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P41240 (CSK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein kinase CSK

EC=2.7.10.2
Alternative name(s):
C-Src kinase
Protein-tyrosine kinase CYL
Gene names
Name:CSK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length450 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.10

Catalytic activity

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

Subunit structure

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. Ref.12 Ref.13 Ref.14 Ref.16 Ref.18 Ref.20 Ref.22 Ref.23

Subcellular location

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

Tissue specificity

Expressed in lung and macrophages. Ref.3

Domain

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.

Post-translational modification

Phosphorylated at Ser-364 by PKA, leading to increased activity. Autophosphorylated. Ref.9 Ref.11 Ref.15

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. CSK subfamily.

Contains 1 protein kinase domain.

Contains 1 SH2 domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Biological processAdaptive immunity
Immunity
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityPolymorphism
   DomainSH2 domain
SH3 domain
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
Tyrosine-protein kinase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell costimulation

Traceable author statement. Source: Reactome

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

adherens junction organization

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

brain development

Inferred from electronic annotation. Source: Ensembl

cellular response to peptide hormone stimulus

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

negative regulation of ERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

negative regulation of Golgi to plasma membrane protein transport

Inferred from direct assay PubMed 20605918. Source: UniProtKB

negative regulation of bone resorption

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of interleukin-6 production

Inferred from electronic annotation. Source: Ensembl

negative regulation of kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of low-density lipoprotein particle clearance

Inferred from electronic annotation. Source: Ensembl

negative regulation of phagocytosis

Inferred from electronic annotation. Source: Ensembl

oligodendrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Traceable author statement Ref.1. Source: GOC

platelet activation

Traceable author statement. Source: Reactome

positive regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Traceable author statement Ref.1. Source: ProtInc

regulation of Fc receptor mediated stimulatory signaling pathway

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell-cell junction

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Traceable author statement PubMed 8890164. Source: HGNC

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

membrane raft

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from physical interaction Ref.13. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

identical protein binding

Inferred from physical interaction Ref.20. Source: IntAct

non-membrane spanning protein tyrosine kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein C-terminus binding

Traceable author statement PubMed 8890164. Source: ProtInc

protein tyrosine kinase activity

Traceable author statement. Source: Reactome

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.19
Chain2 – 450449Tyrosine-protein kinase CSK
PRO_0000088070

Regions

Domain9 – 7062SH3
Domain82 – 17190SH2
Domain195 – 449255Protein kinase
Nucleotide binding201 – 2099ATP By similarity
Region9 – 7062Interaction with PTPN8 By similarity

Sites

Active site3141Proton acceptor By similarity
Binding site2221ATP By similarity

Amino acid modifications

Modified residue21N-acetylserine Ref.19
Modified residue1841Phosphotyrosine Ref.11
Modified residue3041Phosphotyrosine Ref.11
Modified residue3641Phosphoserine; by PKA Ref.15
Modified residue4161Phosphotyrosine

Natural variations

Natural variant451P → L. Ref.25
VAR_041678
Natural variant2871G → D. Ref.6
Corresponds to variant rs34866753 [ dbSNP | Ensembl ].
VAR_025203
Natural variant3981R → Q. Ref.6
Corresponds to variant rs34616395 [ dbSNP | Ensembl ].
VAR_025204
Natural variant4421H → R. Ref.6
Corresponds to variant rs35556162 [ dbSNP | Ensembl ].
VAR_025205

Experimental info

Mutagenesis1841Y → F: Abolishes phosphorylation. Ref.11
Mutagenesis3041Y → F: Decreases activity by two-thirds and alters conformation. Ref.11
Mutagenesis3641S → A: Strong decrease of phosphorylation by PRKACA (catalytic subunit of PKA). Ref.15

Secondary structure

........................................................................ 450
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P41240 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 431023A88C54E00C

FASTA45050,704
        10         20         30         40         50         60 
MSAIQAAWPS GTECIAKYNF HGTAEQDLPF CKGDVLTIVA VTKDPNWYKA KNKVGREGII 

        70         80         90        100        110        120 
PANYVQKREG VKAGTKLSLM PWFHGKITRE QAERLLYPPE TGLFLVREST NYPGDYTLCV 

       130        140        150        160        170        180 
SCDGKVEHYR IMYHASKLSI DEEVYFENLM QLVEHYTSDA DGLCTRLIKP KVMEGTVAAQ 

       190        200        210        220        230        240 
DEFYRSGWAL NMKELKLLQT IGKGEFGDVM LGDYRGNKVA VKCIKNDATA QAFLAEASVM 

       250        260        270        280        290        300 
TQLRHSNLVQ LLGVIVEEKG GLYIVTEYMA KGSLVDYLRS RGRSVLGGDC LLKFSLDVCE 

       310        320        330        340        350        360 
AMEYLEGNNF VHRDLAARNV LVSEDNVAKV SDFGLTKEAS STQDTGKLPV KWTAPEALRE 

       370        380        390        400        410        420 
KKFSTKSDVW SFGILLWEIY SFGRVPYPRI PLKDVVPRVE KGYKMDAPDG CPPAVYEVMK 

       430        440        450 
NCWHLDAAMR PSFLQLREQL EHIKTHELHL 

« Hide

References

« Hide 'large scale' references
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJH0559.
RefSeqNP_001120662.1. NM_001127190.1.
NP_004374.1. NM_004383.2.
XP_005254222.1. XM_005254165.2.
UniGeneHs.77793.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BYGX-ray2.40A177-450[»]
1CSKX-ray2.50A/B/C/D1-71[»]
3D7TX-ray2.90A188-450[»]
3D7UX-ray4.11A/C188-450[»]
3EACX-ray1.37A73-178[»]
3EAZX-ray1.31A73-178[»]
ProteinModelPortalP41240.
SMRP41240. Positions 4-450.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107832. 106 interactions.
IntActP41240. 32 interactions.
MINTMINT-85878.
STRING9606.ENSP00000220003.

Chemistry

BindingDBP41240.
ChEMBLCHEMBL2634.
GuidetoPHARMACOLOGY1994.

PTM databases

PhosphoSiteP41240.

Polymorphism databases

DMDM729887.

2D gel databases

OGPP41240.

Proteomic databases

PaxDbP41240.
PRIDEP41240.

Protocols and materials databases

DNASU1445.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000220003; ENSP00000220003; ENSG00000103653.
ENST00000309470; ENSP00000438808; ENSG00000103653.
ENST00000439220; ENSP00000414764; ENSG00000103653.
ENST00000567571; ENSP00000454906; ENSG00000103653.
GeneID1445.
KEGGhsa:1445.
UCSCuc002ays.2. human.

Organism-specific databases

CTD1445.
GeneCardsGC15P075075.
HGNCHGNC:2444. CSK.
HPACAB011203.
HPA026488.
HPA028425.
MIM124095. gene.
neXtProtNX_P41240.
PharmGKBPA26946.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233858.
HOVERGENHBG008761.
InParanoidP41240.
KOK05728.
OMAERLLCPP.
OrthoDBEOG7SV0V5.
PhylomeDBP41240.
TreeFamTF351634.

Enzyme and pathway databases

BRENDA2.7.10.2. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP41240.

Gene expression databases

ArrayExpressP41240.
BgeeP41240.
CleanExHS_CSK.
GenevestigatorP41240.

Family and domain databases

Gene3D3.30.505.10. 1 hit.
InterProIPR011009. 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]
PfamPF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
PRINTSPR00401. SH2DOMAIN.
PR00109. TYRKINASE.
SMARTSM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS00107. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP41240.
GeneWikiC-src_tyrosine_kinase.
GenomeRNAi1445.
NextBio5937.
PROP41240.
SOURCESearch...

Entry information

Entry nameCSK_HUMAN
AccessionPrimary (citable) accession number: P41240
Secondary accession number(s): Q2M3N2, Q6FGZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 164 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM