Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Proto-oncogene tyrosine-protein kinase Src  

UniProtKB / Swiss-Prot ID :  SRC_HUMAN

Gene Name (Synonyms) : 
SRC, SRC1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell membrane. Mitochondrion inner membrane. Nucleus. Cytoplasm, cytoskeleton. Note=Localizes to focal adhesion sites following integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain. 

Protein 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). 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'. 

Protein Sequence MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAEPKLFGGFNSS...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
176L -> F (in dbSNP:rs6018260). VAR_051699
237A -> T (in dbSNP:rs34881773). VAR_041830
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-myristoyl glycine---MGSNKS
---CCCCCC
39.67HPRD
Link-
2N-myristoyl glycine.---MGSNKS
---CCCCCC
39.67UniProtKB
Link-
12PhosphoserinePKDASQRRR
CCCCCCCCC
34.06PhosphoELM
Link-
12PhosphoserinePKDASQRRR
CCCCCCCCC
34.06Phosphositeplus
Link-
12Phosphoserine (PRKCA)PKDASQRRR
CCCCCCCCC
34.06HPRD
Link-
17PhosphoserineQRRRSLEPA
CCCCCCCCC
34.96Phosphositeplus
Link-
17PhosphoserineQRRRSLEPA
CCCCCCCCC
34.96SysPTM
Link-
17Phosphoserine (PKA_group)QRRRSLEPA
CCCCCCCCC
34.96PhosphoELM
Link-
17Phosphoserine (PRKACA)QRRRSLEPA
CCCCCCCCC
34.96HPRD
Link-
17Phosphoserine.QRRRSLEPA
CCCCCCCCC
34.96UniProtKB
Link-
35Phosphoserine.AFPASQTPS
CCCCCCCCC
34.52UniProtKB
Link-
37PhosphothreoninePASQTPSKP
CCCCCCCCC
27.34SysPTM
Link-
39PhosphoserineSQTPSKPAS
CCCCCCCCC
55.44SysPTM
Link-
45Caspase cleavage aspartic acidPASADGHRG
CCCCCCCCC
51.43Phosphositeplus
Link-
69PhosphoserineGGFNSSDTV
CCCCCCCCC
27.59PhosphoELM
Link-
69PhosphoserineGGFNSSDTV
CCCCCCCCC
27.59Phosphositeplus
Link-
69Phosphoserine.GGFNSSDTV
CCCCCCCCC
27.59UniProtKB
Link-
70PhosphoserineGFNSSDTVT
CCCCCCCCC
38.10Phosphositeplus
Link-
72PhosphothreonineNSSDTVTSP
CCCCCCCCC
27.86Phosphositeplus
Link-
74PhosphothreonineSDTVTSPQR
CCCCCCCCC
36.46HPRD
Link-
74PhosphothreonineSDTVTSPQR
CCCCCCCCC
36.46PhosphoELM
Link-
74PhosphothreonineSDTVTSPQR
CCCCCCCCC
36.46Phosphositeplus
Link-
74PhosphothreonineSDTVTSPQR
CCCCCCCCC
36.46SysPTM
Link-
74Phosphothreonine.SDTVTSPQR
CCCCCCCCC
36.46UniProtKB
Link-
75PhosphoserineDTVTSPQRA
CCCCCCCCC
18.07Phosphositeplus
Link-
75PhosphoserineDTVTSPQRA
CCCCCCCCC
18.07SysPTM
Link-
75Phosphoserine (CDK5)DTVTSPQRA
CCCCCCCCC
18.07HPRD
Link-
75Phosphoserine (CDK_group;CDK5)DTVTSPQRA
CCCCCCCCC
18.07PhosphoELM
Link-
75Phosphoserine; by CDK5.DTVTSPQRA
CCCCCCCCC
18.07UniProtKB
Link-
97PhosphoserineYDYESRTET
CCCCCCCCC
37.97HPRD
Link-
97PhosphoserineYDYESRTET
CCCCCCCCC
37.97PhosphoELM
Link-
97PhosphoserineYDYESRTET
CCCCCCCCC
37.97Phosphositeplus
Link-
187PhosphotyrosineTKGAYCLSV
CCCCEEEEE
11.55Phosphositeplus
Link
216PhosphotyrosineSGGFYITSR
CCCEEECCC
13.43HPRD
Link
216PhosphotyrosineSGGFYITSR
CCCEEECCC
13.43Phosphositeplus
Link
216Phosphotyrosine (SRC)SGGFYITSR
CCCEEECCC
13.43PhosphoELM
Link
306PhosphoserinePGTMSPEAF
CCCCCHHHH
21.30HPRD
Link-
338DePhosphotyrosineEEPIYIVTE
CCCEEEEEE
10.47HPRD
Link-
338PhosphotyrosineEEPIYIVTE
CCCEEEEEE
10.47Phosphositeplus
Link-
338Phosphotyrosine (SRC)EEPIYIVTE
CCCEEEEEE
10.47PhosphoELM
Link-
419DePhosphotyrosineEDNEYTARQ
CCCCEEEEE
16.38HPRD
Link-
419DePhosphotyrosineEDNEYTARQ
CCCCEEEEE
16.38HPRD
Link-
419DePhosphotyrosineEDNEYTARQ
CCCCEEEEE
16.38HPRD
Link-
419DePhosphotyrosineEDNEYTARQ
CCCCEEEEE
16.38HPRD
Link-
419PhosphotyrosineEDNEYTARQ
CCCCEEEEE
16.38Phosphositeplus
Link-
419PhosphotyrosineEDNEYTARQ
CCCCEEEEE
16.38SysPTM
Link-
419Phosphotyrosine (SRC)EDNEYTARQ
CCCCEEEEE
16.38HPRD
Link-
419Phosphotyrosine (SRC)EDNEYTARQ
CCCCEEEEE
16.38HPRD
Link-
419Phosphotyrosine (SRC;SRC;SRC)EDNEYTARQ
CCCCEEEEE
16.38PhosphoELM
Link-
419Phosphotyrosine; by autocatalysis.EDNEYTARQ
CCCCEEEEE
16.38UniProtKB
Link-
420PhosphothreonineDNEYTARQG
CCCEEEEEE
14.80Phosphositeplus
Link-
439PhosphotyrosineEAALYGRFT
HHHHCCCCC
11.09PhosphoELM
Link-
439PhosphotyrosineEAALYGRFT
HHHHCCCCC
11.09Phosphositeplus
Link-
439Phosphotyrosine.EAALYGRFT
HHHHCCCCC
11.09UniProtKB
Link-
511Phosphothreonine.EERPTFEYL
HHCCCHHHH
35.01UniProtKB
Link-
522PhosphotyrosineFLEDYFTST
HHHHHHHCC
10.20Phosphositeplus
Link-
522Phosphotyrosine.FLEDYFTST
HHHHHHHCC
10.20UniProtKB
Link-
525PhosphoserineDYFTSTEPQ
HHHHCCCCC
22.37SysPTM
Link-
530DePhosphotyrosineTEPQYQPGE
CCCCCCCCC
27.65HPRD
Link-
530DePhosphotyrosineTEPQYQPGE
CCCCCCCCC
27.65HPRD
Link-
530DePhosphotyrosineTEPQYQPGE
CCCCCCCCC
27.65HPRD
Link-
530DePhosphotyrosineTEPQYQPGE
CCCCCCCCC
27.65HPRD
Link-
530PhosphotyrosineTEPQYQPGE
CCCCCCCCC
27.65Phosphositeplus
Link-
530Phosphotyrosine (CSK)TEPQYQPGE
CCCCCCCCC
27.65HPRD
Link-
530Phosphotyrosine (CSK)TEPQYQPGE
CCCCCCCCC
27.65HPRD
Link-
530Phosphotyrosine (Csk)TEPQYQPGE
CCCCCCCCC
27.65PhosphoELM
Link-
530Phosphotyrosine (FGR)TEPQYQPGE
CCCCCCCCC
27.65HPRD
Link-
530Phosphotyrosine; by CSK.TEPQYQPGE
CCCCCCCCC
27.65UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
TLR3_HUMANphysical interactionMINT-2841760MINT16858407
TLR3_HUMANcolocalizationMINT-2840132MINT16858407
ADRB2_HUMANphysical interactionMINT-4051805MINT17170700
ADRB2_HUMANdirect interactionMINT-4051585MINT17170700
SRC_HUMANphosphorylation reactionMINT-4301093MINT17170700
MUC1_HUMANphysical interactionMINT-18161MINT11152665
CBL_HUMANphosphorylation reactionMINT-3982451MINT17141222
GUC2C_HUMANphysical interactionMINT-19274MINT12649275
CSK_HUMANphysical interactionMINT-4980220MINT17525734
ARRB1_HUMANphysical interactionMINT-16503MINT10753943
AFAD_HUMANphysical interactionMINT-4961227MINT17491594
AFAD_HUMANphysical interactionMINT-4961253MINT17491594
AFAD_HUMANphysical interactionMINT-4961303MINT17491594
AFAD_HUMANphysical interactionMINT-4961273MINT17491594
AFAD_HUMANdirect interactionMINT-4950584MINT17491594
AFAD_HUMANphysical interactionMINT-4961138MINT17491594
AFAD_HUMANcolocalizationMINT-4961196MINT17491594
CAV1_HUMANphysical interactionMINT-15459MINT8621645
DYN1_HUMANphysical interactionMINT-65950MINT15834155
DYN1_HUMANphysical interactionMINT-65953MINT15834155
FAK1_HUMANphysical interactionMINT-4980071MINT17525734
FAK1_HUMANphysical interactionMINT-3381308MINT16966330
DDR2_HUMANphysical interactionMINT-14765MINT11884411
CDCP1_HUMANphysical interactionMINT-62342MINT15851033
CD2AP_HUMANphosphorylation reactionMINT-17158MINT10339567
CCND1_HUMANphysical interactionDIP:544EDIP8479754
CDN1B_HUMANphosphorylationEBI-1200966
intact17254967
NEMO_HUMANphysical interaction
physical interaction
physical interaction
EBI-697983
EBI-697929
EBI-697
intact15749833
15749833
15749833
IKKB_HUMANphysical interactionEBI-697951
intact15749833
IKKA_HUMANphysical interactionEBI-697951
intact15749833
KHDR1_HUMANphysical interactionEBI-730897
intact16169070
ACTN1_HUMANphysical interaction
physical interaction
EBI-968912
EBI-968854
intact16291744
16291744
STAT3_HUMANin vitro
in vivo
HPRD:01819HPRD8657134
11940572
11294897
10918587
12244095
11350938
12626508
8626374
12576423
14551213
8272872
9566
CD59_HUMANin vivoHPRD:01819HPRD12219031
LRP1_HUMANin vitro
in vivo
HPRD:01819HPRD12789267
11854294
UFO_HUMANin vivoHPRD:01819HPRD9178760
1433F_HUMANin vivoHPRD:01819HPRD8702721
ADRB2_HUMANin vitroHPRD:01819HPRD11013230
ADRB3_HUMANin vitro
in vivo
HPRD:01819HPRD11013230
CEAM1_HUMANin vitroHPRD:01819HPRD9867848
GRB2_HUMANin vitro
in vivo
HPRD:01819HPRD11964172
9016807
AT2B4_HUMANin vivoHPRD:01819HPRD9182531
12540962
CTNB1_HUMANin vitroHPRD:01819HPRD11279024
MCP_HUMANin vitroHPRD:01819HPRD10657632
CXA1_HUMANin vitro
in vivo
HPRD:01819HPRD9278444
11514593
DAG1_HUMANin vitro
in vivo
HPRD:01819HPRD12795607
TNFL6_HUMANin vivoHPRD:01819HPRD11741599
ESR1_HUMANin vivoHPRD:01819HPRD7539106
12736255
FOXO1_HUMANin vivoHPRD:01819HPRD10973497
GFAP_HUMANin vivoHPRD:01819HPRD11379820
NMDE2_HUMANin vitro
in vivo
HPRD:01819HPRD10884433
11024032
11483655
NMDE1_HUMANin vitro
in vivo
HPRD:01819HPRD12932824
10458595
10884433
10846184
10195142
RASA1_HUMANin vivoHPRD:01819HPRD1717825
HNF1A_HUMANin vitro
in vivo
HPRD:01819HPRD10777539
1A68_HUMANin vitroHPRD:01819HPRD6304688
6333425
1B07_HUMANin vitroHPRD:01819HPRD6304688
IL6RA_HUMANin vitroHPRD:01819HPRD10462375
IGF1R_HUMANin vitro
in vivo
HPRD:01819HPRD8940173
AKT1_HUMANin vitro
in vivo
HPRD:01819HPRD11445557
PLCG1_HUMANin vitro
in vivo
HPRD:01819HPRD7510703
8885868
8657103
1689310
7682059
RAF1_HUMANin vitro
in vivo
HPRD:01819HPRD7517401
10205168
8876196
KPCE_HUMANin vitroHPRD:01819HPRD11834516
CD33_HUMANin vitroHPRD:01819HPRD10206955
RET_HUMANin vivoHPRD:01819HPRD10070972
GBLP_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:01819HPRD9584165
11279199
SRC8_HUMANin vitro
in vivo
HPRD:01819HPRD9748248
PECA1_HUMANin vitro
in vivo
HPRD:01819HPRD10858437
CD36_HUMANin vivoHPRD:01819HPRD7521304
MET_HUMANin vivoHPRD:01819HPRD9837958
ERBB2_HUMANin vivoHPRD:01819HPRD7542762
KIT_HUMANin vitroHPRD:01819HPRD12878163
ANXA1_HUMANin vitroHPRD:01819HPRD2457390
ANXA2_HUMANin vitro
in vivo
HPRD:01819HPRD11106497
IKBA_HUMANin vitro
in vivo
HPRD:01819HPRD8797825
12429743
9792645
CBL_HUMANin vivoHPRD:01819HPRD8635998
PTPRA_HUMANin vitro
in vivo
HPRD:01819HPRD11923305
12468645
8647855
9261115
10698938
7518772
P85A_HUMANin vivoHPRD:01819HPRD12210743
MUC1_HUMANin vitro
in vivo
HPRD:01819HPRD11483589
11152665
CDCP1_HUMANin vivoHPRD:01819HPRD14739293
SPTA2_HUMANin vitro
in vivo
HPRD:01819HPRD11971983
KPCZ_HUMANin vivoHPRD:01819HPRD10527887
TERT_HUMANin vitro
in vivo
HPRD:01819HPRD12808100
ABL1_HUMANin vitro
in vivo
HPRD:01819HPRD11781820
12522270
RASH_HUMANin vitroHPRD:01819HPRD12695509
VINC_HUMANin vitroHPRD:01819HPRD15229287
KPCI_HUMANin vitro
in vivo
HPRD:01819HPRD11713277
BMX_HUMANin vitro
in vivo
HPRD:01819HPRD10688651
TXK_HUMANin vitro
in vivo
HPRD:01819HPRD11353545
SHC1_HUMANin vivoHPRD:01819HPRD10482988
9710204
9388490
9096689
HNRPK_HUMANin vitro
in vivo
HPRD:01819HPRD7516469
12052863
FAK1_HUMANin vitro
in vivo
HPRD:01819HPRD7529876
8054685
10931187
9507031
8816475
7997267
11927607
8941336
CAV1_HUMANin vitro
in vivo
HPRD:01819HPRD8910575
8632005
CAV2_HUMANin vivoHPRD:01819HPRD12091389
GRB10_HUMANin vitroHPRD:01819HPRD10871840
GTF2I_HUMANin vitro
in vivo
HPRD:01819HPRD9837922
9012831
11373296
11313464
11934902
DYN1_HUMANin vitro
in vivo
HPRD:01819HPRD9880482
12011079
RGS16_HUMANin vitro
in vivo
HPRD:01819HPRD12588871
11602604
ADA12_HUMANin vitro
in vivo
HPRD:01819HPRD11127814
BCAR1_HUMANin vitroHPRD:01819HPRD12972425
DAB1_HUMANin vitro
in vivo
HPRD:01819HPRD15062102
11279201
10959835
STA5B_HUMANin vitro
in vivo
HPRD:01819HPRD12621061
MPZL1_HUMANin vitro
in vivo
HPRD:01819HPRD11751924
10681522
PAK2_HUMANin vitroHPRD:01819HPRD12215529
PDPK1_HUMANin vitro
in vivo
HPRD:01819HPRD11481331
GRLF1_HUMANin vitro
in vivo
HPRD:01819HPRD9819392
11309200
KPCD1_HUMANin vitroHPRD:01819HPRD12637538
KCNB1_HUMANin vitro
in vivo
HPRD:01819HPRD12615930
ITB3_HUMANin vitro
in vivo
HPRD:01819HPRD11723131
VGFR2_HUMANin vitroHPRD:01819HPRD10455194
EGFR_HUMANin vitroHPRD:01819HPRD11983694
8845374
10075741
VILI_HUMANin vitroHPRD:01819HPRD15342783
PTN11_HUMANin vivoHPRD:01819HPRD14687660
CADH5_HUMANin vitroHPRD:01819HPRD16027153
CTND1_HUMANin vitro
in vivo
HPRD:01819HPRD11382764
PLAK_HUMANin vitroHPRD:01819HPRD14517306
DAPP1_HUMANin vitroHPRD:01819HPRD11524430
IKKA_HUMANin vitro
in vivo
HPRD:01819HPRD12707358
STAT6_HUMANin vivoHPRD:01819HPRD15695802
ESR2_HUMANin vitroHPRD:01819HPRD12095943
TRAF1_HUMANin vitro
in vivo
HPRD:01819HPRD10635328
TRAF3_HUMANin vitro
in vivo
HPRD:01819HPRD10635328
DOK1_HUMANin vitroHPRD:01819HPRD11071635
IKKB_HUMANin vitro
in vivo
HPRD:01819HPRD12707358
TNR11_HUMANin vitroHPRD:01819HPRD10635328
SH2D3_HUMANin vivoHPRD:01819HPRD15272013
FRS2_HUMANin vitroHPRD:01819HPRD10092678
FHIT_HUMANin vitro
in vivo
HPRD:01819HPRD15835917
FYB_HUMANin vitro
in vivo
HPRD:01819HPRD16020549
SRC_HUMANin vitroHPRD:01819HPRD9988270
14661060
NEMO_HUMANin vivoHPRD:01819HPRD15749833
NOS2A_HUMANin vitroHPRD:01819HPRD16116474
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
Kegg drug
D03252 Bosutinib (USAN)
D03658 Dasatinib (INN)
D06414 Dasatinib hydrate (JAN); Dasatinib (USAN); Sprycel (TN)
D09664 Saracatinib (USAN/INN)
D09665 Saracatinib difumarate (USAN)
D09728 Bosutinib hydrate (JAN); Bosutinib monohydrate; Bosulif (TN)
D10423 Ilorasertib (USAN)
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Association of the amino-terminal half of c-Src with focal adhesionsalters their properties and is regulated by phosphorylation oftyrosine 527.";
Kaplan K.B., Bibbins K.B., Swedlow J.R., Arnaud M., Morgan D.O.,Varmus H.E.;
EMBO J. 13:4745-4756(1994).
Cited for: SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYR-530.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-439, AND MASSSPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-69; SER-75 ANDTYR-419, AND MASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; THR-74 AND TYR-419,AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-530, AND MASSSPECTROMETRY.
"New role for the protein tyrosine phosphatase DEP-1 in Akt activationand endothelial cell survival.";
Chabot C., Spring K., Gratton J.P., Elchebly M., Royal I.;
Mol. Cell. Biol. 29:241-253(2009).
Cited for: PHOSPHORYLATION AT TYR-419, AND DEPHOSPHORYLATION BY PTPRJ AT TYR-419.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-35; SER-69;THR-74; SER-75; THR-511; TYR-522 AND TYR-530, AND MASS SPECTROMETRY.
"Cdk5 targets active Src for ubiquitin-dependent degradation byphosphorylating Src(S75).";
Pan Q., Qiao F., Gao C., Norman B., Optican L., Zelenka P.S.;
Cell. Mol. Life Sci. 68:3425-3436(2011).
Cited for: PHOSPHORYLATION AT SER-75.
"Characterization of sites for tyrosine phosphorylation in thetransforming protein of Rous sarcoma virus (pp60v-src) and its normalcellular homologue (pp60c-src).";
Smart J.E., Oppermann H., Czernilofsky A.P., Purchio A.F.,Erikson R.L., Bishop J.M.;
Proc. Natl. Acad. Sci. U.S.A. 78:6013-6017(1981).
Cited for: PHOSPHORYLATION AT TYR-419.
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