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 18420 |
15422 15422 |
16761 16761 |
||||||||
PubChem |
888 888 |
5957 5957 |
6022 6022 |
||||||||
1k9aA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aB01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aC01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aD01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aE01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aF01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1jegA00 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1cskA00 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1cskB00 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1cskC00 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1cskD00 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aA02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aB02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aC02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aD02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aE02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aF02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3eacA00 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3eazA00 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aA03 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aB03 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aC03 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aD03 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aE03 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aF03 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1bygA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3d7tA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3d7uA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3d7uC01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aA04 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aB04 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aC04 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aD04 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aE04 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1k9aF04 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1bygA02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3d7tA02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3d7uA02 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
3d7uC02 | 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 | ||||||||||
1k9aB01 | ||||||||||
1k9aC01 | ||||||||||
1k9aD01 | ||||||||||
1k9aE01 | ||||||||||
1k9aF01 | ||||||||||
1jegA00 | ||||||||||
1cskA00 | ||||||||||
1cskB00 | ||||||||||
1cskC00 | ||||||||||
1cskD00 | ||||||||||
1k9aA02 | ||||||||||
1k9aB02 | ||||||||||
1k9aC02 | ||||||||||
1k9aD02 | ||||||||||
1k9aE02 | ||||||||||
1k9aF02 | ||||||||||
3eacA00 | ||||||||||
3eazA00 | ||||||||||
1k9aA03 | ||||||||||
1k9aB03 | ||||||||||
1k9aC03 | ||||||||||
1k9aD03 | ||||||||||
1k9aE03 | ||||||||||
1k9aF03 | ||||||||||
1bygA01 | ||||||||||
3d7tA01 | ||||||||||
3d7uA01 | ||||||||||
3d7uC01 | ||||||||||
1k9aA04 | ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | ||||||||
1k9aB04 | ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | ||||||||
1k9aC04 | ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | ||||||||
1k9aD04 | ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | ||||||||
1k9aE04 | ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | ||||||||
1k9aF04 | ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | ||||||||
1bygA02 | ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | ||||||||
3d7tA02 | ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | ||||||||
3d7uA02 | ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | ||||||||
3d7uC02 | 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, |
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, |
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), |
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, |
Related PDB | |
Related UniProtKB | |
[16] | |
Resource | |
Comments |
PHOSPHORYLATION AT SER-364 BY PKA, |
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, |
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, |
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, |
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, |
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, |
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, |
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 | |
Related UniProtKB |
Comments |
---|
This enzyme is a nonreceptor tyrosine kinase, Unlike other homologous enzymes, According to the literature, |
Created | Updated |
---|---|
2012-05-22 | 2013-01-28 |