CSK_MOUSE - dbPTM
CSK_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSK_MOUSE
UniProt AC P41241
Protein Name Tyrosine-protein kinase CSK
Gene Name Csk
Organism Mus musculus (Mouse).
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 MSAIQAAWPSGTECIAKYNFHGTAEQDLPFCKGDVLTIVAVTKDPNWYKAKNKVGREGIIPANYVQKREGVKAGTKLSLMPWFHGKITREQAERLLYPPETGLFLVRESTNYPGDYTLCVSCEGKVEHYRIMYHASKLSIDEEVYFENLMQLVEHYTTDADGLCTRLIKPKVMEGTVAAQDEFYRSGWALNMKELKLLQTIGKGEFGDVMLGDYRGNKVAVKCIKNDATAQAFLAEASVMTQLRHSNLVQLLGVIVEEKGGLYIVTEYMAKGSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAVYEVMKNCWHLDAATRPTFLQLREQLEHIKTHELHL
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------MSAIQAAWP
------CCCCCCCCC
33.79-
18PhosphorylationGTECIAKYNFHGTAE
CCEEEEEECCCCCCC
17.6525195567
64PhosphorylationEGIIPANYVQKREGV
CCCCCHHHCCHHHCC
13.3329514104
97PhosphorylationEQAERLLYPPETGLF
HHHHHHCCCCCCEEE
22.72-
184PhosphorylationVAAQDEFYRSGWALN
EECCHHHHHHCCCCC
11.2122817900
193AcetylationSGWALNMKELKLLQT
HCCCCCHHHHHHHHH
59.8423864654
196AcetylationALNMKELKLLQTIGK
CCCHHHHHHHHHHCC
48.5223864654
203AcetylationKLLQTIGKGEFGDVM
HHHHHHCCCCCCCEE
51.9523864654
290GlutathionylationRSVLGGDCLLKFSLD
CCCCCCCCEEEEEHH
5.6124333276
304PhosphorylationDVCEAMEYLEGNNFV
HHHHHHHHHCCCCCC
9.29-
364PhosphorylationALREKKFSTKSDVWS
HHHHCCCCCHHHHHH
43.75-
416PhosphorylationDGCPPAVYEVMKNCW
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

-

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSK_HUMANCSKphysical
20360068
CADH5_MOUSECdh5physical
15861137
CSK_MOUSECskphysical
15861137
ITB3_MOUSEItgb3physical
24558484
DOK1_MOUSEDok1physical
9221755
KCC2G_HUMANCAMK2Gphysical
26496610
COX11_HUMANCOX11physical
26496610
T22D3_HUMANTSC22D3physical
26496610
HMGA1_HUMANHMGA1physical
26496610
PLCG2_HUMANPLCG2physical
26496610
RAD52_HUMANRAD52physical
26496610
RO52_HUMANTRIM21physical
26496610
QCR2_HUMANUQCRC2physical
26496610
ZO2_HUMANTJP2physical
26496610
HOME3_HUMANHOMER3physical
26496610
RBG10_HUMANRABGAP1Lphysical
26496610
RBG1L_HUMANRABGAP1Lphysical
26496610
CELF2_HUMANCELF2physical
26496610
EBP2_HUMANEBNA1BP2physical
26496610
ZFY26_HUMANZFYVE26physical
26496610
SHLB1_HUMANSH3GLB1physical
26496610
AFTIN_HUMANAFTPHphysical
26496610
K1522_HUMANKIAA1522physical
26496610
ZN668_HUMANZNF668physical
26496610
QSER1_HUMANQSER1physical
26496610
LMA2L_HUMANLMAN2Lphysical
26496610
PYM1_HUMANWIBGphysical
26496610
PCGF5_HUMANPCGF5physical
26496610
FRYL_HUMANFRYLphysical
26496610
ITIH6_HUMANITIH6physical
26496610

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

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Related Literatures of Post-Translational Modification

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