GAB1_HUMAN - dbPTM
GAB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GAB1_HUMAN
UniProt AC Q13480
Protein Name GRB2-associated-binding protein 1
Gene Name GAB1
Organism Homo sapiens (Human).
Sequence Length 694
Subcellular Localization
Protein Description Adapter protein that plays a role in intracellular signaling cascades triggered by activated receptor-type kinases. Plays a role in FGFR1 signaling. Probably involved in signaling by the epidermal growth factor receptor (EGFR) and the insulin receptor (INSR)..
Protein Sequence MSGGEVVCSGWLRKSPPEKKLKRYAWKRRWFVLRSGRLTGDPDVLEYYKNDHAKKPIRIIDLNLCQQVDAGLTFNKKEFENSYIFDINTIDRIFYLVADSEEEMNKWVRCICDICGFNPTEEDPVKPPGSSLQAPADLPLAINTAPPSTQADSSSATLPPPYQLINVPPHLETLGIQEDPQDYLLLINCQSKKPEPTRTHADSAKSTSSETDCNDNVPSHKNPASSQSKHGMNGFFQQQMIYDSPPSRAPSASVDSSLYNLPRSYSHDVLPKVSPSSTEADGELYVFNTPSGTSSVETQMRHVSISYDIPPTPGNTYQIPRTFPEGTLGQTSKLDTIPDIPPPRPPKPHPAHDRSPVETCSIPRTASDTDSSYCIPTAGMSPSRSNTISTVDLNKLRKDASSQDCYDIPRAFPSDRSSSLEGFHNHFKVKNVLTVGSVSSEELDENYVPMNPNSPPRQHSSSFTEPIQEANYVPMTPGTFDFSSFGMQVPPPAHMGFRSSPKTPPRRPVPVADCEPPPVDRNLKPDRKVKPAPLEIKPLPEWEELQAPVRSPITRSFARDSSRFPMSPRPDSVHSTTSSSDSHDSEENYVPMNPNLSSEDPNLFGSNSLDGGSSPMIKPKGDKQVEYLDLDLDSGKSTPPRKQKSSGSGSSVADERVDYVVVDQQKTLALKSTREAWTDGRQSTESETPAKSVK
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
2Acetylation------MSGGEVVCS
------CCCCEEEEC
56.3522223895
47PhosphorylationGDPDVLEYYKNDHAK
CCHHHHHHHCCCCCC
18.6423917254
48PhosphorylationDPDVLEYYKNDHAKK
CHHHHHHHCCCCCCC
8.2419881549
83PhosphorylationKKEFENSYIFDINTI
HHHHCCCEEEECCCC
19.7222751113
183PhosphorylationIQEDPQDYLLLINCQ
CCCCCCCEEEEEECC
8.2619534553
197PhosphorylationQSKKPEPTRTHADSA
CCCCCCCCCCCCCCC
46.6821130716
205UbiquitinationRTHADSAKSTSSETD
CCCCCCCCCCCCCCC
59.21-
206PhosphorylationTHADSAKSTSSETDC
CCCCCCCCCCCCCCC
32.9823312004
207PhosphorylationHADSAKSTSSETDCN
CCCCCCCCCCCCCCC
35.2523312004
208PhosphorylationADSAKSTSSETDCND
CCCCCCCCCCCCCCC
33.0125627689
209PhosphorylationDSAKSTSSETDCNDN
CCCCCCCCCCCCCCC
44.6025262027
211PhosphorylationAKSTSSETDCNDNVP
CCCCCCCCCCCCCCC
48.0425159151
221UbiquitinationNDNVPSHKNPASSQS
CCCCCCCCCCCHHHC
69.80-
242PhosphorylationFFQQQMIYDSPPSRA
CCEEEEECCCCCCCC
12.6727273156
244PhosphorylationQQQMIYDSPPSRAPS
EEEEECCCCCCCCCC
23.0327259358
247PhosphorylationMIYDSPPSRAPSASV
EECCCCCCCCCCCCC
44.4522798277
251PhosphorylationSPPSRAPSASVDSSL
CCCCCCCCCCCCHHH
31.9921945579
253PhosphorylationPSRAPSASVDSSLYN
CCCCCCCCCCHHHHC
30.6921945579
256PhosphorylationAPSASVDSSLYNLPR
CCCCCCCHHHHCCCC
21.7821945579
257PhosphorylationPSASVDSSLYNLPRS
CCCCCCHHHHCCCCC
30.3421945579
259PhosphorylationASVDSSLYNLPRSYS
CCCCHHHHCCCCCCC
19.3221945579
264PhosphorylationSLYNLPRSYSHDVLP
HHHCCCCCCCCCCCC
29.1027794612
265PhosphorylationLYNLPRSYSHDVLPK
HHCCCCCCCCCCCCC
16.0023403867
266PhosphorylationYNLPRSYSHDVLPKV
HCCCCCCCCCCCCCC
17.9225159151
274PhosphorylationHDVLPKVSPSSTEAD
CCCCCCCCCCCCCCC
25.7822199227
276PhosphorylationVLPKVSPSSTEADGE
CCCCCCCCCCCCCCC
42.2422199227
277PhosphorylationLPKVSPSSTEADGEL
CCCCCCCCCCCCCCE
33.3822199227
278PhosphorylationPKVSPSSTEADGELY
CCCCCCCCCCCCCEE
39.2622199227
285PhosphorylationTEADGELYVFNTPSG
CCCCCCEEEEECCCC
9.939890893
289PhosphorylationGELYVFNTPSGTSSV
CCEEEEECCCCCCCC
13.8427251275
291PhosphorylationLYVFNTPSGTSSVET
EEEEECCCCCCCCEE
53.3023090842
293PhosphorylationVFNTPSGTSSVETQM
EEECCCCCCCCEEEC
23.3623090842
294PhosphorylationFNTPSGTSSVETQMR
EECCCCCCCCEEECE
35.5923090842
295PhosphorylationNTPSGTSSVETQMRH
ECCCCCCCCEEECEE
24.6623090842
298PhosphorylationSGTSSVETQMRHVSI
CCCCCCEEECEEEEE
26.0527251275
304PhosphorylationETQMRHVSISYDIPP
EEECEEEEEEEECCC
10.3327259358
306PhosphorylationQMRHVSISYDIPPTP
ECEEEEEEEECCCCC
14.8326356563
307PhosphorylationMRHVSISYDIPPTPG
CEEEEEEEECCCCCC
19.0710734310
312PhosphorylationISYDIPPTPGNTYQI
EEEECCCCCCCCEEC
38.1727259358
316PhosphorylationIPPTPGNTYQIPRTF
CCCCCCCCEECCCCC
23.7927259358
317PhosphorylationPPTPGNTYQIPRTFP
CCCCCCCEECCCCCC
14.4025159151
322O-linked_GlycosylationNTYQIPRTFPEGTLG
CCEECCCCCCCCCCC
37.8830379171
355PhosphorylationPHPAHDRSPVETCSI
CCCCCCCCCCCCCCC
39.0819664994
359PhosphorylationHDRSPVETCSIPRTA
CCCCCCCCCCCCCCC
16.2828985074
361PhosphorylationRSPVETCSIPRTASD
CCCCCCCCCCCCCCC
42.9423312004
365O-linked_GlycosylationETCSIPRTASDTDSS
CCCCCCCCCCCCCCC
25.7630379171
365PhosphorylationETCSIPRTASDTDSS
CCCCCCCCCCCCCCC
25.7626356563
367PhosphorylationCSIPRTASDTDSSYC
CCCCCCCCCCCCCCE
40.1927259358
369PhosphorylationIPRTASDTDSSYCIP
CCCCCCCCCCCCEEE
34.9726356563
371PhosphorylationRTASDTDSSYCIPTA
CCCCCCCCCCEEECC
25.8730576142
372PhosphorylationTASDTDSSYCIPTAG
CCCCCCCCCEEECCC
27.1726356563
373PhosphorylationASDTDSSYCIPTAGM
CCCCCCCCEEECCCC
9.8010734310
377PhosphorylationDSSYCIPTAGMSPSR
CCCCEEECCCCCCCC
18.8728450419
381PhosphorylationCIPTAGMSPSRSNTI
EEECCCCCCCCCCCC
20.8530278072
383PhosphorylationPTAGMSPSRSNTIST
ECCCCCCCCCCCCEE
40.8227794612
385PhosphorylationAGMSPSRSNTISTVD
CCCCCCCCCCCEEEE
42.5428450419
387PhosphorylationMSPSRSNTISTVDLN
CCCCCCCCCEEEEHH
19.9729507054
389PhosphorylationPSRSNTISTVDLNKL
CCCCCCCEEEEHHHH
21.9726657352
390PhosphorylationSRSNTISTVDLNKLR
CCCCCCEEEEHHHHC
17.7528450419
401PhosphorylationNKLRKDASSQDCYDI
HHHCCCCCCCCCCCC
38.3722617229
402PhosphorylationKLRKDASSQDCYDIP
HHCCCCCCCCCCCCC
31.5825159151
405PhosphorylationKDASSQDCYDIPRAF
CCCCCCCCCCCCHHC
2.2617016520
406PhosphorylationDASSQDCYDIPRAFP
CCCCCCCCCCCHHCC
25.7910734310
414PhosphorylationDIPRAFPSDRSSSLE
CCCHHCCCCCCCCCC
38.9230624053
417PhosphorylationRAFPSDRSSSLEGFH
HHCCCCCCCCCCCHH
29.3030266825
418PhosphorylationAFPSDRSSSLEGFHN
HCCCCCCCCCCCHHC
39.5830266825
419PhosphorylationFPSDRSSSLEGFHNH
CCCCCCCCCCCHHCC
31.5223401153
434PhosphorylationFKVKNVLTVGSVSSE
CEEEEEEEECCCCHH
20.6625841592
437PhosphorylationKNVLTVGSVSSEELD
EEEEEECCCCHHHHC
17.9425921289
439PhosphorylationVLTVGSVSSEELDEN
EEEECCCCHHHHCCC
33.4628348404
440PhosphorylationLTVGSVSSEELDENY
EEECCCCHHHHCCCC
32.6928348404
447PhosphorylationSEELDENYVPMNPNS
HHHHCCCCCCCCCCC
12.139890893
454PhosphorylationYVPMNPNSPPRQHSS
CCCCCCCCCCCCCCC
37.2230278072
460PhosphorylationNSPPRQHSSSFTEPI
CCCCCCCCCCCCCCC
21.2426356563
461PhosphorylationSPPRQHSSSFTEPIQ
CCCCCCCCCCCCCCH
27.6126356563
462PhosphorylationPPRQHSSSFTEPIQE
CCCCCCCCCCCCCHH
38.9226356563
464PhosphorylationRQHSSSFTEPIQEAN
CCCCCCCCCCCHHCC
42.6826356563
472PhosphorylationEPIQEANYVPMTPGT
CCCHHCCCCCCCCCC
16.999890893
476PhosphorylationEANYVPMTPGTFDFS
HCCCCCCCCCCCCHH
16.7015379552
499PhosphorylationPAHMGFRSSPKTPPR
CCCCCCCCCCCCCCC
49.0528857561
500PhosphorylationAHMGFRSSPKTPPRR
CCCCCCCCCCCCCCC
26.5929496963
503PhosphorylationGFRSSPKTPPRRPVP
CCCCCCCCCCCCCCC
41.7430266825
545 (in isoform 2)Phosphorylation-3.4025850435
547 (in isoform 2)Phosphorylation-19.7228176443
549 (in isoform 2)Phosphorylation-12.1125850435
551PhosphorylationELQAPVRSPITRSFA
HHCCCCCCCCCHHHH
22.3826846344
554PhosphorylationAPVRSPITRSFARDS
CCCCCCCCHHHHCCC
24.5226846344
567PhosphorylationDSSRFPMSPRPDSVH
CCCCCCCCCCCCCCC
20.2815379552
589DephosphorylationSHDSEENYVPMNPNL
CCCCCCCCCCCCCCC
14.8110068651
589PhosphorylationSHDSEENYVPMNPNL
CCCCCCCCCCCCCCC
14.819890893
597PhosphorylationVPMNPNLSSEDPNLF
CCCCCCCCCCCCCCC
38.0215379552
627DephosphorylationKGDKQVEYLDLDLDS
CCCCCEEEEEEECCC
13.4711940581
627PhosphorylationKGDKQVEYLDLDLDS
CCCCCEEEEEEECCC
13.4710734310
634PhosphorylationYLDLDLDSGKSTPPR
EEEEECCCCCCCCCC
56.2523403867
637PhosphorylationLDLDSGKSTPPRKQK
EECCCCCCCCCCCCC
50.0726657352
638PhosphorylationDLDSGKSTPPRKQKS
ECCCCCCCCCCCCCC
40.5819881549
645PhosphorylationTPPRKQKSSGSGSSV
CCCCCCCCCCCCCCH
37.1229255136
646PhosphorylationPPRKQKSSGSGSSVA
CCCCCCCCCCCCCHH
43.9729255136
648PhosphorylationRKQKSSGSGSSVADE
CCCCCCCCCCCHHHH
37.1329255136
650PhosphorylationQKSSGSGSSVADERV
CCCCCCCCCHHHHCC
24.2820363803
651PhosphorylationKSSGSGSSVADERVD
CCCCCCCCHHHHCCC
25.5028152594
658PhosphorylationSVADERVDYVVVDQQ
CHHHHCCCEEEECCC
36.4117016520
659DephosphorylationVADERVDYVVVDQQK
HHHHCCCEEEECCCC
7.7110068651
659PhosphorylationVADERVDYVVVDQQK
HHHHCCCEEEECCCC
7.7110734310
673PhosphorylationKTLALKSTREAWTDG
CEEEEHHHHHHHHCC
30.8321712546
678PhosphorylationKSTREAWTDGRQSTE
HHHHHHHHCCCCCCC
35.3128857561
683PhosphorylationAWTDGRQSTESETPA
HHHCCCCCCCCCCCC
32.5525159151
684PhosphorylationWTDGRQSTESETPAK
HHCCCCCCCCCCCCC
34.8828655764

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
242YPhosphorylationKinaseINSRP06213
PSP
242YPhosphorylationKinaseSRCP12931
PSP
242YPhosphorylationKinaseINSRP06213
GPS
259YPhosphorylationKinaseSRCP12931
PSP
285YPhosphorylationKinaseINSRP06213
PSP
285YPhosphorylationKinaseMETP08581
PhosphoELM
285YPhosphorylationKinaseEGFRP00533
PSP
285YPhosphorylationKinaseEGFRP00533
GPS
285YPhosphorylationKinaseINSRP06213
GPS
307YPhosphorylationKinaseMETP08581
PhosphoELM
307YPhosphorylationKinaseEGFRP00533
PhosphoELM
312TPhosphorylationKinaseMAPK1P28482
GPS
312TPhosphorylationKinaseMAPK3P27361
GPS
317YPhosphorylationKinaseSRCP12931
PSP
373YPhosphorylationKinaseSRCP12931
PSP
373YPhosphorylationKinaseINSRP06213
GPS
373YPhosphorylationKinaseEGFRP00533
GPS
373YPhosphorylationKinaseMETP08581
PhosphoELM
373YPhosphorylationKinaseEGFRP00533
PSP
373YPhosphorylationKinaseINSRP06213
PSP
381SPhosphorylationKinaseMAPK1P28482
GPS
381SPhosphorylationKinaseMAPK3P27361
GPS
406YPhosphorylationKinaseMETP08581
PhosphoELM
406YPhosphorylationKinaseEGFRP00533
GPS
406YPhosphorylationKinaseEGFRP00533
PSP
447YPhosphorylationKinaseINSRP06213
PSP
447YPhosphorylationKinaseMETP08581
PhosphoELM
447YPhosphorylationKinaseEGFRP00533
PSP
447YPhosphorylationKinaseEGFRP00533
GPS
447YPhosphorylationKinaseINSRP06213
GPS
454SPhosphorylationKinaseMAPK3P27361
GPS
454SPhosphorylationKinaseMAPK1P28482
GPS
472YPhosphorylationKinaseMETP08581
PhosphoELM
472YPhosphorylationKinaseEGFRP00533
PSP
472YPhosphorylationKinaseINSRP06213
GPS
472YPhosphorylationKinaseEGFRP00533
GPS
472YPhosphorylationKinaseINSRP06213
PSP
476TPhosphorylationKinaseMAPK1P28482
GPS
476TPhosphorylationKinaseMAPK3P27361
GPS
582SPhosphorylationKinaseMAPK3P27361
GPS
582SPhosphorylationKinaseMAPK1P28482
GPS
589YPhosphorylationKinaseMETP08581
PhosphoELM
589YPhosphorylationKinaseEGFRP00533
PSP
589YPhosphorylationKinaseINSRP06213
PSP
597SPhosphorylationKinaseMAPK3P27361
GPS
597SPhosphorylationKinaseMAPK1P28482
GPS
619YPhosphorylationKinaseINSRP06213
GPS
619YPhosphorylationKinaseEGFRP00533
GPS
627YPhosphorylationKinaseSRCP12931
PSP
627YPhosphorylationKinaseMETP08581
PhosphoELM
627YPhosphorylationKinaseINSRP06213
PSP
627YPhosphorylationKinaseFERP16591
PSP
627YPhosphorylationKinaseEGFRP00533
PSP
657YPhosphorylationKinaseINSRP06213
GPS
657YPhosphorylationKinaseEGFRP00533
GPS
659YPhosphorylationKinaseMETP08581
PhosphoELM
659YPhosphorylationKinaseINSRP06213
PSP
659YPhosphorylationKinaseEGFRP00533
PSP
689YPhosphorylationKinaseINSRP06213
GPS
689YPhosphorylationKinaseEGFRP00533
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GAB1_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 GAB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PLCG1_HUMANPLCG1physical
11507676
C1QBP_HUMANC1QBPphysical
10747014
GRB2_HUMANGRB2physical
11314042
PTN11_HUMANPTPN11physical
11940581
GRB2_HUMANGRB2physical
8596638
PLCG1_HUMANPLCG1physical
8596638
P85A_HUMANPIK3R1physical
8596638
CRKL_HUMANCRKLphysical
10753869
PTN11_HUMANPTPN11physical
9658397
MET_HUMANMETphysical
10871282
GRAP2_HUMANGRAP2physical
12176364
SHC1_HUMANSHC1physical
9804835
GRB2_HUMANGRB2physical
9804835
P85A_HUMANPIK3R1physical
9804835
PTN11_HUMANPTPN11physical
9804835
MET_HUMANMETphysical
9242692
MARK2_HUMANMARK2physical
22883624
PARD3_HUMANPARD3physical
22883624
PTN11_HUMANPTPN11physical
14982882
SHC1_HUMANSHC1physical
14982882
RON_HUMANMST1Rphysical
14982882
TF2AY_HUMANGTF2A1Lphysical
25416956
CRKL_HUMANCRKLphysical
25241761
PTN11_HUMANPTPN11physical
14701753
FRS2_HUMANFRS2physical
25159185
GRB2_HUMANGRB2physical
9890893
SYPH_HUMANSYPphysical
9890893
PTN11_HUMANPTPN11physical
23612964
P85A_HUMANPIK3R1physical
23612964

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 GAB1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Profiling of tyrosine phosphorylation pathways in human cells usingmass spectrometry.";
Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.;
Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-259 AND SER-266, ANDMASS SPECTROMETRY.
"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-183; TYR-259; TYR-373;TYR-406 AND TYR-659, 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 TYR-659, PHOSPHORYLATION[LARGE SCALE ANALYSIS] AT SER-547 (ISOFORM 2), AND MASS SPECTROMETRY.
"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-373; TYR-406; TYR-627AND TYR-659, AND MASS SPECTROMETRY.
"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-406; TYR-627 ANDTYR-659, AND MASS SPECTROMETRY.

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