Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P41240

- CSK_HUMAN

UniProt

P41240 - CSK_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Tyrosine-protein kinase CSK

Gene

CSK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei222 – 2221ATPPROSITE-ProRule annotation
Active sitei314 – 3141Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi201 – 2099ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. non-membrane spanning protein tyrosine kinase activity Source: UniProtKB-EC
  4. protein C-terminus binding Source: ProtInc
  5. protein tyrosine kinase activity Source: Reactome

GO - Biological processi

  1. adherens junction organization Source: Ensembl
  2. blood coagulation Source: Reactome
  3. brain development Source: Ensembl
  4. cellular response to peptide hormone stimulus Source: Ensembl
  5. epidermal growth factor receptor signaling pathway Source: Reactome
  6. negative regulation of bone resorption Source: Ensembl
  7. negative regulation of cell proliferation Source: Ensembl
  8. negative regulation of ERK1 and ERK2 cascade Source: Ensembl
  9. negative regulation of Golgi to plasma membrane protein transport Source: UniProtKB
  10. negative regulation of interleukin-6 production Source: Ensembl
  11. negative regulation of kinase activity Source: Ensembl
  12. negative regulation of low-density lipoprotein particle clearance Source: Ensembl
  13. negative regulation of phagocytosis Source: Ensembl
  14. oligodendrocyte differentiation Source: Ensembl
  15. peptidyl-tyrosine phosphorylation Source: GOC
  16. platelet activation Source: Reactome
  17. positive regulation of MAP kinase activity Source: Ensembl
  18. protein autophosphorylation Source: Ensembl
  19. protein phosphorylation Source: ProtInc
  20. regulation of Fc receptor mediated stimulatory signaling pathway Source: Ensembl
  21. T cell costimulation Source: Reactome
  22. T cell receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Adaptive immunity, Immunity

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.2. 2681.
ReactomeiREACT_12578. GAB1 signalosome.
REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_19324. PD-1 signaling.
SignaLinkiP41240.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein kinase CSK (EC:2.7.10.2)
Alternative name(s):
C-Src kinase
Protein-tyrosine kinase CYL
Gene namesi
Name:CSK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:2444. CSK.

Subcellular locationi

Cytoplasm By similarity. Cell membrane By similarity
Note: Mainly cytoplasmic, also present in lipid rafts.By similarity

GO - Cellular componenti

  1. cell-cell junction Source: Ensembl
  2. cytoplasm Source: HGNC
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. membrane raft Source: Ensembl
  6. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi184 – 1841Y → F: Abolishes phosphorylation. 1 Publication
Mutagenesisi304 – 3041Y → F: Decreases activity by two-thirds and alters conformation. 1 Publication
Mutagenesisi364 – 3641S → A: Strong decrease of phosphorylation by PRKACA (catalytic subunit of PKA). 1 Publication

Organism-specific databases

PharmGKBiPA26946.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 450449Tyrosine-protein kinase CSKPRO_0000088070Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei184 – 1841Phosphotyrosine1 Publication
Modified residuei304 – 3041Phosphotyrosine1 Publication
Modified residuei364 – 3641Phosphoserine; by PKA1 Publication
Modified residuei416 – 4161Phosphotyrosine

Post-translational modificationi

Phosphorylated at Ser-364 by PKA, leading to increased activity. Autophosphorylated.2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP41240.
PaxDbiP41240.
PRIDEiP41240.

2D gel databases

OGPiP41240.

PTM databases

PhosphoSiteiP41240.

Expressioni

Tissue specificityi

Expressed in lung and macrophages.1 Publication

Gene expression databases

BgeeiP41240.
CleanExiHS_CSK.
ExpressionAtlasiP41240. baseline and differential.
GenevestigatoriP41240.

Organism-specific databases

HPAiCAB011203.
HPA026488.
HPA028425.

Interactioni

Subunit structurei

Homodimer (via SH3-domain). Interacts with PTPN8 By similarity. Interacts with phosphorylated SIT1, PAG1, LIME1 and TGFB1I1; these interactions serve to recruit CSK to the membrane where it can phosphorylate and inhibit Src-family kinases. Interacts with SRCIN1. Interacts with RHOH. Interacts (via SH2 domain) with SCIMP.By similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-1380630,EBI-1380630
IGF1RP080695EBI-1380630,EBI-475981
PTPRCP085753EBI-1380630,EBI-1341
PXNP490232EBI-1380630,EBI-702209
SRCP005236EBI-1380630,EBI-848039From a different organism.

Protein-protein interaction databases

BioGridi107832. 47 interactions.
IntActiP41240. 33 interactions.
MINTiMINT-85878.
STRINGi9606.ENSP00000220003.

Structurei

Secondary structure

1
450
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 187
Beta strandi35 – 417
Beta strandi47 – 515
Beta strandi57 – 615
Beta strandi64 – 663
Helixi77 – 793
Beta strandi83 – 864
Helixi89 – 957
Beta strandi103 – 1086
Beta strandi116 – 1227
Beta strandi125 – 1306
Beta strandi132 – 1343
Beta strandi137 – 1448
Beta strandi146 – 1483
Helixi149 – 15810
Beta strandi163 – 1653
Helixi192 – 1943
Beta strandi195 – 2039
Beta strandi208 – 2147
Beta strandi217 – 2237
Helixi231 – 2355
Helixi237 – 2404
Beta strandi251 – 2555
Beta strandi263 – 2664
Helixi274 – 28512
Helixi288 – 30720
Helixi317 – 3193
Beta strandi320 – 3223
Beta strandi328 – 3303
Turni350 – 3523
Helixi355 – 3606
Helixi365 – 38016
Helixi392 – 3943
Helixi395 – 3995
Turni400 – 4023
Helixi413 – 42210
Helixi427 – 4293
Helixi433 – 44614

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BYGX-ray2.40A173-450[»]
1CSKX-ray2.50A/B/C/D1-71[»]
3D7TX-ray2.90A188-450[»]
3D7UX-ray4.11A/C188-450[»]
3EACX-ray1.37A73-178[»]
3EAZX-ray1.31A73-178[»]
ProteinModelPortaliP41240.
SMRiP41240. Positions 4-450.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP41240.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 7062SH3PROSITE-ProRule annotationAdd
BLAST
Domaini82 – 17190SH2PROSITE-ProRule annotationAdd
BLAST
Domaini195 – 449255Protein kinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni9 – 7062Interaction with PTPN8By similarityAdd
BLAST

Domaini

The architecture of this protein is similar to that of Src-family kinases (SFKs) with one N-terminal SH3 domain, one SH2 domain, and a C-terminal kinase domain.

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSK subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 1 SH3 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain, SH3 domain

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000119011.
HOGENOMiHOG000233858.
HOVERGENiHBG008761.
InParanoidiP41240.
KOiK05728.
OMAiERLLCPP.
OrthoDBiEOG7SV0V5.
PhylomeDBiP41240.
TreeFamiTF351634.

Family and domain databases

Gene3Di3.30.505.10. 1 hit.
InterProiIPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PfamiPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTiSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P41240-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSAIQAAWPS GTECIAKYNF HGTAEQDLPF CKGDVLTIVA VTKDPNWYKA
60 70 80 90 100
KNKVGREGII PANYVQKREG VKAGTKLSLM PWFHGKITRE QAERLLYPPE
110 120 130 140 150
TGLFLVREST NYPGDYTLCV SCDGKVEHYR IMYHASKLSI DEEVYFENLM
160 170 180 190 200
QLVEHYTSDA DGLCTRLIKP KVMEGTVAAQ DEFYRSGWAL NMKELKLLQT
210 220 230 240 250
IGKGEFGDVM LGDYRGNKVA VKCIKNDATA QAFLAEASVM TQLRHSNLVQ
260 270 280 290 300
LLGVIVEEKG GLYIVTEYMA KGSLVDYLRS RGRSVLGGDC LLKFSLDVCE
310 320 330 340 350
AMEYLEGNNF VHRDLAARNV LVSEDNVAKV SDFGLTKEAS STQDTGKLPV
360 370 380 390 400
KWTAPEALRE KKFSTKSDVW SFGILLWEIY SFGRVPYPRI PLKDVVPRVE
410 420 430 440 450
KGYKMDAPDG CPPAVYEVMK NCWHLDAAMR PSFLQLREQL EHIKTHELHL
Length:450
Mass (Da):50,704
Last modified:February 1, 1995 - v1
Checksum:i431023A88C54E00C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti45 – 451P → L.1 Publication
VAR_041678
Natural varianti287 – 2871G → D.1 Publication
Corresponds to variant rs34866753 [ dbSNP | Ensembl ].
VAR_025203
Natural varianti398 – 3981R → Q.1 Publication
Corresponds to variant rs34616395 [ dbSNP | Ensembl ].
VAR_025204
Natural varianti442 – 4421H → R.1 Publication
Corresponds to variant rs35556162 [ dbSNP | Ensembl ].
VAR_025205

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X60114 mRNA. Translation: CAA42713.1.
X59932 mRNA. Translation: CAA42556.1.
X74765 Genomic DNA. Translation: CAB58562.1.
CR541960 mRNA. Translation: CAG46758.1.
DQ075211 Genomic DNA. Translation: AAY57329.1.
BC104847 mRNA. Translation: AAI04848.1.
BC104875 mRNA. Translation: AAI04876.1.
BC106073 mRNA. Translation: AAI06074.1.
CCDSiCCDS10269.1.
PIRiJH0559.
RefSeqiNP_001120662.1. NM_001127190.1.
NP_004374.1. NM_004383.2.
XP_005254222.1. XM_005254165.2.
UniGeneiHs.77793.

Genome annotation databases

EnsembliENST00000220003; ENSP00000220003; ENSG00000103653.
ENST00000439220; ENSP00000414764; ENSG00000103653.
ENST00000567571; ENSP00000454906; ENSG00000103653.
GeneIDi1445.
KEGGihsa:1445.
UCSCiuc002ays.2. human.

Polymorphism databases

DMDMi729887.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X60114 mRNA. Translation: CAA42713.1 .
X59932 mRNA. Translation: CAA42556.1 .
X74765 Genomic DNA. Translation: CAB58562.1 .
CR541960 mRNA. Translation: CAG46758.1 .
DQ075211 Genomic DNA. Translation: AAY57329.1 .
BC104847 mRNA. Translation: AAI04848.1 .
BC104875 mRNA. Translation: AAI04876.1 .
BC106073 mRNA. Translation: AAI06074.1 .
CCDSi CCDS10269.1.
PIRi JH0559.
RefSeqi NP_001120662.1. NM_001127190.1.
NP_004374.1. NM_004383.2.
XP_005254222.1. XM_005254165.2.
UniGenei Hs.77793.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BYG X-ray 2.40 A 173-450 [» ]
1CSK X-ray 2.50 A/B/C/D 1-71 [» ]
3D7T X-ray 2.90 A 188-450 [» ]
3D7U X-ray 4.11 A/C 188-450 [» ]
3EAC X-ray 1.37 A 73-178 [» ]
3EAZ X-ray 1.31 A 73-178 [» ]
ProteinModelPortali P41240.
SMRi P41240. Positions 4-450.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107832. 47 interactions.
IntActi P41240. 33 interactions.
MINTi MINT-85878.
STRINGi 9606.ENSP00000220003.

Chemistry

BindingDBi P41240.
ChEMBLi CHEMBL2634.
GuidetoPHARMACOLOGYi 1994.

PTM databases

PhosphoSitei P41240.

Polymorphism databases

DMDMi 729887.

2D gel databases

OGPi P41240.

Proteomic databases

MaxQBi P41240.
PaxDbi P41240.
PRIDEi P41240.

Protocols and materials databases

DNASUi 1445.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000220003 ; ENSP00000220003 ; ENSG00000103653 .
ENST00000439220 ; ENSP00000414764 ; ENSG00000103653 .
ENST00000567571 ; ENSP00000454906 ; ENSG00000103653 .
GeneIDi 1445.
KEGGi hsa:1445.
UCSCi uc002ays.2. human.

Organism-specific databases

CTDi 1445.
GeneCardsi GC15P075075.
HGNCi HGNC:2444. CSK.
HPAi CAB011203.
HPA026488.
HPA028425.
MIMi 124095. gene.
neXtProti NX_P41240.
PharmGKBi PA26946.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000119011.
HOGENOMi HOG000233858.
HOVERGENi HBG008761.
InParanoidi P41240.
KOi K05728.
OMAi ERLLCPP.
OrthoDBi EOG7SV0V5.
PhylomeDBi P41240.
TreeFami TF351634.

Enzyme and pathway databases

BRENDAi 2.7.10.2. 2681.
Reactomei REACT_12578. GAB1 signalosome.
REACT_12582. Phosphorylation of CD3 and TCR zeta chains.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_19324. PD-1 signaling.
SignaLinki P41240.

Miscellaneous databases

EvolutionaryTracei P41240.
GeneWikii C-src_tyrosine_kinase.
GenomeRNAii 1445.
NextBioi 5937.
PROi P41240.
SOURCEi Search...

Gene expression databases

Bgeei P41240.
CleanExi HS_CSK.
ExpressionAtlasi P41240. baseline and differential.
Genevestigatori P41240.

Family and domain databases

Gene3Di 3.30.505.10. 1 hit.
InterProi IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view ]
Pfami PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTi SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "CYL encodes a putative cytoplasmic tyrosine kinase lacking the conserved tyrosine autophosphorylation site (Y416src)."
    Partanen J., Armstrong E., Bergman M., Maekelae T.P., Hirvonen H., Huebner K., Alitalo K.
    Oncogene 6:2013-2018(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Two additional protein-tyrosine kinases expressed in human lung: fourth member of the fibroblast growth factor receptor family and an intracellular protein-tyrosine kinase."
    Braeuninger A., Holtrich U., Strebhardt K., Ruebsamen-Waigmann H.
    Proc. Natl. Acad. Sci. U.S.A. 88:10411-10415(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  3. "Isolation and characterization of a human gene that encodes a new subclass of protein tyrosine kinases."
    Brauninger A., Holtrich U., Strebhardt K., Rubsamen-Waigmann H.
    Gene 110:205-211(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
  4. "Characterization of the human CSK locus."
    Braeuninger A., Karn T., Strebhardt K., Ruebsamen-Waigmann H.
    Oncogene 8:1365-1369(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. NIEHS SNPs program
    Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASP-287; GLN-398 AND ARG-442.
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain and Uterus.
  8. "The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and down regulates its catalytic activity."
    Bergman M., Mustelin T., Oetken C., Partanen J., Flint N.A., Amrein K.E., Autero M., Burn P., Alitalo K.
    EMBO J. 11:2919-2924(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF LCK.
  9. "Recombinant Csk expressed in Escherichia coli is autophosphorylated on tyrosine residue(s)."
    Bougeret C., Rothhut B., Jullien P., Fischer S., Benarous R.
    Oncogene 8:1241-1247(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: AUTOPHOSPHORYLATION.
  10. "Expression, purification, and initial characterization of human Yes protein tyrosine kinase from a bacterial expression system."
    Sun G., Budde R.J.
    Arch. Biochem. Biophys. 345:135-142(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF YES1.
  11. "Identification of csk tyrosine phosphorylation sites and a tyrosine residue important for kinase domain structure."
    Joukov V., Vihinen M., Vainikka S., Sowadski J.M., Alitalo K., Bergman M.
    Biochem. J. 322:927-935(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-184 AND TYR-304, MUTAGENESIS OF TYR-184 AND TYR-304.
  12. "Phosphorylation of Hic-5 at tyrosine 60 by CAKbeta and Fyn."
    Ishino M., Aoto H., Sasaski H., Suzuki R., Sasaki T.
    FEBS Lett. 474:179-183(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TGFB1I1.
  13. "Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation."
    Brdicka T., Pavlistova D., Bruyns E., Leo A., Korinek V., Angelisova P., Scherer J., Shevchenko A., Shevchenko A., Hilgert I., Cerny J., Drbal K., Kuramitsu Y., Horejsi V., Schraven B.
    J. Exp. Med. 191:1591-1604(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PAG1.
  14. "Structural and functional dissection of the cytoplasmic domain of the transmembrane adaptor protein SIT (SHP2-interacting transmembrane adaptor protein)."
    Pfrepper K.-I., Marie-Cardine A., Simeoni L., Kuramitsu Y., Leo A., Spicka J., Hilgert I., Scherer J., Schraven B.
    Eur. J. Immunol. 31:1825-1836(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIT1.
  15. "Activation of the COOH-terminal Src kinase (Csk) by cAMP-dependent protein 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) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-364 BY PKA, MUTAGENESIS OF SER-364.
  16. "LIME: a new membrane raft-associated adaptor protein involved in CD4 and CD8 coreceptor signaling."
    Brdickova N., Brdicka T., Angelisova P., Horvath O., Spicka J., Hilgert I., Paces J., Simeoni L., Kliche S., Merten C., Schraven B., Horejsi V.
    J. Exp. Med. 198:1453-1462(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LIME1.
  17. "C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK)--endogenous negative regulators of Src-family protein kinases."
    Chong Y.P., Mulhern T.D., Cheng H.C.
    Growth Factors 23:233-244(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  18. "p140Cap protein suppresses tumour cell properties, regulating Csk and Src kinase activity."
    Di Stefano P., Damiano L., Cabodi S., Aramu S., Tordella L., Praduroux A., Piva R., Cavallo F., Forni G., Silengo L., Tarone G., Turco E., Defilippi P.
    EMBO J. 26:2843-2855(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SRCIN1.
  19. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  20. "The tyrosine kinase Csk dimerizes through Its SH3 domain."
    Levinson N.M., Visperas P.R., Kuriyan J.
    PLoS ONE 4:E7683-E7683(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "RhoH modulates pre-TCR and TCR signalling by regulating LCK."
    Wang H., Zeng X., Fan Z., Lim B.
    Cell. Signal. 23:249-258(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RHOH.
  23. "SCIMP, a transmembrane adapter protein involved in major histocompatibility complex class II signaling."
    Draber P., Vonkova I., Stepanek O., Hrdinka M., Kucova M., Skopcova T., Otahal P., Angelisova P., Horejsi V., Yeung M., Weiss A., Brdicka T.
    Mol. Cell. Biol. 31:4550-4562(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SCIMP.
  24. "The crystal structure of human CskSH3: structural diversity near the RT-Src and n-Src loop."
    Borchert T.V., Mathieu M., Zeelen J.P., Courtneidge S.A., Wierenga R.K.
    FEBS Lett. 341:79-85(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-71.
  25. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-45.

Entry informationi

Entry nameiCSK_HUMAN
AccessioniPrimary (citable) accession number: P41240
Secondary accession number(s): Q2M3N2, Q6FGZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: October 29, 2014
This is version 170 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3