ZN117_HUMAN - dbPTM
ZN117_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN117_HUMAN
UniProt AC Q03924
Protein Name Zinc finger protein 117
Gene Name ZNF117
Organism Homo sapiens (Human).
Sequence Length 483
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MKRHEMVAKHLVMFYYFAQHLWPEQNIRDSFQKVTLRRYRKCGYENLQLRKGCKSVVECKQHKGDYSGLNQCLKTTLSKIFQCNKYVEVFHKISNSNRHKMRHTENKHFKCKECRKTFCMLSHLTQHKRIQTRVNFYKCEAYGRAFNWSSTLNKHKRIHTGEKPYKCKECGKAFNQTSHLIRHKRIHTEEKPYKCEECGKAFNQSSTLTTHNIIHTGEIPYKCEKCVRAFNQASKLTEHKLIHTGEKRYECEECGKAFNRSSKLTEHKYIHTGEKLYKCEECGKAFNQSSTLTTHKRIHSGEKPYKCEECGKAFKQFSNLTDHKKIHTGEKPYKCEECGKAFNQLSNLTRHKVIHTGEKPYKCGECGKAFNQSSALNTHKIIHTGENPHKCRESGKVFHLSSKLSTCKKIHTGEKLYKCEECGKAFNRSSTLIGHKRIHTGEKPYKCEECGKAFNQSSTLTTHKIIHTEEKQYKCDECGKAST
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
33UbiquitinationNIRDSFQKVTLRRYR
CHHHHHHHHHHHHHH		34.87-
149PhosphorylationYGRAFNWSSTLNKHK
HHHCCCCHHHCCCCC		17.9830576142
150PhosphorylationGRAFNWSSTLNKHKR
HHCCCCHHHCCCCCC		28.6430576142
151PhosphorylationRAFNWSSTLNKHKRI
HCCCCHHHCCCCCCC		28.9130576142
160PhosphorylationNKHKRIHTGEKPYKC
CCCCCCCCCCCCCCC		44.6729496963
165PhosphorylationIHTGEKPYKCKECGK
CCCCCCCCCCCHHHH		39.83-
194SumoylationHTEEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
194UbiquitinationHTEEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
194SumoylationHTEEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
200UbiquitinationYKCEECGKAFNQSST
CCHHHHHHHCCCCCC		62.56-
206PhosphorylationGKAFNQSSTLTTHNI
HHHCCCCCCCEECCE		20.0622468782
207PhosphorylationKAFNQSSTLTTHNII
HHCCCCCCCEECCEE		33.1122468782
234PhosphorylationVRAFNQASKLTEHKL
HHHHHHHHHHHHCCC		20.5928842319
256UbiquitinationYECEECGKAFNRSSK
EEHHHHHHHCCCCCC		62.5622505724
277PhosphorylationIHTGEKLYKCEECGK
ECCCCCEEEHHHHHH		25.35-
278UbiquitinationHTGEKLYKCEECGKA
CCCCCEEEHHHHHHC		45.68-
278SumoylationHTGEKLYKCEECGKA
CCCCCEEEHHHHHHC		45.68-
278SumoylationHTGEKLYKCEECGKA
CCCCCEEEHHHHHHC		45.68-
284UbiquitinationYKCEECGKAFNQSST
EEHHHHHHCCCCCCC		62.5629967540
289PhosphorylationCGKAFNQSSTLTTHK
HHHCCCCCCCCCCCC		26.79-
290PhosphorylationGKAFNQSSTLTTHKR
HHCCCCCCCCCCCCC		20.06-
293PhosphorylationFNQSSTLTTHKRIHS
CCCCCCCCCCCCCCC		27.26-
294PhosphorylationNQSSTLTTHKRIHSG
CCCCCCCCCCCCCCC		28.6324719451
300PhosphorylationTTHKRIHSGEKPYKC
CCCCCCCCCCCCCCH		46.4029496963
306SumoylationHSGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
306UbiquitinationHSGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
306SumoylationHSGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
325UbiquitinationSNLTDHKKIHTGEKP
HCCCCCCCCCCCCCC		35.98-
328PhosphorylationTDHKKIHTGEKPYKC
CCCCCCCCCCCCCCH		50.9729496963
331UbiquitinationKKIHTGEKPYKCEEC
CCCCCCCCCCCHHHH		55.80-
333PhosphorylationIHTGEKPYKCEECGK
CCCCCCCCCHHHHHH		39.06-
334SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
334UbiquitinationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
334SumoylationHTGEKPYKCEECGKA
CCCCCCCCHHHHHHH		43.63-
356PhosphorylationTRHKVIHTGEKPYKC
CCCCEEECCCCCEEC		35.5929496963
362SumoylationHTGEKPYKCGECGKA
ECCCCCEECCCCHHC		44.27-
362SumoylationHTGEKPYKCGECGKA
ECCCCCEECCCCHHC		44.27-
417PhosphorylationIHTGEKLYKCEECGK
CCCCCCEEEHHHHHH		25.35-
418SumoylationHTGEKLYKCEECGKA
CCCCCEEEHHHHHHH		45.68-
418SumoylationHTGEKLYKCEECGKA
CCCCCEEEHHHHHHH		45.68-
418UbiquitinationHTGEKLYKCEECGKA
CCCCCEEEHHHHHHH		45.68-
424UbiquitinationYKCEECGKAFNRSST
EEHHHHHHHCCCCCC		62.5622505724
431PhosphorylationKAFNRSSTLIGHKRI
HHCCCCCCCCCCCCC		24.52-
440PhosphorylationIGHKRIHTGEKPYKC
CCCCCCCCCCCCEEH		44.6729496963
443UbiquitinationKRIHTGEKPYKCEEC
CCCCCCCCCEEHHHH		55.80-
445PhosphorylationIHTGEKPYKCEECGK
CCCCCCCEEHHHHHH		39.06-
446SumoylationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHC		43.63-
446SumoylationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHC		43.63-
446UbiquitinationHTGEKPYKCEECGKA
CCCCCCEEHHHHHHC		43.63-
452UbiquitinationYKCEECGKAFNQSST
EEHHHHHHCCCCCCC		62.56-
457PhosphorylationCGKAFNQSSTLTTHK
HHHCCCCCCCCEEEC		26.79-
458PhosphorylationGKAFNQSSTLTTHKI
HHCCCCCCCCEEECE		20.06-
459PhosphorylationKAFNQSSTLTTHKII
HCCCCCCCCEEECEE		33.11-
461PhosphorylationFNQSSTLTTHKIIHT
CCCCCCCEEECEEEC		27.26-
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 ZN117_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN117_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 ZN117_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN117_HUMAN !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZN117_HUMAN

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Related Literatures of Post-Translational Modification

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