Molecular Target Synopsis
Overview
Domains and Structures
Drugs and Clinical Candidates
Druggability
Chemistry
Ligand Efficiency Plot
Pathways
Family Cladogram
Interaction Network
Gene Expression
Gene Copy Number Variation
RNAi
Mutations
Germline Genetics

SRC (P00523) - Overview - Molecular Target Synopsis

Protein


SRC, Proto-oncogene tyrosine-protein kinase Src
Enzyme Classification 2.7.10.2
UniProt P00523

Also Known as SRC_CHICK, SRC

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 (Probable). When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN) (By similarity). Also active at the sites of cell-cell contact adherens junctions and at gap junctions. Implicated in the regulation of pre-mRNA-processing (Probable). 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 (PubMed:1717492, PubMed:8550628). Involved in anchorage-independent cell growth (PubMed:19307596). Forms a complex with polyoma virus middle T antigen. Interacts with AFAP-110. Interacts with GJA1 and PXN.

5XP5
C-SRC IN COMPLEX WITH ATP-CHF
RCSB/PDB
Inspect Structure
See all 3D Structures for SRC

Isoforms / Transcripts (Protein Coding)


Protein Length Ensembl Gene Ensembl Transcript Ensembl Protein Uniprot Isoform
533P00523-1
193P00523-2

Sub-cellular localization


UniProt: SRC is active in the following subcellular-locations: cell membrane, cytoplasm, cytoskeleton, endosome membrane, mitochondrion inner membrane, nucleus, perinuclear region.
GO terms: SRC is active in the following subcellular-locations: cytoskeleton, cytosol, endosome membrane, extrinsic component of cytoplasmic side of plasma membrane, mitochondrial inner membrane, nucleus, perinuclear region of cytoplasm, protein-containing complex.



UniProt
GO terms

Gene Copy Number Variation


In COSMIC - Cell Lines Project SRC has gain in 0 cell-lines, loss in 0 cell-lines and no signal in 0 cell-lines. (see details)

3D Structures


For SRC there are:
99 structures (171 chains) solved
69 are solved in complex with at least one small molecule ligand
6 are solved with an approved drug

SRC is solved in complex with the approved drug(s):

AMP/ADENOSINE PHOSPHATE (3DQX_A, 3DQX_B),
RXT/RUXOLITINIB (4U5J_A, 4U5J_B),
STI/IMATINIB (2OIQ_A, 3OEZ_A, 3OEZ_B),
1N1/DASATINIB (3G5D_A, 3G5D_B, 3QLG_A, 3QLG_B).

(see details)
Molecular Target 3D Synopsis

Screening and Chemistry


SRC has been screened with 383 compounds (479 bioactivities), 162 compounds have bioactivities that show binding affinity of <= 500nM (205 bioactivities). (see details)