You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Toxin, Toxin Target Database.
NameProto-oncogene tyrosine-protein kinase Src
Synonyms
  • 2.7.10.2
  • p60-Src
  • pp60c-src
  • Proto-oncogene c-Src
  • SRC1
Gene NameSRC
OrganismHuman
Amino acid sequence
>lcl|BSEQ0037090|Proto-oncogene tyrosine-protein kinase Src
MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAE
PKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGD
WWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRES
ETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGL
CHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTL
KPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKY
LRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYT
ARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVER
GYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL
Number of residues536
Molecular Weight59834.295
Theoretical pI7.47
GO Classification
Functions
  • receptor binding
  • hormone receptor binding
  • non-membrane spanning protein tyrosine kinase activity
  • ion channel binding
  • heme binding
  • scaffold protein binding
  • SH2 domain binding
  • SH3/SH2 adaptor activity
  • kinase binding
  • ATP binding
  • enzyme binding
  • phosphoprotein binding
  • kinase activity
  • integrin binding
  • protein kinase activity
  • ephrin receptor binding
  • growth factor receptor binding
  • protein tyrosine kinase activity
Processes
  • regulation of podosome assembly
  • stimulatory C-type lectin receptor signaling pathway
  • positive regulation of protein serine/threonine kinase activity
  • positive regulation of integrin activation
  • axon guidance
  • regulation of intracellular estrogen receptor signaling pathway
  • vascular endothelial growth factor receptor signaling pathway
  • regulation of bone resorption
  • regulation of caveolin-mediated endocytosis
  • cell differentiation
  • forebrain development
  • membrane organization
  • bone resorption
  • regulation of cell projection assembly
  • epidermal growth factor receptor signaling pathway
  • ephrin receptor signaling pathway
  • regulation of protein binding
  • regulation of cell cycle
  • integrin-mediated signaling pathway
  • cellular response to fluid shear stress
  • Fc-gamma receptor signaling pathway involved in phagocytosis
  • negative regulation of intrinsic apoptotic signaling pathway
  • cellular response to reactive oxygen species
  • intracellular signal transduction
  • stress fiber assembly
  • innate immune response
  • peptidyl-tyrosine autophosphorylation
  • uterus development
  • oogenesis
  • small GTPase mediated signal transduction
  • regulation of early endosome to late endosome transport
  • peptidyl-tyrosine phosphorylation
  • viral process
  • negative regulation of protein homooligomerization
  • positive regulation of epithelial cell migration
  • positive regulation of peptidyl-tyrosine phosphorylation
  • positive regulation of protein kinase B signaling
  • regulation of cell-cell adhesion
  • cell cycle
  • regulation of cell proliferation
  • response to interleukin-1
  • platelet activation
  • cellular response to platelet-derived growth factor stimulus
  • signal transduction
  • leukocyte migration
  • negative regulation of focal adhesion assembly
  • negative regulation of telomerase activity
  • positive regulation of ERK1 and ERK2 cascade
  • protein destabilization
  • positive regulation of canonical Wnt signaling pathway
  • progesterone receptor signaling pathway
  • regulation of epithelial cell migration
  • protein autophosphorylation
  • fibroblast growth factor receptor signaling pathway
  • substrate adhesion-dependent cell spreading
  • positive regulation of lamellipodium morphogenesis
  • transforming growth factor beta receptor signaling pathway
  • negative regulation of apoptotic process
  • negative regulation of mitochondrial depolarization
  • negative regulation of extrinsic apoptotic signaling pathway
  • branching involved in mammary gland duct morphogenesis
  • cell adhesion
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic process
  • negative regulation of telomere maintenance via telomerase
  • osteoclast development
  • negative regulation of anoikis
  • blood coagulation
  • neurotrophin TRK receptor signaling pathway
  • cellular response to peptide hormone stimulus
  • angiotensin-activated signaling pathway involved in heart process
  • signal complex assembly
  • positive regulation of podosome assembly
  • Ras protein signal transduction
  • regulation of vascular permeability
  • cellular response to progesterone stimulus
  • T cell costimulation
Components
  • mitochondrial inner membrane
  • ruffle membrane
  • late endosome
  • plasma membrane
  • lysosome
  • caveola
  • cytoplasm
  • mitochondrion
  • actin filament
  • cytosol
  • extracellular exosome
  • extrinsic component of cytoplasmic side of plasma membrane
  • perinuclear region of cytoplasm
  • nucleus
General FunctionSh3/sh2 adaptor activity
Specific FunctionNon-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). 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). 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. Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors. Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation. 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 ADRBK1, 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. 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. 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. Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase. Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731'. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-128'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity. Required for podosome formation (By similarity).
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID10635153
UniProtKB IDP12931
UniProtKB Entry NameSRC_HUMAN
Cellular LocationCell membrane
Gene sequence
>lcl|BSEQ0021959|Proto-oncogene tyrosine-protein kinase Src (SRC)
ATGGGTAGCAACAAGAGCAAGCCCAAGGATGCCAGCCAGCGGCGCCGCAGCCTGGAGCCC
GCCGAGAACGTGCACGGCGCTGGCGGGGGCGCTTTCCCCGCCTCGCAGACCCCCAGCAAG
CCAGCCTCGGCCGACGGCCACCGCGGCCCCAGCGCGGCCTTCGCCCCCGCGGCCGCCGAG
CCCAAGCTGTTCGGAGGCTTCAACTCCTCGGACACCGTCACCTCCCCGCAGAGGGCGGGC
CCGCTGGCCGGTGGAGTGACCACCTTTGTGGCCCTCTATGACTATGAGTCTAGGACGGAG
ACAGACCTGTCCTTCAAGAAAGGCGAGCGGCTCCAGATTGTCAACAACACAGAGGGAGAC
TGGTGGCTGGCCCACTCGCTCAGCACAGGACAGACAGGCTACATCCCCAGCAACTACGTG
GCGCCCTCCGACTCCATCCAGGCTGAGGAGTGGTATTTTGGCAAGATCACCAGACGGGAG
TCAGAGCGGTTACTGCTCAATGCAGAGAACCCGAGAGGGACCTTCCTCGTGCGAGAAAGT
GAGACCACGAAAGGTGCCTACTGCCTCTCAGTGTCTGACTTCGACAACGCCAAGGGCCTC
AACGTGAAGCACTACAAGATCCGCAAGCTGGACAGCGGCGGCTTCTACATCACCTCCCGC
ACCCAGTTCAACAGCCTGCAGCAGCTGGTGGCCTACTACTCCAAACACGCCGATGGCCTG
TGCCACCGCCTCACCACCGTGTGCCCCACGTCCAAGCCGCAGACTCAGGGCCTGGCCAAG
GATGCCTGGGAGATCCCTCGGGAGTCGCTGCGGCTGGAGGTCAAGCTGGGCCAGGGCTGC
TTTGGCGAGGTGTGGATGGGGACCTGGAACGGTACCACCAGGGTGGCCATCAAAACCCTG
AAGCCTGGCACGATGTCTCCAGAGGCCTTCCTGCAGGAGGCCCAGGTCATGAAGAAGCTG
AGGCATGAGAAGCTGGTGCAGTTGTATGCTGTGGTTTCAGAGGAGCCCATTTACATCGTC
ACGGAGTACATGAGCAAGGGGAGTTTGCTGGACTTTCTCAAGGGGGAGACAGGCAAGTAC
CTGCGGCTGCCTCAGCTGGTGGACATGGCTGCTCAGATCGCCTCAGGCATGGCGTACGTG
GAGCGGATGAACTACGTCCACCGGGACCTTCGTGCAGCCAACATCCTGGTGGGAGAGAAC
CTGGTGTGCAAAGTGGCCGACTTTGGGCTGGCTCGGCTCATTGAAGACAATGAGTACACG
GCGCGGCAAGGTGCCAAATTCCCCATCAAGTGGACGGCTCCAGAAGCTGCCCTCTATGGC
CGCTTCACCATCAAGTCGGACGTGTGGTCCTTCGGGATCCTGCTGACTGAGCTCACCACA
AAGGGACGGGTGCCCTACCCTGGGATGGTGAACCGCGAGGTGCTGGACCAGGTGGAGCGG
GGCTACCGGATGCCCTGCCCGCCGGAGTGTCCCGAGTCCCTGCACGACCTCATGTGCCAG
TGCTGGCGGAAGGAGCCTGAGGAGCGGCCCACCTTCGAGTACCTGCAGGCCTTCCTGGAG
GACTACTTCACGTCCACCGAGCCCCAGTACCAGCCCGGGGAGAACCTCTAG
GenBank Gene IDAL133293
GeneCard IDNot Available
GenAtlas IDSRC
HGNC IDHGNC:11283
Chromosome Location20
Locus20q12-q13
References
  1. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. 11780052
  2. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. 15489334
  3. Tanaka A, Gibbs CP, Arthur RR, Anderson SK, Kung HJ, Fujita DJ: DNA sequence encoding the amino-terminal region of the human c-src protein: implications of sequence divergence among src-type kinase oncogenes. Mol Cell Biol. 1987 May;7(5):1978-83. 3299057
  4. Anderson SK, Gibbs CP, Tanaka A, Kung HJ, Fujita DJ: Human cellular src gene: nucleotide sequence and derived amino acid sequence of the region coding for the carboxy-terminal two-thirds of pp60c-src. Mol Cell Biol. 1985 May;5(5):1122-9. 2582238
  5. Pyper JM, Bolen JB: Neuron-specific splicing of C-SRC RNA in human brain. J Neurosci Res. 1989 Sep;24(1):89-96. 2681803
  6. Parker RC, Mardon G, Lebo RV, Varmus HE, Bishop JM: Isolation of duplicated human c-src genes located on chromosomes 1 and 20. Mol Cell Biol. 1985 Apr;5(4):831-8. 2581127
  7. Smart JE, Oppermann H, Czernilofsky AP, Purchio AF, Erikson RL, Bishop JM: Characterization of sites for tyrosine phosphorylation in the transforming protein of Rous sarcoma virus (pp60v-src) and its normal cellular homologue (pp60c-src). Proc Natl Acad Sci U S A. 1981 Oct;78(10):6013-7. 6273838
  8. Rosen N, Bolen JB, Schwartz AM, Cohen P, DeSeau V, Israel MA: Analysis of pp60c-src protein kinase activity in human tumor cell lines and tissues. J Biol Chem. 1986 Oct 15;261(29):13754-9. 3093483
  9. Cartwright CA, Kamps MP, Meisler AI, Pipas JM, Eckhart W: pp60c-src activation in human colon carcinoma. J Clin Invest. 1989 Jun;83(6):2025-33. 2498394
  10. Pyper JM, Bolen JB: Identification of a novel neuronal C-SRC exon expressed in human brain. Mol Cell Biol. 1990 May;10(5):2035-40. 1691439
  11. Kaplan KB, Bibbins KB, Swedlow JR, Arnaud M, Morgan DO, Varmus HE: Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527. EMBO J. 1994 Oct 17;13(20):4745-56. 7525268
  12. Stover DR, Liebetanz J, Lydon NB: Cdc2-mediated modulation of pp60c-src activity. J Biol Chem. 1994 Oct 28;269(43):26885-9. 7929427
  13. David-Pfeuty T, Nouvian-Dooghe Y: Highly specific antibody to Rous sarcoma virus src gene product recognizes nuclear and nucleolar antigens in human cells. J Virol. 1995 Mar;69(3):1699-713. 7853507
  14. Rabinowich H, Manciulea M, Metes D, Sulica A, Herberman RB, Corey SJ, Whiteside TL: Physical and functional association of Fc mu receptor on human natural killer cells with the zeta- and Fc epsilon RI gamma-chains and with src family protein tyrosine kinases. J Immunol. 1996 Aug 15;157(4):1485-91. 8759729
  15. Grano M, Galimi F, Zambonin G, Colucci S, Cottone E, Zallone AZ, Comoglio PM: Hepatocyte growth factor is a coupling factor for osteoclasts and osteoblasts in vitro. Proc Natl Acad Sci U S A. 1996 Jul 23;93(15):7644-8. 8755529
  16. Yang EB, Zhang K, Cheng LY, Mack P: Butein, a specific protein tyrosine kinase inhibitor. Biochem Biophys Res Commun. 1998 Apr 17;245(2):435-8. 9571170
  17. Chang BY, Conroy KB, Machleder EM, Cartwright CA: RACK1, a receptor for activated C kinase and a homolog of the beta subunit of G proteins, inhibits activity of src tyrosine kinases and growth of NIH 3T3 cells. Mol Cell Biol. 1998 Jun;18(6):3245-56. 9584165
  18. Luttrell LM, Ferguson SS, Daaka Y, Miller WE, Maudsley S, Della Rocca GJ, Lin F, Kawakatsu H, Owada K, Luttrell DK, Caron MG, Lefkowitz RJ: Beta-arrestin-dependent formation of beta2 adrenergic receptor-Src protein kinase complexes. Science. 1999 Jan 29;283(5402):655-61. 9924018
  19. Miller WE, Maudsley S, Ahn S, Khan KD, Luttrell LM, Lefkowitz RJ: beta-arrestin1 interacts with the catalytic domain of the tyrosine kinase c-SRC. Role of beta-arrestin1-dependent targeting of c-SRC in receptor endocytosis. J Biol Chem. 2000 Apr 14;275(15):11312-9. 10753943
  20. Rebhun JF, Chen H, Quilliam LA: Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral. J Biol Chem. 2000 May 5;275(18):13406-10. 10747847
  21. Giglione C, Gonfloni S, Parmeggiani A: Differential actions of p60c-Src and Lck kinases on the Ras regulators p120-GAP and GDP/GTP exchange factor CDC25Mm. Eur J Biochem. 2001 Jun;268(11):3275-83. 11389730
  22. Li Y, Kuwahara H, Ren J, Wen G, Kufe D: The c-Src tyrosine kinase regulates signaling of the human DF3/MUC1 carcinoma-associated antigen with GSK3 beta and beta-catenin. J Biol Chem. 2001 Mar 2;276(9):6061-4. Epub 2001 Jan 10. 11152665
  23. Chang BY, Chiang M, Cartwright CA: The interaction of Src and RACK1 is enhanced by activation of protein kinase C and tyrosine phosphorylation of RACK1. J Biol Chem. 2001 Jun 8;276(23):20346-56. Epub 2001 Mar 8. 11279199
  24. Korkaya H, Jameel S, Gupta D, Tyagi S, Kumar R, Zafrullah M, Mazumdar M, Lal SK, Xiaofang L, Sehgal D, Das SR, Sahal D: The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and activates MAPK. J Biol Chem. 2001 Nov 9;276(45):42389-400. Epub 2001 Aug 22. 11518702
  25. Lee H, Park DS, Wang XB, Scherer PE, Schwartz PE, Lisanti MP: Src-induced phosphorylation of caveolin-2 on tyrosine 19. Phospho-caveolin-2 (Tyr(P)19) is localized near focal adhesions, remains associated with lipid rafts/caveolae, but no longer forms a high molecular mass hetero-oligomer with caveolin-1. J Biol Chem. 2002 Sep 13;277(37):34556-67. Epub 2002 Jun 28. 12091389
  26. Wong CW, McNally C, Nickbarg E, Komm BS, Cheskis BJ: Estrogen receptor-interacting protein that modulates its nongenomic activity-crosstalk with Src/Erk phosphorylation cascade. Proc Natl Acad Sci U S A. 2002 Nov 12;99(23):14783-8. Epub 2002 Nov 1. 12415108
  27. Miyazaki T, Neff L, Tanaka S, Horne WC, Baron R: Regulation of cytochrome c oxidase activity by c-Src in osteoclasts. J Cell Biol. 2003 Mar 3;160(5):709-18. 12615910
  28. Vindis C, Cerretti DP, Daniel TO, Huynh-Do U: EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote chemotaxis. J Cell Biol. 2003 Aug 18;162(4):661-71. 12925710
  29. Kamath JR, Liu R, Enstrom AM, Lou Q, Lam KS: Development and characterization of potent and specific peptide inhibitors of p60c-src protein tyrosine kinase using pseudosubstrate-based inhibitor design approach. J Pept Res. 2003 Dec;62(6):260-8. 14632929
  30. Taniyama Y, Weber DS, Rocic P, Hilenski L, Akers ML, Park J, Hemmings BA, Alexander RW, Griendling KK: Pyk2- and Src-dependent tyrosine phosphorylation of PDK1 regulates focal adhesions. Mol Cell Biol. 2003 Nov;23(22):8019-29. 14585963
  31. Wang XB, Lee H, Capozza F, Marmon S, Sotgia F, Brooks JW, Campos-Gonzalez R, Lisanti MP: Tyrosine phosphorylation of caveolin-2 at residue 27: differences in the spatial and temporal behavior of phospho-Cav-2 (pY19 and pY27). Biochemistry. 2004 Nov 2;43(43):13694-706. 15504032
  32. Kim M, Tezuka T, Tanaka K, Yamamoto T: Cbl-c suppresses v-Src-induced transformation through ubiquitin-dependent protein degradation. Oncogene. 2004 Mar 4;23(9):1645-55. 14661060
  33. Benes CH, Wu N, Elia AE, Dharia T, Cantley LC, Soltoff SP: The C2 domain of PKCdelta is a phosphotyrosine binding domain. Cell. 2005 Apr 22;121(2):271-80. 15851033
  34. Yang K, Kim JH, Kim HJ, Park IS, Kim IY, Yang BS: Tyrosine 740 phosphorylation of discoidin domain receptor 2 by Src stimulates intramolecular autophosphorylation and Shc signaling complex formation. J Biol Chem. 2005 Nov 25;280(47):39058-66. Epub 2005 Sep 26. 16186108
  35. Franco M, Furstoss O, Simon V, Benistant C, Hong WJ, Roche S: The adaptor protein Tom1L1 is a negative regulator of Src mitogenic signaling induced by growth factors. Mol Cell Biol. 2006 Mar;26(5):1932-47. 16479011
  36. Maudsley S, Davidson L, Pawson AJ, Freestone SH, Lopez de Maturana R, Thomson AA, Millar RP: Gonadotropin-releasing hormone functionally antagonizes testosterone activation of the human androgen receptor in prostate cells through focal adhesion complexes involving Hic-5. Neuroendocrinology. 2006;84(5):285-300. Epub 2007 Jan 4. 17202804
  37. Huang H, Lu FI, Jia S, Meng S, Cao Y, Wang Y, Ma W, Yin K, Wen Z, Peng J, Thisse C, Thisse B, Meng A: Amotl2 is essential for cell movements in zebrafish embryo and regulates c-Src translocation. Development. 2007 Mar;134(5):979-88. 17293535
  38. Di Stefano P, Damiano L, Cabodi S, Aramu S, Tordella L, Praduroux A, Piva R, Cavallo F, Forni G, Silengo L, Tarone G, Turco E, Defilippi P: p140Cap protein suppresses tumour cell properties, regulating Csk and Src kinase activity. EMBO J. 2007 Jun 20;26(12):2843-55. Epub 2007 May 24. 17525734
  39. Jeulin C, Seltzer V, Bailbe D, Andreau K, Marano F: EGF mediates calcium-activated chloride channel activation in the human bronchial epithelial cell line 16HBE14o-: involvement of tyrosine kinase p60c-src. Am J Physiol Lung Cell Mol Physiol. 2008 Sep;295(3):L489-96. doi: 10.1152/ajplung.90282.2008. Epub 2008 Jun 27. 18586953
  40. Yang KJ, Shin S, Piao L, Shin E, Li Y, Park KA, Byun HS, Won M, Hong J, Kweon GR, Hur GM, Seok JH, Chun T, Brazil DP, Hemmings BA, Park J: Regulation of 3-phosphoinositide-dependent protein kinase-1 (PDK1) by Src involves tyrosine phosphorylation of PDK1 and Src homology 2 domain binding. J Biol Chem. 2008 Jan 18;283(3):1480-91. Epub 2007 Nov 16. 18024423
  41. Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. 18088087
  42. Le Romancer M, Treilleux I, Leconte N, Robin-Lespinasse Y, Sentis S, Bouchekioua-Bouzaghou K, Goddard S, Gobert-Gosse S, Corbo L: Regulation of estrogen rapid signaling through arginine methylation by PRMT1. Mol Cell. 2008 Jul 25;31(2):212-21. doi: 10.1016/j.molcel.2008.05.025. 18657504
  43. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. 18691976
  44. Voss M, Lettau M, Janssen O: Identification of SH3 domain interaction partners of human FasL (CD178) by phage display screening. BMC Immunol. 2009 Oct 6;10:53. doi: 10.1186/1471-2172-10-53. 19807924
  45. Johnsen IB, Nguyen TT, Bergstroem B, Fitzgerald KA, Anthonsen MW: The tyrosine kinase c-Src enhances RIG-I (retinoic acid-inducible gene I)-elicited antiviral signaling. J Biol Chem. 2009 Jul 10;284(28):19122-31. doi: 10.1074/jbc.M808233200. Epub 2009 May 6. 19419966
  46. Chabot C, Spring K, Gratton JP, Elchebly M, Royal I: New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival. Mol Cell Biol. 2009 Jan;29(1):241-53. doi: 10.1128/MCB.01374-08. Epub 2008 Oct 20. 18936167
  47. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. 19369195
  48. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. 19690332
  49. Yao X, Balamurugan P, Arvey A, Leslie C, Zhang L: Heme controls the regulation of protein tyrosine kinases Jak2 and Src. Biochem Biophys Res Commun. 2010 Dec 3;403(1):30-5. doi: 10.1016/j.bbrc.2010.10.101. Epub 2010 Oct 29. 21036157
  50. Goh YM, Cinghu S, Hong ET, Lee YS, Kim JH, Jang JW, Li YH, Chi XZ, Lee KS, Wee H, Ito Y, Oh BC, Bae SC: Src kinase phosphorylates RUNX3 at tyrosine residues and localizes the protein in the cytoplasm. J Biol Chem. 2010 Mar 26;285(13):10122-9. doi: 10.1074/jbc.M109.071381. Epub 2010 Jan 25. 20100835
  51. Ryan PE, Sivadasan-Nair N, Nau MM, Nicholas S, Lipkowitz S: The N terminus of Cbl-c regulates ubiquitin ligase activity by modulating affinity for the ubiquitin-conjugating enzyme. J Biol Chem. 2010 Jul 30;285(31):23687-98. doi: 10.1074/jbc.M109.091157. Epub 2010 Jun 4. 20525694
  52. Mund T, Pelham HR: Regulation of PTEN/Akt and MAP kinase signaling pathways by the ubiquitin ligase activators Ndfip1 and Ndfip2. Proc Natl Acad Sci U S A. 2010 Jun 22;107(25):11429-34. doi: 10.1073/pnas.0911714107. Epub 2010 Jun 7. 20534535
  53. Chan W, Sit ST, Manser E: The Cdc42-associated kinase ACK1 is not autoinhibited but requires Src for activation. Biochem J. 2011 Apr 15;435(2):355-64. doi: 10.1042/BJ20102156. 21309750
  54. Pan Q, Qiao F, Gao C, Norman B, Optican L, Zelenka PS: Cdk5 targets active Src for ubiquitin-dependent degradation by phosphorylating Src(S75). Cell Mol Life Sci. 2011 Oct;68(20):3425-36. doi: 10.1007/s00018-011-0638-1. Epub 2011 Mar 27. 21442427
  55. Brown MT, Cooper JA: Regulation, substrates and functions of src. Biochim Biophys Acta. 1996 Jun 7;1287(2-3):121-49. 8672527
  56. Thomas SM, Brugge JS: Cellular functions regulated by Src family kinases. Annu Rev Cell Dev Biol. 1997;13:513-609. 9442882
  57. Ma YC, Huang XY: Novel regulation and function of Src tyrosine kinase. Cell Mol Life Sci. 2002 Mar;59(3):456-62. 11964124
  58. Wang Y, Cao H, Chen J, McNiven MA: A direct interaction between the large GTPase dynamin-2 and FAK regulates focal adhesion dynamics in response to active Src. Mol Biol Cell. 2011 May;22(9):1529-38. doi: 10.1091/mbc.E10-09-0785. Epub 2011 Mar 16. 21411625
  59. Zhang P, Guo A, Possemato A, Wang C, Beard L, Carlin C, Markowitz SD, Polakiewicz RD, Wang Z: Identification and functional characterization of p130Cas as a substrate of protein tyrosine phosphatase nonreceptor 14. Oncogene. 2013 Apr 18;32(16):2087-95. doi: 10.1038/onc.2012.220. Epub 2012 Jun 18. 22710723
  60. Yoshida S, Tsutsumi S, Muhlebach G, Sourbier C, Lee MJ, Lee S, Vartholomaiou E, Tatokoro M, Beebe K, Miyajima N, Mohney RP, Chen Y, Hasumi H, Xu W, Fukushima H, Nakamura K, Koga F, Kihara K, Trepel J, Picard D, Neckers L: Molecular chaperone TRAP1 regulates a metabolic switch between mitochondrial respiration and aerobic glycolysis. Proc Natl Acad Sci U S A. 2013 Apr 23;110(17):E1604-12. doi: 10.1073/pnas.1220659110. Epub 2013 Apr 5. 23564345
  61. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. 24275569
  62. Xu W, Harrison SC, Eck MJ: Three-dimensional structure of the tyrosine kinase c-Src. Nature. 1997 Feb 13;385(6617):595-602. 9024657
  63. Charifson PS, Shewchuk LM, Rocque W, Hummel CW, Jordan SR, Mohr C, Pacofsky GJ, Peel MR, Rodriguez M, Sternbach DD, Consler TG: Peptide ligands of pp60(c-src) SH2 domains: a thermodynamic and structural study. Biochemistry. 1997 May 27;36(21):6283-93. 9174343
  64. Xu RX, Word JM, Davis DG, Rink MJ, Willard DH Jr, Gampe RT Jr: Solution structure of the human pp60c-src SH2 domain complexed with a phosphorylated tyrosine pentapeptide. Biochemistry. 1995 Feb 21;34(7):2107-21. 7532003
  65. Takeshita K, Tezuka T, Isozaki Y, Yamashita E, Suzuki M, Kim M, Yamanashi Y, Yamamoto T, Nakagawa A: Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c. J Biochem. 2012 Nov;152(5):487-95. doi: 10.1093/jb/mvs085. Epub 2012 Aug 9. 22888118
  66. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. 17344846