ZN418_HUMAN - dbPTM
ZN418_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN418_HUMAN
UniProt AC Q8TF45
Protein Name Zinc finger protein 418
Gene Name ZNF418
Organism Homo sapiens (Human).
Sequence Length 676
Subcellular Localization Nucleus .
Protein Description Transcriptional repressor..
Protein Sequence MQGTVAFEDVAVNFSQEEWSLLSEVQRCLYHDVMLENWVLISSLGCWCGSEDEEAPSKKSISIQRVSQVSTPGAGVSPKKAHSCEMCGAILGDILHLADHQGTHHKQKLHRCEAWGNKLYDSSNRPHQNQYLGEKPYRSSVEEALFVKRCKFHVSEESSIFIQSGKDFLPSSGLLLQEATHTGEKSNSKPECESPFQWGDTHYSCGECMKHSSTKHVFVQQQRLPSREECYCWECGKSFSKYDSVSNHQRVHTGKRPYECGECGKSFSHKGSLVQHQRVHTGKRPYECGECGKSFSHKGSLVQHQRVHTGERPYECGECGKSFSQNGTLIKHQRVHTGERPYECEECGKCFTQKGNLIQHQRGHTSERPYECEECGKCFSQKGTLTEHHRVHTRERPYECGECGKSFSRKGHLRNHQRGHTGERPYECGECGKSFSRKGNLIQHQRSHTGERPYECRECRKLFRGKSHLIEHQRVHTGERPYECNECGKSFQDSSGFRVHQRVHTGEKPFECSECGKSFPQSCSLLRHRRVHTGERPYECGECGKSFHQSSSLLRHQKTHTAERPYECRECGKFFSSLLEHRRVHTGERPYECRECGKTFTRRSAHFKHQRLHTRGKPYECSECGKSFAETFSLTEHRRVHTGERPYECSECGKSFHRSSSLLRHQRVHTERSPYK
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
77PhosphorylationSTPGAGVSPKKAHSC
CCCCCCCCHHHCCCC
30.0424719451
98PhosphorylationLGDILHLADHQGTHH
HHHHHHHHCCCCCCH
11.07-
106UbiquitinationDHQGTHHKQKLHRCE
CCCCCCHHHHHHHHH
41.33-
127UbiquitinationYDSSNRPHQNQYLGE
CCCCCCCCCCCCCCC
35.6721906983
214PhosphorylationECMKHSSTKHVFVQQ
HHHHCCCCCEEEEEC
28.34-
235PhosphorylationEECYCWECGKSFSKY
CCEEECCCCCCCCCC
3.44-
238PhosphorylationYCWECGKSFSKYDSV
EECCCCCCCCCCCCC
21.7524719451
309PhosphorylationVQHQRVHTGERPYEC
EEEEECCCCCCCCCC
37.5728674419
314PhosphorylationVHTGERPYECGECGK
CCCCCCCCCCCCCCC
30.03-
337PhosphorylationIKHQRVHTGERPYEC
EEEEECCCCCCCEEC
37.57-
406PhosphorylationECGECGKSFSRKGHL
ECCCCCCCCCCCCCC
17.4617081983
408PhosphorylationGECGKSFSRKGHLRN
CCCCCCCCCCCCCCC
39.9317081983
434PhosphorylationECGECGKSFSRKGNL
CCCCCCCCCCCCCCC
17.4617081983
436PhosphorylationGECGKSFSRKGNLIQ
CCCCCCCCCCCCCCC
39.9317081983
477PhosphorylationIEHQRVHTGERPYEC
EECCCCCCCCCCEEC
37.57-
505PhosphorylationRVHQRVHTGEKPFEC
EEEEEEECCCCCEEC
44.15-
533PhosphorylationLRHRRVHTGERPYEC
HHCCCCCCCCCCCCC
37.5728674419
538PhosphorylationVHTGERPYECGECGK
CCCCCCCCCCCCCCC
30.03-
551PhosphorylationGKSFHQSSSLLRHQK
CCCHHHHHHHHHCCC
20.5924719451
552PhosphorylationKSFHQSSSLLRHQKT
CCHHHHHHHHHCCCC
36.3524719451
586PhosphorylationLEHRRVHTGERPYEC
HHCCCCCCCCCCCCH
37.5729214152
642PhosphorylationTEHRRVHTGERPYEC
CCCCCCCCCCCCEEC
37.5727251275
647PhosphorylationVHTGERPYECSECGK
CCCCCCCEECCCCCC
35.47-
650PhosphorylationGERPYECSECGKSFH
CCCCEECCCCCCCCH
24.7927251275
660PhosphorylationGKSFHRSSSLLRHQR
CCCCHHHHHHHHHHH
25.5924719451
661PhosphorylationKSFHRSSSLLRHQRV
CCCHHHHHHHHHHHH
32.4424719451

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 ZN418_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN418_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 ZN418_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR107_HUMANKRTAP10-7physical
25416956

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 ZN418_HUMAN

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Related Literatures of Post-Translational Modification

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