CSK_HUMAN - dbPTM
CSK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSK_HUMAN
UniProt AC P41240
Protein Name Tyrosine-protein kinase CSK
Gene Name CSK
Organism Homo sapiens (Human).
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..
Protein Sequence MSAIQAAWPSGTECIAKYNFHGTAEQDLPFCKGDVLTIVAVTKDPNWYKAKNKVGREGIIPANYVQKREGVKAGTKLSLMPWFHGKITREQAERLLYPPETGLFLVRESTNYPGDYTLCVSCDGKVEHYRIMYHASKLSIDEEVYFENLMQLVEHYTSDADGLCTRLIKPKVMEGTVAAQDEFYRSGWALNMKELKLLQTIGKGEFGDVMLGDYRGNKVAVKCIKNDATAQAFLAEASVMTQLRHSNLVQLLGVIVEEKGGLYIVTEYMAKGSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAVYEVMKNCWHLDAAMRPSFLQLREQLEHIKTHELHL
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		33.7919413330
2Phosphorylation------MSAIQAAWP
------CCCCCCCCC		33.7919413330
10PhosphorylationAIQAAWPSGTECIAK
CCCCCCCCCCEEEEE		47.8728348404
12PhosphorylationQAAWPSGTECIAKYN
CCCCCCCCEEEEEEC		31.8328348404
18PhosphorylationGTECIAKYNFHGTAE
CCEEEEEECCCCCCC		17.6528152594
23PhosphorylationAKYNFHGTAEQDLPF
EEECCCCCCCCCCCC		20.6028152594
43UbiquitinationLTIVAVTKDPNWYKA
EEEEEEECCCCHHHC		65.67-
49UbiquitinationTKDPNWYKAKNKVGR
ECCCCHHHCCCCCCC		44.49-
64PhosphorylationEGIIPANYVQKREGV
CCCCCHHHCCHHHCC		13.3327642862
72UbiquitinationVQKREGVKAGTKLSL
CCHHHCCCCCCCCCC		52.54-
76AcetylationEGVKAGTKLSLMPWF
HCCCCCCCCCCCCCC		34.8525953088
76UbiquitinationEGVKAGTKLSLMPWF
HCCCCCCCCCCCCCC		34.85-
78PhosphorylationVKAGTKLSLMPWFHG
CCCCCCCCCCCCCCC		24.9527461979
86UbiquitinationLMPWFHGKITREQAE
CCCCCCCCCCHHHHH		32.13-
97PhosphorylationEQAERLLYPPETGLF
HHHHHHCCCCCCEEE		22.7228064214
136PhosphorylationYRIMYHASKLSIDEE
EEEEEEHHCCCCCHH		22.3327251275
169UbiquitinationGLCTRLIKPKVMEGT
CHHHHHCCCCCCCCC		43.29-
171UbiquitinationCTRLIKPKVMEGTVA
HHHHCCCCCCCCCEE		49.57-
173SulfoxidationRLIKPKVMEGTVAAQ
HHCCCCCCCCCEECC		4.9930846556
176PhosphorylationKPKVMEGTVAAQDEF
CCCCCCCCEECCHHH		8.1524719451
184PhosphorylationVAAQDEFYRSGWALN
EECCHHHHHHCCCCC		11.2128674151
186PhosphorylationAQDEFYRSGWALNMK
CCHHHHHHCCCCCHH		27.5721552520
193UbiquitinationSGWALNMKELKLLQT
HCCCCCHHHHHHHHH		59.84-
193AcetylationSGWALNMKELKLLQT
HCCCCCHHHHHHHHH		59.8425953088
196AcetylationALNMKELKLLQTIGK
CCCHHHHHHHHHHCC		48.5225953088
196UbiquitinationALNMKELKLLQTIGK
CCCHHHHHHHHHHCC		48.5221890473
200PhosphorylationKELKLLQTIGKGEFG
HHHHHHHHHCCCCCC		31.5028060719
203UbiquitinationKLLQTIGKGEFGDVM
HHHHHHCCCCCCCEE		51.95-
210SulfoxidationKGEFGDVMLGDYRGN
CCCCCCEEEECCCCC		4.0530846556
214PhosphorylationGDVMLGDYRGNKVAV
CCEEEECCCCCEEEE		20.7223898821
218UbiquitinationLGDYRGNKVAVKCIK
EECCCCCEEEEEECC		34.10-
222AcetylationRGNKVAVKCIKNDAT
CCCEEEEEECCCCHH		22.0925953088
222UbiquitinationRGNKVAVKCIKNDAT
CCCEEEEEECCCCHH		22.09-
246PhosphorylationVMTQLRHSNLVQLLG
HHHHHHHCCHHHHHC		25.9829083192
263PhosphorylationVEEKGGLYIVTEYMA
EEECCCEEEEEEEEC		9.1626074081
266PhosphorylationKGGLYIVTEYMAKGS
CCCEEEEEEEECCCC		16.3126074081
268PhosphorylationGLYIVTEYMAKGSLV
CEEEEEEEECCCCHH		7.9426074081
273PhosphorylationTEYMAKGSLVDYLRS
EEEECCCCHHHHHHH		25.2326074081
277PhosphorylationAKGSLVDYLRSRGRS
CCCCHHHHHHHCCCC		9.1326074081
284PhosphorylationYLRSRGRSVLGGDCL
HHHHCCCCCCCCCCE		25.23-
304PhosphorylationDVCEAMEYLEGNNFV
HHHHHHHHHCCCCCC		9.2919060867
329UbiquitinationVSEDNVAKVSDFGLT
ECCCCEEEEHHCCCE		37.68-
337UbiquitinationVSDFGLTKEASSTQD
EHHCCCEECCCCCCC		57.22-
347UbiquitinationSSTQDTGKLPVKWTA
CCCCCCCCCCCCCCC		52.27-
347AcetylationSSTQDTGKLPVKWTA
CCCCCCCCCCCCCCC		52.2725953088
351UbiquitinationDTGKLPVKWTAPEAL
CCCCCCCCCCCCHHH		36.57-
351AcetylationDTGKLPVKWTAPEAL
CCCCCCCCCCCCHHH		36.5725953088
364PhosphorylationALREKKFSTKSDVWS
HHHHCCCCCHHHHHH		43.7512600271
393UbiquitinationPYPRIPLKDVVPRVE
CCCCCCHHHCCCCCC		43.02-
404UbiquitinationPRVEKGYKMDAPDGC
CCCCCCCCCCCCCCC		38.68-
411GlutathionylationKMDAPDGCPPAVYEV
CCCCCCCCCHHHHHH		4.8122555962
416PhosphorylationDGCPPAVYEVMKNCW
CCCCHHHHHHHHHCC		12.6225147952
420UbiquitinationPAVYEVMKNCWHLDA
HHHHHHHHHCCCCCH		54.88-
444UbiquitinationREQLEHIKTHELHL-
HHHHHHHHHHCCCC-		45.82-
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
364SPhosphorylationKinasePRKACAP17612
GPS
364SPhosphorylationKinasePKA-FAMILY-GPS
364SPhosphorylationKinasePKA-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
364SPhosphorylation

11181701
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
INSR_HUMANINSRphysical
10026153
IGF1R_HUMANIGF1Rphysical
10026153
FYN_HUMANFYNphysical
8262983
TGFI1_HUMANTGFB1I1physical
9858471
HNRPK_HUMANHNRNPKphysical
12052863
PHAG1_HUMANPAG1physical
10790433
SHC1_HUMANSHC1physical
12048194
FAK1_HUMANPTK2physical
7529872
PAXI_HUMANPXNphysical
7529872
PECA1_HUMANPECAM1physical
9624175
RASA1_HUMANRASA1physical
7544435
SRC_HUMANSRCphysical
7513429
JUN_HUMANJUNphysical
16740711
G3BP1_HUMANG3BP1physical
15743820
SRCN1_HUMANSRCIN1physical
17525734
ID3_HUMANID3physical
18255255
KHDR1_HUMANKHDRBS1physical
7512694
RGS16_HUMANRGS16physical
12588871
ZAP70_HUMANZAP70physical
8621646
CD3E_HUMANCD3Ephysical
8621646
CD3Z_HUMANCD247physical
8621646
PHAG1_HUMANPAG1physical
12665526
FRK_HUMANFRKphysical
23455922
TNS2_HUMANTENC1physical
23455922
AKT2_HUMANAKT2physical
26344197
CLIC4_HUMANCLIC4physical
26344197
IF4E_HUMANEIF4Ephysical
26344197
ILKAP_HUMANILKAPphysical
26344197
PDCD6_HUMANPDCD6physical
26344197
PSMD9_HUMANPSMD9physical
26344197
PDPK1_HUMANPDPK1physical
25814554
MATK_HUMANMATKphysical
28514442
FRK_HUMANFRKphysical
28514442
PHAG1_HUMANPAG1physical
28514442
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
D09950 Ponatinib (USAN/INN)
D09951 Ponatinib hydrochloride (USAN); Iclusig (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CSK_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Activation of the COOH-terminal Src kinase (Csk) by cAMP-dependentprotein kinase inhibits signaling through the T cell receptor.";
Vang T., Torgersen K.M., Sundvold V., Saxena M., Levy F.O.,Skalhegg B.S., Hansson V., Mustelin T., Tasken K.;
J. Exp. Med. 193:497-507(2001).
Cited for: PHOSPHORYLATION AT SER-364 BY PKA, AND MUTAGENESIS OF SER-364.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-184, AND MASSSPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-184, AND MASSSPECTROMETRY.
"Identification of csk tyrosine phosphorylation sites and a tyrosineresidue important for kinase domain structure.";
Joukov V., Vihinen M., Vainikka S., Sowadski J.M., Alitalo K.,Bergman M.;
Biochem. J. 322:927-935(1997).
Cited for: PHOSPHORYLATION AT TYR-184 AND TYR-304, AND MUTAGENESIS OF TYR-184 ANDTYR-304.

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