P25020
Gene name |
V-SRC |
Protein name |
Tyrosine-protein kinase transforming protein Src |
Names |
pp60v-src, p60-Src, v-Src |
Species |
Rous sarcoma virus (strain H-19) |
KEGG Pathway |
|
EC number |
2.7.10.2: Protein-tyrosine kinases |
Protein Class |
|
Descriptions
Autoinhibitory domains (AIDs)
Target domain |
267-517 (Protein kinase domain) |
Relief mechanism |
Ligand binding |
Assay |
|
Target domain |
267-517 (Protein kinase domain) |
Relief mechanism |
Ligand binding |
Assay |
|
Accessory elements
No accessory elements
References
- Williams JC et al. (1997) "The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions", Journal of molecular biology, 274, 757-75
- Boggon TJ et al. (2004) "Structure and regulation of Src family kinases", Oncogene, 23, 7918-27
- Meng Y et al. (2014) "Locking the active conformation of c-Src kinase through the phosphorylation of the activation loop", Journal of molecular biology, 426, 423-35
- Register AC et al. (2014) "SH2-catalytic domain linker heterogeneity influences allosteric coupling across the SFK family", Biochemistry, 53, 6910-23
Autoinhibited structure
Activated structure
0 structures for P25020
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|
No variants for P25020
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P25020 | |||||
No associated diseases with P25020
7 regional properties for P25020
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Protein kinase domain | 267 - 517 | IPR000719 |
| domain | SH2 domain | 146 - 245 | IPR000980 |
| domain | Serine-threonine/tyrosine-protein kinase, catalytic domain | 267 - 516 | IPR001245 |
| domain | SH3 domain | 81 - 142 | IPR001452 |
| active_site | Tyrosine-protein kinase, active site | 382 - 394 | IPR008266 |
| binding_site | Protein kinase, ATP binding site | 273 - 295 | IPR017441 |
| domain | Tyrosine-protein kinase, catalytic domain | 267 - 516 | IPR020635 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.10.2 | Protein-tyrosine kinases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| metal ion binding | Binding to a metal ion. |
| non-membrane spanning protein tyrosine kinase activity | Catalysis of the reaction: ATP + protein L-tyrosine = ADP + protein L-tyrosine phosphate by a non-membrane spanning protein. |
| protein serine/threonine/tyrosine kinase activity | Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; ATP + a protein threonine = ADP + protein threonine phosphate; and ATP + a protein tyrosine = ADP + protein tyrosine phosphate. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGSSKSKPKD | PSQRRRSLEP | PDSTHHGGFP | ASQTPDETAA | PDAHRNPSRS | FGTVATEPKL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FWGFNTSDTV | TSPQRAGALA | GGVTTFVALY | DYESWTETDL | SFKKGERLQI | VNNTEGDWWL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AHSLTTGQTG | YIPSNYVAPS | DSIQAEEWYF | GKITRRESER | LLLNPENPRG | TFLVRKSETA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KGAYCLSVSD | FDNAKGPNVK | HYKICKLYSG | GFYITSRTQF | GSLQQLVAYY | SKHADGLCHR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LTNVCPTSKP | QTQGLAKDAW | EIPRESLRLE | AKLGQGCFGE | VWMGTWNGTT | RVAIKTLKPG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TMSPEAFLQE | AQVMKKLRHE | KLVQLYAVVS | EEPIYIVIEY | MSKGSLLDFL | KGEMGKYLRL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PQLVDMAAQI | ASGMAYVERM | NYVHRDLRAA | NILVGENLVC | KVADFGLARL | IEDNEYTARQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GAKFPIKWTA | PEAALYGRFT | IKSDVWSFGI | LLTELTTKGR | VPYPGMVNRE | VLDQVERAYR |
| 490 | 500 | 510 | 520 | ||
| MPCPPECPES | LHDLMCQCWR | KDPEERPTFK | YLQAQLLPAC | VLEVAE |