ZNF99_HUMAN - dbPTM
ZNF99_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZNF99_HUMAN
UniProt AC A8MXY4
Protein Name Zinc finger protein 99
Gene Name ZNF99
Organism Homo sapiens (Human).
Sequence Length 864
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MGSLTFWDVTIEFALEEWQCLDMAQQNLYRNVMLENYRNLVFLGIAVSKLDLITCLKQGKEPWNMKRHEMVTKPPVISSHFTQDFWPDQSIKDSFQEIILRTYARCGHKNLRLRKDCESVNEGKMHEEAYNKLNQCWTTTQGKIFQCNKYVKVFHKYSNSNRYKIRHTKKKTFKCMKCSKSFFMLSHLIQHKRIHTRENIYKCEERGKAFKWFSTLIKHKIIHTEDKPYKYKKCGKAFNISSMFTKCKIIHTGKKPCKCEECGKVFNNSSTLMKHKIIHTGKKPYKCEECGKAFKQSSHLTRHKAIHTGEKPYKCEECGKAFNHFSALRKHQIIHTGKKPYKCEECGKAFSQSSTLRKHEIIHTEEKPYKYEECGKAFSNLSALRKHEIIHTGQKPYKCEECGKAFKWSSKLTVHKVIHTAEKPCKCEECGKAFKRFSALRKHKIIHTGKQPYKCEECSKAFSNFSALRKHEIIHTGEKPYKCEECGKAFKWSSKLTVHKVIHMEEKPCKCEECGKAFKHFSALRKHKIIHTGKKPYKCEECGKAFNNSSTLMKHKIIHTGKKPYKCEECGKAFKQSSHLTRHKAIHTGEKPYKCEECGKAFNHFSALRKHQIIHTGKKPYKCEECGKAFSQSSTLRKHEIIHTGEKPYKCEECGKAFKWSSHLTRHKVIHTEEKPYKCEECGKAFNHFSALRKHKIIHTGKKPYKCEECGKAFSQSSTLRKHEIIHTGEKPYKCEECGKAFKWSSKLTVHKVIHTAEKPCKCEECGKAFKHFSALRKHKIIHTGKKPYKCEECGKAFNNSSTLRKHEIIHTGEKSYKCEECGKAFQWSSKLTLHKVIHMERNPANVKNVAKLLNISQPLENMR
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
149UbiquitinationGKIFQCNKYVKVFHK
CCEEECCCEEEEEEE		41.60-
152UbiquitinationFQCNKYVKVFHKYSN
EECCCEEEEEEECCC		49.76-
157PhosphorylationYVKVFHKYSNSNRYK
EEEEEEECCCCCCEE		3.2025003641
160PhosphorylationVFHKYSNSNRYKIRH
EEEECCCCCCEEEEE		7.8225003641
163PhosphorylationKYSNSNRYKIRHTKK
ECCCCCCEEEEECCC		23.9625003641
164AcetylationYSNSNRYKIRHTKKK
CCCCCCEEEEECCCC		30.4518524793
170AcetylationYKIRHTKKKTFKCMK
EEEEECCCCCEEECC		60.0718524799
170UbiquitinationYKIRHTKKKTFKCMK
EEEEECCCCCEEECC		60.07-
201PhosphorylationIHTRENIYKCEERGK
CCCCCCHHCHHHHHH		63.41-
269PhosphorylationCGKVFNNSSTLMKHK
CCCCCCCCHHHHEEE		46.8322798277
270PhosphorylationGKVFNNSSTLMKHKI
CCCCCCCHHHHEEEE		2.5322798277
271PhosphorylationKVFNNSSTLMKHKII
CCCCCCHHHHEEEEE		2.7522798277
286SumoylationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHH		9.82-
286UbiquitinationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHH		9.82-
286SumoylationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHH		9.82-
308PhosphorylationTRHKAIHTGEKPYKC
HCCCCCCCCCCCCCC		4.3729496963
311SumoylationKAIHTGEKPYKCEEC
CCCCCCCCCCCCHHH		2.94-
311UbiquitinationKAIHTGEKPYKCEEC
CCCCCCCCCCCCHHH		2.94-
311SumoylationKAIHTGEKPYKCEEC
CCCCCCCCCCCCHHH		2.94-
313PhosphorylationIHTGEKPYKCEECGK
CCCCCCCCCCHHHHH		63.41-
314UbiquitinationHTGEKPYKCEECGKA
CCCCCCCCCHHHHHH		9.13-
314SumoylationHTGEKPYKCEECGKA
CCCCCCCCCHHHHHH		9.13-
314SumoylationHTGEKPYKCEECGKA
CCCCCCCCCHHHHHH		9.13-
342SumoylationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHC		10.65-
342UbiquitinationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHC		10.65-
342SumoylationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHC		10.65-
364PhosphorylationRKHEIIHTEEKPYKY
CCCCEEECCCCCCCH		4.37-
367SumoylationEIIHTEEKPYKYEEC
CEEECCCCCCCHHHH		2.06-
367SumoylationEIIHTEEKPYKYEEC
CEEECCCCCCCHHHH		2.06-
398SumoylationHTGQKPYKCEECGKA
ECCCCCEECCCCCCC		9.13-
398UbiquitinationHTGQKPYKCEECGKA
ECCCCCEECCCCCCC		9.13-
398SumoylationHTGQKPYKCEECGKA
ECCCCCEECCCCCCC		9.13-
476PhosphorylationRKHEIIHTGEKPYKC
HHCCEEECCCCCEEC		4.3729496963
479UbiquitinationEIIHTGEKPYKCEEC
CEEECCCCCEECCCC		2.94-
481PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECCCCCC		63.41-
482SumoylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCC		11.36-
482UbiquitinationHTGEKPYKCEECGKA
ECCCCCEECCCCCCC		11.36-
482SumoylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCC		11.36-
497PhosphorylationFKWSSKLTVHKVIHM
CCCCCCCEEEEEECC		40.71-
538SumoylationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHC		8.46-
538SumoylationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHC		8.46-
538UbiquitinationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHC		8.46-
566SumoylationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHH		9.13-
566SumoylationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHH		9.13-
566UbiquitinationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHH		9.13-
587UbiquitinationLTRHKAIHTGEKPYK
HHCCCCCCCCCCCCC		43.63-
588PhosphorylationTRHKAIHTGEKPYKC
HCCCCCCCCCCCCCC		4.3729496963
591SumoylationKAIHTGEKPYKCEEC
CCCCCCCCCCCCHHH		2.94-
591UbiquitinationKAIHTGEKPYKCEEC
CCCCCCCCCCCCHHH		2.94-
591SumoylationKAIHTGEKPYKCEEC
CCCCCCCCCCCCHHH		2.94-
593PhosphorylationIHTGEKPYKCEECGK
CCCCCCCCCCHHHHH		62.56-
594SumoylationHTGEKPYKCEECGKA
CCCCCCCCCHHHHHH		8.85-
594UbiquitinationHTGEKPYKCEECGKA
CCCCCCCCCHHHHHH		8.85-
594SumoylationHTGEKPYKCEECGKA
CCCCCCCCCHHHHHH		8.85-
622SumoylationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHC		8.46-
622UbiquitinationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHC		8.46-
622SumoylationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHC		8.46-
644PhosphorylationRKHEIIHTGEKPYKC
CCCCEEECCCCCEEC		4.3729496963
647UbiquitinationEIIHTGEKPYKCEEC
CEEECCCCCEECCCC		2.94-
649PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECCCCCC		63.41-
650SumoylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCC		9.13-
650UbiquitinationHTGEKPYKCEECGKA
ECCCCCEECCCCCCC		9.13-
650SumoylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCC		9.13-
678SumoylationHTEEKPYKCEECGKA
ECCCCCCCHHHHHHH		12.19-
678UbiquitinationHTEEKPYKCEECGKA
ECCCCCCCHHHHHHH		12.19-
678SumoylationHTEEKPYKCEECGKA
ECCCCCCCHHHHHHH		12.19-
706UbiquitinationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHC		9.55-
706SumoylationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHC		9.55-
706SumoylationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHC		9.55-
728PhosphorylationRKHEIIHTGEKPYKC
CCCCEEECCCCCEEC		3.9629496963
731UbiquitinationEIIHTGEKPYKCEEC
CEEECCCCCEECCCC		1.70-
733PhosphorylationIHTGEKPYKCEECGK
EECCCCCEECCCCCC		13.01-
734SumoylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCC		21.54-
734UbiquitinationHTGEKPYKCEECGKA
ECCCCCEECCCCCCC		21.54-
734SumoylationHTGEKPYKCEECGKA
ECCCCCEECCCCCCC		21.54-
790UbiquitinationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHC		25.88-
790SumoylationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHC		25.88-
790SumoylationHTGKKPYKCEECGKA
ECCCCCCCCHHHHHC		25.88-
812PhosphorylationRKHEIIHTGEKSYKC
CCCEEEECCCCEEEC		52.9427251275
815UbiquitinationEIIHTGEKSYKCEEC
EEEECCCCEEECCHH		39.62-
818SumoylationHTGEKSYKCEECGKA
ECCCCEEECCHHHHH		53.58-
818SumoylationHTGEKSYKCEECGKA
ECCCCEEECCHHHHH		53.58-
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 ZNF99_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZNF99_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 ZNF99_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZNF99_HUMAN !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZNF99_HUMAN

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Related Literatures of Post-Translational Modification

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