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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Proto-oncogene tyrosine-protein kinase Src

UniprotKB/SwissProt ID: SRC_CHICK (P00523)

Gene Name: SRC

Organism: Gallus gallus (Chicken).

Function: Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein- coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates involved in this process. When cells adhere via focal adhesions to the extra- cellular matrix, signals are transmitted by integrins into the cell and result in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN). Also active at the sites of cell-cell contact adherens junctions and at gap junctions. Implicated in the regulation of pre-mRNA- processing. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus.

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cell membrane (By similarity). Mitochondrion inner membrane (By similarity). Endosome membrane; Peripheral membrane protein. Nucleus (By similarity). Cytoplasm, cytoskeleton (By similarity). Note=Localizes to focal adhesion sites after integrin engagemen

PDB :
( If your security settings prevent Jmol from running, please register http://140.138.144.145/ as a safe location in your Java settings. )

Graphical Visualization of S-nitrosylation Sites:
Overview of Protein S-nitrosylation Sites with Functional and Structural Information
InterPro ID Domain
IPR000719
IPR000980
IPR001245
IPR001452
IPR008266
IPR011009

3D Structure Databases:
3D structure databases
EntryMethodResolution (A)ChainPositionsView
1F1W X-ray 2.10 A A145-246Link
1F2F X-ray 1.70 A A145-246Link
1NLO NMR - C81-140Link
1NLP NMR - C81-140Link
1P13 X-ray 1.63 A A/B145-245Link
1PRL NMR - C77-139Link
1PRM NMR - C77-139Link
1RLP NMR - C77-139Link
1RLQ NMR - C77-139Link
1SRL NMR - A77-140Link
1SRM NMR - A77-140Link
2HWO X-ray 2.50 A A/B251-532Link
2HWP X-ray 2.48 A A/B251-532Link
2OIQ X-ray 2.07 A A/B251-532Link
2PTK X-ray 2.35 A A81-533Link
2QI8 X-ray 2.32 A A/B251-533Link
2QLQ X-ray 2.33 A A/B251-533Link
2QQ7 X-ray 2.38 A A/B251-533Link
3D7T X-ray 2.90 A B258-533Link
3D7U X-ray 4.11 A B/D260-523Link
3DQW X-ray 2.02 A A/B/C/D251-533Link
3DQX X-ray 2.30 A A/B251-533Link
3EL7 X-ray 2.80 A A251-533Link
3EL8 X-ray 2.30 A A/B251-533Link
3EN4 X-ray 2.55 A A/B251-533Link
3EN5 X-ray 2.66 A A/B251-533Link
3EN6 X-ray 2.39 A A/B251-533Link
3EN7 X-ray 2.81 A A/B251-533Link
3F3T X-ray 2.50 A A/B251-533Link
3F3U X-ray 2.50 A A/B251-533Link
3F3V X-ray 2.60 A A/B251-533Link
3F3W X-ray 2.60 A A/B251-533Link
3F6X X-ray 2.35 A A/B/C/D251-533Link
3FJ5 X-ray 1.65 A A/B85-140Link
3G5D X-ray 2.20 A A/B251-533Link
3G6G X-ray 2.31 A A/B251-533Link
3G6H X-ray 2.35 A A/B251-533Link
3GEQ X-ray 2.20 A A/B251-533Link
3LOK X-ray 2.48 A A/B251-533Link
3OEZ X-ray 2.40 A A/B251-533Link
3OF0 X-ray 2.70 A A/B251-533Link
3QLF X-ray 2.75 A A/B251-533Link
3QLG X-ray 2.75 A A/B251-533Link
3SVV X-ray 2.20 A A/B251-533Link
3TZ7 X-ray 3.30 A A/B251-533Link
3TZ8 X-ray 2.70 A A/B251-533Link
3TZ9 X-ray 3.10 A A/B251-533Link
3U4W X-ray 1.90 A A259-533Link
3U51 X-ray 2.24 A A/B259-533Link
3UQF X-ray 2.27 A A/B251-533Link
3UQG X-ray 2.20 A A/B251-533Link
4AGW X-ray 2.60 A A/B251-533Link
4DGG X-ray 2.65 A A/B251-533Link
4FIC X-ray 2.50 A A/B251-533Link
4HVU X-ray 0.98 A A85-141Link
4HVV X-ray 1.10 A A85-140Link
4HVW X-ray 0.98 A A85-141Link
4LGG X-ray 2.41 A A/B264-533Link
4LGH X-ray 2.84 A A/B257-533Link
4MCV X-ray 2.73 A A/B256-533Link

The S-nitrosylation sites of SRC_CHICK

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site Substrate Motifs PubMed ID Experiment
1498PESLHDLMCQ C WRKDPEERPT CHHHHHHHHH H HHHCHHHCCC 3.02%N/A22178444-
2498PESLHDLMCQ C WRKDPEERPT CHHHHHHHHH H HHHCHHHCCC 3.02%N/A19948721-