CK2N1_HUMAN - dbPTM
CK2N1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CK2N1_HUMAN
UniProt AC Q7Z7J9
Protein Name Calcium/calmodulin-dependent protein kinase II inhibitor 1
Gene Name CAMK2N1
Organism Homo sapiens (Human).
Sequence Length 78
Subcellular Localization Cell junction, synapse, synaptosome. Cell junction, synapse, postsynaptic cell membrane, postsynaptic density.
Protein Description Potent and specific inhibitor of CaM-kinase II (CAMK2)..
Protein Sequence MSEVLPYGDEKLSPYGDGGDVGQIFSCRLQDTNNFFGAGQNKRPPKLGQIGRSKRVVIEDDRIDDVLKNMTDKAPPGV
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
2Phosphorylation------MSEVLPYGD
------CCCCCCCCC
36.0928348404
53PhosphorylationKLGQIGRSKRVVIED
CCCCCCCCCEEEEEC
21.43-

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 CK2N1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CK2N1_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 CK2N1_HUMAN !!

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

Oops, there are no PPI records of CK2N1_HUMAN !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CK2N1_HUMAN

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Related Literatures of Post-Translational Modification

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