Product: Phospho-Src (Tyr419) Antibody
Catalog: AF3162
Description: Rabbit polyclonal antibody to Phospho-Src (Tyr419)
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Zebrafish, Bovine, Horse, Sheep, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.: 60kDa; 60kD(Calculated).
Uniprot: P12931
RRID: AB_2834597

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 100ul $280 In stock
 200ul $350 In stock

Lead Time: Same day delivery

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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Prediction:
Pig(100%), Zebrafish(100%), Bovine(100%), Horse(100%), Sheep(100%), Rabbit(100%), Dog(100%), Chicken(100%), Xenopus(100%)
Clonality:
Polyclonal
Specificity:
Phospho-Src (Tyr419) Antibody detects endogenous levels of Src only when phosphorylated at Tyrosine 419.
RRID:
AB_2834597
Cite Format: Affinity Biosciences Cat# AF3162, RRID:AB_2834597.
Conjugate:
Unconjugated.
Purification:
The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

ASV; Avian sarcoma virus; c SRC; CDNA FLJ14219 fis clone NT2RP3003800 highly similar to Rattus norvegicus tyrosine protein kinase pp60 c src mRNA; cSrc; EC 2.7.10.2; Neuronal CSRC tyrosine specific protein kinase; Neuronal SRC; Oncogene SRC; OTTHUMP00000174476; OTTHUMP00000174477; p60 Src; p60-Src; p60Src; pp60c src; pp60c-src; pp60csrc; Proto oncogene tyrosine protein kinase Src; Proto-oncogene c-Src; Proto-oncogene tyrosine-protein kinase Src; Protooncogene SRC; Protooncogene SRC Rous sarcoma; Src; SRC Oncogene; SRC proto oncogene non receptor tyrosine kinase; SRC_HUMAN; SRC1; Tyrosine kinase pp60c src; Tyrosine protein kinase SRC 1; Tyrosine protein kinase SRC1; v src avian sarcoma (Schmidt Ruppin A2) viral oncogene homolog; V src sarcoma (Schmidt Ruppin A 2) viral oncogene homolog (avian); v src sarcoma (Schmidt Ruppin A 2) viral oncogene homolog avian;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Expression:
P12931 SRC_HUMAN:

Expressed ubiquitously. Platelets, neurons and osteoclasts express 5-fold to 200-fold higher levels than most other tissues.

Description:
This gene is highly similar to the v-src gene of Rous sarcoma virus. This proto-oncogene may play a role in the regulation of embryonic development and cell growth. The protein encoded by this gene is a tyrosine-protein kinase whose activity can be inhibited by phosphorylation by c-SRC kinase.
Sequence:
MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLRHEKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKGETGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQPGENL

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Horse
100
Bovine
100
Sheep
100
Dog
100
Xenopus
100
Zebrafish
100
Chicken
100
Rabbit
100
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - P12931 As Substrate

Site PTM Type Enzyme
G2 Myristoylation
S12 Phosphorylation Q05655 (PRKCD)
S17 Phosphorylation P17612 (PRKACA)
S35 Phosphorylation
T37 Phosphorylation
S39 Phosphorylation
S43 Phosphorylation
S51 Phosphorylation
K62 Acetylation
S69 Phosphorylation
S70 Phosphorylation
T72 Phosphorylation
T74 Phosphorylation
S75 Phosphorylation Q00535 (CDK5)
Y93 Phosphorylation
S97 Phosphorylation
S104 Phosphorylation
Y139 Phosphorylation P09619 (PDGFRB)
T182 Phosphorylation
T183 Phosphorylation
Y187 Phosphorylation
Y216 Phosphorylation P12931 (SRC)
T246 Phosphorylation
T250 Phosphorylation
T255 Phosphorylation
S269 Phosphorylation
T304 Phosphorylation
S306 Phosphorylation
Y338 Phosphorylation P12931 (SRC)
S348 Phosphorylation
Y385 Phosphorylation
Y419 Phosphorylation P12931 (SRC) , P16234 (PDGFRA) , P09619 (PDGFRB) , P17612 (PRKACA)
T420 Phosphorylation
K426 Acetylation
K426 Ubiquitination
K430 Acetylation
K430 Ubiquitination
Y439 Phosphorylation
Y514 Phosphorylation
Y522 Phosphorylation
S525 Phosphorylation
T526 Phosphorylation
Y530 Phosphorylation P41240 (CSK) , P42679 (MATK) , P12931 (SRC)

PTMs - P12931 As Enzyme

Substrate Site Source
A1X283 (SH3PXD2B) Y508 Uniprot
O00560 (SDCBP) Y4 Uniprot
O14641 (DVL2) Y18 Uniprot
O14641 (DVL2) Y27 Uniprot
O14641 (DVL2) Y275 Uniprot
O14641 (DVL2) Y295 Uniprot
O14641 (DVL2) Y463 Uniprot
O14746 (TERT) Y707 Uniprot
O14920 (IKBKB) Y188 Uniprot
O14920 (IKBKB) Y199 Uniprot
O14939 (PLD2) Y511 Uniprot
O14965 (AURKA) Y148 Uniprot
O14976 (GAK) Y412 Uniprot
O15056 (SYNJ2) Y490 Uniprot
O15162 (PLSCR1) Y69 Uniprot
O15162 (PLSCR1) Y74 Uniprot
O15259 (NPHP1) Y721 Uniprot
O15357 (INPPL1) Y986 Uniprot
O15357 (INPPL1) Y987 Uniprot
O15455 (TLR3) Y759 Uniprot
O15492 (RGS16) Y168 Uniprot
O15492 (RGS16) Y177 Uniprot
O15530-4 (PDPK1) Y9 Uniprot
O15530 (PDPK1) T33 Uniprot
O15530-4 (PDPK1) Y246 Uniprot
O15530-4 (PDPK1) Y358 Uniprot
O15530 (PDPK1) Y373 Uniprot
O15530 (PDPK1) Y376 Uniprot
O15530-1 (PDPK1) Y485 Uniprot
O15530 (PDPK1) T513 Uniprot
O43353 (RIPK2) Y381 Uniprot
O43490 (PROM1) Y828 Uniprot
O43490 (PROM1) Y852 Uniprot
O43597 (SPRY2) Y55 Uniprot
O43613 (HCRTR1) Y358 Uniprot
O43823 (AKAP8) Y51 Uniprot
O43823 (AKAP8) Y53 Uniprot
O43823 (AKAP8) Y80 Uniprot
O43823 (AKAP8) Y146 Uniprot
O43823 (AKAP8) Y150 Uniprot
O43823 (AKAP8) Y152 Uniprot
O43823 (AKAP8) Y154 Uniprot
O43823 (AKAP8) Y170 Uniprot
O43823 (AKAP8) Y311 Uniprot
O43823 (AKAP8) Y436 Uniprot
O43823 (AKAP8) Y539 Uniprot
O60331 (PIP5K1C) Y649 Uniprot
O60496 (DOK2) Y271 Uniprot
O60496 (DOK2) Y299 Uniprot
O60496 (DOK2) Y345 Uniprot
O60716-6 (CTNND1) Y96 Uniprot
O60716-6 (CTNND1) Y112 Uniprot
O60716 (CTNND1) Y217 Uniprot
O60716 (CTNND1) Y228 Uniprot
O60716-6 (CTNND1) Y257 Uniprot
O60716-6 (CTNND1) Y280 Uniprot
O60716-6 (CTNND1) Y291 Uniprot
O60716-6 (CTNND1) Y296 Uniprot
O60716-6 (CTNND1) Y302 Uniprot
O75116 (ROCK2) Y722 Uniprot
O75553-6 (DAB1) Y185 Uniprot
O75553-6 (DAB1) Y198 Uniprot
O75553-6 (DAB1) Y200 Uniprot
O75553-6 (DAB1) Y220 Uniprot
O75553-6 (DAB1) Y232 Uniprot
O75955 (FLOT1) Y56 Uniprot
O75955 (FLOT1) Y149 Uniprot
O95297-1 (MPZL1) Y241 Uniprot
O95297 (MPZL1) Y263 Uniprot
P00338 (LDHA) Y10 Uniprot
P00519 (ABL1) Y226 Uniprot
P00519-2 (ABL1) Y245 Uniprot
P00519-1 (ABL1) Y393 Uniprot
P00519-2 (ABL1) Y412 Uniprot
P00519-2 (ABL1) Y488 Uniprot
P00533 (EGFR) Y727 Uniprot
P00533 (EGFR) Y764 Uniprot
P00533 (EGFR) Y869 Uniprot
P00533 (EGFR) Y915 Uniprot
P00533-1 (EGFR) Y944 Uniprot
P00533-1 (EGFR) Y998 Uniprot
P00533 (EGFR) Y1016 Uniprot
P00533-1 (EGFR) Y1092 Uniprot
P00533 (EGFR) Y1110 Uniprot
P00533 (EGFR) Y1125 Uniprot
P00533 (EGFR) Y1172 Uniprot
P01111 (NRAS) Y32 Uniprot
P01112 (HRAS) Y32 Uniprot
P01112 (HRAS) Y64 Uniprot
P01112 (HRAS) Y96 Uniprot
P01350 (GAST) Y87 Uniprot
P01889 (HLA-B) Y344 Uniprot
P01892 (HLA-A) Y344 Uniprot
P02786 (TFRC) Y20 Uniprot
P03372 (ESR1) Y537 Uniprot
P04049-1 (RAF1) S338 Uniprot
P04049-1 (RAF1) S339 Uniprot
P04049-1 (RAF1) Y340 Uniprot
P04049-1 (RAF1) Y341 Uniprot
P04083 (ANXA1) Y21 Uniprot
P04083 (ANXA1) T216 Uniprot
P04406 (GAPDH) Y42 Uniprot
P04439 (HLA-A) Y344 Uniprot
P05106 (ITGB3) Y773 Uniprot
P05106 (ITGB3) Y785 Uniprot
P06396 (GSN) Y86 Uniprot
P06396 (GSN) Y409 Uniprot
P06396 (GSN) Y465 Uniprot
P06396 (GSN) Y603 Uniprot
P06396 (GSN) Y651 Uniprot
P06493 (CDK1) Y15 Uniprot
P06733 (ENO1) Y44 Uniprot
P07355 (ANXA2) Y24 Uniprot
P07737 (PFN1) Y129 Uniprot
P07949 (RET) Y905 Uniprot
P08069 (IGF1R) Y973 Uniprot
P08069 (IGF1R) Y980 Uniprot
P08069 (IGF1R) Y1161 Uniprot
P08069 (IGF1R) Y1165 Uniprot
P08069 (IGF1R) Y1166 Uniprot
P08238 (HSP90AB1) Y301 Uniprot
P08727 (KRT19) Y391 Uniprot
P09327 (VIL1) Y46 Uniprot
P09327-1 (VIL1) Y60 Uniprot
P09327 (VIL1) Y64 Uniprot
P09327 (VIL1) Y81 Uniprot
P09327 (VIL1) Y256 Uniprot
P10275 (AR) Y535 Uniprot
P10301 (RRAS) Y66 Uniprot
P10398 (ARAF) Y301 Uniprot
P10398 (ARAF) Y302 Uniprot
P10636-8 (MAPT) Y18 Uniprot
P10721 (KIT) Y900 Uniprot
P10828 (THRB) Y406 Uniprot
P11413 (G6PD) Y428 Uniprot
P11413 (G6PD) Y507 Uniprot
P11511 (CYP19A1) Y361 Uniprot
P11802 (CDK4) Y17 Uniprot
P12235 (SLC25A4) Y195 Uniprot
P12931 (SRC) Y216 Uniprot
P12931 (SRC) Y338 Uniprot
P12931-1 (SRC) Y419 Uniprot
P12931 (SRC) Y530 Uniprot
P12956 (XRCC6) Y530 Uniprot
P13688-1 (CEACAM1) Y493 Uniprot
P13688-1 (CEACAM1) Y520 Uniprot
P14923 (JUP) Y644 Uniprot
P15311 (EZR) Y146 Uniprot
P15311 (EZR) Y478 Uniprot
P15529-4 (CD46) Y354 Uniprot
P15941 (MUC1) Y1229 Uniprot
P16591 (FER) Y714 Uniprot
P16662 (UGT2B7) Y438 Uniprot
P16885 (PLCG2) Y753 Uniprot
P16885 (PLCG2) Y759 Uniprot
P17302 (GJA1) Y247 Uniprot
P17302 (GJA1) Y265 Uniprot
P18206-2 (VCL) Y100 Uniprot
P18206-2 (VCL) Y1065 Uniprot
P18206 (VCL) Y1133 Uniprot
P18433-6 (PTPRA) Y789 Uniprot
P18433-5 (PTPRA) Y798 Uniprot
P19022 (CDH2) Y820 Uniprot
P19022 (CDH2) Y852 Uniprot
P19022 (CDH2) Y860 Uniprot
P19022 (CDH2) Y884 Uniprot
P19022 (CDH2) Y886 Uniprot
P19174-1 (PLCG1) Y783 Uniprot
P19367 (HK1) Y732 Uniprot
P19404 (NDUFV2) Y193 Uniprot
P20138-1 (CD33) Y340 Uniprot
P22001 (KCNA3) Y187 Uniprot
P22001 (KCNA3) Y447 Uniprot
P22001 (KCNA3) Y499 Uniprot
P22681 (CBL) Y731 Uniprot
P22681 (CBL) Y774 Uniprot
P23246 (SFPQ) Y597 Uniprot
P23246 (SFPQ) Y691 Uniprot
P23528 (CFL1) Y68 Uniprot
P23634-6 (ATP2B4) Y1176 Uniprot
P23743 (DGKA) Y335 Uniprot
P25098 (GRK2) Y13 Uniprot
P25098 (GRK2) Y86 Uniprot
P25098 (GRK2) Y92 Uniprot
P25963 (NFKBIA) Y42 Uniprot
P26010 (ITGB7) Y753 Uniprot
P26010 (ITGB7) Y758 Uniprot
P27986 (PIK3R1) Y607 Uniprot
P29317 (EPHA2) Y594 Uniprot
P29350 (PTPN6) Y536 Uniprot
P29350 (PTPN6) Y564 Uniprot
P29353-3 (SHC1) Y194 Uniprot
P29353-3 (SHC1) Y195 Uniprot
P29353-7 (SHC1) Y239 Uniprot
P29353-7 (SHC1) Y240 Uniprot
P29353-3 (SHC1) Y272 Uniprot
P29353 (SHC1) Y349 Uniprot
P29353 (SHC1) Y350 Uniprot
P29353 (SHC1) Y427 Uniprot
P30411 (BDKRB2) Y177 Uniprot
P30411 (BDKRB2) Y347 Uniprot
P30443 (HLA-A) Y344 Uniprot
P30556 (AGTR1) Y319 Uniprot
P31040 (SDHA) Y215 Uniprot
P31431 (SDC4) Y180 Uniprot
P31749 (AKT1) Y315 Uniprot
P31749-1 (AKT1) Y326 Uniprot
P32004 (L1CAM) Y1176 Uniprot
P32248 (CCR7) Y155 Uniprot
P33151 (CDH5) Y658 Uniprot
P33151 (CDH5) Y685 Uniprot
P33151-1 (CDH5) Y731 Uniprot
P34741 (SDC2) Y179 Uniprot
P34947 (GRK5) Y251 Uniprot
P34947 (GRK5) Y253 Uniprot
P35222 (CTNNB1) Y86 Uniprot
P35222 (CTNNB1) Y333 Uniprot
P35222 (CTNNB1) Y654 Uniprot
P35228 (NOS2) Y151 Uniprot
P35228 (NOS2) Y1055 Uniprot
P35579 (MYH9) Y158 Uniprot
P35637 (FUS) Y526 Uniprot
P35790 (CHKA) Y197 Uniprot
P35790 (CHKA) Y333 Uniprot
P35916 (FLT4) Y830 Uniprot
P35916 (FLT4) Y833 Uniprot
P35916 (FLT4) Y853 Uniprot
P35916 (FLT4) Y1063 Uniprot
P35916 (FLT4) Y1333 Uniprot
P35916 (FLT4) Y1337 Uniprot
P35968 (KDR) Y1175 Uniprot
P36544 (CHRNA7) Y386 Uniprot
P36544 (CHRNA7) Y442 Uniprot
P37173 (TGFBR2) Y284 Uniprot
P37840 (SNCA) Y125 Uniprot
P40763-2 (STAT3) Y704 Uniprot
P40763-1 (STAT3) Y705 Uniprot
P41235 (HNF4A) Y23 Uniprot
P41235 (HNF4A) Y286 Uniprot
P41235 (HNF4A) Y288 Uniprot
P41743 (PRKCI) Y265 Uniprot
P41743 (PRKCI) Y280 Uniprot
P41743 (PRKCI) Y334 Uniprot
P42224 (STAT1) Y701 Uniprot
P42229 (STAT5A) Y694 Uniprot
P42681 (TXK) Y420 Uniprot
P46527 (CDKN1B) Y74 Uniprot
P46527 (CDKN1B) Y88 Uniprot
P46527 (CDKN1B) Y89 Uniprot
P48048 (KCNJ1) Y337 Uniprot
P48167 (GLRB) Y435 Uniprot
P49023 (PXN) Y40 Uniprot
P49023 (PXN) Y88 Uniprot
P49407 (ARRB1) Y54 Uniprot
P49789 (FHIT) Y114 Uniprot
P50281 (MMP14) Y573 Uniprot
P50402 (EMD) Y19 Uniprot
P50402 (EMD) Y41 Uniprot
P50402 (EMD) Y59 Uniprot
P50402 (EMD) Y74 Uniprot
P50402 (EMD) Y85 Uniprot
P50402 (EMD) Y90 Uniprot
P50402 (EMD) Y94 Uniprot
P50402 (EMD) Y95 Uniprot
P50402 (EMD) Y99 Uniprot
P50402 (EMD) Y105 Uniprot
P50402 (EMD) Y161 Uniprot
P50402 (EMD) Y167 Uniprot
P50402 (EMD) Y181 Uniprot
P50402 (EMD) Y182 Uniprot
P51636 (CAV2) Y19 Uniprot
P51636 (CAV2) Y27 Uniprot
P51692 (STAT5B) Y679 Uniprot
P51692 (STAT5B) Y699 Uniprot
P51809 (VAMP7) Y45 Uniprot
P51812 (RPS6KA3) Y470 Uniprot
P51812 (RPS6KA3) Y483 Uniprot
P51812 (RPS6KA3) Y488 Uniprot
P51812 (RPS6KA3) Y529 Uniprot
P51812 (RPS6KA3) Y580 Uniprot
P51812 (RPS6KA3) Y644 Uniprot
P51812 (RPS6KA3) Y707 Uniprot
P51813 (BMX) Y566 Uniprot
P52565 (ARHGDIA) Y27 Uniprot
P52565 (ARHGDIA) Y156 Uniprot
P52566 (ARHGDIB) Y24 Uniprot
P52566 (ARHGDIB) Y153 Uniprot
P52757 (CHN2) Y21 Uniprot
P53355 (DAPK1) Y490 Uniprot
P53355 (DAPK1) Y491 Uniprot
P53801 (PTTG1IP) Y174 Uniprot
P56945-1 (BCAR1) Y115 Uniprot
P56945 (BCAR1) Y128 Uniprot
P56945-1 (BCAR1) Y165 Uniprot
P56945-1 (BCAR1) Y179 Uniprot
P56945-1 (BCAR1) Y192 Uniprot
P56945-1 (BCAR1) Y234 Uniprot
P56945 (BCAR1) Y249 Uniprot
P56945-1 (BCAR1) Y267 Uniprot
P56945-1 (BCAR1) Y287 Uniprot
P56945-1 (BCAR1) Y362 Uniprot
P56945-1 (BCAR1) Y387 Uniprot
P56945 (BCAR1) Y653 Uniprot
P56945 (BCAR1) Y664 Uniprot
P56945 (BCAR1) Y666 Uniprot
P57737 (CORO7) Y288 Uniprot
P57737 (CORO7) Y758 Uniprot
P60484 (PTEN) Y46 Uniprot
P60484 (PTEN) Y68 Uniprot
P60484 (PTEN) Y155 Uniprot
P60484 (PTEN) Y174 Uniprot
P60484 (PTEN) Y240 Uniprot
P60484 (PTEN) Y315 Uniprot
P60484 (PTEN) Y377 Uniprot
P60953 (CDC42) Y64 Uniprot
P61978 (HNRNPK) Y72 Uniprot
P61978-2 (HNRNPK) Y225 Uniprot
P61978 (HNRNPK) Y230 Uniprot
P61978 (HNRNPK) Y234 Uniprot
P61978 (HNRNPK) Y236 Uniprot
P61978 (HNRNPK) Y380 Uniprot
P61978 (HNRNPK) Y458 Uniprot
P62993-2 (GRB2) Y119 Uniprot
P62993-1 (GRB2) Y160 Uniprot
P63000 (RAC1) Y64 Uniprot
P63010 (AP2B1) Y737 Uniprot
P63244 (RACK1) Y228 Uniprot
P63244 (RACK1) Y246 Uniprot
P67775 (PPP2CA) Y307 Uniprot
P78347-2 (GTF2I) Y248 Uniprot
P78347 (GTF2I) Y249 Uniprot
P78347-2 (GTF2I) Y611 Uniprot
P78347-4 (GTF2I) Y631 Uniprot
P78347-3 (GTF2I) Y632 Uniprot
P78347-1 (GTF2I) Y652 Uniprot
P78352 (DLG4) Y523 Uniprot
P98161 (PKD1) Y4237 Uniprot
P98175-2 (RBM10) Y16 Uniprot
P98175-2 (RBM10) Y434 Uniprot
P98175-2 (RBM10) Y905 Uniprot
Q00610 (CLTC) Y1477 Uniprot
Q00987 (MDM2) Y281 Uniprot
Q00987 (MDM2) Y302 Uniprot
Q01844 (EWSR1) Y278 Uniprot
Q02153 (GUCY1B1) Y192 Uniprot
Q03135-1 (CAV1) Y14 Uniprot
Q05193-1 (DNM1) Y231 Uniprot
Q05193-1 (DNM1) Y597 Uniprot
Q05397 (PTK2) Y194 Uniprot
Q05397 (PTK2) Y397 Uniprot
Q05397 (PTK2) Y407 Uniprot
Q05397 (PTK2) Y441 Uniprot
Q05397 (PTK2) Y576 Uniprot
Q05397 (PTK2) Y577 Uniprot
Q05397 (PTK2) Y742 Uniprot
Q05397 (PTK2) Y861 Uniprot
Q05397 (PTK2) Y898 Uniprot
Q05397-1 (PTK2) Y925 Uniprot
Q05397 (PTK2) Y1007 Uniprot
Q05586 (GRIN1) Y837 Uniprot
Q05655 (PRKCD) Y313 Uniprot
Q05655 (PRKCD) Y334 Uniprot
Q06187 (BTK) Y551 Uniprot
Q07912 (TNK2) Y284 Uniprot
Q07954 (LRP1) Y4473 Uniprot
Q07954-1 (LRP1) Y4507 Uniprot
Q12879-1 (GRIN2A) Y1105 Uniprot
Q12879 (GRIN2A) Y1184 Uniprot
Q12879-1 (GRIN2A) Y1267 Uniprot
Q12879 (GRIN2A) Y1325 Uniprot
Q12879-1 (GRIN2A) Y1387 Uniprot
Q12879 (GRIN2A) Y1423 Uniprot
Q12913 (PTPRJ) Y1311 Uniprot
Q12913 (PTPRJ) Y1320 Uniprot
Q13002 (GRIK2) Y590 Uniprot
Q13017 (ARHGAP5) Y1109 Uniprot
Q13177 (PAK2) Y130 Uniprot
Q13224 (GRIN2B) Y1474 Uniprot
Q13283 (G3BP1) Y133 Uniprot
Q13322-3 (GRB10) Y9 Uniprot
Q13322 (GRB10) Y67 Uniprot
Q13435 (SF3B2) Y379 Uniprot
Q13435 (SF3B2) Y592 Uniprot
Q13444 (ADAM15) Y715 Uniprot
Q13444 (ADAM15) Y735 Uniprot
Q13480 (GAB1) Y242 Uniprot
Q13480 (GAB1) Y259 Uniprot
Q13480 (GAB1) Y317 Uniprot
Q13480 (GAB1) Y373 Uniprot
Q13480 (GAB1) Y627 Uniprot
Q13813 (SPTAN1) Y1073 Uniprot
Q13813 (SPTAN1) Y1176 Uniprot
Q13905 (RAPGEF1) Y504 Uniprot
Q13936 (CACNA1C) Y2217 Uniprot
Q14118 (DAG1) Y892 Uniprot
Q14247 (CTTN) Y334 Uniprot
Q14247-3 (CTTN) Y384 Uniprot
Q14247-1 (CTTN) Y421 Uniprot
Q14247-3 (CTTN) Y433 Uniprot
Q14247 (CTTN) Y446 Uniprot
Q14247-3 (CTTN) Y449 Uniprot
Q14247 (CTTN) Y470 Uniprot
Q14247 (CTTN) Y486 Uniprot
Q14289 (PTK2B) Y402 Uniprot
Q14289 (PTK2B) Y881 Uniprot
Q14721 (KCNB1) Y128 Uniprot
Q14790 (CASP8) Y380 Uniprot
Q15139 (PRKD1) Y95 Uniprot
Q15139 (PRKD1) Y432 Uniprot
Q15139 (PRKD1) Y463 Uniprot
Q15139 (PRKD1) Y502 Uniprot
Q15417 (CNN3) Y10 Uniprot
Q15642-3 (TRIP10) Y471 Uniprot
Q15654 (TRIP6) Y55 Uniprot
Q15746 (MYLK) Y464 Uniprot
Q15746 (MYLK) Y471 Uniprot
Q16595 (FXN) Y118 Uniprot
Q16625 (OCLN) Y398 Uniprot
Q16625 (OCLN) Y402 Uniprot
Q16832 (DDR2) Y471 Uniprot
Q16832 (DDR2) Y736 Uniprot
Q16832 (DDR2) Y740 Uniprot
Q16832 (DDR2) Y741 Uniprot
Q3V6T2 (CCDC88A) Y1799 Uniprot
Q658W2 (DKFZp666O0110) Y429 Uniprot
Q658W2 (DKFZp666O0110) Y598 Uniprot
Q658W2 (DKFZp666O0110) Y599 Uniprot
Q658W2 (DKFZp666O0110) Y883 Uniprot
Q658W2 (DKFZp666O0110) Y947 Uniprot
Q68CZ2 (TNS3) Y1173 Uniprot
Q68CZ2 (TNS3) Y1206 Uniprot
Q68CZ2 (TNS3) Y1256 Uniprot
Q6UN15 (FIP1L1) Y110 Uniprot
Q7L0Q8 (RHOU) Y254 Uniprot
Q86UR1 (NOXA1) Y110 Uniprot
Q8IXH7-4 (NELFCD) Y6 Uniprot
Q8IXJ6 (SIRT2) Y104 Uniprot
Q8IZL8 (PELP1) Y920 Uniprot
Q8N556-1 (AFAP1) Y93 Uniprot
Q8N556-1 (AFAP1) Y94 Uniprot
Q8N556 (AFAP1) Y125 Uniprot
Q8N556-1 (AFAP1) Y451 Uniprot
Q8N556 (AFAP1) Y453 Uniprot
Q8NER1 (TRPV1) Y200 Uniprot
Q8WUM4-1 (PDCD6IP) Y319 Uniprot
Q8WWM7 (ATXN2L) Y744 Uniprot
Q92529-2 (SHC3) Y218 Uniprot
Q92529-2 (SHC3) Y219 Uniprot
Q92529-2 (SHC3) Y256 Uniprot
Q92529-2 (SHC3) Y257 Uniprot
Q92529-2 (SHC3) Y283 Uniprot
Q92529-2 (SHC3) Y301 Uniprot
Q92556 (ELMO1) Y720 Uniprot
Q92556 (ELMO1) Y724 Uniprot
Q92558 (WASF1) Y125 Uniprot
Q92734 (TFG) Y33 Uniprot
Q92734 (TFG) Y247 Uniprot
Q92945 (KHSRP) Y317 Uniprot
Q92945 (KHSRP) Y583 Uniprot
Q92945 (KHSRP) Y688 Uniprot
Q969H4 (CNKSR1) Y26 Uniprot
Q969H4 (CNKSR1) Y519 Uniprot
Q969H4 (CNKSR1) Y665 Uniprot
Q969T9 (WBP2) Y192 Uniprot
Q969T9 (WBP2) Y231 Uniprot
Q96AC1 (FERMT2) Y193 Uniprot
Q96AE4 (FUBP1) Y58 Uniprot
Q96AE4 (FUBP1) Y268 Uniprot
Q96AE4 (FUBP1) Y625 Uniprot
Q96J92 (WNK4) Y1113 Uniprot
Q96J92 (WNK4) Y1115 Uniprot
Q96J92 (WNK4) Y1164 Uniprot
Q96KB5 (PBK) Y74 Uniprot
Q96KB5 (PBK) Y272 Uniprot
Q96KG7 (MEGF10) Y1030 Uniprot
Q96P31 (FCRL3) Y650 Uniprot
Q96P31 (FCRL3) Y662 Uniprot
Q96P31 (FCRL3) Y692 Uniprot
Q96P31 (FCRL3) Y722 Uniprot
Q96TC7 (RMDN3) Y176 Uniprot
Q99439 (CNN2) Y12 Uniprot
Q99961 (SH3GL1) Y315 Uniprot
Q9BXP5 (SRRT) Y92 Uniprot
Q9BXP5 (SRRT) Y175 Uniprot
Q9BXP5 (SRRT) Y798 Uniprot
Q9BXP5 (SRRT) Y836 Uniprot
Q9H2X6 (HIPK2) Y361 Uniprot
Q9H5V8 (CDCP1) Y734 Uniprot
Q9H5V8 (CDCP1) Y743 Uniprot
Q9H5V8 (CDCP1) Y762 Uniprot
Q9H7P9 (PLEKHG2) Y489 Uniprot
Q9NR80-3 (ARHGEF4) Y94 Uniprot
Q9NR80 (ARHGEF4) Y165 Uniprot
Q9NRY4 (ARHGAP35) Y1105 Uniprot
Q9NV92 (NDFIP2) Y167 Uniprot
Q9NV92 (NDFIP2) Y171 Uniprot
Q9NWQ8 (PAG1) Y317 Uniprot
Q9NYF8 (BCLAF1) Y80 Uniprot
Q9NYF8 (BCLAF1) Y81 Uniprot
Q9NYF8 (BCLAF1) Y93 Uniprot
Q9NYF8 (BCLAF1) Y150 Uniprot
Q9NYF8 (BCLAF1) Y284 Uniprot
Q9NYF8 (BCLAF1) Y408 Uniprot
Q9NZC7-1 (WWOX) Y33 Uniprot
Q9NZQ3 (NCKIPSD) Y161 Uniprot
Q9NZQ3 (NCKIPSD) Y227 Uniprot
Q9UBS0 (RPS6KB2) Y45 Uniprot
Q9UGK3 (STAP2) Y22 Uniprot
Q9UGK3 (STAP2) Y250 Uniprot
Q9UGK3-1 (STAP2) Y310 Uniprot
Q9UGK3 (STAP2) Y322 Uniprot
Q9UHR4 (BAIAP2L1) Y37 Uniprot
Q9UHR4 (BAIAP2L1) Y156 Uniprot
Q9UHR4 (BAIAP2L1) Y163 Uniprot
Q9UHR4 (BAIAP2L1) Y274 Uniprot
Q9UHR4 (BAIAP2L1) Y293 Uniprot
Q9UHR4 (BAIAP2L1) Y439 Uniprot
Q9UJM3 (ERRFI1) Y395 Uniprot
Q9UK17 (KCND3) Y108 Uniprot
Q9UKT4 (FBXO5) Y142 Uniprot
Q9UKW4 (VAV3) Y173 Uniprot
Q9UL51 (HCN2) Y476 Uniprot
Q9ULV8 (CBLC) Y341 Uniprot
Q9UN19 (DAPP1) Y139 Uniprot
Q9UPT8 (ZC3H4) Y158 Uniprot
Q9UPT8 (ZC3H4) Y247 Uniprot
Q9UPT8 (ZC3H4) Y1218 Uniprot
Q9Y2W1 (THRAP3) Y68 Uniprot
Q9Y2W1 (THRAP3) Y107 Uniprot
Q9Y2W1 (THRAP3) Y118 Uniprot
Q9Y2W1 (THRAP3) Y344 Uniprot
Q9Y2X7 (GIT1) Y321 Uniprot
Q9Y371 (SH3GLB1) Y80 Uniprot
Q9Y3Q4 (HCN4) Y531 Uniprot
Q9Y613 (FHOD1) Y99 Uniprot
Q9Y6K9 (IKBKG) Y374 Uniprot

Research Backgrounds

Function:

Non-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase (PTK) families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates 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). 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. 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 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. 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. Involved in anchorage-independent cell growth. Required for podosome formation (By similarity).

PTMs:

Myristoylated at Gly-2, and this is essential for targeting to membranes.

Dephosphorylated at Tyr-530 by PTPRJ (By similarity). Phosphorylated on Tyr-530 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-419. Normally maintained in an inactive conformation with the SH2 domain engaged with Tyr-530, the SH3 domain engaged with the SH2-kinase linker, and Tyr-419 dephosphorylated. Dephosphorylation of Tyr-530 as a result of protein tyrosine phosphatase (PTP) action disrupts the intramolecular interaction between the SH2 domain and Tyr-530, Tyr-419 can then become autophosphorylated, resulting in SRC activation. Phosphorylation of Tyr-530 by CSK allows this interaction to reform, resulting in SRC inactivation. CDK5-mediated phosphorylation at Ser-75 targets SRC to ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this enhances kinase activity. Phosphorylated by PTK2B/PYK2; this enhances kinase activity.

S-nitrosylation is important for activation of its kinase activity.

Ubiquitinated in response to CDK5-mediated phosphorylation. Ubiquitination mediated by CBLC requires SRC autophosphorylation at Tyr-419 and may lead to lysosomal degradation.

Subcellular Location:

Cell membrane>Lipid-anchor. Mitochondrion inner membrane. Nucleus. Cytoplasm>Cytoskeleton. Cytoplasm>Perinuclear region. Cell junction>Focal adhesion.
Note: 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).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Expressed ubiquitously. Platelets, neurons and osteoclasts express 5-fold to 200-fold higher levels than most other tissues.

Subunit Structure:

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. 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. Interacts with the cytoplasmic domain of MUC1, phosphorylates it and increases binding of MUC1 with beta-catenin. Interacts with RALGPS1; via the SH3 domain. Interacts with CAV2 (tyrosine phosphorylated form). 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. Interacts with SRCIN1. Interacts with NDFIP2 and more weakly with NDFIP1. Interacts with PIK3CA and/or PIK3C2B, PTK2/FAK1 and ESR1 (dimethylated on arginine). Interacts with FASLG. Interacts (via SH2 domain) with the 'Tyr-402' phosphorylated form of PTK2B/PYK2. 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. Interacts (via protein kinase domain) with the tyrosine phosphorylated form of RUNX3 (via runt domain). Interacts with TRAF3 (via RING-type zinc finger domain). Interacts with DDX58, MAVS and TBK1. Interacts (via SH2 domain) with RACK1; the interaction is enhanced by tyrosine phosphorylation of RACK1 and inhibits SRC activity. Interacts with EPHB1; activates the MAPK/ERK cascade to regulate cell migration. Interacts with FCAMR. Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of PDPK1. Interacts with AMOTL2; this interaction regulates the translocation of phosphorylated SRC to peripheral cell-matrix adhesion sites. Interacts with TRAP1. Interacts with CBLC; the interaction is enhanced when SRC is phosphorylated at Tyr-419. Interacts with ARHGEF5 (By similarity). Interacts (via cytoplasmic domain) with CEACAM1 (via SH2 domain); this interaction is regulated by trans-homophilic cell adhesion. Interacts with MPP2. Interacts with PRR7. 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. Interacts with P85 (PIK3R1 or PIK3R2). Interacts with HNRNPA2B1.

(Microbial infection) Interacts with HEV ORF3 protein; via the SH3 domain.

Family&Domains:

The SH2 and SH3 domains are important for the intramolecular and intermolecular interactions that regulate catalytic activity, localization, and substrate recruitment.

Belongs to the protein kinase superfamily. Tyr protein kinase family. SRC subfamily.

Research Fields

· Cellular Processes > Transport and catabolism > Endocytosis.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Focal adhesion.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Adherens junction.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Tight junction.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Gap junction.   (View pathway)

· Cellular Processes > Cell motility > Regulation of actin cytoskeleton.   (View pathway)

· Environmental Information Processing > Signal transduction > ErbB signaling pathway.   (View pathway)

· Environmental Information Processing > Signal transduction > Rap1 signaling pathway.   (View pathway)

· Human Diseases > Drug resistance: Antineoplastic > EGFR tyrosine kinase inhibitor resistance.

· Human Diseases > Drug resistance: Antineoplastic > Endocrine resistance.

· Human Diseases > Infectious diseases: Bacterial > Bacterial invasion of epithelial cells.

· Human Diseases > Infectious diseases: Bacterial > Epithelial cell signaling in Helicobacter pylori infection.

· Human Diseases > Infectious diseases: Bacterial > Shigellosis.

· Human Diseases > Infectious diseases: Bacterial > Tuberculosis.

· Human Diseases > Infectious diseases: Viral > Hepatitis B.

· Human Diseases > Cancers: Overview > Viral carcinogenesis.

· Human Diseases > Cancers: Overview > Proteoglycans in cancer.

· Human Diseases > Cancers: Specific types > Bladder cancer.   (View pathway)

· Organismal Systems > Immune system > Chemokine signaling pathway.   (View pathway)

· Organismal Systems > Development > Axon guidance.   (View pathway)

· Organismal Systems > Immune system > Platelet activation.   (View pathway)

· Organismal Systems > Nervous system > GABAergic synapse.

· Organismal Systems > Sensory system > Inflammatory mediator regulation of TRP channels.   (View pathway)

· Organismal Systems > Endocrine system > Estrogen signaling pathway.   (View pathway)

· Organismal Systems > Endocrine system > Prolactin signaling pathway.   (View pathway)

· Organismal Systems > Endocrine system > Thyroid hormone signaling pathway.   (View pathway)

· Organismal Systems > Endocrine system > Oxytocin signaling pathway.

· Organismal Systems > Endocrine system > Relaxin signaling pathway.

References

1). Src acts as the target of matrine to inhibit the proliferation of cancer cells by regulating phosphorylation signaling pathways. Cell Death & Disease, 2021 (PubMed: 34642304) [IF=9.0]

Application: WB    Species: Human    Sample: HT-29, MCF7, A549, BxPC-3, SKOV3, and HeLa cells

Fig. 4 Matrine was a non-ATP-competitive inhibitor of Src kinase. A The effect of matrine on Src kinase activity in cancer cells, including HT-29, MCF7, A549, BxPC-3, SKOV3, and HeLa, were determined according to the instructions of Src kinase activity detection kit. Results are representative of three experiments (*P 

2). Anti-proliferation and anti-migration effects of Yishen Tongbi decoction in experimental rheumatoid arthritis by suppressing SLC3A2/integrin β3 signaling pathways. Phytomedicine, 2023 (PubMed: 36990010) [IF=7.9]

3). Formononetin Protects LPS-Induced Mastitis Through Suppressing Inflammation and Enhancing Blood-Milk Barrier Integrity via AhR-Induced Src Inactivation. Frontiers in Immunology, 2022 (PubMed: 35185907) [IF=7.3]

Application: WB    Species: Mice    Sample:

Figure 8 FOR increases AhR expression and inhibits the phosphorylation level of Src. The present results are displayed as the mean ± SEM of triple parallel measurements. #(P < 0.01) is significantly different from control group; **(P < 0.01) is significantly different from LPS group.

4). Jinfukang regulates integrin/Src pathway and anoikis mediating circulating lung cancer cells migration. JOURNAL OF ETHNOPHARMACOLOGY, 2021 (PubMed: 33068649) [IF=5.4]

Application: WB    Species: human    Sample: CTC-TJH-01 cells

Fig. 5. |Jinfukang inhibited the cell migration via Integrin/Src axis in lung cancer cells. Cells were incubated with Jinfukang (100 μg/mL), ATN-161 (10 μmol/L) or a combination of both for 24 h. A Western blot assay was used to measure the protein expression levels of Integrin β1, Src, and p-Src in CTC-TJH-01 (A) and H1975 (B)cells. GAPDH was used as an internal standard.

5). Cyclin G2 inhibits oral squamous cell carcinoma growth and metastasis by binding to IGFBP3 and regulating the FAK-SRC-STAT signaling pathway. Frontiers in Oncology, 2020 (PubMed: 33240810) [IF=4.7]

Application: WB    Species: Human    Sample: Oral squamous cell carcinoma (OSCC)

FIGURE 5 | Cyclin G2 inhibits the FAK-SRC-STAT pathway in vitro and in vivo. (A) The protein expressions along with quantification of FAK, P-FAK, SRC, P-SRC, STAT3, P-STAT3, Bcl-2, c-Myc, and MMP9 in the FAK-SRC-STAT pathway. (B–D) The relative mRNA expressions of Bcl-2, c-Myc and MMP9. (E) Analysis of MMP9 secretion and its quantification in SCC-9 cells. (F, G) Immunohistochemical staining and analysis of the expression of cyclin G2, p-FAK, p-SRC and p-STAT3. Scale bar = 100 µm. *p < 0.05, **p < 0.01, ***p < 0.001 vs. vector.

6). Ethoxy-erianin phosphate and afatinib synergistically inhibit liver tumor growth and angiogenesis via regulating VEGF and EGFR signaling pathways. Toxicology and Applied Pharmacology, 2022 (PubMed: 35143806) [IF=3.8]

7). Inorganic arsenic exposure promotes malignant progression by HDAC6-mediated down-regulation of HTRA1. Journal of Applied Toxicology, 2023 (PubMed: 36861143) [IF=3.3]

Application: WB    Species: Human    Sample: Caco-2 cells

FIGURE 3 Molecular profiling for iAs-induced changes in Caco-2 cells. (A) Protein levels of claudin 3 and cofilin were determined by Western blot analysis. (B) Transcript levels of IL-6, TNF-α, and MMP13 were determined by RT-qPCR, with GAPDH as an internal control. (C) The levels of EGF in the culture supernatant were examined by ELISA. (D) A marked increase in the phosphorylated levels of EGFR, Src, AKT, and p38 was shown by Western blot analysis. RT-qPCR (E) and Western blot analysis (F) results showed the down-regulation of HTRA1 expression caused by chronic iAs exposure. Data were representatives of at least three independent experiments, shown as mean ± SD. The significance threshold for Student's t-test:

8). Overexpression of Laminin 5γ2 Chain Correlates with Tumor Cell Proliferation, Invasion, and Poor Prognosis in Laryngeal Squamous Cell Carcinoma. Journal of Oncology, 2022 (PubMed: 36284634)

Application: WB    Species: Human    Sample: AMC-HN-8 cells

Figure 6 LAMC2 activated the integrin β1/FAK/Src/AKT signaling pathway in TU177 and AMC-HN-8 cells. (a) LAMC2 overexpression promotes integrin β1/FAK/Src/AKT protein expression in TU177 cells. (b) LAMC2 knockdown inhibited integrin β1/FAK/Src/AKT protein expression in AMC-HN-8 cells. Data were expressed as mean ± SD, n = 3. Compared to the vector group, #P < 0.05, ##P < 0.01. Compared to the shNC group, ∗P < 0.05, ∗∗P < 0.01.

9). Cyclin G2 inhibits oral squamous cell carcinoma growth and metastasis by binding to insulin-like growth factor binding protein 3 and regulating the FAK-SRC-STAT signaling pathway. bioRxiv, 2020

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