEECCCH		41.06-
373PhosphorylationTTHKIIHTGEKRYKC
CCEEEEECCCHHEEH		36.3128270605
385UbiquitinationYKCLECGKAFKQLST
EEHHHHHHHHHHHHH		63.41-
407SumoylationHVGEKLYKCEECGKG
ECCCCEEECCCCCCC		45.68-
407UbiquitinationHVGEKLYKCEECGKG
ECCCCEEECCCCCCC		45.68-
407SumoylationHVGEKLYKCEECGKG
ECCCCEEECCCCCCC		45.68-
418PhosphorylationCGKGFNRSSNLTTHK
CCCCCCCCCCCCCCE		25.3627732954
419PhosphorylationGKGFNRSSNLTTHKI
CCCCCCCCCCCCCEE		32.4027732954
422PhosphorylationFNRSSNLTTHKIIHT
CCCCCCCCCCEEEEC		30.9827732954
423PhosphorylationNRSSNLTTHKIIHTG
CCCCCCCCCEEEECC		25.0827732954
425UbiquitinationSSNLTTHKIIHTGEK
CCCCCCCEEEECCCC		41.06-
429PhosphorylationTTHKIIHTGEKPYKC
CCCEEEECCCCCEEC		36.3129496963
432UbiquitinationKIIHTGEKPYKCEEC
EEEECCCCCEECCCC		55.80-
434PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECCCCCC		39.06-
435SumoylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCE		43.63-
435AcetylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCE		43.6319825529
435SumoylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCE		43.63-
435UbiquitinationHTGEKPYKCEECGKA
ECCCCCEECCCCCCE		43.63-
451UbiquitinationIWSSTLTKHKRIHTR
EEECCCCCCCCCCCC		50.68-
463SumoylationHTREKPYKCEECGKA
CCCCCCEECHHHCCE		43.63-
463UbiquitinationHTREKPYKCEECGKA
CCCCCCEECHHHCCE		43.63-
463SumoylationHTREKPYKCEECGKA
CCCCCCEECHHHCCE		43.63-
491SumoylationHTGEKPYKCEECGKS
CCCCCCCCCHHHCCC		43.63-
491SumoylationHTGEKPYKCEECGKS
CCCCCCCCCHHHCCC		43.63-
491UbiquitinationHTGEKPYKCEECGKS
CCCCCCCCCHHHCCC		43.63-
502PhosphorylationCGKSFSQSSTLTTHK
HCCCCCCCCCCEEEE		24.88-
503PhosphorylationGKSFSQSSTLTTHKI
CCCCCCCCCCEEEEE		21.57-
506PhosphorylationFSQSSTLTTHKIIHT
CCCCCCCEEEEEEEC		27.26-
509SumoylationSSTLTTHKIIHTGEK
CCCCEEEEEEECCCC		41.06-
509UbiquitinationSSTLTTHKIIHTGEK
CCCCEEEEEEECCCC		41.06-
509SumoylationSSTLTTHKIIHTGEK
CCCCEEEEEEECCCC		41.06-
513PhosphorylationTTHKIIHTGEKPYKC
EEEEEEECCCCCEEC		36.3129496963
516UbiquitinationKIIHTGEKPYKCEEC
EEEECCCCCEECCCC		55.80-
518PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECCCCCC		39.06-
519AcetylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCC		43.6319825535
519SumoylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCC		43.63-
519UbiquitinationHTGEKPYKCEECGKA
ECCCCCEECCCCCCC		43.63-
519SumoylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCC		43.63-
535UbiquitinationNWSSTLTKHKIIHTE
CCCCCCCCCCEEECC		46.11-
544SumoylationKIIHTEEKPYKCEKC
CEEECCCCCCCCCCC		47.63-
544SumoylationKIIHTEEKPYKCEKC
CEEECCCCCCCCCCC		47.63-
569PhosphorylationTNHKRIHTGEKPYKC
CCCCCCCCCCCCEEC		44.6729496963
572UbiquitinationKRIHTGEKPYKCEEC
CCCCCCCCCEECHHC		55.80-
574PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEECHHCCC		39.06-
575SumoylationHTGEKPYKCEECGKS
CCCCCCEECHHCCCC		43.63-
575UbiquitinationHTGEKPYKCEECGKS
CCCCCCEECHHCCCC		43.63-
575SumoylationHTGEKPYKCEECGKS
CCCCCCEECHHCCCC		43.63-
603UbiquitinationHTGVKPYKCEECGKA
ECCCCCEECCHHCCE		43.63-
603SumoylationHTGVKPYKCEECGKA
ECCCCCEECCHHCCE		43.63-
603SumoylationHTGVKPYKCEECGKA
ECCCCCEECCHHCCE		43.63-
619UbiquitinationFWSSTLTKHKRIHTG
EEECCCCCCCCCCCC		50.68-
625PhosphorylationTKHKRIHTGEQPYKW
CCCCCCCCCCCCCCH		39.7917924679
642PhosphorylationFGKAFNRSSHLTTDK
HHHHCCCCCCCCCCC		24.1826074081
643PhosphorylationGKAFNRSSHLTTDKI
HHHCCCCCCCCCCCH		21.1926074081
646PhosphorylationFNRSSHLTTDKITHW
CCCCCCCCCCCHHCH		27.7626074081
647PhosphorylationNRSSHLTTDKITHWR
CCCCCCCCCCHHCHH		41.4726074081
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 ZN254_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN254_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 ZN254_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TIF1B_HUMANTRIM28physical
28514442
ZN479_HUMANZNF479physical
28514442
CP24A_HUMANCYP24A1physical
28514442
TIF1A_HUMANTRIM24physical
28514442
Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN254_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-625, AND MASSSPECTROMETRY.

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