LYN_HUMAN - dbPTM
LYN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LYN_HUMAN
UniProt AC P07948
Protein Name Tyrosine-protein kinase Lyn
Gene Name LYN
Organism Homo sapiens (Human).
Sequence Length 512
Subcellular Localization Cell membrane. Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Golgi apparatus. Membrane
Lipid-anchor . Accumulates in the nucleus by inhibition of CRM1-mediated nuclear export. Nuclear accumulation is increased by inhibition of its kinase activ
Protein Description Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors and plays an important role in the regulation of innate and adaptive immune responses, hematopoiesis, responses to growth factors and cytokines, integrin signaling, but also responses to DNA damage and genotoxic agents. Functions primarily as negative regulator, but can also function as activator, depending on the context. Required for the initiation of the B-cell response, but also for its down-regulation and termination. Plays an important role in the regulation of B-cell differentiation, proliferation, survival and apoptosis, and is important for immune self-tolerance. Acts downstream of several immune receptors, including the B-cell receptor, CD79A, CD79B, CD5, CD19, CD22, FCER1, FCGR2, FCGR1A, TLR2 and TLR4. Plays a role in the inflammatory response to bacterial lipopolysaccharide. Mediates the responses to cytokines and growth factors in hematopoietic progenitors, platelets, erythrocytes, and in mature myeloid cells, such as dendritic cells, neutrophils and eosinophils. Acts downstream of EPOR, KIT, MPL, the chemokine receptor CXCR4, as well as the receptors for IL3, IL5 and CSF2. Plays an important role in integrin signaling. Regulates cell proliferation, survival, differentiation, migration, adhesion, degranulation, and cytokine release. Down-regulates signaling pathways by phosphorylation of immunoreceptor tyrosine-based inhibitory motifs (ITIM), that then serve as binding sites for phosphatases, such as PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1, that modulate signaling by dephosphorylation of kinases and their substrates. Phosphorylates LIME1 in response to CD22 activation. Phosphorylates BTK, CBL, CD5, CD19, CD72, CD79A, CD79B, CSF2RB, DOK1, HCLS1, LILRB3/PIR-B, MS4A2/FCER1B, PTK2B/PYK2, SYK and TEC. Promotes phosphorylation of SIRPA, PTPN6/SHP-1, PTPN11/SHP-2 and INPP5D/SHIP-1. Mediates phosphorylation of the BCR-ABL fusion protein. Required for rapid phosphorylation of FER in response to FCER1 activation. Mediates KIT phosphorylation. Acts as an effector of EPOR (erythropoietin receptor) in controlling KIT expression and may play a role in erythroid differentiation during the switch between proliferation and maturation. Depending on the context, activates or inhibits several signaling cascades. Regulates phosphatidylinositol 3-kinase activity and AKT1 activation. Regulates activation of the MAP kinase signaling cascade, including activation of MAP2K1/MEK1, MAPK1/ERK2, MAPK3/ERK1, MAPK8/JNK1 and MAPK9/JNK2. Mediates activation of STAT5A and/or STAT5B. Phosphorylates LPXN on 'Tyr-72'. Kinase activity facilitates TLR4-TLR6 heterodimerization and signal initiation..
Protein Sequence MGCIKSKGKDSLSDDGVDLKTQPVRNTERTIYVRDPTSNKQQRPVPESQLLPGQRFQTKDPEEQGDIVVALYPYDGIHPDDLSFKKGEKMKVLEEHGEWWKAKSLLTKKEGFIPSNYVAKLNTLETEEWFFKDITRKDAERQLLAPGNSAGAFLIRESETLKGSFSLSVRDFDPVHGDVIKHYKIRSLDNGGYYISPRITFPCISDMIKHYQKQADGLCRRLEKACISPKPQKPWDKDAWEIPRESIKLVKRLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQAFLEEANLMKTLQHDKLVRLYAVVTREEPIYIITEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKFPIKWTAPEAINFGCFTIKSDVWSFGILLYEIVTYGKIPYPGRTNADVMTALSQGYRMPRVENCPDELYDIMKMCWKEKAEERPTFDYLQSVLDDFYTATEGQYQQQP
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Myristoylation------MGCIKSKGK
------CCCCCCCCC		23.1218817770
3S-palmitoylation-----MGCIKSKGKD
-----CCCCCCCCCC		3.2317537435
6Phosphorylation--MGCIKSKGKDSLS
--CCCCCCCCCCCCC		27.0823403867
9UbiquitinationGCIKSKGKDSLSDDG
CCCCCCCCCCCCCCC		48.1321906983
9 (in isoform 2)Ubiquitination-48.1321890473
9 (in isoform 1)Ubiquitination-48.1321890473
11PhosphorylationIKSKGKDSLSDDGVD
CCCCCCCCCCCCCCC		33.0022167270
11 (in isoform 2)Phosphorylation-33.0029743597
13PhosphorylationSKGKDSLSDDGVDLK
CCCCCCCCCCCCCCC		37.2919664994
13 (in isoform 2)Phosphorylation-37.2929743597
20 (in isoform 1)Ubiquitination-40.4221890473
20UbiquitinationSDDGVDLKTQPVRNT
CCCCCCCCCCCCCCC		40.422190698
20 (in isoform 2)Ubiquitination-40.4221890473
21PhosphorylationDDGVDLKTQPVRNTE
CCCCCCCCCCCCCCE		45.4626434776
30PhosphorylationPVRNTERTIYVRDPT
CCCCCEEEEEEECCC		15.4928152594
32PhosphorylationRNTERTIYVRDPTSN
CCCEEEEEEECCCCC		6.7127273156
37PhosphorylationTIYVRDPTSNKQQRP
EEEEECCCCCCCCCC		49.5828152594
38PhosphorylationIYVRDPTSNKQQRPV
EEEECCCCCCCCCCC		47.6323401153
40UbiquitinationVRDPTSNKQQRPVPE
EECCCCCCCCCCCCH		47.80-
48PhosphorylationQQRPVPESQLLPGQR
CCCCCCHHHCCCCCC		21.7625002506
58PhosphorylationLPGQRFQTKDPEEQG
CCCCCCCCCCHHHCC		34.4022115753
59UbiquitinationPGQRFQTKDPEEQGD
CCCCCCCCCHHHCCC		61.58-
74PhosphorylationIVVALYPYDGIHPDD
EEEEEEECCCCCCCC		17.1627642862
80 (in isoform 2)Ubiquitination-56.1521890473
83PhosphorylationGIHPDDLSFKKGEKM
CCCCCCCCCCCCCCC		41.8524719451
85UbiquitinationHPDDLSFKKGEKMKV
CCCCCCCCCCCCCCH		57.39-
101 (in isoform 1)Ubiquitination-47.1921890473
101UbiquitinationEEHGEWWKAKSLLTK
HHCCCHHHHHHHHHC		47.1921890473
104PhosphorylationGEWWKAKSLLTKKEG
CCHHHHHHHHHCCCC		33.2124719451
109AcetylationAKSLLTKKEGFIPSN
HHHHHHCCCCCCCHH		58.8126051181
109UbiquitinationAKSLLTKKEGFIPSN
HHHHHHCCCCCCCHH		58.81-
115PhosphorylationKKEGFIPSNYVAKLN
CCCCCCCHHHHHCCC		35.6625884760
117PhosphorylationEGFIPSNYVAKLNTL
CCCCCHHHHHCCCCC		13.2128152594
132UbiquitinationETEEWFFKDITRKDA
CCCHHHCCCCCHHHH		38.45-
135PhosphorylationEWFFKDITRKDAERQ
HHHCCCCCHHHHHHH		41.63-
149PhosphorylationQLLAPGNSAGAFLIR
HCCCCCCCCCEEEEE		33.71-
158PhosphorylationGAFLIRESETLKGSF
CEEEEEECCCCCCEE		26.49-
164PhosphorylationESETLKGSFSLSVRD
ECCCCCCEEEEEEEC		15.2930108239
166PhosphorylationETLKGSFSLSVRDFD
CCCCCEEEEEEECCC		22.7930108239
168PhosphorylationLKGSFSLSVRDFDPV
CCCEEEEEEECCCCC		17.5730108239
181UbiquitinationPVHGDVIKHYKIRSL
CCCCCEEEEEEEEEC		40.50-
187PhosphorylationIKHYKIRSLDNGGYY
EEEEEEEECCCCCEE		43.4824719451
193PhosphorylationRSLDNGGYYISPRIT
EECCCCCEEECCCEE		10.0620007894
194PhosphorylationSLDNGGYYISPRITF
ECCCCCEEECCCEEC		9.7427273156
196PhosphorylationDNGGYYISPRITFPC
CCCCEEECCCEECCC		7.6328152594
213UbiquitinationDMIKHYQKQADGLCR
HHHHHHHHHHHHHHH		40.04-
224UbiquitinationGLCRRLEKACISPKP
HHHHHHHHHCCCCCC		53.82-
228PhosphorylationRLEKACISPKPQKPW
HHHHHCCCCCCCCCC		27.1025159151
246PhosphorylationAWEIPRESIKLVKRL
CCCCCHHHHHHHHHH		26.7130108239
265PhosphorylationFGEVWMGYYNNSTKV
CCCEEEEEECCCCEE		6.2128450419
266PhosphorylationGEVWMGYYNNSTKVA
CCEEEEEECCCCEEE		11.3527259358
269PhosphorylationWMGYYNNSTKVAVKT
EEEEECCCCEEEEEE		26.4330108239
270PhosphorylationMGYYNNSTKVAVKTL
EEEECCCCEEEEEEC		31.4930108239
276PhosphorylationSTKVAVKTLKPGTMS
CCEEEEEECCCCCEE		33.15-
281PhosphorylationVKTLKPGTMSVQAFL
EEECCCCCEEHHHHH		18.14-
283PhosphorylationTLKPGTMSVQAFLEE
ECCCCCEEHHHHHHH		15.77-
296PhosphorylationEEANLMKTLQHDKLV
HHHCHHHHHHHCCCC		20.06-
306PhosphorylationHDKLVRLYAVVTREE
HCCCCEEEEEEECCC		6.1820007894
310PhosphorylationVRLYAVVTREEPIYI
CEEEEEEECCCCEEE		26.2626356563
316PhosphorylationVTREEPIYIITEYMA
EECCCCEEEEEEHHH		9.2927273156
319PhosphorylationEEPIYIITEYMAKGS
CCCEEEEEEHHHCCC		16.1126356563
321PhosphorylationPIYIITEYMAKGSLL
CEEEEEEHHHCCCHH		8.1726356563
326PhosphorylationTEYMAKGSLLDFLKS
EEHHHCCCHHHHHHC		25.6727251275
332UbiquitinationGSLLDFLKSDEGGKV
CCHHHHHHCCCCCEE		56.72-
338UbiquitinationLKSDEGGKVLLPKLI
HHCCCCCEEEHHHHH		40.33-
381S-palmitoylationLVSESLMCKIADFGL
EECHHHHHHHHHHCE		3.3231142470
397PhosphorylationRVIEDNEYTAREGAK
EEEECCCEECCCCCC		16.3819664994
397DephosphorylationRVIEDNEYTAREGAK
EEEECCCEECCCCCC		16.3811042209
398PhosphorylationVIEDNEYTAREGAKF
EEECCCEECCCCCCC		17.0421945579
404UbiquitinationYTAREGAKFPIKWTA
EECCCCCCCCCCCCC		63.63-
438PhosphorylationILLYEIVTYGKIPYP
HHHHHHHHHCCCCCC		32.02-
439PhosphorylationLLYEIVTYGKIPYPG
HHHHHHHHCCCCCCC		12.91-
448PhosphorylationKIPYPGRTNADVMTA
CCCCCCCCCHHHHHH		40.45-
454PhosphorylationRTNADVMTALSQGYR
CCCHHHHHHHHCCCC		25.0520860994
456 (in isoform 2)Ubiquitination-2.6321890473
457PhosphorylationADVMTALSQGYRMPR
HHHHHHHHCCCCCCC		21.0620071362
460PhosphorylationMTALSQGYRMPRVEN
HHHHHCCCCCCCCCC		8.9727259358
473PhosphorylationENCPDELYDIMKMCW
CCCCHHHHHHHHHHH		11.0227273156
477UbiquitinationDELYDIMKMCWKEKA
HHHHHHHHHHHHHHH		31.1021890473
477 (in isoform 1)Ubiquitination-31.1021890473
489PhosphorylationEKAEERPTFDYLQSV
HHHHHCCCHHHHHHH		35.0518691976
492PhosphorylationEERPTFDYLQSVLDD
HHCCCHHHHHHHHHH		11.4926356563
495PhosphorylationPTFDYLQSVLDDFYT
CCHHHHHHHHHHHHH		23.2726356563
501PhosphorylationQSVLDDFYTATEGQY
HHHHHHHHHHCCCCC		11.4925159151
502PhosphorylationSVLDDFYTATEGQYQ
HHHHHHHHHCCCCCC		27.3925159151
504PhosphorylationLDDFYTATEGQYQQQ
HHHHHHHCCCCCCCC		32.6125159151
508DephosphorylationYTATEGQYQQQP---
HHHCCCCCCCCC---		21.1010415030
508PhosphorylationYTATEGQYQQQP---
HHHCCCCCCCCC---		21.1025159151
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
32YPhosphorylationKinaseEGFRP00533
PSP
397YPhosphorylationKinaseLYNP07948
PSP
397YPhosphorylationKinaseAXLP30530
PSP
508YPhosphorylationKinaseCSKP41240
Uniprot
508YPhosphorylationKinaseLYNP07948
PSP
508YPhosphorylationKinaseCTKP42679
PSP
-KUbiquitinationE3 ubiquitin ligaseCBLP22681
PMID:15190072
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:10683340
-KUbiquitinationE3 ubiquitin ligaseSOCS1O15524
PMID:17905674
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LYN_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of LYN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MUC1_HUMANMUC1physical
12750561
PDE4A_HUMANPDE4Aphysical
10206997
CD22_HUMANCD22physical
10748054
PTN6_HUMANPTPN6physical
10574931
CDK1_HUMANCDK1physical
8051175
U119A_HUMANUNC119physical
12496276
GAB2_HUMANGAB2physical
11971018
DOK1_HUMANDOK1physical
11071635
CASL_HUMANNEDD9physical
9020138
BCAR1_HUMANBCAR1physical
9020138
PLCG2_HUMANPLCG2physical
8395016
GAB3_HUMANGAB3physical
11739737
JAK2_HUMANJAK2physical
9573010
EPOR_HUMANEPORphysical
9573010
SKAP2_HUMANSKAP2physical
9837776
CDK1_HUMANCDK1physical
8910336
KS6B1_HUMANRPS6KB1physical
16640565
KS6B2_HUMANRPS6KB2physical
16640565
KIT_HUMANKITphysical
11825908
DOK1_HUMANDOK1physical
11825908
SKAP1_HUMANSKAP1physical
9195899
IL3RB_HUMANCSF2RBphysical
9973406
PRKDC_HUMANPRKDCphysical
9748231
EVL_HUMANEVLphysical
10945997
PR15A_HUMANPPP1R15Aphysical
11517336
PECA1_HUMANPECAM1physical
10858437
PHAG1_HUMANPAG1physical
10790433
TRAT1_HUMANTRAT1physical
10790433
CBL_HUMANCBLphysical
12244174
NMT1_HUMANNMT1physical
11594778
TYK2_HUMANTYK2physical
9633884
CD72_HUMANCD72physical
9590210
RL10_HUMANRPL10physical
12138090
KIT_HUMANKITphysical
9341198
SHC1_HUMANSHC1physical
7650013
HCLS1_HUMANHCLS1physical
7682714
PP1R8_HUMANPPP1R8physical
11104670
PK3CG_HUMANPIK3CGphysical
10318860
BCAR1_HUMANBCAR1physical
9581808
PTPRC_HUMANPTPRCphysical
7516335
TRPV4_HUMANTRPV4physical
12538589
CSF1R_HUMANCSF1Rphysical
7636265
IL3RB_HUMANCSF2RBphysical
7636265
TNFL6_HUMANFASLGphysical
17164290
CENPV_HUMANCENPVphysical
19930468
NFIP2_HUMANNDFIP2physical
20534535
KHDR1_HUMANKHDRBS1physical
22745667
SH3K1_HUMANSH3KBP1physical
15707590
KHDR1_HUMANKHDRBS1physical
15190072
CBL_HUMANCBLphysical
15190072
FGFR2_HUMANFGFR2physical
15190072
P53_HUMANTP53physical
12642697
CBL_HUMANCBLphysical
18235045
CBP_HUMANCREBBPphysical
22364282
CBL_HUMANCBLphysical
7782294
PK3CG_HUMANPIK3CGphysical
7721825
CBL_HUMANCBLphysical
7721825
LYN_HUMANLYNphysical
11157475
PDE4D_HUMANPDE4Dphysical
10571082
ACSL3_HUMANACSL3physical
20605918
SH21A_HUMANSH2D1Aphysical
23503679
ANR54_HUMANANKRD54physical
23503679
HNRPK_HUMANHNRNPKphysical
23503679
RN180_HUMANRNF180physical
23503679
KHDR2_HUMANKHDRBS2physical
23503679
LNP1_HUMANLNP1physical
23503679
P55G_HUMANPIK3R3physical
23503679
PAK1_HUMANPAK1physical
23503679
SH2D3_HUMANSH2D3Cphysical
23503679
HBS1L_HUMANHBS1Lphysical
23503679
RADI_HUMANRDXphysical
23503679
SH24A_HUMANSH2D4Aphysical
23503679
CFA91_HUMANMAATS1physical
23503679
DTX3_HUMANDTX3physical
23503679
HXC4_HUMANHOXC4physical
23503679
CBX6_HUMANCBX6physical
23503679
ZN189_HUMANZNF189physical
23503679
FRS2_HUMANFRS2physical
23503679
UPAR_HUMANPLAURphysical
23503679
KPCB_HUMANPRKCBphysical
23503679
5HT2A_HUMANHTR2Aphysical
23503679
SLIK4_HUMANSLITRK4physical
23503679
ANGP2_HUMANANGPT2physical
23503679
YETS4_HUMANYEATS4physical
23503679
LAMP2_HUMANLAMP2physical
23503679
TPTE2_HUMANTPTE2physical
23503679
TYW1_HUMANTYW1physical
23503679
RIMS2_HUMANRIMS2physical
23503679
OSB11_HUMANOSBPL11physical
23503679
CP4V2_HUMANCYP4V2physical
23503679
TGDS_HUMANTGDSphysical
23503679
DVL2_HUMANDVL2physical
23503679
UGPA_HUMANUGP2physical
23503679
ZN423_HUMANZNF423physical
23503679
TTYH3_HUMANTTYH3physical
23503679
NKAPL_HUMANNKAPLphysical
23503679
ERO1A_HUMANERO1Lphysical
23503679
FSD1L_HUMANFSD1Lphysical
23503679
ENPL_HUMANHSP90B1physical
23503679
NFYB_HUMANNFYBphysical
23503679
OCLN_HUMANOCLNphysical
23503679
RBM11_HUMANRBM11physical
23503679
TAD2A_HUMANTADA2Aphysical
23503679
DNA2_HUMANDNA2physical
23503679
LRIQ3_HUMANLRRIQ3physical
23503679
DEN2C_HUMANDENND2Cphysical
23503679
CNO10_HUMANCNOT10physical
23503679
HDGR3_HUMANHDGFRP3physical
23503679
TNF12_HUMANTNFSF12physical
23503679
PRUN2_HUMANPRUNE2physical
23503679
CPT1A_HUMANCPT1Aphysical
23503679
TMX1_HUMANTMX1physical
23503679
TBB4A_HUMANTUBB4Aphysical
23503679
GTPB3_HUMANGTPBP3physical
23503679
MCL1_HUMANMCL1physical
23503679
ZCHC7_HUMANZCCHC7physical
23503679
ZN577_HUMANZNF577physical
23503679
TFDP3_HUMANTFDP3physical
23503679
SCIMP_HUMANSCIMPphysical
23503679
ADA22_HUMANADAM22physical
23503679
DOXA1_HUMANDUOXA1physical
23503679
E2F6_HUMANE2F6physical
23503679
CU059_HUMANC21orf59physical
23503679
PKHH2_HUMANPLEKHH2physical
23503679
S12A4_HUMANSLC12A4physical
23503679
FBX28_HUMANFBXO28physical
23503679
RHG19_HUMANARHGAP19physical
23503679
DTL_HUMANDTLphysical
23503679
DDX21_HUMANDDX21physical
23503679
SPESP_HUMANSPESP1physical
23503679
SCG3_HUMANSCG3physical
23503679
S22AG_HUMANSLC22A16physical
23503679
KYNU_HUMANKYNUphysical
23503679
MAIP1_HUMANC2orf47physical
23503679
RASF8_HUMANRASSF8physical
23503679
CAD23_HUMANCDH23physical
23503679
CDN1B_HUMANCDKN1Bphysical
17254966
TNFA_HUMANTNFphysical
9230816
IL1B_HUMANIL1Bphysical
9230816
RGS16_HUMANRGS16physical
12588871
TIF1B_HUMANTRIM28physical
23645696
NEMO_HUMANIKBKGphysical
23131831
FAK1_HUMANPTK2physical
25814554
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D10202 Bafetinib (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LYN_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-6; SER-11; SER-13;THR-30; TYR-32; THR-37; TYR-193; TYR-194; SER-228; TYR-265; TYR-306;TYR-316; TYR-473; THR-489; THR-502 AND TYR-508, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND SER-13, AND MASSSPECTROMETRY.
"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-11; SER-13; TYR-32;TYR-194; SER-228; TYR-397; TYR-473 AND TYR-508, 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-13 AND TYR-397, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, 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-13, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11 AND TYR-508, 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-193; TYR-397 ANDTYR-508, AND MASS SPECTROMETRY.
"Oncogenic association of the Cbp/PAG adaptor protein with the Lyntyrosine kinase in human B-NHL rafts.";
Tauzin S., Ding H., Khatib K., Ahmad I., Burdevet D.,van Echten-Deckert G., Lindquist J.A., Schraven B., Din N.U.,Borisch B., Hoessli D.C.;
Blood 111:2310-2320(2008).
Cited for: FUNCTION, PHOSPHORYLATION AT TYR-397 AND TYR-508, INTERACTION WITHPAG1 AND STAT3, AND SUBCELLULAR LOCATION.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-316, AND MASSSPECTROMETRY.
"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-193; TYR-194; TYR-306;TYR-397; TYR-473 AND TYR-508, AND MASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-508, AND MASSSPECTROMETRY.
"Translocation of the Csk homologous kinase (Chk/Hyl) controlsactivity of CD36-anchored Lyn tyrosine kinase in thrombin-stimulatedplatelets.";
Hirao A., Hamaguchi I., Suda T., Yamaguchi N.;
EMBO J. 16:2342-2351(1997).
Cited for: PHOSPHORYLATION AT TYR-508 BY MATK.
"Functional analysis of Csk in signal transduction through the B-cellantigen receptor.";
Hata A., Sabe H., Kurosaki T., Takata M., Hanafusa H.;
Mol. Cell. Biol. 14:7306-7313(1994).
Cited for: PHOSPHORYLATION AT TYR-397 AND TYR-508, AND ENZYME REGULATION.

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