DB code: M00304

RLCP classification 3.103.130000.1162 : Transfer
CATH domain 2.30.30.40 : SH3 type barrels.
3.30.505.10 : SHC Adaptor Protein
3.30.200.20 : Phosphorylase Kinase; domain 1
1.10.510.10 : Transferase(Phosphotransferase); domain 1 Catalytic domain
E.C. 2.7.10.2
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
1.10.510.10 : Transferase(Phosphotransferase); domain 1 M00125 M00124 M00131 T00224 M00127 M00129 M00130 M00132 M00136 M00196 M00197 M00198 M00323 M00325 M00326 M00327 M00328 M00329 M00330 M00331 M00332 M00333 M00335 M00339 M00344
2.30.30.40 : SH3 type barrels. M00183 M00043 M00130 T00256 M00335
3.30.200.20 : Phosphorylase Kinase; domain 1 M00125 M00124 M00131 T00224 M00127 M00129 M00130 M00132 M00136 M00196 M00197 M00198 M00323 M00325 M00326 M00327 M00328 M00329 M00330 M00331 M00332 M00333 M00335 M00339 M00344 D00298
3.30.505.10 : SHC Adaptor Protein M00183 M00043 M00130 M00148 T00256 M00333 M00339 M00344 T00221

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P32577 Tyrosine-protein kinase CSK
EC 2.7.10.2
C-Src kinase
NP_001025210.1 (Protein)
NM_001030039.1 (DNA/RNA sequence)
PF07714 (Pkinase_Tyr)
PF00017 (SH2)
PF00018 (SH3_1)
[Graphical View]
P41241 Tyrosine-protein kinase CSK
EC 2.7.10.2
C-Src kinase
Protein-tyrosine kinase MPK-2
p50CSK
NP_031809.2 (Protein)
NM_007783.2 (DNA/RNA sequence)
PF07714 (Pkinase_Tyr)
PF00017 (SH2)
PF00018 (SH3_1)
[Graphical View]
P41240 Tyrosine-protein kinase CSK
EC 2.7.10.2
C-Src kinase
Protein-tyrosine kinase CYL
NP_001120662.1 (Protein)
NM_001127190.1 (DNA/RNA sequence)
NP_004374.1 (Protein)
NM_004383.2 (DNA/RNA sequence)
PF07714 (Pkinase_Tyr)
PF00017 (SH2)
PF00018 (SH3_1)
[Graphical View]

KEGG enzyme name
Non-specific protein-tyrosine kinase
ATP:protein-tyrosine O-phosphotransferase (ambiguous)
CSK
CYL
Cytoplasmic protein tyrosine kinase
MATK
Protein-tyrosine kinase (ambiguous)
SRC
SRC2

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P32577 CSK_RAT ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Homodimer (via SH3-domain). Interacts with PTPN8. 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 (By similarity). Cytoplasm (By similarity). Cell membrane (By similarity). Note: Mainly cytoplasmic, also present in lipid rafts (By similarity).
P41241 CSK_MOUSE ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Homodimer (via SH3-domain). Interacts with PTPN8. 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 (By similarity). Cytoplasm. Cell membrane. Note: Mainly cytoplasmic, also present in lipid rafts.
P41240 CSK_HUMAN ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. 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. Cytoplasm (By similarity). Cell membrane (By similarity). Note: Mainly cytoplasmic, also present in lipid rafts (By similarity).

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00305 C00002 C00585 C00008 C01167
E.C.
Compound Magnesium ATP [protein]-L-tyrosine ADP [protein]-L-tyrosine phosphate
Type divalent metal (Ca2+, Mg2+) amine group,nucleotide aromatic ring (only carbon atom),peptide/protein amine group,nucleotide aromatic ring (only carbon atom),peptide/protein,phosphate group/phosphate ion
ChEBI 18420
15422
16761
PubChem 888
5957
6022
1k9aA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aF01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1jegA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1cskA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1cskB00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1cskC00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1cskD00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aF02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3eacA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3eazA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aC03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aD03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aE03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aF03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1bygA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3d7tA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3d7uA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3d7uC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aB04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aC04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aD04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aE04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1k9aF04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
1bygA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3d7tA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3d7uA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound
3d7uC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [6], [34]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1k9aA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aB01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aD01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aE01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aF01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1jegA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1cskA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1cskB00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1cskC00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1cskD00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aB02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aD02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aE02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aF02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3eacA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3eazA00 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aA03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aB03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aC03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aD03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aE03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aF03 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1bygA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3d7tA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3d7uA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
3d7uC01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1k9aA04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 314;ARG 318 ASN 319;ASP 332(Magnesium binding)
1k9aB04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 314;ARG 318 ASN 319;ASP 332(Magnesium binding)
1k9aC04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 314;ARG 318 ASN 319;ASP 332(Magnesium binding)
1k9aD04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 314;ARG 318 ASN 319;ASP 332(Magnesium binding)
1k9aE04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 314;ARG 318 ASN 319;ASP 332(Magnesium binding)
1k9aF04 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 314;ARG 318 ASN 319;ASP 332(Magnesium binding)
1bygA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 314;ARG 318 ASN 319;ASP 332(Magnesium binding)
3d7tA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 314;ARG 318 ASN 319;ASP 332(Magnesium binding)
3d7uA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 314;ARG 318 ASN 319;ASP 332(Magnesium binding)
3d7uC02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ASP 314;ARG 318 ASN 319;ASP 332(Magnesium binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[6]
FIG.4
[8]
Figure 2
[34]
Figure 7, p.344-345

References
[1]
Resource
Comments FUNCTION IN PHOSPHORYLATION OF LYN AND FYN.
Medline ID
PubMed ID 1722201
Journal J Biol Chem
Year 1991
Volume 266
Pages 24249-52
Authors Okada M, Nada S, Yamanashi Y, Yamamoto T, Nakagawa H
Title CSK: a protein-tyrosine kinase involved in regulation of src family kinases.
Related PDB
Related UniProtKB
[2]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-71.
Medline ID
PubMed ID 7511113
Journal FEBS Lett
Year 1994
Volume 341
Pages 79-85
Authors Borchert TV, Mathieu M, Zeelen JP, Courtneidge SA, Wierenga RK
Title The crystal structure of human CskSH3: structural diversity near the RT-Src and n-Src loop.
Related PDB 1csk
Related UniProtKB P41240
[3]
Resource
Comments
Medline ID
PubMed ID 7527038
Journal J Biol Chem
Year 1994
Volume 269
Pages 30880-7
Authors Cole PA, Burn P, Takacs B, Walsh CT
Title Evaluation of the catalytic mechanism of recombinant human Csk (C-terminal Src kinase) using nucleotide analogs and viscosity effects.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 7518562
Journal Mol Cell Biol
Year 1994
Volume 14
Pages 5402-11
Authors Howell BW, Cooper JA
Title Csk suppression of Src involves movement of Csk to sites of Src activity.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 7513429
Journal Proc Natl Acad Sci U S A
Year 1994
Volume 91
Pages 3984-8
Authors Sabe H, Hata A, Okada M, Nakagawa H, Hanafusa H
Title Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 7673185
Journal J Biol Chem
Year 1995
Volume 270
Pages 22105-8
Authors Cole PA, Grace MR, Phillips RS, Burn P, Walsh CT
Title The role of the catalytic base in the protein tyrosine kinase Csk.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 9048573
Journal Biochemistry
Year 1997
Volume 36
Pages 1874-81
Authors Grace MR, Walsh CT, Cole PA
Title Divalent ion effects and insights into the catalytic mechanism of protein tyrosine kinase Csk.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID
Journal J Am Chem Soc
Year 1998
Volume 120
Pages 9851-8
Authors Kim K, Cole PA
Title Kinetic analysis of a protein tyrosine kinase reaction transition state in the forward and reverse directions.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 10395732
Journal Arch Biochem Biophys
Year 1999
Volume 367
Pages 167-72
Authors Sun G, Budde RJ
Title Mutations in the N-terminal regulatory region reduce the catalytic activity of Csk, but do not affect its recognition of Src.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 10460171
Journal Biochemistry
Year 1999
Volume 38
Pages 11147-55
Authors Sondhi D, Cole PA
Title Domain interactions in protein tyrosine kinase Csk.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 9878439
Journal J Mol Biol
Year 1999
Volume 285
Pages 713-25
Authors Lamers MB, Antson AA, Hubbard RE, Scott RK, Williams DH
Title Structure of the protein tyrosine kinase domain of C-terminal Src kinase (CSK) in complex with staurosporine.
Related PDB 1byg
Related UniProtKB P41240
[12]
Resource
Comments
Medline ID
PubMed ID 10918051
Journal J Biol Chem
Year 2000
Volume 275
Pages 29183-6
Authors Takeuchi S, Takayama Y, Ogawa A, Tamura K, Okada M
Title Transmembrane phosphoprotein Cbp positively regulates the activity of the carboxyl-terminal Src kinase, Csk.
Related PDB
Related UniProtKB
[13]
Resource
Comments INTERACTION WITH PAG1.
Medline ID
PubMed ID 10790433
Journal J Exp Med
Year 2000
Volume 191
Pages 1591-604
Authors Brdicka T, Pavlistova D, Leo A, Bruyns E, Korinek V, Angelisova P, Scherer J, Shevchenko A, Hilgert I, Cerny J, Drbal K, Kuramitsu Y, Kornacker B, Horejsi V, Schraven B
Title 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.
Related PDB
Related UniProtKB
[14]
Resource
Comments INTERACTION WITH PAG1.
Medline ID
PubMed ID 10801129
Journal Nature
Year 2000
Volume 404
Pages 999-1003
Authors Kawabuchi M, Satomi Y, Takao T, Shimonishi Y, Nada S, Nagai K, Tarakhovsky A, Okada M
Title Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 11551213
Journal Biochemistry
Year 2001
Volume 40
Pages 11149-55
Authors Shaffer J, Sun G, Adams JA
Title Nucleotide release and associated conformational changes regulate function in the COOH-terminal Src kinase, Csk.
Related PDB
Related UniProtKB
[16]
Resource
Comments PHOSPHORYLATION AT SER-364 BY PKA, MUTAGENESIS OF SER-364.
Medline ID
PubMed ID 11181701
Journal J Exp Med
Year 2001
Volume 193
Pages 497-507
Authors Vang T, Torgersen KM, Sundvold V, Saxena M, Levy FO, Skalhegg BS, Hansson V, Mustelin T, Tasken K
Title Activation of the COOH-terminal Src kinase (Csk) by cAMP-dependent protein kinase inhibits signaling through the T cell receptor.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 11724538
Journal J Mol Biol
Year 2001
Volume 314
Pages 129-38
Authors Shekhtman A, Ghose R, Wang D, Cole PA, Cowburn D
Title Novel mechanism of regulation of the non-receptor protein tyrosine kinase Csk: insights from NMR mapping studies and site-directed mutagenesis.
Related PDB
Related UniProtKB
[18]
Resource
Comments STRUCTURE BY NMR OF 1-83.
Medline ID
PubMed ID 11685249
Journal Nat Struct Biol
Year 2001
Volume 8
Pages 998-1004
Authors Ghose R, Shekhtman A, Goger MJ, Ji H, Cowburn D
Title A novel, specific interaction involving the Csk SH3 domain and its natural ligand.
Related PDB 1jeg
Related UniProtKB P41241
[19]
Resource
Comments
Medline ID
PubMed ID 11884384
Journal J Biol Chem
Year 2002
Volume 277
Pages 14351-4
Authors Ogawa A, Takayama Y, Sakai H, Chong KT, Takeuchi S, Nakagawa A, Nada S, Okada M, Tsukihara T
Title Structure of the carboxyl-terminal Src kinase, Csk.
Related PDB 1k9a
Related UniProtKB P32577
[20]
Resource
Comments
Medline ID
PubMed ID 12417200
Journal J Mol Biol
Year 2002
Volume 323
Pages 871-81
Authors Hamuro Y, Wong L, Shaffer J, Kim JS, Stranz DD, Jennings PA, Woods VL Jr, Adams JA
Title Phosphorylation driven motions in the COOH-terminal Src kinase, CSK, revealed through enhanced hydrogen-deuterium exchange and mass spectrometry (DXMS).
Related PDB
Related UniProtKB
[21]
Resource
Comments
Medline ID
PubMed ID 12600271
Journal Biochem J
Year 2003
Volume 372
Pages 271-8
Authors Yaqub S, Abrahamsen H, Zimmerman B, Kholod N, Torgersen KM, Mustelin T, Herberg FW, Tasken K, Vang T
Title Activation of C-terminal Src kinase (Csk) by phosphorylation at serine-364 depends on the Csk-Src homology 3 domain.
Related PDB
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 12686554
Journal J Biol Chem
Year 2003
Volume 278
Pages 24072-7
Authors Lin X, Lee S, Sun G
Title Functions of the activation loop in Csk protein-tyrosine kinase.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 15504335
Journal Biochem Biophys Res Commun
Year 2004
Volume 324
Pages 1155-64
Authors Roskoski R Jr
Title Src protein-tyrosine kinase structure and regulation.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 15312765
Journal J Mol Biol
Year 2004
Volume 341
Pages 93-106
Authors Wong L, Lieser S, Chie-Leon B, Miyashita O, Aubol B, Shaffer J, Onuchic JN, Jennings PA, Woods VL Jr, Adams JA
Title Dynamic coupling between the SH2 domain and active site of the COOH terminal Src kinase, Csk.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 15683240
Journal Biochemistry
Year 2005
Volume 44
Pages 1561-7
Authors Lin X, Ayrapetov MK, Lee S, Parang K, Sun G
Title Probing the communication between the regulatory and catalytic domains of a protein tyrosine kinase, Csk.
Related PDB
Related UniProtKB
[26]
Resource
Comments REVIEW.
Medline ID
PubMed ID 16243715
Journal Growth Factors
Year 2005
Volume 23
Pages 233-44
Authors Chong YP, Mulhern TD, Cheng HC
Title C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK)--endogenous negative regulators of Src-family protein kinases.
Related PDB
Related UniProtKB
[27]
Resource
Comments
Medline ID
PubMed ID 15623523
Journal J Biol Chem
Year 2005
Volume 280
Pages 7769-76
Authors Lieser SA, Shindler C, Aubol BE, Lee S, Sun G, Adams JA
Title Phosphoryl transfer step in the C-terminal Src kinase controls Src recognition.
Related PDB
Related UniProtKB
[28]
Resource
Comments
Medline ID
PubMed ID 16002086
Journal J Mol Biol
Year 2005
Volume 351
Pages 131-43
Authors Wong L, Lieser SA, Miyashita O, Miller M, Tasken K, Onuchic JN, Adams JA, Woods VL Jr, Jennings PA
Title Coupled motions in the SH2 and kinase domains of Csk control Src phosphorylation.
Related PDB
Related UniProtKB
[29]
Resource
Comments
Medline ID
PubMed ID 17018524
Journal J Biol Chem
Year 2006
Volume 281
Pages 38004-12
Authors Lieser SA, Shaffer J, Adams JA
Title SRC tail phosphorylation is limited by structural changes in the regulatory tyrosine kinase Csk.
Related PDB
Related UniProtKB
[30]
Resource
Comments
Medline ID
PubMed ID 16483606
Journal J Mol Biol
Year 2006
Volume 357
Pages 1263-73
Authors Lin X, Wang Y, Ahmadibeni Y, Parang K, Sun G
Title Structural basis for domain-domain communication in a protein tyrosine kinase, the C-terminal Src kinase.
Related PDB
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 17137590
Journal J Mol Biol
Year 2007
Volume 365
Pages 1460-8
Authors Mills JE, Whitford PC, Shaffer J, Onuchic JN, Adams JA, Jennings PA
Title A novel disulfide bond in the SH2 Domain of the C-terminal Src kinase controls catalytic activity.
Related PDB
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 18614016
Journal Cell
Year 2008
Volume 134
Pages 124-34
Authors Levinson NM, Seeliger MA, Cole PA, Kuriyan J
Title Structural basis for the recognition of c-Src by its inactivator Csk.
Related PDB 3d7t 3d7u
Related UniProtKB P41240
[33]
Resource
Comments
Medline ID
PubMed ID 19244618
Journal J Mol Biol
Year 2009
Volume 386
Pages 1066-77
Authors Huang K, Wang YH, Brown A, Sun G
Title Identification of N-terminal lobe motifs that determine the kinase activity of the catalytic domains and regulatory strategies of Src and Csk protein tyrosine kinases.
Related PDB
Related UniProtKB
[34]
Resource
Comments
Medline ID
PubMed ID 20476842
Journal Growth Factors
Year 2010
Volume 28
Pages 329-50
Authors Ia KK, Mills RD, Hossain MI, Chan KC, Jarasrassamee B, Jorissen RN, Cheng HC
Title Structural elements and allosteric mechanisms governing regulation and catalysis of CSK-family kinases and their inhibition of Src-family kinases.
Related PDB
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Comments
This enzyme is a nonreceptor tyrosine kinase, whose catalytic domain is homologous to that of proto-oncogene tyrosine-protein kinase ABL1 (M00130 in EzCatDB). This enzyme is composed of SH2 domain, SH3 domain and catalytic domain.
Unlike other homologous enzymes, this enzyme is not regulated by autophosphorylation of its activation loop and does not have a phosphorylation site in the C-terminus.
According to the literature, this enzyme is involved in the regulation of the Src family tyrosine kinases (SFKs), which are also homologous to this enzyme. This enzyme phosphorylate the C-terminal tail of SFKs, which could repress the activity of those enzymes. Src is one of SFKs.

Created Updated
2012-05-22 2013-01-28