ZNF93_HUMAN - dbPTM
ZNF93_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNF93_HUMAN
UniProt AC P35789
Protein Name Zinc finger protein 93
Gene Name ZNF93
Organism Homo sapiens (Human).
Sequence Length 620
Subcellular Localization Nucleus .
Protein Description Transcription factor specifically required to repress long interspersed nuclear element 1 (L1) retrotransposons: recognizes and binds L1 sequences and repress their expression by recruiting a repressive complex containing TRIM28/KAP1. [PubMed: 25274305 Not able to repress expression of all subtypes of L1 elements. Binds to the 5' end of L1PA4, L1PA5 and L1PA6 subtypes, and some L1PA3 subtypes. Does not bind to L1PA7 or older subtypes nor at the most recently evolved L1PA2 and L1Hs. 50% of L1PA3 elements have lost the ZNF93-binding site, explaining why ZNF93 is not able to repress their expression]
Protein Sequence MGPLQFRDVAIEFSLEEWHCLDTAQRNLYRNVMLENYSNLVFLGIVVSKPDLIAHLEQGKKPLTMKRHEMVANPSVICSHFAQDLWPEQNIKDSFQKVILRRYEKRGHGNLQLIKRCESVDECKVHTGGYNGLNQCSTTTQSKVFQCDKYGKVFHKFSNSNRHNIRHTEKKPFKCIECGKAFNQFSTLITHKKIHTGEKPYICEECGKAFKYSSALNTHKRIHTGEKPYKCDKCDKAFIASSTLSKHEIIHTGKKPYKCEECGKAFNQSSTLTKHKKIHTGEKPYKCEECGKAFNQSSTLTKHKKIHTGEKPYVCEECGKAFKYSRILTTHKRIHTGEKPYKCNKCGKAFIASSTLSRHEFIHMGKKHYKCEECGKAFIWSSVLTRHKRVHTGEKPYKCEECGKAFKYSSTLSSHKRSHTGEKPYKCEECGKAFVASSTLSKHEIIHTGKKPYKCEECGKAFNQSSSLTKHKKIHTGEKPYKCEECGKAFNQSSSLTKHKKIHTGEKPYKCEECGKAFNQSSTLIKHKKIHTREKPYKCEECGKAFHLSTHLTTHKILHTGEKPYRCRECGKAFNHSATLSSHKKIHSGEKPYECDKCGKAFISPSSLSRHEIIHTGEKP
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
14PhosphorylationRDVAIEFSLEEWHCL
HHEEEEEECCHHHHH		23.29-
29PhosphorylationDTAQRNLYRNVMLEN
HHHHHHHHHHHHHHC		12.04-
48PhosphorylationVFLGIVVSKPDLIAH
EEEEEEECCHHHHHH		27.81-
97UbiquitinationNIKDSFQKVILRRYE
CHHHHHHHHHHHHHH		29.27-
192AcetylationFSTLITHKKIHTGEK
HHHHHHCCCCCCCCC		44.787696005
193AcetylationSTLITHKKIHTGEKP
HHHHHCCCCCCCCCC		31.927696013
196PhosphorylationITHKKIHTGEKPYIC
HHCCCCCCCCCCEEE		50.9723403867
201PhosphorylationIHTGEKPYICEECGK
CCCCCCCEEEHHHHH		29.3023403867
224PhosphorylationNTHKRIHTGEKPYKC
CCCCCCCCCCCCCCC		44.6729496963
255AcetylationEIIHTGKKPYKCEEC
CEEECCCCCEEHHHH		55.7312654435
258SumoylationHTGKKPYKCEECGKA
ECCCCCEEHHHHHHH		43.63-
258UbiquitinationHTGKKPYKCEECGKA
ECCCCCEEHHHHHHH		43.63-
258AcetylationHTGKKPYKCEECGKA
ECCCCCEEHHHHHHH		43.6312654445
258SumoylationHTGKKPYKCEECGKA
ECCCCCEEHHHHHHH		43.63-
269PhosphorylationCGKAFNQSSTLTKHK
HHHHCCCCCCCCCCC		26.7929978859
270PhosphorylationGKAFNQSSTLTKHKK
HHHCCCCCCCCCCCC		20.0629978859
271PhosphorylationKAFNQSSTLTKHKKI
HHCCCCCCCCCCCCC		43.6329978859
274UbiquitinationNQSSTLTKHKKIHTG
CCCCCCCCCCCCCCC		57.44-
276AcetylationSSTLTKHKKIHTGEK
CCCCCCCCCCCCCCC		55.7812654455
277UbiquitinationSTLTKHKKIHTGEKP
CCCCCCCCCCCCCCC		39.17-
280PhosphorylationTKHKKIHTGEKPYKC
CCCCCCCCCCCCEEH		50.9729496963
283UbiquitinationKKIHTGEKPYKCEEC
CCCCCCCCCEEHHHH		55.80-
283AcetylationKKIHTGEKPYKCEEC
CCCCCCCCCEEHHHH		55.8012654465
285PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEEHHHHHH		39.06-
286SumoylationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
286SumoylationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
286UbiquitinationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
286AcetylationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHH		43.6312654475
297PhosphorylationCGKAFNQSSTLTKHK
HHHHCCCCCCCCCCC		26.7929978859
298PhosphorylationGKAFNQSSTLTKHKK
HHHCCCCCCCCCCCC		20.0629978859
299PhosphorylationKAFNQSSTLTKHKKI
HHCCCCCCCCCCCCC		43.6329978859
302UbiquitinationNQSSTLTKHKKIHTG
CCCCCCCCCCCCCCC		57.44-
304AcetylationSSTLTKHKKIHTGEK
CCCCCCCCCCCCCCC		55.7812654485
305UbiquitinationSTLTKHKKIHTGEKP
CCCCCCCCCCCCCCC		39.17-
308PhosphorylationTKHKKIHTGEKPYVC
CCCCCCCCCCCCEEE		50.97-
330PhosphorylationKYSRILTTHKRIHTG
HHHHHHCCCCCCCCC		23.1924719451
336PhosphorylationTTHKRIHTGEKPYKC
CCCCCCCCCCCCCCC		44.6729496963
353PhosphorylationCGKAFIASSTLSRHE
CCCEEEEECCCCHHH		21.0229414761
392PhosphorylationTRHKRVHTGEKPYKC
HCCCCCCCCCCCEEC		44.1529496963
395SumoylationKRVHTGEKPYKCEEC
CCCCCCCCCEECCHH		55.80-
395UbiquitinationKRVHTGEKPYKCEEC
CCCCCCCCCEECCHH		55.80-
395SumoylationKRVHTGEKPYKCEEC
CCCCCCCCCEECCHH		55.80-
397PhosphorylationVHTGEKPYKCEECGK
CCCCCCCEECCHHCC		39.06-
398SumoylationHTGEKPYKCEECGKA
CCCCCCEECCHHCCE		43.63-
398UbiquitinationHTGEKPYKCEECGKA
CCCCCCEECCHHCCE		43.63-
398SumoylationHTGEKPYKCEECGKA
CCCCCCEECCHHCCE		43.63-
420PhosphorylationSSHKRSHTGEKPYKC
CCCCCCCCCCCCEEC		48.5624719451
426SumoylationHTGEKPYKCEECGKA
CCCCCCEECHHHCCE		43.63-
426UbiquitinationHTGEKPYKCEECGKA
CCCCCCEECHHHCCE		43.63-
426SumoylationHTGEKPYKCEECGKA
CCCCCCEECHHHCCE		43.63-
454SumoylationHTGKKPYKCEECGKA
ECCCCCEEHHHHHHH		43.63-
454UbiquitinationHTGKKPYKCEECGKA
ECCCCCEEHHHHHHH		43.63-
454SumoylationHTGKKPYKCEECGKA
ECCCCCEEHHHHHHH		43.63-
473UbiquitinationSSLTKHKKIHTGEKP
CCCCCCCCCCCCCCC		39.17-
476PhosphorylationTKHKKIHTGEKPYKC
CCCCCCCCCCCCEEH		50.9729496963
479UbiquitinationKKIHTGEKPYKCEEC
CCCCCCCCCEEHHHH		55.80-
481PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEEHHHHHH		39.06-
482SumoylationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
482SumoylationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
482UbiquitinationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHH		43.63-
501UbiquitinationSSLTKHKKIHTGEKP
CCCCCCCCCCCCCCC		39.17-
504PhosphorylationTKHKKIHTGEKPYKC
CCCCCCCCCCCCCCH		50.9729496963
507UbiquitinationKKIHTGEKPYKCEEC
CCCCCCCCCCCHHHH		55.80-
509PhosphorylationIHTGEKPYKCEECGK
CCCCCCCCCHHHHHH		39.06-
510UbiquitinationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
510SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
510SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
521PhosphorylationCGKAFNQSSTLIKHK
HHHHHCCCCCCEECC		26.7922964224
526UbiquitinationNQSSTLIKHKKIHTR
CCCCCCEECCCCCCC		53.11-
538UbiquitinationHTREKPYKCEECGKA
CCCCCCEECHHCCCE		43.63-
538SumoylationHTREKPYKCEECGKA
CCCCCCEECHHCCCE		43.63-
538SumoylationHTREKPYKCEECGKA
CCCCCCEECHHCCCE		43.63-
560PhosphorylationTTHKILHTGEKPYRC
CCCCEECCCCCCEEC		43.5224719451
563UbiquitinationKILHTGEKPYRCREC
CEECCCCCCEECCCC		49.01-
604PhosphorylationKCGKAFISPSSLSRH
CCCCEEECHHHHCCC		16.5722199227
606PhosphorylationGKAFISPSSLSRHEI
CCEEECHHHHCCCCE		36.8022199227
607O-linked_GlycosylationKAFISPSSLSRHEII
CEEECHHHHCCCCEE		33.4730379171
607PhosphorylationKAFISPSSLSRHEII
CEEECHHHHCCCCEE		33.4722199227
609O-linked_GlycosylationFISPSSLSRHEIIHT
EECHHHHCCCCEEEC		33.2730379171
616PhosphorylationSRHEIIHTGEKP---
CCCCEEECCCCC---		36.3121857030
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 ZNF93_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNF93_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 ZNF93_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZNF93_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 ZNF93_HUMAN

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Related Literatures of Post-Translational Modification

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