ZNF92_HUMAN - dbPTM
ZNF92_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNF92_HUMAN
UniProt AC Q03936
Protein Name Zinc finger protein 92
Gene Name ZNF92
Organism Homo sapiens (Human).
Sequence Length 586
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MGPLTFRDVKIEFSLEEWQCLDTAQRNLYRDVMLENYRNLVFLGIAVSKPDLITWLEQGKEPWNLKRHEMVDKTPVMCSHFAQDVWPEHSIKDSFQKVILRTYGKYGHENLQLRKDHKSVDACKVYKGGYNGLNQCLTTTDSKIFQCDKYVKVFHKFPNVNRNKIRHTGKKPFKCKNRGKSFCMLSQLTQHKKIHTREYSYKCEECGKAFNWSSTLTKHKIIHTGEKPYKCEECGKAFNRSSNLTKHKIIHTGEKPYKCEECGKAFNRSSTLTKHKRIHTEEKPYKCEECGKAFNQFSILNKHKRIHMEDKPYKCEECGKAFRVFSILKKHKIIHTGEKPYKCEECGKAFNQFSNLTKHKIIHTGEKPYKCDECGKAFNQSSTLTKHKRIHTGEKPYKCEECGKAFKQSSTLTEHKIIHTGEKPYKCEKCGKAFSWSSAFTKHKRNHMEDKPYKCEECGKAFSVFSTLTKHKIIHTREKPYKCEECGKAFNQSSIFTKHKIIHTEGKSYKCEKCGNAFNQSSNLTARKIIYTGEKPYKYEECDKAFNKFSTLITHQIIYTGEKPCKHECGRAFNKSSNYTKEKLQT
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
14PhosphorylationRDVKIEFSLEEWQCL
CCEEEEEEECHHHHH		23.2926074081
23PhosphorylationEEWQCLDTAQRNLYR
CHHHHHHHHHHHHHH		16.2526074081
29PhosphorylationDTAQRNLYRDVMLEN
HHHHHHHHHHHHHHH		14.3326074081
73UbiquitinationKRHEMVDKTPVMCSH
CCCCCCCCCCEEHHH		43.23-
92UbiquitinationVWPEHSIKDSFQKVI
CCCCCCCCHHHHHHH		50.78-
97UbiquitinationSIKDSFQKVILRTYG
CCCHHHHHHHHHHHH		29.27-
105UbiquitinationVILRTYGKYGHENLQ
HHHHHHHHHCCCCCC		37.33-
115UbiquitinationHENLQLRKDHKSVDA
CCCCCCCCCCCCCCC		73.17-
124UbiquitinationHKSVDACKVYKGGYN
CCCCCCCCHHCCCCC		50.77-
127UbiquitinationVDACKVYKGGYNGLN
CCCCCHHCCCCCCHH		49.17-
149UbiquitinationSKIFQCDKYVKVFHK
CCCEECCCHHEEHHC		60.62-
150PhosphorylationKIFQCDKYVKVFHKF
CCEECCCHHEEHHCC		7.7022817900
152UbiquitinationFQCDKYVKVFHKFPN
EECCCHHEEHHCCCC		35.77-
156UbiquitinationKYVKVFHKFPNVNRN
CHHEEHHCCCCCCCC		51.56-
202SumoylationHTREYSYKCEECGKA
CCCCCEEECHHCCCC		29.27-
202SumoylationHTREYSYKCEECGKA
CCCCCEEECHHCCCC		29.27-
202UbiquitinationHTREYSYKCEECGKA
CCCCCEEECHHCCCC		29.27-
218UbiquitinationNWSSTLTKHKIIHTG
CCCCCCCCCEEEECC		46.11-
220UbiquitinationSSTLTKHKIIHTGEK
CCCCCCCEEEECCCC		44.93-
224PhosphorylationTKHKIIHTGEKPYKC
CCCEEEECCCCCCCH		36.3129496963
227UbiquitinationKIIHTGEKPYKCEEC
EEEECCCCCCCHHHH		55.80-
229PhosphorylationIHTGEKPYKCEECGK
EECCCCCCCHHHHHH		39.06-
230AcetylationHTGEKPYKCEECGKA
ECCCCCCCHHHHHHC		43.6319825637
230SumoylationHTGEKPYKCEECGKA
ECCCCCCCHHHHHHC		43.63-
230UbiquitinationHTGEKPYKCEECGKA
ECCCCCCCHHHHHHC		43.63-
230SumoylationHTGEKPYKCEECGKA
ECCCCCCCHHHHHHC		43.63-
236UbiquitinationYKCEECGKAFNRSSN
CCHHHHHHCCCCCCC		62.56-
248UbiquitinationSSNLTKHKIIHTGEK
CCCCCCCCEEECCCC		44.93-
252PhosphorylationTKHKIIHTGEKPYKC
CCCCEEECCCCCEEH		36.3129496963
255UbiquitinationKIIHTGEKPYKCEEC
CEEECCCCCEEHHHH		55.80-
257PhosphorylationIHTGEKPYKCEECGK
EECCCCCEEHHHHHH		39.06-
258AcetylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHC		43.6319825643
258SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHC		43.63-
258UbiquitinationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHC		43.63-
258SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHC		43.63-
264UbiquitinationYKCEECGKAFNRSST
EEHHHHHHCCCCCCC		62.56-
274UbiquitinationNRSSTLTKHKRIHTE
CCCCCCCCCCCCCCC		50.68-
286SumoylationHTEEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
286SumoylationHTEEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
286UbiquitinationHTEEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
292UbiquitinationYKCEECGKAFNQFSI
CCHHHHHHHHHHHHH		62.56-
298PhosphorylationGKAFNQFSILNKHKR
HHHHHHHHHHCCCCC		19.1923186163
314SumoylationHMEDKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
314SumoylationHMEDKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
314UbiquitinationHMEDKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
326PhosphorylationGKAFRVFSILKKHKI
HHHHHHHHHHHHCCE		24.9324719451
332UbiquitinationFSILKKHKIIHTGEK
HHHHHHCCEEECCCC		52.84-
336PhosphorylationKKHKIIHTGEKPYKC
HHCCEEECCCCCEEH		36.3129496963
339UbiquitinationKIIHTGEKPYKCEEC
CEEECCCCCEEHHHH		55.80-
341PhosphorylationIHTGEKPYKCEECGK
EECCCCCEEHHHHHH		39.06-
342AcetylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		43.6319825649
342SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		43.63-
342UbiquitinationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		43.63-
342SumoylationHTGEKPYKCEECGKA
ECCCCCEEHHHHHHH		43.63-
348UbiquitinationYKCEECGKAFNQFSN
EEHHHHHHHHHHHHC		62.56-
358SumoylationNQFSNLTKHKIIHTG
HHHHCCCCCCEEECC		46.17-
358SumoylationNQFSNLTKHKIIHTG
HHHHCCCCCCEEECC		46.17-
358UbiquitinationNQFSNLTKHKIIHTG
HHHHCCCCCCEEECC		46.17-
360UbiquitinationFSNLTKHKIIHTGEK
HHCCCCCCEEECCCC		44.93-
364PhosphorylationTKHKIIHTGEKPYKC
CCCCEEECCCCCEEC		36.3129496963
367UbiquitinationKIIHTGEKPYKCDEC
CEEECCCCCEECCCC		55.80-
370UbiquitinationHTGEKPYKCDECGKA
ECCCCCEECCCCCCC		43.68-
376UbiquitinationYKCDECGKAFNQSST
EECCCCCCCCCCCCC		62.56-
381PhosphorylationCGKAFNQSSTLTKHK
CCCCCCCCCCCCCCC		26.7929978859
382PhosphorylationGKAFNQSSTLTKHKR
CCCCCCCCCCCCCCC		20.0629978859
383PhosphorylationKAFNQSSTLTKHKRI
CCCCCCCCCCCCCCC		43.6329978859
386UbiquitinationNQSSTLTKHKRIHTG
CCCCCCCCCCCCCCC		50.68-
392PhosphorylationTKHKRIHTGEKPYKC
CCCCCCCCCCCCCCH		44.6729496963
395UbiquitinationKRIHTGEKPYKCEEC
CCCCCCCCCCCHHHH		55.80-
397PhosphorylationIHTGEKPYKCEECGK
CCCCCCCCCHHHHHH		39.06-
398SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
398UbiquitinationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
398SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
409PhosphorylationCGKAFKQSSTLTEHK
HHHHHHCCCCCCCCC		26.36-
410PhosphorylationGKAFKQSSTLTEHKI
HHHHHCCCCCCCCCE		25.58-
411PhosphorylationKAFKQSSTLTEHKII
HHHHCCCCCCCCCEE		42.84-
416UbiquitinationSSTLTEHKIIHTGEK
CCCCCCCCEEECCCC		36.80-
420PhosphorylationTEHKIIHTGEKPYKC
CCCCEEECCCCCEEC		36.3129496963
423UbiquitinationKIIHTGEKPYKCEKC
CEEECCCCCEECCCC		55.80-
425PhosphorylationIHTGEKPYKCEKCGK
EECCCCCEECCCCCC		39.06-
426AcetylationHTGEKPYKCEKCGKA
ECCCCCEECCCCCCC		44.4319825655
441PhosphorylationFSWSSAFTKHKRNHM
EEHHHHHHHHHHHCC		31.77-
454"N6,N6-dimethyllysine"HMEDKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
454SumoylationHMEDKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
454UbiquitinationHMEDKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
454MethylationHMEDKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
463PhosphorylationEECGKAFSVFSTLTK
HHHHHHHHHHHHHHC		27.4119413330
470UbiquitinationSVFSTLTKHKIIHTR
HHHHHHHCCCCEECC		46.11-
482SumoylationHTREKPYKCEECGKA
ECCCCCCCCHHHHHH		43.63-
482SumoylationHTREKPYKCEECGKA
ECCCCCCCCHHHHHH		43.63-
482UbiquitinationHTREKPYKCEECGKA
ECCCCCCCCHHHHHH		43.63-
493PhosphorylationCGKAFNQSSIFTKHK
HHHHCCCCHHCCCCC		26.89-
494PhosphorylationGKAFNQSSIFTKHKI
HHHCCCCHHCCCCCE		16.38-
497PhosphorylationFNQSSIFTKHKIIHT
CCCCHHCCCCCEEEC		30.48-
500UbiquitinationSSIFTKHKIIHTEGK
CHHCCCCCEEECCCC		44.93-
504PhosphorylationTKHKIIHTEGKSYKC
CCCCEEECCCCEEEC		35.7029396449
513UbiquitinationGKSYKCEKCGNAFNQ
CCEEECCCCCCCCCC		57.84-
519N-linked_GlycosylationEKCGNAFNQSSNLTA
CCCCCCCCCCCCCCC		38.11-
519N-linked_GlycosylationEKCGNAFNQSSNLTA
CCCCCCCCCCCCCCC		38.1119522481
528UbiquitinationSSNLTARKIIYTGEK
CCCCCCCEEEECCCC		30.87-
535UbiquitinationKIIYTGEKPYKYEEC
EEEECCCCCCCHHHH		55.80-
538UbiquitinationYTGEKPYKYEECDKA
ECCCCCCCHHHHHHH		55.50-
575UbiquitinationECGRAFNKSSNYTKE
HHHCCCCCCCCCCHH		49.13-
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 ZNF92_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNF92_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 ZNF92_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZNF92_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 ZNF92_HUMAN

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Related Literatures of Post-Translational Modification

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