P41240 (CSK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein kinase CSK
EC=2.7.10.2

Alternative name(s):
C-Src kinase
Protein-tyrosine kinase CYL

Gene names

Name:

CSK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	450 AA.
Sequence status	Complete.
Protein existence	Evidence 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.21 Ref.22
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 process	Adaptive immunity Immunity
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Polymorphism
Domain	SH2 domain SH3 domain
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase Tyrosine-protein kinase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T 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: Compara brain development Inferred from electronic annotation. Source: Compara cellular response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara epidermal growth factor receptor signaling pathway Traceable author statement. Source: Reactome negative regulation of ERK1 and ERK2 cascade Inferred from electronic annotation. Source: Compara 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: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of interleukin-6 production Inferred from electronic annotation. Source: Compara negative regulation of kinase activity Inferred from electronic annotation. Source: Compara negative regulation of low-density lipoprotein particle clearance Inferred from electronic annotation. Source: Compara negative regulation of phagocytosis Inferred from electronic annotation. Source: Compara oligodendrocyte differentiation Inferred from electronic annotation. Source: Compara platelet activation Traceable author statement. Source: Reactome positive regulation of MAP kinase activity Inferred from electronic annotation. Source: Compara protein autophosphorylation Inferred from electronic annotation. Source: Compara regulation of Fc receptor mediated stimulatory signaling pathway Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA cell-cell junction Inferred from electronic annotation. Source: Compara centrosome Inferred from direct assay. Source: HPA cytosol Traceable author statement. Source: Reactome membrane raft Inferred from electronic annotation. Source: Compara plasma membrane Inferred from physical interaction Ref.13. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW non-membrane spanning protein tyrosine kinase activity Inferred from electronic annotation. Source: 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

With	Entry	#Exp.	IntAct	Notes
SRC	P00523	6	EBI-1380630,EBI-848039	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 450

450

Tyrosine-protein kinase CSK

PRO_0000088070

Regions

Domain

9 – 70

62

SH3

Domain

82 – 171

90

SH2

Domain

195 – 449

255

Protein kinase

Nucleotide binding

201 – 209

9

ATP By similarity

Region

9 – 70

62

Interaction with PTPN8 By similarity

Sites

Active site

314

1

Proton acceptor By similarity

Binding site

222

1

ATP By similarity

Amino acid modifications

Modified residue

184

1

Phosphotyrosine Ref.11

Modified residue

304

1

Phosphotyrosine Ref.11

Modified residue

364

1

Phosphoserine; by PKA Ref.15

Modified residue

416

1

Phosphotyrosine

Natural variations

Natural variant

45

1

P → L. Ref.24

VAR_041678

Natural variant

287

1

G → D. Ref.6
Corresponds to variant rs34866753 [ dbSNP | Ensembl ].

VAR_025203

Natural variant

398

1

R → Q. Ref.6
Corresponds to variant rs34616395 [ dbSNP | Ensembl ].

VAR_025204

Natural variant

442

1

H → R. Ref.6
Corresponds to variant rs35556162 [ dbSNP | Ensembl ].

VAR_025205

Experimental info

Mutagenesis

184

1

Y → F: Abolishes phosphorylation. Ref.11

Mutagenesis

304

1

Y → F: Decreases activity by two-thirds and alters conformation. Ref.11

Mutagenesis

364

1

S → A: Strong decrease of phosphorylation by PRKACA (catalytic subunit of PKA). Ref.15

Secondary structure

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450

Helix Strand Turn

Details...

Beta strand

12 – 18

7

Beta strand

35 – 41

7

Beta strand

47 – 51

5

Beta strand

57 – 61

5

Beta strand

64 – 66

3

Helix

77 – 79

3

Beta strand

83 – 86

4

Helix

89 – 95

7

Beta strand

103 – 108

6

Beta strand

116 – 122

7

Beta strand

125 – 130

6

Beta strand

132 – 134

3

Beta strand

137 – 144

8

Beta strand

146 – 148

3

Helix

149 – 158

10

Beta strand

163 – 165

3

Helix

192 – 194

3

Beta strand

195 – 203

9

Beta strand

208 – 214

7

Beta strand

217 – 223

7

Helix

231 – 235

5

Helix

237 – 240

4

Beta strand

251 – 255

5

Beta strand

263 – 266

4

Helix

274 – 285

12

Helix

288 – 307

20

Helix

317 – 319

3

Beta strand

320 – 322

3

Beta strand

328 – 330

3

Turn

350 – 352

3

Helix

355 – 360

6

Helix

365 – 380

16

Helix

392 – 394

3

Helix

395 – 399

5

Turn

400 – 402

3

Helix

413 – 422

10

Helix

427 – 429

3

Helix

433 – 446

14

Sequences

	Sequence		Length	Mass (Da)
	P41240 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 431023A88C54E00C	FASTA	450	50,704
	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

References

	« Hide 'large scale' referencesShow '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]	"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: HOMODIMER.
[20]	"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].
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

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.

IPI

IPI00013212.

PIR

JH0559.

RefSeq

NP_001120662.1. NM_001127190.1.
NP_004374.1. NM_004383.2.

UniGene

Hs.77793.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BYG	X-ray	2.40	A	177-450	[»]
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	[»]

ProteinModelPortal

P41240.

ModBase

Search...

Protein-protein interaction databases

IntAct

P41240. 20 interactions.

MINT

MINT-85878.

STRING

9606.ENSP00000220003.

PTM databases

PhosphoSite

P41240.

Polymorphism databases

DMDM

729887.

2D gel databases

OGP

P41240.

Proteomic databases

PaxDb

P41240.

PRIDE

P41240.

Protocols and materials databases

DNASU

1445.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000220003; ENSP00000220003; ENSG00000103653.
ENST00000309470; ENSP00000438808; ENSG00000103653.
ENST00000439220; ENSP00000414764; ENSG00000103653.
ENST00000567571; ENSP00000454906; ENSG00000103653.

GeneID

1445.

KEGG

hsa:1445.

UCSC

uc002ays.2. human.

Organism-specific databases

CTD

1445.

GeneCards

GC15P075075.

HGNC

HGNC:2444. CSK.

HPA

CAB011203.
HPA026488.
HPA028425.

MIM

124095. gene.

neXtProt

NX_P41240.

PharmGKB

PA26946.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000233858.

HOVERGEN

HBG008761.

InParanoid

P41240.

KO

K05728.

OMA

QDEFFRS.

OrthoDB

EOG44BB23.

PhylomeDB

P41240.

Enzyme and pathway databases

BRENDA

2.7.10.2. 2681.

Pathway_Interaction_DB

bcr_5pathway. BCR signaling pathway.
pdgfrbpathway. PDGFR-beta signaling pathway.
ptp1bpathway. Signaling events mediated by PTP1B.
tcrpathway. TCR signaling in naive CD4+ T cells.
cd8tcrpathway. TCR signaling in naive CD8+ T cells.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_604. Hemostasis.
REACT_6900. Immune System.

SignaLink

P41240.

Gene expression databases

ArrayExpress

P41240.

Bgee

P41240.

CleanEx

HS_CSK.

Genevestigator

P41240.

GermOnline

ENSG00000103653. Homo sapiens.

Family and domain databases

Gene3D

3.30.505.10. 1 hit.

InterPro

IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_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]

Pfam

PF07714. Pkinase_Tyr. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.
PR00109. TYRKINASE.

SMART

SM00252. SH2. 1 hit.
SM00326. SH3. 1 hit.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.
SSF50044. SH3. 1 hit.

PROSITE

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]

ProtoNet

Search...

Other

BindingDB

P41240.

ChEMBL

CHEMBL2634.

EvolutionaryTrace

P41240.

GenomeRNAi

1445.

NextBio

5937.

SOURCE

Search...

Entry information

Entry name

CSK_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 154 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.