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 |
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| 1k9aA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aB01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aC01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aD01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aE01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aF01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1jegA00 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1cskA00 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1cskB00 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1cskC00 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1cskD00 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aB02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aC02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aD02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aE02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aF02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3eacA00 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3eazA00 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aB03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aC03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aD03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aE03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aF03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1bygA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3d7tA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3d7uA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3d7uC01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aA04 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aB04 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aC04 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aD04 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aE04 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1k9aF04 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 1bygA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3d7tA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3d7uA02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | |
| 3d7uC02 |
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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 |
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| 1k9aB01 |
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| 1k9aC01 |
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| 1k9aD01 |
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| 1k9aE01 |
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| 1k9aF01 |
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| 1jegA00 |
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| 1cskA00 |
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| 1cskB00 |
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| 1cskC00 |
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| 1cskD00 |
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| 1k9aA02 |
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| 1k9aB02 |
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| 1k9aC02 |
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| 1k9aD02 |
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| 1k9aE02 |
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| 1k9aF02 |
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| 3eacA00 |
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| 3eazA00 |
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| 1k9aA03 |
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| 1k9aB03 |
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| 1k9aC03 |
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| 1k9aD03 |
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| 1k9aE03 |
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| 1k9aF03 |
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| 1bygA01 |
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| 3d7tA01 |
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| 3d7uA01 |
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| 3d7uC01 |
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| 1k9aA04 |
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ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | |||
| 1k9aB04 |
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ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | |||
| 1k9aC04 |
|
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ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | |||
| 1k9aD04 |
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ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | |||
| 1k9aE04 |
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ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | |||
| 1k9aF04 |
|
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ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | |||
| 1bygA02 |
|
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ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | |||
| 3d7tA02 |
|
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ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | |||
| 3d7uA02 |
|
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ASP 314;ARG 318 | ASN 319;ASP 332(Magnesium binding) | |||
| 3d7uC02 |
|
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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 |