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P12931 SRC_HUMAN

General info Cross-references Sequences Orthologs Ortholog sequences Validation experiments Predictions Palmitoyl-proteomes References

Palmitoyl-proteomes

5/22 articles for human
10 orthologs

Palmitoyl-proteome experiments

Validation experiments

3 experiments
1 ortholog

Validation experiments

Curated sites & Enzymes

0 site from validation experiments^*
0 site from palmitoyl-proteomes^*
No PAT known
No APT known
^*In main isoform only

Predictions

Predicted

1 cysteine in main isoform

Predictions

Protein general information from UniProt

Protein names

Proto-oncogene tyrosine-protein kinase Src, EC 2.7.10.2; Proto-oncogene c-Src; pp60c-src, p60-Src

Subcellular location

Cell membrane (By similarity); Mitochondrion inner membrane (Probable); Nucleus (Probable); Cytoplasm (Probable); cytoskeleton; perinuclear region; Cytoskeleton (Probable); Perinuclear region (Probable); Cell junction (Probable); Focal adhesion (Probable)

Isoforms & protein length

Isoform 1 (main): 536 aa; Isoform 2 : 542 aa

Known functions

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 such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (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) (PubMed:21411625). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (By similarity). Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1 (PubMed:11389730). Plays a role in EGF-mediated calcium-activated chloride channel activation (PubMed:18586953). Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor (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:7853507). Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:8755529, PubMed:14585963). Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase (PubMed:12615910). Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation (PubMed:16186108). Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731' (PubMed:20100835, PubMed:21309750). Enhances DDX58/RIG-I-elicited antiviral signaling (PubMed:19419966). Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376' (PubMed:14585963). Phosphorylates BCAR1 at 'Tyr-128' (PubMed:22710723). Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity (PubMed:20525694). Phosphorylates synaptic vesicle protein synaptophysin (SYP) (By similarity). Involved in anchorage-independent cell growth (PubMed:19307596). Required for podosome formation (By similarity). Mediates IL6 signaling by activating YAP1-NOTCH pathway to induce inflammation-induced epithelial regeneration (PubMed:25731159). Non-receptor protein tyrosine kinase which phosphorylates synaptophysin with high affinity. Non-receptor protein tyrosine kinase which shows higher basal kinase activity than isoform 1, possibly due to weakened intramolecular interactions which enhance autophosphorylation of Tyr-419 and subsequent activation (By similarity). The SH3 domain shows reduced affinity with the linker sequence between the SH2 and kinase domains which may account for the increased basal activity (By similarity). Displays altered substrate specificity compared to isoform 1, showing weak affinity for synaptophysin and for peptide substrates containing class I or class II SH3 domain-binding motifs (By similarity). Plays a role in L1CAM-mediated neurite elongation, possibly by acting downstream of L1CAM to drive cytoskeletal rearrangements involved in neurite outgrowth (By similarity). Non-receptor protein tyrosine kinase which shows higher basal kinase activity than isoform 1, possibly due to weakened intramolecular interactions which enhance autophosphorylation of Tyr-419 and subsequent activation (By similarity). The SH3 domain shows reduced affinity with the linker sequence between the SH2 and kinase domains which may account for the increased basal activity (By similarity). Displays altered substrate specificity compared to isoform 1, showing weak affinity for synaptophysin and for peptide substrates containing class I or class II SH3 domain-binding motifs (By similarity). Plays a role in neurite elongation (By similarity). ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein] ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein] ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein] ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein] Phosphorylation by CSK at Tyr-530 inhibits kinase activity. Inhibitory phosphorylation at Tyr-530 is enhanced by heme. Further phosphorylation by CDK1 partially reactivates CSK-inactivated SRC and facilitates complete reactivation by protein tyrosine phosphatase PTPRC. Integrin engagement stimulates kinase activity. Phosphorylation by PTK2/FAK1 enhances kinase activity. Butein and pseudosubstrate-based peptide inhibitors like CIYKYYF act as inhibitors. Phosphorylation at Tyr-419 increases kinase activity. Part of a complex comprised of PTPRA, BCAR1, BCAR3 (via SH2 domain) and SRC; the formation of the complex is dependent on integrin mediated-tyrosine phosphorylation of PTPRA (PubMed:22801373). Interacts with DDEF1/ASAP1; via the SH3 domain (By similarity). Interacts with CCPG1 (By similarity). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN (By similarity). Interacts with ERBB2, STAT1 and PNN (By similarity). Interacts with DDR1, DDR2 and DAB2 (By similarity). Interacts with CDCP1, TGFB1I1 and TOM1L2 (PubMed:15851033, PubMed:16479011, PubMed:17202804). Interacts with the cytoplasmic domain of MUC1, phosphorylates it and increases binding of MUC1 with beta-catenin (PubMed:11152665). Interacts with RALGPS1; via the SH3 domain (PubMed:10747847). Interacts with CAV2 (tyrosine phosphorylated form) (PubMed:12091389, PubMed:15504032). Interacts (via the SH3 domain and the protein kinase domain) with ARRB1; the interaction is independent of the phosphorylation state of SRC C-terminus (By similarity). Interacts with ARRB1 and ARRB2 (PubMed:10753943, PubMed:9924018). Interacts with SRCIN1 (PubMed:17525734). Interacts with NDFIP2 and more weakly with NDFIP1 (PubMed:20534535). Interacts with PIK3CA and/or PIK3C2B, PTK2/FAK1 and ESR1 (dimethylated on arginine) (PubMed:18657504, PubMed:21411625). Interacts with FASLG (PubMed:19807924). Interacts (via SH2 domain) with the 'Tyr-402' phosphorylated form of PTK2B/PYK2 (PubMed:14585963). Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated) (By similarity). Interacts with PDGFRA (tyrosine phosphorylated) (By similarity). Interacts with CSF1R (By similarity). Interacts (via SH2 and SH3 domain) with TNK2 (PubMed:21309750). Interacts (via protein kinase domain) with the tyrosine phosphorylated form of RUNX3 (via runt domain) (PubMed:20100835). Interacts with TRAF3 (via RING-type zinc finger domain) (PubMed:19419966). Interacts with DDX58, MAVS and TBK1 (PubMed:19419966). Interacts (via SH2 domain) with RACK1; the interaction is enhanced by tyrosine phosphorylation of RACK1 and inhibits SRC activity (PubMed:9584165, PubMed:11279199). Interacts with EPHB1; activates the MAPK/ERK cascade to regulate cell migration (PubMed:12925710). Interacts with FCAMR (PubMed:8759729). Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1 (PubMed:18024423). Interacts with AMOTL2; this interaction regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites (PubMed:17293535). Interacts with TRAP1 (PubMed:23564345). Interacts with CBLC; the interaction is enhanced when SRC is phosphorylated at Tyr-419 (PubMed:14661060, PubMed:22888118). Interacts with ARHGEF5 (By similarity). Interacts (via cytoplasmic domain) with CEACAM1 (via SH2 domain); this interaction is regulated by trans-homophilic cell adhesion (PubMed:7478590). Interacts with MPP2 (PubMed:19665017). Interacts with PRR7 (PubMed:21460222). Interacts (via kinase domain and to a lesser extent the SH2 domain) directly with PDLIM4; this interaction results in PTPN13-mediated dephosphorylation of this protein leading to its inactivation (PubMed:19307596). Interacts with P85 (PIK3R1 or PIK3R2) (PubMed:28903391). Interacts with HNRNPA2B1 (PubMed:31320558). Interacts with IL6ST/gp130 (PubMed:25731159). Interacts (via SH3 domain) with PELP1 in the presence of 17-beta-estradiol. Interacts with AMBRA1 (By similarity). (Microbial infection) Interacts with HEV ORF3 protein; via the SH3 domain. (Microbial infection) Interacts (via SH2 domain) with HCV non-structural protein 5A (via N-terminus). Localizes to focal adhesion sites following integrin engagement (PubMed:22801373). Localization to focal adhesion sites requires myristoylation and the SH3 domain (PubMed:7525268). Colocalizes with PDLIM4 at the perinuclear region, but not at focal adhesions (PubMed:19307596). Phosphorylation by CSK at Tyr-530 inhibits kinase activity. Inhibitory phosphorylation at Tyr-530 is enhanced by heme. Further phosphorylation by CDK1 partially reactivates CSK-inactivated SRC and facilitates complete reactivation by protein tyrosine phosphatase PTPRC. Integrin engagement stimulates kinase activity. Phosphorylation by PTK2/FAK1 enhances kinase activity. Butein and pseudosubstrate-based peptide inhibitors like CIYKYYF act as inhibitors. Phosphorylation at Tyr-419 increases kinase activity. 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 such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (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) (PubMed:21411625). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (By similarity). Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1 (PubMed:11389730). Plays a role in EGF-mediated calcium-activated chloride channel activation (PubMed:18586953). Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor (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:7853507). Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:8755529, PubMed:14585963). Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase (PubMed:12615910). Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation (PubMed:16186108). Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731' (PubMed:20100835, PubMed:21309750). Enhances DDX58/RIG-I-elicited antiviral signaling (PubMed:19419966). Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376' (PubMed:14585963). Phosphorylates BCAR1 at 'Tyr-128' (PubMed:22710723). Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity (PubMed:20525694). Involved in anchorage-independent cell growth (PubMed:19307596). Required for podosome formation (By similarity). ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Interacts with DDEF1/ASAP1; via the SH3 domain (By similarity). Interacts with CCPG1 (By similarity). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN (By similarity). Interacts with ERBB2, STAT1 and PNN (By similarity). Interacts with DDR1, DDR2 and DAB2 (By similarity). Interacts with CDCP1, PELP1, TGFB1I1 and TOM1L2 (PubMed:12415108, PubMed:15851033, PubMed:16479011, PubMed:17202804). Interacts with the cytoplasmic domain of MUC1, phosphorylates it and increases binding of MUC1 with beta-catenin (PubMed:11152665). Interacts with RALGPS1; via the SH3 domain (PubMed:10747847). Interacts with CAV2 (tyrosine phosphorylated form) (PubMed:12091389, PubMed:15504032). Interacts (via the SH3 domain and the protein kinase domain) with ARRB1; the interaction is independent of the phosphorylation state of SRC C-terminus (By similarity). Interacts with ARRB1 and ARRB2 (PubMed:10753943, PubMed:9924018). Interacts with SRCIN1 (PubMed:17525734). Interacts with NDFIP2 and more weakly with NDFIP1 (PubMed:20534535). Interacts with PIK3CA and/or PIK3C2B, PTK2/FAK1 and ESR1 (dimethylated on arginine) (PubMed:18657504, PubMed:21411625). Interacts with FASLG (PubMed:19807924). Interacts (via SH2 domain) with the 'Tyr-402' phosphorylated form of PTK2B/PYK2 (PubMed:14585963). Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated) (By similarity). Interacts with PDGFRA (tyrosine phosphorylated) (By similarity). Interacts with CSF1R (By similarity). Interacts (via SH2 and SH3 domain) with TNK2 (PubMed:21309750). Interacts (via protein kinase domain) with the tyrosine phosphorylated form of RUNX3 (via runt domain) (PubMed:20100835). Interacts with TRAF3 (via RING-type zinc finger domain) (PubMed:19419966). Interacts with DDX58, MAVS and TBK1 (PubMed:19419966). Interacts (via SH2 domain) with RACK1; the interaction is enhanced by tyrosine phosphorylation of RACK1 and inhibits SRC activity (PubMed:9584165, PubMed:11279199). Interacts with EPHB1; activates the MAPK/ERK cascade to regulate cell migration (PubMed:12925710). Interacts with FCAMR (PubMed:8759729). Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1 (PubMed:18024423). Interacts with AMOTL2; this interaction regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites (PubMed:17293535). Interacts with TRAP1 (PubMed:23564345). Interacts with CBLC; the interaction is enhanced when SRC is phosphorylated at Tyr-419 (PubMed:14661060, PubMed:22888118). Interacts with ARHGEF5 (By similarity). Interacts (via cytoplasmic domain) with CEACAM1 (via SH2 domain); this interaction is regulated by trans-homophilic cell adhesion (PubMed:7478590). Interacts with MPP2 (PubMed:19665017). Interacts with PRR7 (PubMed:21460222). Interacts (via kinase domain and to a lesser extent the SH2 domain) directly with PDLIM4; this interaction results in PTPN13-mediated dephosphorylation of this protein leading to its inactivation (PubMed:19307596). (Microbial infection) Interacts with HEV ORF3 protein; via the SH3 domain. Localizes to focal adhesion sites following integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain (PubMed:7525268). Colocalizes with PDLIM4 at the perinuclear region, but not at focal adhesions (PubMed:19307596). 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 such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin (CTTN) (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) (PubMed:21411625). In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP). Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43 (GJA1). SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1 (Probable). Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors (By similarity). Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1 (PubMed:11389730). Plays a role in EGF-mediated calcium-activated chloride channel activation (PubMed:18586953). Required for epidermal growth factor receptor (EGFR) internalization through phosphorylation of clathrin heavy chain (CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1 and ARRB2) desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor (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:7853507). Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function (PubMed:8755529, PubMed:14585963). Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase (PubMed:12615910). Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation (PubMed:16186108). Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731' (PubMed:20100835, PubMed:21309750). Enhances DDX58/RIG-I-elicited antiviral signaling (PubMed:19419966). Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376' (PubMed:14585963). Phosphorylates BCAR1 at 'Tyr-128' (PubMed:22710723). Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity (PubMed:20525694). Involved in anchorage-independent cell growth (PubMed:19307596). Required for podosome formation (By similarity). ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein] Phosphorylation by CSK at Tyr-530 inhibits kinase activity. Inhibitory phosphorylation at Tyr-530 is enhanced by heme. Further phosphorylation by CDK1 partially reactivates CSK-inactivated SRC and facilitates complete reactivation by protein tyrosine phosphatase PTPRC. Integrin engagement stimulates kinase activity. Phosphorylation by PTK2/FAK1 enhances kinase activity. Butein and pseudosubstrate-based peptide inhibitors like CIYKYYF act as inhibitors. Phosphorylation at Tyr-419 increases kinase activity. Interacts with DDEF1/ASAP1; via the SH3 domain (By similarity). Interacts with CCPG1 (By similarity). Identified in a complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN (By similarity). Interacts with ERBB2, STAT1 and PNN (By similarity). Interacts with DDR1, DDR2 and DAB2 (By similarity). Interacts with CDCP1, PELP1, TGFB1I1 and TOM1L2 (PubMed:12415108, PubMed:15851033, PubMed:16479011, PubMed:17202804). Interacts with the cytoplasmic domain of MUC1, phosphorylates it and increases binding of MUC1 with beta-catenin (PubMed:11152665). Interacts with RALGPS1; via the SH3 domain (PubMed:10747847). Interacts with CAV2 (tyrosine phosphorylated form) (PubMed:12091389, PubMed:15504032). Interacts (via the SH3 domain and the protein kinase domain) with ARRB1; the interaction is independent of the phosphorylation state of SRC C-terminus (By similarity). Interacts with ARRB1 and ARRB2 (PubMed:10753943, PubMed:9924018). Interacts with SRCIN1 (PubMed:17525734). Interacts with NDFIP2 and more weakly with NDFIP1 (PubMed:20534535). Interacts with PIK3CA and/or PIK3C2B, PTK2/FAK1 and ESR1 (dimethylated on arginine) (PubMed:18657504, PubMed:21411625). Interacts with FASLG (PubMed:19807924). Interacts (via SH2 domain) with the 'Tyr-402' phosphorylated form of PTK2B/PYK2 (PubMed:14585963). Interacts (via SH2 domain) with FLT3 (tyrosine phosphorylated) (By similarity). Interacts with PDGFRA (tyrosine phosphorylated) (By similarity). Interacts with CSF1R (By similarity). Interacts (via SH2 and SH3 domain) with TNK2 (PubMed:21309750). Interacts (via protein kinase domain) with the tyrosine phosphorylated form of RUNX3 (via runt domain) (PubMed:20100835). Interacts with TRAF3 (via RING-type zinc finger domain) (PubMed:19419966). Interacts with DDX58, MAVS and TBK1 (PubMed:19419966). Interacts (via SH2 domain) with RACK1; the interaction is enhanced by tyrosine phosphorylation of RACK1 and inhibits SRC activity (PubMed:9584165, PubMed:11279199). Interacts with EPHB1; activates the MAPK/ERK cascade to regulate cell migration (PubMed:12925710). Interacts with FCAMR (PubMed:8759729). Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1 (PubMed:18024423). Interacts with AMOTL2; this interaction regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites (PubMed:17293535). Interacts with TRAP1 (PubMed:23564345). Interacts with CBLC; the interaction is enhanced when SRC is phosphorylated at Tyr-419 (PubMed:14661060, PubMed:22888118). Interacts with ARHGEF5 (By similarity). Interacts (via cytoplasmic domain) with CEACAM1 (via SH2 domain); this interaction is regulated by trans-homophilic cell adhesion (PubMed:7478590). Interacts with MPP2 (PubMed:19665017). Interacts with PRR7 (PubMed:21460222). Interacts (via kinase domain and to a lesser extent the SH2 domain) directly with PDLIM4; this interaction results in PTPN13-mediated dephosphorylation of this protein leading to its inactivation (PubMed:19307596). Interacts with P85 (PIK3R1 or PIK3R2) (PubMed:28903391). (Microbial infection) Interacts with HEV ORF3 protein; via the SH3 domain. Localizes to focal adhesion sites following integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain (PubMed:7525268). Colocalizes with PDLIM4 at the perinuclear region, but not at focal adhesions (PubMed:19307596).

Cross-references

Source	Identifiers
UniProt gene names	SRC, SRC1
UniProt secondary AC	E1P5V4, Q76P87, Q86VB9, Q9H5A8
Refseq protein ID	XP_011527315.1, XP_011527316.1, NP_005408.1, NP_938033.1
IPI ID	IPI00328867, IPI00641230, IPI00847526, IPI00646197, IPI00479211, IPI00419639, IPI00217725

Source	Identifiers
Ensembl protein	ENSP00000350941, ENSP00000353950, ENSP00000362659, ENSP00000362668, ENSP00000362680, ENSP00000408503
Ensembl gene	ENSG00000197122

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Isoform sequence alignment

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Orthologs

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UniProt AC	UniProt ID	Orthology source	Organism	Gene names	Protein name	Palmitome articles	Times validated	Techniques	Predicted
P05480	SRC_MOUSE	OrthoDB, OMA, Ensembl, InParanoid, MetaPhors	M. musculus	Src	Proto-oncogene tyrosine-protein kinase Src, EC 2.7.10.2	3/23	0	2	Yes
F1LM93	YES_RAT	OrthoDB	R. norvegicus	Yes1	Tyrosine-protein kinase Yes, EC 2.7.10.2	1/3	0	2	Yes
O22558	STY8_ARATH	InParanoid	A. thaliana	STY8, At2g17700	Serine/threonine-protein kinase STY8, EC 2.7.11.1	0/1	0	0	Yes
F4JTP5	STY46_ARATH	InParanoid	A. thaliana	STY46, At4g38470, F20M13.30	Serine/threonine-protein kinase STY46, EC 2.7.11.1	0/1	0	0	No
Q9ZQ31	STY13_ARATH	InParanoid	A. thaliana	STY13, At2g24360, T28I24.9	Serine/threonine-protein kinase STY13, EC 2.7.11.1	0/1	0	0	Yes
Q9M085	Q9M085_ARATH	InParanoid	A. thaliana	At4g31170, F6E21.90, F6E21_90	AT4G31170 protein	0/1	0	0	Yes
Q8RWL6	STY17_ARATH	InParanoid	A. thaliana	STY17, At4g35780, F8D20.290	Serine/threonine-protein kinase STY17, EC 2.7.11.1	0/1	0	0	No
Q2MHE4	HT1_ARATH	InParanoid	A. thaliana	SUU, HT1, At1g62400, F24O1.13	Serine/threonine/tyrosine-protein kinase HT1, EC 2.7.10.1, EC 2.7.11.1	0/1	0	0	Yes
O22100	O22100_ARATH	InParanoid	A. thaliana	F16M2_110, ATMRK1, At3g63260	ATMRK1	1/1	0	1	Yes
Q9LT56	Q9LT56_ARATH	InParanoid	A. thaliana	ATN1, At3g27560	AT3g27560/MMJ24_11	0/1	0	0	Yes
Q9LUI6	Q9LUI6_ARATH	InParanoid	A. thaliana	At3g22750	Kinase-like protein	0/1	0	0	Yes
Q9FGS7	Q9FGS7_ARATH	InParanoid	A. thaliana	At5g50180, K6A12.4, K6A12_4	At5g50180	0/1	0	0	Yes
Q9FM43	Q9FM43_ARATH	InParanoid	A. thaliana	MNF13.60, MNF13_60, At5g40540	Protein kinase ATN1	0/1	0	0	Yes
O23334	O23334_ARATH	InParanoid	A. thaliana	dl3430w, At4g14780, At4g14780/dl3430w, Dl3430W, FCAALL.308	Kinase like protein	0/1	0	0	Yes
Q8L6Y9	Q8L6Y9_ARATH	InParanoid	A. thaliana	At5g01850, T20L15.120, T20L15_120	Protein kinase ATN1-like protein	0/1	0	0	No
Q9SSA4	Q9SSA4_ARATH	InParanoid	A. thaliana	At3g01490, F4P13.4, F4P13_4	AT3g01490/F4P13_4	0/1	0	0	Yes
Q9FGB1	Q9FGB1_ARATH	InParanoid	A. thaliana	MPF21.1, MPF21_1, At5g50000	Protein kinase	1/1	0	1	Yes
P41892	CDC7_SCHPO	MetaPhors	S. pombe	cdc7, SPBC21.06c	Cell division control protein 7	0/1	0	0	Yes
P36582	PCK1_SCHPO	MetaPhors	S. pombe	pck1, SPAC17G8.14c, SPAC22H10.01c	Protein kinase C-like 1	0/1	0	0	Yes
P50527	STE20_SCHPO	MetaPhors	S. pombe	shk1, orb2, pak1, ste20, SPBC1604.14c	Serine/threonine-protein kinase shk1/pak1	0/1	0	0	No
O74749	HSE1_SCHPO	MetaPhors	S. pombe	hse1, SPBC1734.08	Class E vacuolar protein-sorting machinery protein hse1	0/1	0	0	No
Q09795	YAA1_SCHPO	MetaPhors	S. pombe	SPAC22G7.01c, SPAPJ696.03c	Uncharacterized peptidase C22G7.01c	0/1	0	0	No
Q9LYN8	EMS1_ARATH	MetaPhors	A. thaliana	EXS, EMS1, ESP, At5g07280, T28J14.220	Leucine-rich repeat receptor protein kinase EMS1, EC 2.7.11.1	0/1	0	0	No
O04533	LRK52_ARATH	MetaPhors	A. thaliana	LECRK52, LECRKB1, At1g70130, F20P5.15	Putative L-type lectin-domain containing receptor kinase V.2, Arabidopsis thaliana lectin-receptor kinase b1, AthlecRK-b1, LecRK-V.2, EC 2.7.11.1	0/1	0	0	Yes
Q9FXF2	RKF1_ARATH	MetaPhors	A. thaliana	RKF1, At1g29750, F1N18.19, T3M22.1	Probable LRR receptor-like serine/threonine-protein kinase RFK1, EC 2.7.11.1	0/1	0	0	Yes
Q9LVI6	RLK90_ARATH	MetaPhors	A. thaliana	RLK902, At3g17840, MEB5.6	Probable inactive receptor kinase RLK902	0/1	0	0	No
Q9M2S4	LRKS4_ARATH	MetaPhors	A. thaliana	LECRKS4, At3g55550, T22E16.210	L-type lectin-domain containing receptor kinase S.4, LecRK-S.4, EC 2.7.11.1	0/1	0	0	No
F4K964	F4K964_ARATH	MetaPhors	A. thaliana	At5g57035	U-box domain-containing protein kinase family protein	0/1	0	0	Yes
F4JZW1	PBL13_ARATH	MetaPhors	A. thaliana	PBL13, At5g35580, K2K18.3	Serine/threonine-protein kinase PBL13, EC 2.7.11.1	0/1	0	0	Yes
O22932	CIPKB_ARATH	MetaPhors	A. thaliana	CIPK11, PKS5, SIP4, SnRK3.22, At2g30360, T9D9.17	CBL-interacting serine/threonine-protein kinase 11, EC 2.7.11.1	0/1	0	0	No
Q9ZVR7	PSKR1_ARATH	MetaPhors	A. thaliana	PSKR1, PSKR, At2g02220, F5O4.1	Phytosulfokine receptor 1, AtPSKR1, EC 2.7.11.1, EC 4.6.1.2	0/1	0	0	Yes
P43298	TMK1_ARATH	MetaPhors	A. thaliana	BLK1, TMK1, At1g66150, F15E12.4	Receptor protein kinase TMK1, EC 2.7.11.1	0/1	0	0	Yes
O22833	LRK54_ARATH	MetaPhors	A. thaliana	LECRK54, LECRKC1, At2g43700, F18O19.19	L-type lectin-domain containing receptor kinase V.4, Arabidopsis thaliana lectin-receptor kinase c1, AthlecRK-c1, LecRK-V.4, EC 2.7.11.1	0/1	0	0	Yes
O64770	Y1649_ARATH	MetaPhors	A. thaliana	At1g61490, T1F9.1	G-type lectin S-receptor-like serine/threonine-protein kinase At1g61490, EC 2.7.11.1	0/1	0	0	Yes
O64781	Y1639_ARATH	MetaPhors	A. thaliana	At1g61390, T1F9.12	G-type lectin S-receptor-like serine/threonine-protein kinase At1g61390, EC 2.7.11.1	0/1	0	0	Yes
Q66GN2	LRK64_ARATH	MetaPhors	A. thaliana	LECRK64, LECRKA4.3, At5g01560, F7A7.80	Lectin-domain containing receptor kinase VI.4, LecRK-VI.4, EC 2.7.11.1	0/1	0	0	Yes
Q8RY11	AMPP2_ARATH	MetaPhors	A. thaliana	APP2, T12H1.32, T12H1_32, At3g05350	Aminopeptidase P2, AtAPP2, EC 3.4.11.9	0/1	0	0	No
Q96285	LRK55_ARATH	MetaPhors	A. thaliana	LECRK55, LECRKA1, At3g59700, T16L24.250	L-type lectin-domain containing receptor kinase V.5, Arabidopsis thaliana lectin-receptor kinase a1, Ath.lecRK1, AthlecRK-a1, LecRK-V.5, EC 2.7.11.1	0/1	0	0	Yes
Q9FHG4	LRKS7_ARATH	MetaPhors	A. thaliana	LECRKS7, At5g55830, MDF20.27	Probable L-type lectin-domain containing receptor kinase S.7, LecRK-S.7, EC 2.7.11.1	0/1	0	0	Yes
Q9FYK0	TMK2_ARATH	MetaPhors	A. thaliana	TMK2, BLK3, At1g24650, F21J9.31, F5A9.23	Receptor-like kinase TMK2, EC 2.7.11.1	0/1	0	0	Yes
Q9LP77	Y1848_ARATH	MetaPhors	A. thaliana	RKL1, At1g48480, T1N15.9	Probable inactive receptor kinase At1g48480	1/1	0	1	Yes
Q9M020	LRK63_ARATH	MetaPhors	A. thaliana	LECRK63, LECRKA4.2, At5g01550, F7A7.70	Lectin-domain containing receptor kinase VI.3, LecRK-VI.3, EC 2.7.11.1	0/1	0	0	Yes
Q9M1Z9	LRK58_ARATH	MetaPhors	A. thaliana	LECRK58, At3g59750, F24G16.20	Putative L-type lectin-domain containing receptor kinase V.8, LecRK-V.8, EC 2.7.11.1	0/1	0	0	No
Q9S9U1	LRK71_ARATH	MetaPhors	A. thaliana	LECRK71, At4g04960, T32N4.9	L-type lectin-domain containing receptor kinase VII.1, LecRK-VII.1, EC 2.7.11.1	0/1	0	0	No
Q9SY95	Y1155_ARATH	MetaPhors	A. thaliana	At1g61550, T25B24.10	G-type lectin S-receptor-like serine/threonine-protein kinase At1g61550, EC 2.7.11.1	0/1	0	0	Yes
Q93ZS4	NIK3_ARATH	MetaPhors	A. thaliana	NIK3, At1g60800, F8A5.31	Protein NSP-INTERACTING KINASE 3, EC 2.7.11.1	0/1	0	0	No
Q9C7S5	PSYR1_ARATH	MetaPhors	A. thaliana	PSY1R, PSYR1, At1g72300, T9N14.20	Tyrosine-sulfated glycopeptide receptor 1, EC 2.7.11.1	0/1	0	0	Yes
Q9FII5	TDR_ARATH	MetaPhors	A. thaliana	TDR, PXY, At5g61480, MCI2.4	Leucine-rich repeat receptor-like protein kinase TDR, EC 2.7.11.1	0/1	0	0	Yes
Q9FN37	PSKR2_ARATH	MetaPhors	A. thaliana	PSKR2, At5g53890, K19P17.5	Phytosulfokine receptor 2, AtPSKR2, EC 2.7.11.1	0/1	0	0	Yes
Q9CAD5	YODA_ARATH	MetaPhors	A. thaliana	YDA, At1g63700, F24D7.11	Mitogen-activated protein kinase kinase kinase YODA, EC 2.7.11.25	0/1	0	0	No
Q1PDV6	PBL27_ARATH	MetaPhors	A. thaliana	PBL27, T28N17.90, AT5G18610, At5g18610	Serine/threonine-protein kinase PBL27, EC 2.7.11.1	1/1	0	1	Yes
O49840	PBL3_ARATH	MetaPhors	A. thaliana	PBL3, KIN2, PIX14, APK2B, At2g02800, T20F6.6	Probable serine/threonine-protein kinase PBL3, EC 2.7.11.1	0/1	0	0	Yes
Q7X8C5	WAKLB_ARATH	MetaPhors	A. thaliana	WAKL2, At1g16130, T24D18.21	Wall-associated receptor kinase-like 2, EC 2.7.11.-	0/1	0	0	Yes
Q8H1E3	PBL17_ARATH	MetaPhors	A. thaliana	PBL17, At2g07180	Probable serine/threonine-protein kinase PBL17, EC 2.7.11.1	0/1	0	0	Yes
Q8VYY5	NCRK_ARATH	MetaPhors	A. thaliana	NCRK, At2g28250, T3B23.8	Receptor-like serine/threonine-protein kinase NCRK, EC 2.7.11.1	0/1	0	0	Yes
Q8VZJ9	CRCK2_ARATH	MetaPhors	A. thaliana	CRCK2, At4g00330, A_IG005I10.8, F5I10.8	Calmodulin-binding receptor-like cytoplasmic kinase 2, EC 2.7.11.1	1/1	0	1	No
Q9FNE1	CRK42_ARATH	MetaPhors	A. thaliana	CRK42, At5g40380, MPO12.90	Cysteine-rich receptor-like protein kinase 42, Cysteine-rich RLK42, EC 2.7.11.-	0/1	0	0	Yes
Q9LSC2	Y3589_ARATH	MetaPhors	A. thaliana	At3g15890, MVC8.1	PTI1-like tyrosine-protein kinase At3g15890, EC 2.7.10.2	1/1	0	1	Yes
Q9LSE1	CDG1_ARATH	MetaPhors	A. thaliana	CDG1, At3g26940, MOJ10.2	Serine/threonine-protein kinase CDG1, EC 2.7.11.1	0/1	0	0	Yes
Q9M0X5	CRK25_ARATH	MetaPhors	A. thaliana	CRK25, At4g05200, C17L7.120, C6L9.3	Cysteine-rich receptor-like protein kinase 25, Cysteine-rich RLK25, EC 2.7.11.-	0/1	0	0	Yes
Q9M1Q2	Q9M1Q2_ARATH	MetaPhors	A. thaliana	T17J13.180, At3g62220	At3g62220	0/1	0	0	Yes
Q9SX31	PERK9_ARATH	MetaPhors	A. thaliana	PERK9, At1g68690, F24J5.8	Proline-rich receptor-like protein kinase PERK9, EC 2.7.11.1	0/1	0	0	Yes
Q9SY91	PBL15_ARATH	MetaPhors	A. thaliana	PBL15, PIX1, At1g61590, T25B24.6	Probable serine/threonine-protein kinase PBL15, EC 2.7.11.1	0/1	0	0	Yes
Q9ZUF4	RIPK_ARATH	MetaPhors	A. thaliana	RIPK, PBL14, PIX8, At2g05940	Serine/threonine-protein kinase RIPK, EC 2.7.11.1	0/1	0	0	Yes
Q1PE89	PBL24_ARATH	MetaPhors	A. thaliana	PBL24, At4g13190, F17N18.80	Probable serine/threonine-protein kinase PBL24, EC 2.7.11.1	0/1	0	0	Yes
O64778	Y1142_ARATH	MetaPhors	A. thaliana	At1g61420, T1F9.9	G-type lectin S-receptor-like serine/threonine-protein kinase At1g61420, EC 2.7.11.1	0/1	0	0	Yes
Q9ZR79	LRK57_ARATH	MetaPhors	A. thaliana	LECRK57, LECRKA3, At3g59740, F24G16.10, T16L24.290	L-type lectin-domain containing receptor kinase V.7, Arabidopsis thaliana lectin-receptor kinase a3, AthlecRK-a3, LecRK-V.7, EC 2.7.11.1	0/1	0	0	No
O64783	Y1137_ARATH	MetaPhors	A. thaliana	At1g61370, T1F9.14	G-type lectin S-receptor-like serine/threonine-protein kinase At1g61370, EC 2.7.11.1	0/1	0	0	Yes
B9DFG5	PTI13_ARATH	MetaPhors	A. thaliana	PTI13, At3g59350, F25L23.210	PTI1-like tyrosine-protein kinase 3, PTI1-3, EC 2.7.10.2	1/1	0	1	Yes
Q8GWJ7	CRK19_ARATH	MetaPhors	A. thaliana	CRK19, At4g23270, F21P8.160	Cysteine-rich receptor-like protein kinase 19, Cysteine-rich RLK19, EC 2.7.11.-	0/1	0	0	Yes
O64771	Y1148_ARATH	MetaPhors	A. thaliana	At1g61480, T1F9.2	G-type lectin S-receptor-like serine/threonine-protein kinase At1g61480, EC 2.7.11.1	0/1	0	0	Yes
Q9C660	PEK10_ARATH	MetaPhors	A. thaliana	PERK10, At1g26150, F28B23.17	Proline-rich receptor-like protein kinase PERK10, EC 2.7.11.1	0/1	0	0	Yes
C0LGD7	Y1684_ARATH	MetaPhors	A. thaliana	At1g06840, F4H5.8	Probable LRR receptor-like serine/threonine-protein kinase At1g06840, EC 2.7.11.1	0/1	0	0	Yes
F4JQH3	AMPP1_ARATH	MetaPhors	A. thaliana	C7A10.600, At4g36760, aminopeptidase P1, AP22.64, AP22_64, ATAPP1, APP1	Aminopeptidase P1, AtAPP1, EC 3.4.11.9	0/1	0	0	No
F4IRL7	F4IRL7_ARATH	MetaPhors	A. thaliana	At2g25220	Protein kinase superfamily protein	0/1	0	0	No
F4JWD4	F4JWD4_ARATH	MetaPhors	A. thaliana	At5g11020	Protein kinase superfamily protein	0/1	0	0	Yes
C0LGE0	Y1765_ARATH	MetaPhors	A. thaliana	At1g07650, F24B9.28, F24B9.29	Probable LRR receptor-like serine/threonine-protein kinase At1g07650, EC 2.7.11.1	0/1	0	0	Yes
F4I0Z0	F4I0Z0_ARATH	MetaPhors	A. thaliana	At1g09440, F14J9.10, F14J9_10	Protein kinase superfamily protein	0/1	0	0	No
Q9LDQ3	CRK34_ARATH	MetaPhors	A. thaliana	CRK34, CRK35, At4g11530, F25E4.150	Cysteine-rich receptor-like protein kinase 34, Cysteine-rich RLK34, EC 2.7.11.1	0/1	0	0	Yes
Q9SXB3	Y1112_ARATH	MetaPhors	A. thaliana	At1g11280, T28P6.7	G-type lectin S-receptor-like serine/threonine-protein kinase At1g11280, EC 2.7.11.1	0/1	0	0	Yes
A0A654EQA1	A0A654EQA1_ARATH	MetaPhors	A. thaliana	AN1_LOCUS5176, C24_LOCUS5055	Protein kinase domain-containing protein	0/1	0	0	No
A0A654FKI5	A0A654FKI5_ARATH	MetaPhors	A. thaliana	AN1_LOCUS16800	Receptor-like serine/threonine-protein kinase	0/1	0	0	No
E1BIM8	E1BIM8_BOVIN	OrthoDB, OMA, Ensembl, InParanoid	B. taurus	SRC	Tyrosine-protein kinase	0/2	0	0	Yes
F1PSB7	F1PSB7_CANLF	OrthoDB	C. familiaris	YES1	Tyrosine-protein kinase	0/1	0	0	Yes
P00528	SRC64_DROME	OrthoDB, Ensembl, MetaPhors	D. melanogaster	Src64B, Src1, CG7524	Tyrosine-protein kinase Src64B, Dsrc64, EC 2.7.10.2	0/1	0	0	Yes
E2RSH8	E2RSH8_CANLF	OMA, Ensembl, OrthoDB, InParanoid	C. familiaris	SRC	Tyrosine-protein kinase	0/1	0	0	Yes
Q9WUD9	SRC_RAT	OMA, Ensembl, InParanoid, MetaPhors	R. norvegicus	Src	Proto-oncogene tyrosine-protein kinase Src, EC 2.7.10.2	0/3	0	0	Yes
Q04736	YES_MOUSE	OrthoDB	M. musculus	Yes1, Yes	Tyrosine-protein kinase Yes, EC 2.7.10.2	8/23	1	3	Yes
A7MB57	A7MB57_BOVIN	OrthoDB	B. taurus	YES1	Tyrosine-protein kinase	0/2	0	0	Yes
P00522	ABL_DROME	OrthoDB	D. melanogaster	Abl, ABL-1, Dash, CG4032	Tyrosine-protein kinase Abl, EC 2.7.10.2	0/1	0	0	No
Q8IIT5	PTKL_PLAF7	InParanoid	P. falciparum	pTKL, PF3D7_1106800	Inactive protein tyrosine kinase pTKL	0/1	0	0	Yes

Ortholog sequence alignment (CLUSTALW)

Validation experiments

ID of the experiment	Reference	Year	Organism	Cell type	Subcellular location	Technique(s)
SPalmE:1410	Mariscal J et al.	2020	Homo sapiens	PC3	Total membrane	LB-ABE, MS, NH2OH cleavage of thioester bond
SPalmE:1411	Mariscal J et al.	2020	Homo sapiens	PC3	Total cell lysate	LB-ABE, MS
SPalmE:1412	Mariscal J et al.	2020	Homo sapiens	PC3	Extracellular Vesicles	LB-ABE, NH2OH cleavage of thioester bond

Cysteine summary and predictions

Pos in alignment	194	247	254	286	409	492	496	505	507
Subcell. location	C	C	C	C	C	C	C	C	C
Disulfide	no	no	no	no	no	no	no	no	no
PSIPRED v.4.02 prediction
UniProt secondary structure
Pos in isoform 1 [Main] CSS-Palm 4.0 PalmPred	Cys¹⁸⁸	Cys²⁴¹	Cys²⁴⁸	Cys²⁸⁰	Cys⁴⁰³ HC	Cys⁴⁸⁶ MC	Cys⁴⁹⁰	Cys⁴⁹⁹	Cys⁵⁰¹
Pos in isoform 2 CSS-Palm 4.0 PalmPred	Cys¹⁹⁴	Cys²⁴⁷	Cys²⁵⁴	Cys²⁸⁶	Cys⁴⁰⁹ HC	Cys⁴⁹² MC	Cys⁴⁹⁶	Cys⁵⁰⁵	Cys⁵⁰⁷

Legend

Subcell. location

U Undefined E Extracellular/Lumenal T Transmembrane C Cytosolic/Nuclear

Prediction confidence

Cysteine position: Predicted (high confidence prediction with CSS-Palm or/and PalmPred) and validated (in terms of disulfide bonds and cellular location) / Predicted but not validated (in terms of disulfide bond and cellular location) / Not predicted
CSS-Palm 4.0: High confidence, Medium confidence, Low confidence, Not predicted.
PalmPred: High confidence (score > 0.4), Medium confidence (0.1 < score < 0.4), Low confidence (score < 0.1), Not predicted.

Palmitoyl-proteome experiments

List of palmitoyl-proteomes

Tip: Keep CTRL key pressed down while clicking on column headers to do multiple sorting. This applies to any sortable table on this site.

ID of the experiment	Reference	Year	Organism	Cell type	Subcellular location	Technique(s)	Found?	In list	All lists
SPalmE:14	Roth AF et al.	2006	Saccharomyces cerevisiae	Isogenic LRB759	Total membrane	ABE	x		HC HC: 48 hits
SPalmE:13	Kang R et al.	2008	Rattus norvegicus	Cortical neuron	Synaptosomal membrane	ABE	x		HC: 107 hits LC: 308 hits
SPalmE:6	Martin BR et al.	2009	Homo sapiens	Jurkat	Total membrane	Click chemistry	x		HC: 127 hits LC: 188 hits List: 0 hits
SPalmE:1	Yang W et al.	2010	Homo sapiens	DU145	Total membrane	ABE	x		HC: 162 hits LC: 218 hits
SPalmE:10	Yount JS et al.	2010	Mus musculus	Dendritic cell	Total cell lysate	Click chemistry	x		HC: 59 hits LC: 105 hits
SPalmE:578	Yang W et al.	2010	Homo sapiens	DU145	Lipid raft	ABE	x		HC: 102 hits LC: 73 hits
SPalmE:577	Yang W et al.	2010	Homo sapiens	DU145	Non-lipid raft	ABE	x		HC: 63 hits LC: 147 hits
SPalmE:12	Martin BR et al.	2011	Mus musculus	BW5147-derived mouse T-cell hybridoma cell	Total membrane	Click chemistry	x		HC HC: 352 hits LC LC: 8 hits
SPalmE:2	Dowal L et al.	2011	Homo sapiens	Platelet	Total membrane	ABE	x		List: 214 hits
SPalmE:8	Merrick BA et al.	2011	Mus musculus	Macrophage Raw 264.7	Total membrane	ABE	x		List: 69 hits
SPalmE:511	Emmer BT et al.	2011	Trypanosoma brucei brucei	NA	Total cell lysate	ABE	x		List: 126 hits
SPalmE:5	Forrester MT et al.	2011	Homo sapiens	HEK293	Total membrane	ARAC	x		List: 69 hits
SPalmE:7	Wilson JP et al.	2011	Homo sapiens	Jurkat	Total cell lysate	Click chemistry	x		HC: 164 hits LC: 178 hits
SPalmE:3	Ivaldi C et al.	2012	Homo sapiens	B-cell	Total membrane	ABE	x		HC HC: 93 hits
SPalmE:580	Jones ML et al.	2012	Plasmodium falciparum	Whole organism	Total cell lysate	Click chemistry, SILAC	x		HC: 79 hits LC: 89 hits
SPalmE:162	Jones ML et al.	2012	Plasmodium falciparum	Whole organism	Total cell lysate	ABE	x		HC: 100 hits LC: 217 hits
SPalmE:11	Li Y et al.	2012	Mus musculus	Neural stem cell	Total cell lysate	Click chemistry	Ortholog	in HC [YES, SRC]	HC HC: 254 hits
SPalmE:4	Marin EP et al.	2012	Homo sapiens	Umbilical vein blood	NA	ABE	Found	in List	List: 154 hits
SPalmE:9	Ren W et al.	2013	Mus musculus	3T3-L1 and epididymal fat pads	Total membrane	ARAC	Ortholog	in List [YES, SRC]	List: 664 hits
SPalmE:15	Hemsley PA et al.	2013	Arabidopsis thaliana	Heyn Col-4 ecotype root cell suspension	Microsomal membrane	ABE	Ortholog	in LC,HC,MC [Q9FGB1, O22100, PBL27, PTI13, Y1848, Y3589, CRCK2]	HC: 122 hits MC: 94 hits LC: 366 hits
SPalmE:119	Wan J et al.	2013	Mus musculus	Brain	Total cell lysate	ABE	Ortholog	in List [YES, SRC]	List: 378 hits
SPalmE:160	Zhang MM et al.	2013	Schizosaccharomyces pombe	Whole organism	Total cell lysate	Click chemistry	x		List: 238 hits
SPalmE:507	Chesarino NM et al.	2014	Mus musculus	DC2.4	Total cell lysate	Click chemistry	x		List: 246 hits
SPalmE:508	Chesarino NM et al.	2014	Mus musculus	MEF	Total cell lysate	Click chemistry	Ortholog	in List [YES, SRC]	List: 436 hits
SPalmE:184	Wei X et al.	2014	Homo sapiens	HUVEC	Total cell lysate	ABE	x		Palm decreased: 40 hits Palm increased: 33 hits List: 367 hits
SPalmE:619	Peng T et al.	2015	Homo sapiens	HEK293	Total cell lysate	Alk16 Labeling	x		List: 354 hits
SPalmE:504	Serwa RA et al.	2015	Homo sapiens	RPE-1	Total cell lysate	SILAC, 16-HDYA labeling	x		List: 1348 hits
SPalmE:620	Peng T et al.	2015	Homo sapiens	HEK293	Total cell lysate	Photo cleavable x-alk16 labeling	x		List: 354 hits
SPalmE:506	Morrison E et al.	2015	Homo sapiens	Jurkat	Total cell lysate	Click chemistry, SILAC	x		List: 226 hits
SPalmE:540	Gould NS et al.	2015	Mus musculus	Liver	Total cell lysate	APE	x		List: 780 hits
SPalmE:529	Colquhoun DR et al.	2015	Homo sapiens	174 x CEM.T1	Total cell lysate	Click-IT Palmitic Acid labeling	x		List: 113 hits
SPalmE:510	Santiago-Tirado FH et al.	2015	Cryptococcus neoformans	NA	Total cell lysate	Click chemistry	x		List: 354 hits
SPalmE:509	Santiago-Tirado FH et al.	2015	Cryptococcus neoformans	NA	Total cell lysate	Click chemistry	x		List: 426 hits
SPalmE:505	Morrison E et al.	2015	Homo sapiens	Primary CD4 + T cells	Total cell lysate	ABE, In gel SILAC labeling	x		List: 274 hits
SPalmE:536	Foe IT et al.	2015	Toxoplasma gondii	NA	Total membrane	Click chemistry	x		HC: 210 hits MC: 72 hits
SPalmE:902	Caballero MC et al.	2016	Toxoplasma gondii	whole parasite lysates	NA	ABE	x		HC: 164 hits
SPalmE:829	Upadhyay S et al.	2016	Aspergillus fumigatus	Conidia	NA	ABE	x		List: 133 hits
SPalmE:724	Fang C et al.	2016	Homo sapiens	SW480	NA	ARAC	x		List: 100 hits
SPalmE:909	Thinon E et al.	2016	Mus musculus	Macrophage Raw 264.7	Total cell lysate	Alk16 Labeling	x		HC: 197 hits MC: 143 hits LC: 302 hits
SPalmE:723	Hernandez JL et al.	2016	Homo sapiens	MCF7	Total cell lysate	Alk16 Labeling	x		List: 1353 hits
SPalmE:698	Pinner AL et al.	2016	Homo sapiens	Brain	Total cell lysate	ABE	x		List: 216 hits
SPalmE:993	Shen LF et al.	2017	Mus musculus	Liver	Total membrane	ARAC	x		ZDHHC13 substrates: 16 hits
SPalmE:903	Collins MO et al.	2017	Mus musculus	Forebrain	NA	ABE	x		HC: 1079 hits
SPalmE:907	Edmonds MJ et al.	2017	Rattus norvegicus	Brain	NA	ARAC	x		List: 95 hits
SPalmE:906	Edmonds MJ et al.	2017	Rattus norvegicus	Brain	NA	ABE	x		List: 193 hits
SPalmE:855	Shen LF et al.	2017	Mus musculus	Liver	Total membrane	ARAC	x		List: 865 hits
SPalmE:1183	Thinon E et al.	2018	Homo sapiens	HeLa	Total cell lysate	NH2OH cleavage of thioester bond, Alk16 Labeling	Found	in MC	HC: 132 hits MC: 138 hits LC: 110 hits
SPalmE:1184	Thinon E et al.	2018	Homo sapiens	HeLa	Total cell lysate	ARAC	x		HC: 545 hits MC: 415 hits LC: 219 hits
SPalmE:1182	Thinon E et al.	2018	Mus musculus	Macrophage Raw 264.7	Total cell lysate	ARAC	Ortholog	in LC [YES, SRC]	HC: 198 hits MC: 143 hits LC: 120 hits
SPalmE:1186	Thinon E et al.	2018	Mus musculus	Macrophage Raw 264.7	Total cell lysate	NH2OH cleavage of thioester bond, Alk16 Labeling	x		HC: 177 hits MC: 162 hits LC: 123 hits
SPalmE:1181	Thinon E et al.	2018	Mus musculus	Macrophage Raw 264.7	Total cell lysate	NH2OH cleavage of thioester bond, Alk16 Labeling	x		HC: 244 hits MC: 187 hits LC: 120 hits
SPalmE:1191	Won SJ et al.	2018	Homo sapiens	HEK293T	Total cell lysate	Click chemistry	x		List: 195 hits
SPalmE:1192	Won SJ et al.	2018	Homo sapiens	HAP1	Total cell lysate	Click chemistry	x		List: 984 hits
SPalmE:1193	Won SJ et al.	2018	Homo sapiens	HAP1	Total cell lysate	ARAC	x		List: 1394 hits
SPalmE:1194	Won SJ et al.	2018	Homo sapiens	HAP1	Total cell lysate	ARAC,	Found	in List	List: 1404 hits
SPalmE:1203	Zhang X et al.	2018	Mus musculus	Brain	Total membrane	Enrichment by magnetic nanoparticles	Ortholog	in HC [YES, SRC]	HC: 917 hits MC: 352 hits LC: 15 hits
SPalmE:1259	Dumoulin A et al.	2018	Mus musculus	F11	Total membrane	ABE, NH2OH cleavage of thioester bond, LC-MS	x		HC: 1 hits MC: 10 hits LC: 4 hits
SPalmE:1260	Wang Z et al.	2018	Bos taurus	Lens fiber cell	Total cell lysate	ABE, NH2OH cleavage of thioester bond, LC-MS	x		List: 52 hits
SPalmE:920	Sobocińska J et al.	2018	Mus musculus	Macrophage Raw 264.7	Total cell lysate	Click chemistry	x		LPS treatment: 646 hits
SPalmE:919	Sobocińska J et al.	2018	Mus musculus	Macrophage Raw 264.7	Total cell lysate	Click chemistry	x		List: 646 hits
SPalmE:908	Sobocińska J et al.	2018	Mus musculus	Macrophage Raw 264.7	Total cell lysate	Click chemistry	x		Palm. up with LPS: 156 hits Palm. down with LPS: 189 hits
SPalmE:1185	Thinon E et al.	2018	Homo sapiens	HeLa	Total cell lysate	NH2OH cleavage of thioester bond, LC-MS, Alk16 Labeling	x		Chymotrypsin: 286 hits Trypsin: 1291 hits
SPalmE:1187	Thinon E et al.	2018	Mus musculus	Macrophage Raw 264.7	Total cell lysate	ARAC	x		HC: 281 hits MC: 139 hits LC: 113 hits
SPalmE:1303	Zaręba-Kozioł M et al.	2019	Mus musculus	Brain	Postsynaptic density fraction	ABE, NH2OH cleavage of thioester bond, LC-MS	x
SPalmE:1270	Strassburger K et al.	2019	Drosophila melanogaster	Circa 160 L2 larvae	Total cell lysate	ABE, NH2OH cleavage of thioester bond, PAT KO, MS	x		List: 13 hits
SPalmE:1266	Strassburger K et al.	2019	Drosophila melanogaster	Circa 160 L2 larvae	Total cell lysate	ABE, NH2OH cleavage of thioester bond, PAT KO, MS	x		List: 157 hits
SPalmE:1265	Wang J et al.	2019	Mus musculus	3T3-L1	Total membrane	MS, BioID	x		List: 9 hits
SPalmE:1333	Zaręba-Kozioł M et al.	2019	Mus musculus	Brain	Postsynaptic density fraction	ABE, NH2OH cleavage of thioester bond, LC-MS	x
SPalmE:1433	Zhou B et al.	2019	Homo sapiens	LNCaP	Total cell lysate	NH2OH cleavage of thioester bond, LC-MS, LB-ABE, ABE	x		List: 2929 hits
SPalmE:1432	Zhou B et al.	2019	Homo sapiens	LNCaP	Total cell lysate	ABE, SILAC, NH2OH cleavage of thioester bond, LC-MS	x		List: 590 hits
SPalmE:1434	Wegleiter T et al.	2019	Mus musculus	Neural stem cell	Total cell lysate	ABE, NH2OH cleavage of thioester bond, LC-MS	Ortholog	in List [YES, SRC]	List: 370 hits
SPalmE:1438	Mariscal J et al.	2020	Homo sapiens	PC3	Total membrane	ARAC, NH2OH cleavage of thioester bond, LC-MS, LB-ABE	Found	in HC	HC: 1837 hits
SPalmE:1439	Mariscal J et al.	2020	Homo sapiens	PC3	Large Extracellular Vesicles	ARAC, NH2OH cleavage of thioester bond, LC-MS, LB-ABE	Found	in HC	HC: 1350 hits
SPalmE:1440	Mariscal J et al.	2020	Homo sapiens	PC3	Small Extracellular Vesicles	ARAC, NH2OH cleavage of thioester bond, LC-MS, LB-ABE	x		HC: 600 hits
SPalmE:1435	Morrison E et al.	2020	Homo sapiens	Jurkat	Total cell lysate	ABE, NH2OH cleavage of thioester bond, LC-MS, SILAC	x		Unstimulated: 37 hits
SPalmE:1436	Morrison E et al.	2020	Homo sapiens	Jurkat	Total cell lysate	ABE, NH2OH cleavage of thioester bond, LC-MS, SILAC	x		List: 185 hits
SPalmE:1458	Morrison E et al.	2020	Homo sapiens	Jurkat	Total cell lysate	ABE, NH2OH cleavage of thioester bond, LC-MS, SILAC	x		Stimulated: 148 hits
SPalmE:1437	Mariscal J et al.	2020	Homo sapiens	PC3	Total cell lysate	ARAC, NH2OH cleavage of thioester bond, LC-MS, LB-ABE	Found	in HC	HC: 1869 hits
SPalmE:1450	Zaręba-Kozioł M et al.	2021	Mus musculus	Brain	Synaptoneurosomal fraction	ABE, NH2OH cleavage of thioester bond, LC-MS	Ortholog	in List [YES, SRC]	List: 1093 hits
SPalmE:1444	Miles MR et al.	2021	Homo sapiens	Heart	Total cell lysate	ARAC, NH2OH cleavage of thioester bond, LC-MS	x		List: 687 hits
SPalmE:1447	Pradhan AJ et al.	2021	Homo sapiens	HT-29	Total cell lysate	Labeling of substrate with C20 AlkFA (Alk-18), LC-MS	Found	in List	List: 1173 hits
SPalmE:1448	Pradhan AJ et al.	2021	Homo sapiens	HT-29	Total cell lysate	Labeling of substrate with C20 AlkFA (Alk-18), LC-MS	x		List: 770 hits
SPalmE:1449	Ripamonti M et al.	2021	Mus musculus	NIH-3T3	Total cell lysate	ARAC, NH2OH cleavage of thioester bond, LC-MS	Ortholog	in List [YES, SRC]	List: 199 hits
SPalmE:1445	Miles MR et al.	2021	Rattus norvegicus	Heart	Total cell lysate	ARAC, NH2OH cleavage of thioester bond, LC-MS	Ortholog	in List [YES]	List: 399 hits
SPalmE:1451	Zaręba-Kozioł M et al.	2021	Mus musculus	Brain	Synaptoneurosomal fraction	ABE, NH2OH cleavage of thioester bond, LC-MS	Ortholog	in List [YES, SRC]	List: 1048 hits
SPalmE:1452	Zaręba-Kozioł M et al.	2021	Mus musculus	Brain	Synaptoneurosomal fraction	ABE, NH2OH cleavage of thioester bond, LC-MS	Ortholog	in List [YES, SRC]	List: 1112 hits
SPalmE:1453	Zaręba-Kozioł M et al.	2021	Mus musculus	Brain	Synaptoneurosomal fraction	ABE, NH2OH cleavage of thioester bond, LC-MS	Ortholog	in List [YES, SRC]	List: 1040 hits
SPalmE:1455	Ziemlińska E et al.	2021	Mus musculus	Liver	Total membrane	ABE, NH2OH cleavage of thioester bond, LC-MS	Ortholog	in HC [YES, SRC]	HC: 850 hits MC: 303 hits LC: 21 hits
SPalmE:1446	Miles MR et al.	2021	Canis familiaris	Heart	Total cell lysate	ARAC, NH2OH cleavage of thioester bond, LC-MS	x		List: 464 hits
SPalmE:1454	Ziemlińska E et al.	2021	Mus musculus	Liver	Total membrane	ABE, NH2OH cleavage of thioester bond, LC-MS	Ortholog	in MC [YES, SRC]	HC: 675 hits MC: 360 hits LC: 27 hits
SPalmE:1443	Uzbekova S et al.	2021	Bos taurus	Bovine follicular cells	Total cell lysate	ABE, NH2OH cleavage of thioester bond, LC-MS	x		List: 80 hits
SPalmE:1456	Gao J et al.	2022	Mus musculus	Testis	Total cell lysate	ABE, NH2OH cleavage of thioester bond, LC-MS	Ortholog	in HC [YES, SRC]	HC: 4107 hits
SPalmE:1442	Gorenberg EL et al.	2022	Mus musculus	Brain	Total cell lysate	ARAC, NH2OH cleavage of thioester bond, LC-MS	x		List: 1597 hits
SPalmE:1441	Gorenberg EL et al.	2022	Mus musculus	Brain	Synaptic fraction	ARAC, NH2OH cleavage of thioester bond, LC-MS	x		List: 1378 hits
SPalmE:1457	Gao J et al.	2022	Mus musculus	Testis	Total cell lysate	ABE, NH2OH cleavage of thioester bond, LC-MS	Ortholog	in HC [YES, SRC]	HC: 3870 hits

Summary table by organism

Organism	Total number of palmitoyl-proteome articles	Total number of palmitoyl-proteomes	Number of palmitoyl-proteomes containing this protein or an ortholog	% of palmitoyl-proteomes containing this protein or an ortholog	Orthologs
S. cerevisiae S288c	1	1	0	0.0	NA
R. norvegicus	3	4	1	25.0	YES_RAT
H. sapiens	22	38	7	18.4	NA
M. musculus	23	37	16	43.2	YES_MOUSE , SRC_MOUSE
T. brucei brucei	1	1	0	0.0	NA
P. falciparum	1	2	0	0.0	NA
A. thaliana	1	1	1	100.0	Q9FGB1_ARATH , O22100_ARATH , PBL27_ARATH , PTI13_ARATH , Y1848_ARATH , Y3589_ARATH , CRCK2_ARATH
S. pombe	1	1	0	0.0	NA
C. neoformans var. grubii serotype A strain H99	1	2	0	0.0	NA
T. gondii	2	2	0	0.0	NA
A. fumigatus	1	1	0	0.0	NA
B. taurus	2	2	0	0.0	NA
D. melanogaster	1	2	0	0.0	SRC64_DROME
C. familiaris	1	1	0	0.0	NA

References

Authors	Year	Reference title	PMID
Kang R et al.	2008	Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylation.	19092927
Ren W et al.	2013	Proteomic analysis of protein palmitoylation in adipocytes.	23599907
Marin EP et al.	2012	Endothelial cell palmitoylproteomic identifies novel lipid-modified targets and potential substrates for protein acyl transferases.	22496122
Li Y et al.	2012	DHHC5 protein palmitoylates flotillin-2 and is rapidly degraded on induction of neuronal differentiation in cultured cells.	22081607
Martin BR et al.	2011	Global profiling of dynamic protein palmitoylation.	22056678
Dowal L et al.	2011	Proteomic analysis of palmitoylated platelet proteins.	21813449
Merrick BA et al.	2011	Proteomic profiling of S-acylated macrophage proteins identifies a role for palmitoylation in mitochondrial targeting of phospholipid scramblase 3.	21785166
Wilson JP et al.	2011	Proteomic analysis of fatty-acylated proteins in mammalian cells with chemical reporters reveals S-acylation of histone H3 variants.	21076176
Forrester MT et al.	2011	Site-specific analysis of protein S-acylation by resin-assisted capture.	21044946
Yount JS et al.	2010	Palmitoylome profiling reveals S-palmitoylation-dependent antiviral activity of IFITM3.	20601941
Yang W et al.	2010	Proteome scale characterization of human S-acylated proteins in lipid raft-enriched and non-raft membranes.	19801377
Martin BR et al.	2009	Large-scale profiling of protein palmitoylation in mammalian cells.	19137006
Roth AF et al.	2006	Global analysis of protein palmitoylation in yeast.	16751107
Hemsley PA et al.	2013	A proteomic approach identifies many novel palmitoylated proteins in Arabidopsis.	23252521
Ivaldi C et al.	2012	Proteomic analysis of S-acylated proteins in human B cells reveals palmitoylation of the immune regulators CD20 and CD23.	22615937
Wan J et al.	2013	Tracking brain palmitoylation change: predominance of glial change in a mouse model of Huntington's disease.	24211138
Zhang MM et al.	2013	Quantitative control of protein S-palmitoylation regulates meiotic entry in fission yeast.	23843742
Jones ML et al.	2012	Analysis of protein palmitoylation reveals a pervasive role in Plasmodium development and pathogenesis.	22901544
Wei X et al.	2014	Insulin-regulated protein palmitoylation impacts endothelial cell function.	24357059
Serwa RA et al.	2015	Systems Analysis of Protein Fatty Acylation in Herpes Simplex Virus-Infected Cells Using Chemical Proteomics.	26256475
Morrison E et al.	2015	Quantitative analysis of the human T cell palmitome.	26111759
Chesarino NM et al.	2014	Chemoproteomics reveals Toll-like receptor fatty acylation.	25371237
Santiago-Tirado FH et al.	2015	A Single Protein S-acyl Transferase Acts through Diverse Substrates to Determine Cryptococcal Morphology, Stress Tolerance, and Pathogenic Outcome.	25970403
Emmer BT et al.	2011	Global analysis of protein palmitoylation in African trypanosomes.	21193548
Colquhoun DR et al.	2015	Bioorthogonal mimetics of palmitoyl-CoA and myristoyl-CoA and their subsequent isolation by click chemistry and characterization by mass spectrometry reveal novel acylated host-proteins modified by HIV-1 infection.	25914232
Foe IT et al.	2015	Global Analysis of Palmitoylated Proteins in Toxoplasma gondii.	26468752
Gould NS et al.	2015	Site-Specific Proteomic Mapping Identifies Selectively Modified Regulatory Cysteine Residues in Functionally Distinct Protein Networks.	26165157
Peng T et al.	2015	Bifunctional fatty acid chemical reporter for analyzing S-palmitoylated membrane protein-protein interactions in mammalian cells.	25575299
Pinner AL et al.	2016	Decreased protein S-palmitoylation in dorsolateral prefrontal cortex in schizophrenia.	26876311
Hernandez JL et al.	2016	Correlated S-palmitoylation profiling of Snail-induced epithelial to mesenchymal transition.	27030425
Fang C et al.	2016	Identification of Palmitoylated Transitional Endoplasmic Reticulum ATPase by Proteomic Technique and Pan Antipalmitoylation Antibody.	26865113
Caballero MC et al.	2016	Identification of new palmitoylated proteins in Toxoplasma gondii.	26825284
Upadhyay S et al.	2016	Interactions between Melanin Enzymes and Their Atypical Recruitment to the Secretory Pathway by Palmitoylation.	27879337
Edmonds MJ et al.	2017	Analysis of the brain palmitoyl-proteome using both acyl-biotin exchange and acyl-resin-assisted capture methods.	28607426
Shen LF et al.	2017	Role of S-Palmitoylation by ZDHHC13 in Mitochondrial function and Metabolism in Liver.	28526873
Sobocińska J et al.	2018	Lipopolysaccharide Upregulates Palmitoylated Enzymes of the Phosphatidylinositol Cycle: An Insight from Proteomic Studies.	29217618
Collins MO et al.	2017	Global, site-specific analysis of neuronal protein S-acylation.	28680068
Thinon E et al.	2016	Bioorthogonal Chemical Reporters for Monitoring Unsaturated Fatty-Acylated Proteins.	27350074
Thinon E et al.	2018	Selective Enrichment and Direct Analysis of Protein S-Palmitoylation Sites.	29575903
Zhang X et al.	2018	Ultradeep Palmitoylomics Enabled by Dithiodipyridine-Functionalized Magnetic Nanoparticles.	29660268
Won SJ et al.	2018	Temporal Profiling Establishes a Dynamic S-Palmitoylation Cycle.	29733200
Dumoulin A et al.	2018	S-palmitoylation Is Required for the Control of Growth Cone Morphology of DRG Neurons by CNP-Induced cGMP Signaling.	30319353
Wang Z et al.	2018	Proteomic Analysis of S-Palmitoylated Proteins in Ocular Lens Reveals Palmitoylation of AQP5 and MP20.	30489624
Wang J et al.	2019	DHHC4 and DHHC5 Facilitate Fatty Acid Uptake by Palmitoylating and Targeting CD36 to the Plasma Membrane.	30605677
Strassburger K et al.	2019	Drosophila ZDHHC8 palmitoylates scribble and Ras64B and controls growth and viability.	30735487
Zhou B et al.	2019	Low-background Acyl-biotinyl Exchange Largely Eliminates the Co-isolation of Non-S-acylated Proteins and Enables Deep S-acylproteomic Analysis.	31251020
Zaręba-Kozioł M et al.	2019	Stress-induced changes in the S-palmitoylation and S-nitrosylation of synaptic proteins.	31311849
Wegleiter T et al.	2019	Palmitoylation of BMPR1a regulates neural stem cell fate.	31772009
Morrison E et al.	2020	Dynamic palmitoylation events following T-cell receptor signaling.	32651440
Mariscal J et al.	2020	Comprehensive palmitoyl-proteomic analysis identifies distinct protein signatures for large and small cancer-derived extracellular vesicles.	32944167
Gorenberg EL et al.	2022	Identification of substrates of palmitoyl protein thioesterase 1 highlights roles of depalmitoylation in disulfide bond formation and synaptic function.	35358180
Uzbekova S et al.	2021	Protein Palmitoylation in Bovine Ovarian Follicle.	34769186
Miles MR et al.	2021	Global identification of S-palmitoylated proteins and detection of palmitoylating (DHHC) enzymes in heart.	33636221
Pradhan AJ et al.	2021	Protein acylation by saturated very long chain fatty acids and endocytosis are involved in necroptosis.	33848465
Ripamonti M et al.	2021	Structural and functional analysis of LIM domain-dependent recruitment of paxillin to αvβ3 integrin-positive focal adhesions.	33782527
Zaręba-Kozioł M et al.	2021	S-Palmitoylation of Synaptic Proteins as a Novel Mechanism Underlying Sex-Dependent Differences in Neuronal Plasticity.	34200797
Ziemlińska E et al.	2021	Palm Oil-Rich Diet Affects Murine Liver Proteome and <i>S</i>-Palmitoylome.	34884899
Gao J et al.	2022	Proteome-wide identification of palmitoylated proteins in mouse testis.	35477839