ZN664_HUMAN - dbPTM
ZN664_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN664_HUMAN
UniProt AC Q8N3J9
Protein Name Zinc finger protein 664
Gene Name ZNF664 {ECO:0000312|HGNC:HGNC:25406}
Organism Homo sapiens (Human).
Sequence Length 261
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MIYKCPMCREFFSERADLFMHQKIHTAEKPHKCDKCDKGFFHISELHIHWRDHTGEKVYKCDDCGKDFSTTTKLNRHKKIHTVEKPYKCYECGKAFNWSSHLQIHMRVHTGEKPYVCSECGRGFSNSSNLCMHQRVHTGEKPFKCEECGKAFRHTSSLCMHQRVHTGEKPYKCYECGKAFSQSSSLCIHQRVHTGEKPYRCCGCGKAFSQSSSLCIHQRVHTGEKPFKCDECGKAFSQSTSLCIHQRVHTKERNHLKISVI
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
4Sumoylation----MIYKCPMCREF
----CCCCCHHHHHH
22.42-
4Sumoylation----MIYKCPMCREF
----CCCCCHHHHHH
22.42-
26PhosphorylationFMHQKIHTAEKPHKC
HHHCHHHCCCCCCCC
39.73-
38AcetylationHKCDKCDKGFFHISE
CCCCCCCCCEEEEEE
68.0620167786
44PhosphorylationDKGFFHISELHIHWR
CCCEEEEEEEEEEEE
26.07-
69PhosphorylationDDCGKDFSTTTKLNR
CCCCCCCCCCCCCCC
34.6730206219
70PhosphorylationDCGKDFSTTTKLNRH
CCCCCCCCCCCCCCC
38.1830206219
71PhosphorylationCGKDFSTTTKLNRHK
CCCCCCCCCCCCCCC
22.2730206219
72PhosphorylationGKDFSTTTKLNRHKK
CCCCCCCCCCCCCCC
33.3530206219
73SumoylationKDFSTTTKLNRHKKI
CCCCCCCCCCCCCCE
41.49-
73UbiquitinationKDFSTTTKLNRHKKI
CCCCCCCCCCCCCCE
41.49-
73SumoylationKDFSTTTKLNRHKKI
CCCCCCCCCCCCCCE
41.49-
88SumoylationHTVEKPYKCYECGKA
EEECCCEEEECCCCC
38.58-
88SumoylationHTVEKPYKCYECGKA
EEECCCEEEECCCCC
38.58-
110PhosphorylationQIHMRVHTGEKPYVC
EEEEEEECCCCCEEE
44.1524719451
113SumoylationMRVHTGEKPYVCSEC
EEEECCCCCEEECCC
42.89-
113SumoylationMRVHTGEKPYVCSEC
EEEECCCCCEEECCC
42.89-
138PhosphorylationCMHQRVHTGEKPFKC
CCCEECCCCCCCCCH
44.1523898821
144SumoylationHTGEKPFKCEECGKA
CCCCCCCCHHHHHHH
49.62-
144SumoylationHTGEKPFKCEECGKA
CCCCCCCCHHHHHHH
49.62-
166PhosphorylationCMHQRVHTGEKPYKC
CCCCCCCCCCCCEEE
44.1529496963
169SumoylationQRVHTGEKPYKCYEC
CCCCCCCCCEEEECC
55.80-
169SumoylationQRVHTGEKPYKCYEC
CCCCCCCCCEEEECC
55.80-
169UbiquitinationQRVHTGEKPYKCYEC
CCCCCCCCCEEEECC
55.80-
172SumoylationHTGEKPYKCYECGKA
CCCCCCEEEECCCCC
38.58-
172SumoylationHTGEKPYKCYECGKA
CCCCCCEEEECCCCC
38.58-
194PhosphorylationCIHQRVHTGEKPYRC
EEEEEEECCCCCEEE
44.15-
197UbiquitinationQRVHTGEKPYRCCGC
EEEECCCCCEEECCC
49.01-
222PhosphorylationCIHQRVHTGEKPFKC
EEEEEECCCCCCEEC
44.1523898821
257SumoylationTKERNHLKISVI---
CCCCCCEEEEEC---
25.9428112733

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 ZN664_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN664_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 ZN664_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN664_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 ZN664_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP