GIT1_HUMAN - dbPTM
GIT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GIT1_HUMAN
UniProt AC Q9Y2X7
Protein Name ARF GTPase-activating protein GIT1
Gene Name GIT1
Organism Homo sapiens (Human).
Sequence Length 761
Subcellular Localization Cytoplasm . Cycles between at least 3 distinct intracellular compartments, including focal adhesions, cytoplasmic complexes and membrane protrusions. During cell migration, when cells detach, moves from the adhesions into the cytoplasmic complexes to
Protein Description GTPase-activating protein for the ADP ribosylation factor family. May serve as a scaffold to bring together molecules to form signaling modules controlling vesicle trafficking, adhesion and cytoskeletal organization. Increases the speed of cell migration, as well as the size and rate of formation of protrusions, possibly by targeting PAK1 to adhesions and the leading edge of lamellipodia. Sequesters inactive non-tyrosine-phosphorylated paxillin in cytoplasmic complexes. Involved in the regulation of cytokinesis; the function may involve SDCCAG3 and PTPN13 (By similarity)..
Protein Sequence MSRKGPRAEVCADCSAPDPGWASISRGVLVCDECCSVHRSLGRHISIVKHLRHSAWPPTLLQMVHTLASNGANSIWEHSLLDPAQVQSGRRKANPQDKVHPIKSEFIRAKYQMLAFVHKLPCRDDDGVTAKDLSKQLHSSVRTGNLETCLRLLSLGAQANFFHPEKGTTPLHVAAKAGQTLQAELLVVYGADPGSPDVNGRTPIDYARQAGHHELAERLVECQYELTDRLAFYLCGRKPDHKNGHYIIPQMADSLDLSELAKAAKKKLQALSNRLFEELAMDVYDEVDRRENDAVWLATQNHSTLVTERSAVPFLPVNPEYSATRNQGRQKLARFNAREFATLIIDILSEAKRRQQGKSLSSPTDNLELSLRSQSDLDDQHDYDSVASDEDTDQEPLRSTGATRSNRARSMDSSDLSDGAVTLQEYLELKKALATSEAKVQQLMKVNSSLSDELRRLQREIHKLQAENLQLRQPPGPVPTPPLPSERAEHTPMAPGGSTHRRDRQAFSMYEPGSALKPFGGPPGDELTTRLQPFHSTELEDDAIYSVHVPAGLYRIRKGVSASAVPFTPSSPLLSCSQEGSRHTSKLSRHGSGADSDYENTQSGDPLLGLEGKRFLELGKEEDFHPELESLDGDLDPGLPSTEDVILKTEQVTKNIQELLRAAQEFKHDSFVPCSEKIHLAVTEMASLFPKRPALEPVRSSLRLLNASAYRLQSECRKTVPPEPGAPVDFQLLTQQVIQCAYDIAKAAKQLVTITTREKKQ
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
23PhosphorylationAPDPGWASISRGVLV
CCCCCCCCCCCCEEE
18.0027251275
25PhosphorylationDPGWASISRGVLVCD
CCCCCCCCCCEEECH
22.0827251275
36PhosphorylationLVCDECCSVHRSLGR
EECHHHHHHHHHHHH
32.3927251275
46PhosphorylationRSLGRHISIVKHLRH
HHHHHHHHHHHHHHH
18.4024719451
49UbiquitinationGRHISIVKHLRHSAW
HHHHHHHHHHHHCCC
34.94-
49 (in isoform 3)Ubiquitination-34.94-
54PhosphorylationIVKHLRHSAWPPTLL
HHHHHHHCCCCHHHH
26.12-
103UbiquitinationQDKVHPIKSEFIRAK
CCCCCCCHHHHHHHH
48.67-
104PhosphorylationDKVHPIKSEFIRAKY
CCCCCCHHHHHHHHH
38.1629514088
111PhosphorylationSEFIRAKYQMLAFVH
HHHHHHHHHHHHHHH
9.7329759185
119AcetylationQMLAFVHKLPCRDDD
HHHHHHHCCCCCCCC
49.1525953088
134PhosphorylationGVTAKDLSKQLHSSV
CCCHHHHHHHHHHHH
28.6117287340
135UbiquitinationVTAKDLSKQLHSSVR
CCHHHHHHHHHHHHH
65.26-
135 (in isoform 3)Malonylation-65.2626320211
135 (in isoform 3)Ubiquitination-65.26-
139PhosphorylationDLSKQLHSSVRTGNL
HHHHHHHHHHHHCCH
38.8428857561
154PhosphorylationETCLRLLSLGAQANF
HHHHHHHHHCCCCEE
29.3728857561
166AcetylationANFFHPEKGTTPLHV
CEEECCCCCCCCHHH
67.0425953088
168PhosphorylationFFHPEKGTTPLHVAA
EECCCCCCCCHHHHH
35.99-
169PhosphorylationFHPEKGTTPLHVAAK
ECCCCCCCCHHHHHH
32.30-
202PhosphorylationSPDVNGRTPIDYARQ
CCCCCCCCHHHHHHH
26.4521712546
224PhosphorylationERLVECQYELTDRLA
HHHHHHHHHHHHHHH
25.2728152594
227PhosphorylationVECQYELTDRLAFYL
HHHHHHHHHHHHHHH
13.7228152594
246PhosphorylationPDHKNGHYIIPQMAD
CCCCCCCCCHHHCCC
11.2730576142
254PhosphorylationIIPQMADSLDLSELA
CHHHCCCCCCHHHHH
17.7828348404
258PhosphorylationMADSLDLSELAKAAK
CCCCCCHHHHHHHHH
30.1730576142
261PhosphorylationSLDLSELAKAAKKKL
CCCHHHHHHHHHHHH
8.73-
261 (in isoform 3)Phosphorylation-8.7322817900
263PhosphorylationDLSELAKAAKKKLQA
CHHHHHHHHHHHHHH
20.93-
263 (in isoform 3)Phosphorylation-20.9322817900
284PhosphorylationEELAMDVYDEVDRRE
HHHHHHHHHHHHHHH
11.3416825424
293PhosphorylationEVDRRENDAVWLATQ
HHHHHHCCCEEEECC
37.43-
303PhosphorylationWLATQNHSTLVTERS
EEECCCCCCCEECCC
30.8728857561
304PhosphorylationLATQNHSTLVTERSA
EECCCCCCCEECCCC
20.0728857561
307PhosphorylationQNHSTLVTERSAVPF
CCCCCCEECCCCCCC
28.8828857561
321PhosphorylationFLPVNPEYSATRNQG
CCCCCHHHCCCCCHH
12.5920689073
322PhosphorylationLPVNPEYSATRNQGR
CCCCHHHCCCCCHHH
22.8528348404
324PhosphorylationVNPEYSATRNQGRQK
CCHHHCCCCCHHHHH
24.9828348404
333PhosphorylationNQGRQKLARFNAREF
CHHHHHHHHHHHHHH
22.5127251275
358UbiquitinationAKRRQQGKSLSSPTD
HHHHHCCCCCCCCCC
43.83-
359PhosphorylationKRRQQGKSLSSPTDN
HHHHCCCCCCCCCCC
40.0630266825
361PhosphorylationRQQGKSLSSPTDNLE
HHCCCCCCCCCCCHH
41.1729255136
362PhosphorylationQQGKSLSSPTDNLEL
HCCCCCCCCCCCHHH
36.7929255136
364PhosphorylationGKSLSSPTDNLELSL
CCCCCCCCCCHHHHC
39.1929255136
370PhosphorylationPTDNLELSLRSQSDL
CCCCHHHHCCCCCCC
16.6225159151
371PhosphorylationTDNLELSLRSQSDLD
CCCHHHHCCCCCCCC
10.7724719451
373PhosphorylationNLELSLRSQSDLDDQ
CHHHHCCCCCCCCCC
39.0523927012
375PhosphorylationELSLRSQSDLDDQHD
HHHCCCCCCCCCCCC
41.1923927012
379PhosphorylationRSQSDLDDQHDYDSV
CCCCCCCCCCCHHHC
55.8227251275
382PhosphorylationSDLDDQHDYDSVASD
CCCCCCCCHHHCCCC
43.21-
383PhosphorylationDLDDQHDYDSVASDE
CCCCCCCHHHCCCCC
14.1623927012
384PhosphorylationLDDQHDYDSVASDED
CCCCCCHHHCCCCCC
42.57-
385PhosphorylationDDQHDYDSVASDEDT
CCCCCHHHCCCCCCC
17.2220201521
388PhosphorylationHDYDSVASDEDTDQE
CCHHHCCCCCCCCCC
39.1020201521
392PhosphorylationSVASDEDTDQEPLRS
HCCCCCCCCCCCHHH
37.2223927012
394PhosphorylationASDEDTDQEPLRSTG
CCCCCCCCCCHHHCC
57.1924719451
397PhosphorylationEDTDQEPLRSTGATR
CCCCCCCHHHCCCCH
7.1324719451
399PhosphorylationTDQEPLRSTGATRSN
CCCCCHHHCCCCHHH
38.5921406692
400PhosphorylationDQEPLRSTGATRSNR
CCCCHHHCCCCHHHC
25.1321406692
401PhosphorylationQEPLRSTGATRSNRA
CCCHHHCCCCHHHCC
26.63-
403PhosphorylationPLRSTGATRSNRARS
CHHHCCCCHHHCCCC
35.6630576142
410PhosphorylationTRSNRARSMDSSDLS
CHHHCCCCCCHHHCC
26.4223927012
413PhosphorylationNRARSMDSSDLSDGA
HCCCCCCHHHCCCCC
19.6730266825
414PhosphorylationRARSMDSSDLSDGAV
CCCCCCHHHCCCCCE
38.0030278072
417PhosphorylationSMDSSDLSDGAVTLQ
CCCHHHCCCCCEEHH
38.7030278072
419PhosphorylationDSSDLSDGAVTLQEY
CHHHCCCCCEEHHHH
20.6924719451
422PhosphorylationDLSDGAVTLQEYLEL
HCCCCCEEHHHHHHH
23.3823927012
423PhosphorylationLSDGAVTLQEYLELK
CCCCCEEHHHHHHHH
2.68-
426PhosphorylationGAVTLQEYLELKKAL
CCEEHHHHHHHHHHH
7.7823403867
448PhosphorylationQQLMKVNSSLSDELR
HHHHHHCCHHHHHHH
35.3322817900
449PhosphorylationQLMKVNSSLSDELRR
HHHHHCCHHHHHHHH
27.0422817900
451PhosphorylationMKVNSSLSDELRRLQ
HHHCCHHHHHHHHHH
30.8727251275
457PhosphorylationLSDELRRLQREIHKL
HHHHHHHHHHHHHHH
4.56-
458PhosphorylationSDELRRLQREIHKLQ
HHHHHHHHHHHHHHH
38.8727251275
463AcetylationRLQREIHKLQAENLQ
HHHHHHHHHHHHHCC
48.2125953088
480PhosphorylationQPPGPVPTPPLPSER
CCCCCCCCCCCCCHH
37.4630266825
485PhosphorylationVPTPPLPSERAEHTP
CCCCCCCCHHCCCCC
47.6123403867
489PhosphorylationPLPSERAEHTPMAPG
CCCCHHCCCCCCCCC
55.2924719451
491PhosphorylationPSERAEHTPMAPGGS
CCHHCCCCCCCCCCC
13.2820068231
498PhosphorylationTPMAPGGSTHRRDRQ
CCCCCCCCCCCCCCC
27.2723401153
499PhosphorylationPMAPGGSTHRRDRQA
CCCCCCCCCCCCCCC
23.7623401153
500PhosphorylationMAPGGSTHRRDRQAF
CCCCCCCCCCCCCCH
25.1924719451
507PhosphorylationHRRDRQAFSMYEPGS
CCCCCCCHHCCCCCC
3.0627251275
508PhosphorylationRRDRQAFSMYEPGSA
CCCCCCHHCCCCCCC
24.3821945579
510PhosphorylationDRQAFSMYEPGSALK
CCCCHHCCCCCCCCC
20.1321945579
514PhosphorylationFSMYEPGSALKPFGG
HHCCCCCCCCCCCCC
40.9421945579
517MethylationYEPGSALKPFGGPPG
CCCCCCCCCCCCCCC
37.71-
517PhosphorylationYEPGSALKPFGGPPG
CCCCCCCCCCCCCCC
37.7127251275
519PhosphorylationPGSALKPFGGPPGDE
CCCCCCCCCCCCCCH
19.77-
536PhosphorylationTRLQPFHSTELEDDA
CCCCCCCCCCCCCCC
24.7722617229
537PhosphorylationRLQPFHSTELEDDAI
CCCCCCCCCCCCCCE
35.7022617229
545PhosphorylationELEDDAIYSVHVPAG
CCCCCCEEEEEECCC
13.3227273156
546PhosphorylationLEDDAIYSVHVPAGL
CCCCCEEEEEECCCH
10.3027273156
554PhosphorylationVHVPAGLYRIRKGVS
EEECCCHHHHCCCCC
11.7715570572
555PhosphorylationHVPAGLYRIRKGVSA
EECCCHHHHCCCCCC
27.55-
561O-linked_GlycosylationYRIRKGVSASAVPFT
HHHCCCCCCCCCCCC
25.7728657654
561PhosphorylationYRIRKGVSASAVPFT
HHHCCCCCCCCCCCC
25.7729255136
563PhosphorylationIRKGVSASAVPFTPS
HCCCCCCCCCCCCCC
23.4629255136
568PhosphorylationSASAVPFTPSSPLLS
CCCCCCCCCCCCCCC
19.0529255136
570PhosphorylationSAVPFTPSSPLLSCS
CCCCCCCCCCCCCCC
41.3429255136
571PhosphorylationAVPFTPSSPLLSCSQ
CCCCCCCCCCCCCCC
22.2923401153
572PhosphorylationVPFTPSSPLLSCSQE
CCCCCCCCCCCCCCC
41.4827251275
575PhosphorylationTPSSPLLSCSQEGSR
CCCCCCCCCCCCCCC
21.2929255136
577PhosphorylationSSPLLSCSQEGSRHT
CCCCCCCCCCCCCHH
28.0829255136
579PhosphorylationPLLSCSQEGSRHTSK
CCCCCCCCCCCHHHH
42.7327251275
580PhosphorylationLLSCSQEGSRHTSKL
CCCCCCCCCCHHHHH
23.4924719451
581PhosphorylationLSCSQEGSRHTSKLS
CCCCCCCCCHHHHHH
21.8228348404
584PhosphorylationSQEGSRHTSKLSRHG
CCCCCCHHHHHHHCC
26.8430576142
585PhosphorylationQEGSRHTSKLSRHGS
CCCCCHHHHHHHCCC
26.0230576142
586PhosphorylationEGSRHTSKLSRHGSG
CCCCHHHHHHHCCCC
52.1927251275
588PhosphorylationSRHTSKLSRHGSGAD
CCHHHHHHHCCCCCC
26.4325849741
592PhosphorylationSKLSRHGSGADSDYE
HHHHHCCCCCCCCCC
25.3629255136
594PhosphorylationLSRHGSGADSDYENT
HHHCCCCCCCCCCCC
18.1624719451
596PhosphorylationRHGSGADSDYENTQS
HCCCCCCCCCCCCCC
41.3729255136
598PhosphorylationGSGADSDYENTQSGD
CCCCCCCCCCCCCCC
18.2829255136
601PhosphorylationADSDYENTQSGDPLL
CCCCCCCCCCCCCCC
16.5123927012
603PhosphorylationSDYENTQSGDPLLGL
CCCCCCCCCCCCCCC
43.0330266825
605PhosphorylationYENTQSGDPLLGLEG
CCCCCCCCCCCCCCC
35.6024719451
607PhosphorylationNTQSGDPLLGLEGKR
CCCCCCCCCCCCCHH
7.63-
610PhosphorylationSGDPLLGLEGKRFLE
CCCCCCCCCCHHHHH
8.71-
613UbiquitinationPLLGLEGKRFLELGK
CCCCCCCHHHHHCCC
30.51-
630PhosphorylationDFHPELESLDGDLDP
CCCHHHHHCCCCCCC
44.3722817900
639PhosphorylationDGDLDPGLPSTEDVI
CCCCCCCCCCHHHHH
3.54-
670PhosphorylationAQEFKHDSFVPCSEK
HHHHCCCCCCCCHHH
28.0625849741
675PhosphorylationHDSFVPCSEKIHLAV
CCCCCCCHHHHHHHH
35.5423403867
677AcetylationSFVPCSEKIHLAVTE
CCCCCHHHHHHHHHH
21.0911794205
679PhosphorylationVPCSEKIHLAVTEMA
CCCHHHHHHHHHHHH
20.8527251275
700PhosphorylationPALEPVRSSLRLLNA
CCCHHHHHHHHHHCH
33.6816797488
701PhosphorylationALEPVRSSLRLLNAS
CCHHHHHHHHHHCHH
13.6222817900
708PhosphorylationSLRLLNASAYRLQSE
HHHHHCHHHHHHHHH
25.4321406692
709PhosphorylationLRLLNASAYRLQSEC
HHHHCHHHHHHHHHH
7.34-
710PhosphorylationRLLNASAYRLQSECR
HHHCHHHHHHHHHHH
14.9021406692
749AcetylationYDIAKAAKQLVTITT
HHHHHHHHHHHEEEC
49.3725953088
753PhosphorylationKAAKQLVTITTREKK
HHHHHHHEEECCCCC
22.6223917254
755PhosphorylationAKQLVTITTREKKQ-
HHHHHEEECCCCCC-
15.5023186163

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
46SPhosphorylationKinasePRKD3O94806
PSP
246YPhosphorylationKinaseSRCP12931
PSP
284YPhosphorylationKinaseSRCP12931
PSP
321YPhosphorylationKinasePTK2Q05397
GPS
321YPhosphorylationKinaseSRCP12931
PSP
508SPhosphorylationKinasePAK1Q13153
PSP
700SPhosphorylationKinasePAK1Q13153
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GIT1_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 GIT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLCG1_HUMANPLCG1physical
14523024
LIPA4_HUMANPPFIA4physical
12629171
LIPA1_HUMANPPFIA1physical
12629171
FAK1_HUMANPTK2physical
12629171
FAK2_HUMANPTK2Bphysical
12629171
PTPRF_HUMANPTPRFphysical
12629171
PAXI_HUMANPXNphysical
12629171
ARBK1_HUMANADRBK1physical
10896954
PCLO_HUMANPCLOphysical
12473661
ARHG7_HUMANARHGEF7physical
12473661
FAK1_HUMANPTK2physical
12473661
GIT1_HUMANGIT1physical
12473661
GIT2_HUMANGIT2physical
12473661
FAK1_HUMANPTK2physical
10938112
PTPRZ_HUMANPTPRZ1physical
11381105
ARHG6_HUMANARHGEF6physical
10428811
ARHG7_HUMANARHGEF7physical
10428811
ARBK1_HUMANADRBK1physical
9826657
ARBK2_HUMANADRBK2physical
9826657
HD_HUMANHTTphysical
15383276
LRIF1_HUMANLRIF1physical
15383276
HAP1_HUMANHAP1physical
15383276
SNRPA_HUMANSNRPAphysical
22863883
PKN3_HUMANPKN3physical
27173435
NCK5L_HUMANNCKAP5Lphysical
27173435

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
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GIT1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; THR-364; SER-375;TYR-383; SER-385; SER-388; THR-392; SER-410; TYR-545; SER-561;SER-592; SER-596 AND THR-601, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; TYR-383; SER-388;SER-592 AND TYR-598, AND MASS SPECTROMETRY.
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385 AND SER-388, ANDMASS 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-362; SER-373; TYR-383;SER-385; SER-388; THR-392; SER-410; SER-592 AND SER-596, AND MASSSPECTROMETRY.
"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-385; SER-388; SER-592AND TYR-598, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, 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-385; SER-388; SER-592AND TYR-598, AND MASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388, 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-545, AND MASSSPECTROMETRY.
"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-545, AND MASSSPECTROMETRY.
"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-545 AND TYR-554, ANDMASS SPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-545, AND MASSSPECTROMETRY.
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-598, AND MASSSPECTROMETRY.

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