A database built with INDRA combining content from numerous readers and databases. This page allows you to curate the loaded statements. For more information please see the manual.

IndraLab

Statements

databases
phosphosite cbn pc11 biopax bel_lc signor biogrid tas lincs_drug hprd trrust | geneways tees isi trips rlimsp medscan sparser reach
reading

SRC is active
57 21 | 2
SRC phosphorylated on Y419 is active. 10 / 65
57 8 |
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
biopax:pid
No evidence text available
signor
"The increased Src activity is mainly due to the phosphorylation of Tyr-419, rather than the dephosphorylation of Tyr-530 of Src protein. PDGFR, not FAK or EGFR, appears to be the upstream protein tyrosine kinase responsible for the detachment-induced Src activation in the lung tumor cells."
biopax:pid
No evidence text available
Phosphorylated SRC is active. 3 / 3
3 |
signor
"Ror1 binds to and phosphorylates c-src / ror1 kinase-dependent c-src activation"
signor
"Instead, shh rapidly and locally stimulated phosphorylation of the src family kinase (sfk) members src and fyn in a smo-dependent fashion."
signor
"We found that tcptp dephosphorylates and inactivates src family kinases to regulate t cell responses._"
SRC phosphorylated on S17 is active. 2 / 2
2 |
signor
"PKA activated Src both in vitro and in vivo by phosphorylating Src on serine 17 within its amino terminus"
signor
"Pka activated src both in vitro and in vivo by phosphorylating src on serine 17"
SRC phosphorylated on S12 is active. 2 / 2
2 |
signor
"We show that PR55gamma binds c-SRC and modulates the phosphorylation of serine 12 of c-SRC, a residue we demonstrate to be required for JNK activation by c-SRC"
signor
"We conclude that treatment with either UV or PMA induces the phosphorylation of the PKC site Ser12 on c-SRC and that this specific phosphorylation event is significantly diminished in cells overexpressing PR55"
SRC phosphorylated on Y216 is active. 1 / 1
1 |
signor
"This study establishes that her2/hrg signaling selectively upregulates tyr phosphorylation of c-src at tyr-215 located within the sh2 domain, increases c-src kinase activity"
SRC in the cytoplasm is active. 1 / 1
| 1
trips
"Src kinases are activated and relocalize to the cytoplasm during mitosis, but their mitotic function has remained elusive."
SRC phosphorylated on Y530 is active. 1 / 1
1 |
signor
"PTPRG activation by the P1-WD peptide affected the tyrosine phosphorylation of several signaling molecules. Data analysis identified 31 molecules whose phosphorylation was modified in a statistically significant manner (Table I). inhibition of ABL1, BMX, BTK, DAB1, ITGB1, JAK2, KDR, KIT, LIMK1, MET, PDGFRB, SHC1, and VCL correlates with tyrosine dephosphorylation. In contrast, SRC inhibition correlates with hyperphosphorylation of the inhibitory Tyr530 residue and with dephosphorylation of the activatory Tyr419. Moreover, CDK2 and CTTN inhibition correlates with a hyperphosphorylation of the inhibitory Tyr15 and Tyr470, respectively. In contrast, a subgroup of 13 proteins, including BLNK, DOK2, ERBB2, GRIN2B, INSR, PDGFRA, PRKCD, PXN, STAT1, STAT2, STAT3, STAT5A, and ZAP70, appears to be activated by PTPRG activity."
SRC phosphorylated on S75 is active. 1 / 1
1 |
signor
"These results present compelling evidence that cdk5/p35 kinase is responsible for the novel phosphorylation of c-src at ser75 in neuronal cells, raising the intriguing possibility that c-src acts as an effector of cdk5/p35 kinase during neuronal development."
SRC bound to EPHA3 is active. 1 / 1
1 |
signor
"We propose src kinase as a downstream effector that mediates the neuron's response to eph receptor activation."
SRC bound to EPHB2 is active. 1 / 1
1 |
signor
"We propose src kinase as a downstream effector that mediates the neuron's response to eph receptor activation"
SRC-Y527F is active. 1 / 1
| 1
trips
"active Src Y527F"
SRC bound to DOK4 is active. 1 / 1
1 |
signor
"Insulin receptor-phosphorylated irs5/dok4 associates with rasgap, crk, src, and fyn, but not phosphatidylinositol 3-kinase p85, grb2, shp-2, nck, or phospholipase cgamma src homology 2 domains, and activates mapk in cells."
SRC is not active
17 |
SRC phosphorylated on Y530 is inactive. 10 / 15
15 |
signor
"Tyrosine phosphatase epsilonM stimulates migration and survival of porcine aortic endothelial cells by activating c-Src|PTPepsilonM activated c-Src kinase probably by directly dephosphorylating phospho-Tyr527, a negative regulatory site of c-Src."
signor
"The rat tyrosine phosphatase eta increases cell adhesion by activating c-Src through dephosphorylation of its inhibitory phosphotyrosine residue"
signor
"LMWPTP dephosphorylated pY(527)-Src and pY(416)-Src in vitro, with greater specificity for pY(527)Src. Activation of LMWPTP produced strong activation of Src mediated by fast dephosphorylation of pY(527)-Src, followed by slower deactivation of this kinase via dephosphorylation of pY(416)Src."
signor
"Dephosphorylation of Y527 was more pronounced in cells expressing PTPD1 at each time point tested. PTPD1C1108S drastically inhibited Y527 dephosphorylation|Activation of src requires dephosphorylation of src residue Y527. This promotes displacement of the SH2 domain from this residue and subsequent autophosphorylation of residue Y416 within the activation loop"
signor
"Overexpression of PTP1B increased Src specific activity in colon cancer cells by reducing phosphorylation at Y530 of Src."
signor
"Several protein tyrosine phosphatases are capable of activating Src by dephosphorylating Y530 (reviewed in ref. 9). These include PTP-α, PTP-λ, SHP-1, SHP-2, and PTP1B"
signor
"The tyrosine kinase pp60c-src has also been identified as a good substrate of ptp1b leading to an activation of this kinase (27)."
signor
"Protein tyrosine phosphatase alpha (PTPalpha) is believed to dephosphorylate physiologically the Src proto-oncogene at phosphotyrosine (pTyr)527, a critical negative-regulatory residue. It thereby activates Src, and PTPalpha overexpression neoplastically transforms NIH 3T3 cells."
signor
"Several protein tyrosine phosphatases are capable of activating Src by dephosphorylating Y530 (reviewed in ref. 9). These include PTP-α, PTP-λ, SHP-1, SHP-2, and PTP1B"
signor
"Ptpd1 activates src tyrosine kinase and increases the magnitude and duration of epidermal growth factor (egf) signaling."
SRC phosphorylated on Y419 is inactive. 1 / 1
1 |
signor
"Incubation of the inactivated c-Src with PTP1B results in a dose-dependent reactivation of c-Src tyrosine kinase activity. Incubation of c-Src with 2 or 10 g of PTP1B results in partial or full restoration of c-Src kinase activity, respectively. The activation is accompanied by dephosphorylation of c-Src, both of Tyr-419 and of Tyr-530"
SRC bound to PPP2R2C is inactive. 1 / 1
1 |
signor
"We show that PR55gamma binds c-SRC and modulates the phosphorylation of serine 12 of c-SRC, a residue we demonstrate to be required for JNK activation by c-SRC"
SRC affects kinase, and True
12 |
SRC phosphorylated on Y419 is kinase-active. 5 / 5
5 |
bel
"In cells expressing RPTPkappa RNAi, phosphorylation of Src at Tyr527 was increased and (activating) phosphorylation of Src at Tyr416 was reduced."
bel
"The chief phosphorylation sites of Src include tyrosine 416 that results in activation from autophosphorylation and tyrosine 527 that results in inhibition from phosphorylation by C-terminal Src kinase"
bel
"The autophosphorylation and dephosphorylation of Y419 are directly correlated with the level of src TK activity."
bel
"In this paper, we present a comprehensive pathway map of EGFR signaling and other related pathways."
bel
"In parallel to activation, autophosphorylation at Tyr-416 of Src kinase increased Aldosterone led to increased association of Src with HSP84"
SRC phosphorylated on Y418 is kinase-active. 4 / 4
4 |
bel
"Bacterially expressed wild-type PTP-BL phosphatase domain, but not a cata-lytically inactive point mutant of PTP-BL (PTP-BL-CS), dephosphorylated Src specifically on Y418, a tyrosine autophosphorylation site required for Src activation (re-viewed in Bjorge et al., 2000)."
bel
"Ox-PAPC and its component phospholipids induced a rapid and transient phosphorylation of c-src Tyr418, a hallmark of c-src activation, in human aortic endothelial cells (HAEC)."
bel
"ESULTS: TUDC induced a rapid activation of focal adhesion kinase (FAK) and Src, as shown by an increase in Y418 phosphorylation and a decrease in Y529 phosphorylation of Src."
bel
"Here we show that EphB stimulates a metalloproteinase cleavage of ephrinB2, producing a carboxy-terminal fragment that is further processed by PS1/gamma-secretase to produce intracellular peptide ephrinB2/CTF2. This peptide binds Src and inhibits its association with inhibitory kinase Csk, allowing autophosphorylation of Src at residue tyr418."
SRC phosphorylated on Y216 is kinase-active. 1 / 1
1 |
bel
"This study establishes that HER2/HRG signaling selectively upregulates Tyr phosphorylation of c-Src at Tyr-215 located within the SH2 domain, increases c-Src kinase activity and selectively upregulates Tyr phosphorylation of FAK at Tyr-861. HER2-overexpressing tumors showed increased levels of c-Src phosphorylation at Tyr-215. These findings suggest that HER2/HRG influence metastasis of breast cancer cells through a novel signaling pathway involving phosphorylation of FAK tyrosine 861 via activation of c-Src tyrosine 215."
Phosphorylated SRC is kinase-active. 1 / 1
1 |
bel
"c-Src and c-Src-as1 cells displayed similar patterns of overall phosphorylation upon PDGF stimulation"
Tyrosine-phosphorylated SRC is kinase-active. 1 / 1
1 |
bel
"GSK PI3K Phase 2, part 1: List of non-position specific phosphorylation effects on parent protein's activity, derived from existing causal assertions of position-specific phosphorylations on the parent protein activity."
SRC affects kinase, and False
1 |
Tyrosine-phosphorylated SRC is kinase-inactive. 1 / 1
1 |
bel
"GSK PI3K Phase 2, part 1: List of non-position specific phosphorylation effects on parent protein's activity, derived from existing causal assertions of position-specific phosphorylations on the parent protein activity."