CSK_RAT - dbPTM
CSK_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSK_RAT
UniProt AC P32577
Protein Name Tyrosine-protein kinase CSK
Gene Name Csk
Organism Rattus norvegicus (Rat).
Sequence Length 450
Subcellular Localization Cytoplasm. Cell membrane. Mainly cytoplasmic, also present in lipid rafts..
Protein Description Non-receptor tyrosine-protein kinase that plays an important role in the regulation of cell growth, differentiation, migration and immune response. Phosphorylates tyrosine residues located in the C-terminal tails of Src-family kinases (SFKs) including LCK, SRC, HCK, FYN, LYN or YES1. Upon tail phosphorylation, Src-family members engage in intramolecular interactions between the phosphotyrosine tail and the SH2 domain that result in an inactive conformation. To inhibit SFKs, CSK is recruited to the plasma membrane via binding to transmembrane proteins or adapter proteins located near the plasma membrane. Suppresses signaling by various surface receptors, including T-cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating and maintaining inactive several positive effectors such as FYN or LCK (By similarity)..
Protein Sequence MSAIQASWPSGTECIAKYNFHGTAEQDLPFCKGDVLTIVAVTKDPNWYKAKNKVGREGIIPANYVQKREGVKAGTKLSLMPWFHGKITREQAERLLYPPETGLFLVRESTNYPGDYTLCVSCEGKVEHYRIMYHASKLSIDEEVYFENLMQLVEHYTTDADGLCTRLIKPKVMEGTVAAQDEFYRSGWALNMKELKLLQTIGKGEFGDVMLGDYRGNKVAVKCIKNDATAQAFLAEASVMTQLRHSNLVQLLGVIVEEKGGLYIVTEYMAKGSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAVYDVMKNCWHLDAATRPTFLQLREQLEHIRTHELHL
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
2Acetylation------MSAIQASWP
------CCCCCCCCC
33.79-
2Phosphorylation------MSAIQASWP
------CCCCCCCCC
33.7923984901
184PhosphorylationVAAQDEFYRSGWALN
EECCHHHHHHCCCCC
11.2121940666
263PhosphorylationVEEKGGLYIVTEYMA
EEECCCEEEEEEEEC
9.1628689409
273PhosphorylationTEYMAKGSLVDYLRS
EEEECCCCHHHHHHH
25.2328689409
277PhosphorylationAKGSLVDYLRSRGRS
CCCCHHHHHHHCCCC
9.1328689409
304PhosphorylationDVCEAMEYLEGNNFV
HHHHHHHHHCCCCCC
9.29-
364PhosphorylationALREKKFSTKSDVWS
HHHHCCCCCHHHHHH
43.75-
416PhosphorylationDGCPPAVYDVMKNCW
CCCCHHHHHHHHHCC
12.62-

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
364SPhosphorylationKinasePKA-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
364SPhosphorylation

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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 CSK_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PHAG1_RATPag1genetic
10801129
CXA1_RATGja1physical
27391443

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

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Related Literatures of Post-Translational Modification

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