GAB2_HUMAN - dbPTM
GAB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GAB2_HUMAN
UniProt AC Q9UQC2
Protein Name GRB2-associated-binding protein 2
Gene Name GAB2
Organism Homo sapiens (Human).
Sequence Length 676
Subcellular Localization Cytoplasm . Cell membrane .
Protein Description Adapter protein which acts downstream of several membrane receptors including cytokine, antigen, hormone, cell matrix and growth factor receptors to regulate multiple signaling pathways. Regulates osteoclast differentiation mediating the TNFRSF11A/RANK signaling. In allergic response, it plays a role in mast cells activation and degranulation through PI-3-kinase regulation. Also involved in the regulation of cell proliferation and hematopoiesis..
Protein Sequence MSGGGDVVCTGWLRKSPPEKKLRRYAWKKRWFILRSGRMSGDPDVLEYYKNDHSKKPLRIINLNFCEQVDAGLTFNKKELQDSFVFDIKTSERTFYLVAETEEDMNKWVQSICQICGFNQAEESTDSLRNVSSAGHGPRSSPAELSSSSQHLLRERKSSAPSHSSQPTLFTFEPPVSNHMQPTLSTSAPQEYLYLHQCISRRAENARSASFSQGTRASFLMRSDTAVQKLAQGNGHCVNGISGQVHGFYSLPKPSRHNTEFRDSTYDLPRSLASHGHTKGSLTGSETDNEDVYTFKTPSNTLCREFGDLLVDNMDVPATPLSAYQIPRTFTLDKNHNAMTVATPGDSAIAPPPRPPKPSQAETPRWGSPQQRPPISENSRSVAATIPRRNTLPAMDNSRLHRASSCETYEYPQRGGESAGRSAESMSDGVGSFLPGKMIVGRSDSTNSEDNYVPMNPGSSTLLAMERAGDNSQSVYIPMSPGAHHFDSLGYPSTTLPVHRGPSRGSEIQPPPVNRNLKPDRKAKPTPLDLRNNTVIDELPFKSPITKSWSRANHTFNSSSSQYCRPISTQSITSTDSGDSEENYVPMQNPVSASPVPSGTNSPAPKKSTGSVDYLALDFQPSSPSPHRKPSTSSVTSDEKVDYVQVDKEKTQALQNTMQEWTDVRQSSEPSKGAKL
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
2Phosphorylation------MSGGGDVVC
------CCCCCCEEE
46.2623186163
15UbiquitinationVCTGWLRKSPPEKKL
EECCCCCCCCCHHHH
66.2124816145
48PhosphorylationGDPDVLEYYKNDHSK
CCHHHHHHHHCCCCC
18.6423917254
49PhosphorylationDPDVLEYYKNDHSKK
CHHHHHHHHCCCCCC
8.2423917254
56AcetylationYKNDHSKKPLRIINL
HHCCCCCCCEEEEEC
52.917664735
103PhosphorylationYLVAETEEDMNKWVQ
EEEEECHHHHHHHHH
70.7232142685
124PhosphorylationGFNQAEESTDSLRNV
CCCCHHHCCHHHHCH
29.0827251275
125PhosphorylationFNQAEESTDSLRNVS
CCCHHHCCHHHHCHH
32.6527251275
127PhosphorylationQAEESTDSLRNVSSA
CHHHCCHHHHCHHHC
29.3527251275
132PhosphorylationTDSLRNVSSAGHGPR
CHHHHCHHHCCCCCC
20.3020873877
133PhosphorylationDSLRNVSSAGHGPRS
HHHHCHHHCCCCCCC
33.7128188228
140PhosphorylationSAGHGPRSSPAELSS
HCCCCCCCCHHHHCH
43.7523401153
141PhosphorylationAGHGPRSSPAELSSS
CCCCCCCCHHHHCHH
29.4325159151
146PhosphorylationRSSPAELSSSSQHLL
CCCHHHHCHHHHHHH
21.4922617229
147PhosphorylationSSPAELSSSSQHLLR
CCHHHHCHHHHHHHH
46.7828348404
148PhosphorylationSPAELSSSSQHLLRE
CHHHHCHHHHHHHHH
30.5519172738
149PhosphorylationPAELSSSSQHLLRER
HHHHCHHHHHHHHHH
24.4619172738
159PhosphorylationLLRERKSSAPSHSSQ
HHHHHHCCCCCCCCC
47.4319172738
162PhosphorylationERKSSAPSHSSQPTL
HHHCCCCCCCCCCEE
35.4028348404
164PhosphorylationKSSAPSHSSQPTLFT
HCCCCCCCCCCEEEE
34.7027251275
165PhosphorylationSSAPSHSSQPTLFTF
CCCCCCCCCCEEEEE
34.4528348404
168PhosphorylationPSHSSQPTLFTFEPP
CCCCCCCEEEEECCC
27.2028348404
171PhosphorylationSSQPTLFTFEPPVSN
CCCCEEEEECCCCCC
30.15-
177PhosphorylationFTFEPPVSNHMQPTL
EEECCCCCCCCCCCC
27.1328348404
185PhosphorylationNHMQPTLSTSAPQEY
CCCCCCCCCCCCHHH
23.8532142685
194PhosphorylationSAPQEYLYLHQCISR
CCCHHHHHHHHHHHH
10.96-
204PhosphorylationQCISRRAENARSASF
HHHHHHHHHHHHCCC
50.0032142685
208PhosphorylationRRAENARSASFSQGT
HHHHHHHHCCCCCCC
26.3423403867
210PhosphorylationAENARSASFSQGTRA
HHHHHHCCCCCCCHH
27.0330278072
212PhosphorylationNARSASFSQGTRASF
HHHHCCCCCCCHHHH
25.7923403867
215PhosphorylationSASFSQGTRASFLMR
HCCCCCCCHHHHHHC
18.5423403867
218PhosphorylationFSQGTRASFLMRSDT
CCCCCHHHHHHCCHH
18.6723403867
223PhosphorylationRASFLMRSDTAVQKL
HHHHHHCCHHHHHHH
25.9123401153
225PhosphorylationSFLMRSDTAVQKLAQ
HHHHCCHHHHHHHHC
29.9423403867
242PhosphorylationGHCVNGISGQVHGFY
CCCCCCCCCCEEEEE
25.2728450419
249PhosphorylationSGQVHGFYSLPKPSR
CCCEEEEECCCCCCC
17.5628450419
250PhosphorylationGQVHGFYSLPKPSRH
CCEEEEECCCCCCCC
35.6125884760
255PhosphorylationFYSLPKPSRHNTEFR
EECCCCCCCCCCCCC
52.9128450419
259PhosphorylationPKPSRHNTEFRDSTY
CCCCCCCCCCCCCCC
30.3129255136
264PhosphorylationHNTEFRDSTYDLPRS
CCCCCCCCCCCCCHH
25.3023401153
265PhosphorylationNTEFRDSTYDLPRSL
CCCCCCCCCCCCHHH
25.9129255136
266PhosphorylationTEFRDSTYDLPRSLA
CCCCCCCCCCCHHHH
21.3111334882
271PhosphorylationSTYDLPRSLASHGHT
CCCCCCHHHHHCCCC
26.7530177828
274PhosphorylationDLPRSLASHGHTKGS
CCCHHHHHCCCCCCC
34.9824719451
278PhosphorylationSLASHGHTKGSLTGS
HHHHCCCCCCCCCCC
41.5127251275
281PhosphorylationSHGHTKGSLTGSETD
HCCCCCCCCCCCCCC
25.0621082442
283PhosphorylationGHTKGSLTGSETDNE
CCCCCCCCCCCCCCC
40.1229507054
285PhosphorylationTKGSLTGSETDNEDV
CCCCCCCCCCCCCCC
31.8928355574
287PhosphorylationGSLTGSETDNEDVYT
CCCCCCCCCCCCCEE
45.9125159151
293PhosphorylationETDNEDVYTFKTPSN
CCCCCCCEEEECCCC
20.8411334882
294PhosphorylationTDNEDVYTFKTPSNT
CCCCCCEEEECCCCH
20.6421722762
319PhosphorylationDNMDVPATPLSAYQI
CCCCCCCCCCCCCCC
20.7726356563
322PhosphorylationDVPATPLSAYQIPRT
CCCCCCCCCCCCCCE
26.5725884760
324PhosphorylationPATPLSAYQIPRTFT
CCCCCCCCCCCCEEE
12.0021082442
330PhosphorylationAYQIPRTFTLDKNHN
CCCCCCEEEECCCCC
7.2432142685
331PhosphorylationYQIPRTFTLDKNHNA
CCCCCEEEECCCCCE
33.1719172738
367PhosphorylationQAETPRWGSPQQRPP
CCCCCCCCCCCCCCC
30.6333259812
368PhosphorylationAETPRWGSPQQRPPI
CCCCCCCCCCCCCCC
16.7528102081
376PhosphorylationPQQRPPISENSRSVA
CCCCCCCCCCCCCCH
36.1823403867
379PhosphorylationRPPISENSRSVAATI
CCCCCCCCCCCHHCC
23.1423403867
381PhosphorylationPISENSRSVAATIPR
CCCCCCCCCHHCCCC
18.8722985185
385PhosphorylationNSRSVAATIPRRNTL
CCCCCHHCCCCCCCC
23.0623403867
391PhosphorylationATIPRRNTLPAMDNS
HCCCCCCCCCCCCCC
32.1023401153
404PhosphorylationNSRLHRASSCETYEY
CCCCCCCCCCEEECC
35.1623401153
405PhosphorylationSRLHRASSCETYEYP
CCCCCCCCCEEECCC
18.2630278072
408PhosphorylationHRASSCETYEYPQRG
CCCCCCEEECCCCCC
26.4423898821
409PhosphorylationRASSCETYEYPQRGG
CCCCCEEECCCCCCC
7.3821082442
411PhosphorylationSSCETYEYPQRGGES
CCCEEECCCCCCCCC
8.3428796482
418PhosphorylationYPQRGGESAGRSAES
CCCCCCCCCCCCCCH
39.0223312004
422PhosphorylationGGESAGRSAESMSDG
CCCCCCCCCCHHCCC
35.1629255136
425PhosphorylationSAGRSAESMSDGVGS
CCCCCCCHHCCCCCC
24.2529255136
427PhosphorylationGRSAESMSDGVGSFL
CCCCCHHCCCCCCCC
40.2628450419
432PhosphorylationSMSDGVGSFLPGKMI
HHCCCCCCCCCCCEE
22.6227732954
442PhosphorylationPGKMIVGRSDSTNSE
CCCEEECCCCCCCCC
26.7932142685
443PhosphorylationGKMIVGRSDSTNSED
CCEEECCCCCCCCCC
29.9528450419
445PhosphorylationMIVGRSDSTNSEDNY
EEECCCCCCCCCCCC
30.6328450419
446PhosphorylationIVGRSDSTNSEDNYV
EECCCCCCCCCCCCE
47.9928450419
448PhosphorylationGRSDSTNSEDNYVPM
CCCCCCCCCCCCEEC
46.5528450419
452PhosphorylationSTNSEDNYVPMNPGS
CCCCCCCCEECCCCC
20.4611334882
455UbiquitinationSEDNYVPMNPGSSTL
CCCCCEECCCCCCCE
7.2524816145
459PhosphorylationYVPMNPGSSTLLAME
CEECCCCCCCEEEEE
22.7727732954
460PhosphorylationVPMNPGSSTLLAMER
EECCCCCCCEEEEEE
29.0522210691
461PhosphorylationPMNPGSSTLLAMERA
ECCCCCCCEEEEEEC
27.7327080861
472PhosphorylationMERAGDNSQSVYIPM
EEECCCCCCCEEEEC
28.6828796482
474PhosphorylationRAGDNSQSVYIPMSP
ECCCCCCCEEEECCC
19.4028796482
476PhosphorylationGDNSQSVYIPMSPGA
CCCCCCEEEECCCCC
12.4511334882
480PhosphorylationQSVYIPMSPGAHHFD
CCEEEECCCCCCCCC
18.1523401153
488PhosphorylationPGAHHFDSLGYPSTT
CCCCCCCCCCCCCCC
23.8128796482
491PhosphorylationHHFDSLGYPSTTLPV
CCCCCCCCCCCCCCC
10.1728796482
493PhosphorylationFDSLGYPSTTLPVHR
CCCCCCCCCCCCCCC
26.0728796482
494PhosphorylationDSLGYPSTTLPVHRG
CCCCCCCCCCCCCCC
28.0428796482
495PhosphorylationSLGYPSTTLPVHRGP
CCCCCCCCCCCCCCC
33.1428796482
503PhosphorylationLPVHRGPSRGSEIQP
CCCCCCCCCCCCCCC
52.6929978859
506PhosphorylationHRGPSRGSEIQPPPV
CCCCCCCCCCCCCCC
30.3429978859
534PhosphorylationPLDLRNNTVIDELPF
CCCCCCCCEECCCCC
23.5323403867
542MethylationVIDELPFKSPITKSW
EECCCCCCCCCCCCH
54.07-
543PhosphorylationIDELPFKSPITKSWS
ECCCCCCCCCCCCHH
23.1623401153
546PhosphorylationLPFKSPITKSWSRAN
CCCCCCCCCCHHHCC
23.5529255136
550PhosphorylationSPITKSWSRANHTFN
CCCCCCHHHCCCCCC
28.7116674116
563PhosphorylationFNSSSSQYCRPISTQ
CCCCCCCCEEECCCC
7.7423917254
584PhosphorylationSGDSEENYVPMQNPV
CCCCCCCEECCCCCC
14.8111334882
608PhosphorylationNSPAPKKSTGSVDYL
CCCCCCCCCCCCCEE
44.0928857561
609PhosphorylationSPAPKKSTGSVDYLA
CCCCCCCCCCCCEEE
42.2128857561
611PhosphorylationAPKKSTGSVDYLALD
CCCCCCCCCCEEEEE
16.3528796482
614PhosphorylationKSTGSVDYLALDFQP
CCCCCCCEEEEECCC
7.5411334882
622PhosphorylationLALDFQPSSPSPHRK
EEEECCCCCCCCCCC
44.0625159151
623PhosphorylationALDFQPSSPSPHRKP
EEECCCCCCCCCCCC
35.7625159151
625PhosphorylationDFQPSSPSPHRKPST
ECCCCCCCCCCCCCC
34.9723663014
631PhosphorylationPSPHRKPSTSSVTSD
CCCCCCCCCCCCCCC
43.9123663014
632PhosphorylationSPHRKPSTSSVTSDE
CCCCCCCCCCCCCCC
33.2823663014
633PhosphorylationPHRKPSTSSVTSDEK
CCCCCCCCCCCCCCC
27.4423663014
634PhosphorylationHRKPSTSSVTSDEKV
CCCCCCCCCCCCCCC
29.5123663014
636PhosphorylationKPSTSSVTSDEKVDY
CCCCCCCCCCCCCCE
32.2023663014
637PhosphorylationPSTSSVTSDEKVDYV
CCCCCCCCCCCCCEE
41.4323663014
637UbiquitinationPSTSSVTSDEKVDYV
CCCCCCCCCCCCCEE
41.4324816145
643DephosphorylationTSDEKVDYVQVDKEK
CCCCCCCEEEECHHH
8.8611812650
643PhosphorylationTSDEKVDYVQVDKEK
CCCCCCCEEEECHHH
8.8625159151
651PhosphorylationVQVDKEKTQALQNTM
EEECHHHHHHHHHHH
21.84-
657PhosphorylationKTQALQNTMQEWTDV
HHHHHHHHHHHHHHH
13.79-
675UbiquitinationSEPSKGAKL------
CCCCCCCCC------
64.5024816145

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
159SPhosphorylationKinaseAKT1P31749
PSP
159SPhosphorylationKinaseAKT-FAMILY-GPS
159SPhosphorylationKinasePKB_GROUP-PhosphoELM
614YPhosphorylationKinaseZAP70P43403
PSP
623SPhosphorylationKinaseMAPK1P28482
GPS
623SPhosphorylationKinaseMAPK3P27361
GPS
623SPhosphorylationKinaseERK-SUBFAMILY-GPS
643YPhosphorylationKinaseJAK2O60674
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GAB2_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 GAB2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHG32_HUMANARHGAP32physical
12819203
PLCG2_HUMANPLCG2physical
12135708
PTN11_HUMANPTPN11physical
12135708
ZAP70_HUMANZAP70physical
11572860
CD3Z_HUMANCD247physical
11572860
LAT_HUMANLATphysical
11572860
PTN6_HUMANPTPN6physical
11895767
SHC1_HUMANSHC1physical
11782427
PTN11_HUMANPTPN11physical
11782427
GRB2_HUMANGRB2physical
11782427
P85A_HUMANPIK3R1physical
11782427
AKT1_HUMANAKT1physical
11782427
PTN11_HUMANPTPN11physical
10391903
P85A_HUMANPIK3R1physical
11334882
PTN11_HUMANPTPN11physical
11334882
CRKL_HUMANCRKLphysical
11334882
MET_HUMANMETphysical
10871282
CRKL_HUMANCRKLphysical
10871282
PTN11_HUMANPTPN11physical
10871282
P85A_HUMANPIK3R1physical
10871282
PTN11_HUMANPTPN11physical
19909739
MARK2_HUMANMARK2physical
22883624
PTN11_HUMANPTPN11physical
14982882
SHC1_HUMANSHC1physical
14982882
GAB1_HUMANGAB1physical
14982882
GAB2_HUMANGAB2physical
14982882
PTN11_HUMANPTPN11physical
15356145
FRS2_HUMANFRS2physical
25159185
KCTD3_HUMANKCTD3physical
27173435
KI13B_HUMANKIF13Bphysical
27173435
ZBT21_HUMANZBTB21physical
27173435
GGYF1_HUMANGIGYF1physical
27173435
LRFN1_HUMANLRFN1physical
27173435
DEN1A_HUMANDENND1Aphysical
27173435
SRGP2_HUMANSRGAP2physical
27173435
SI1L1_HUMANSIPA1L1physical
27173435
LIMA1_HUMANLIMA1physical
27173435
MAGI1_HUMANMAGI1physical
27173435
TESK2_HUMANTESK2physical
27173435
DCLK1_HUMANDCLK1physical
27173435
ZN638_HUMANZNF638physical
27173435
SRS12_HUMANSRSF12physical
27173435
RTKN_HUMANRTKNphysical
27173435
MAST3_HUMANMAST3physical
27173435
SYDE1_HUMANSYDE1physical
27173435
PPM1H_HUMANPPM1Hphysical
27173435
AGAP1_HUMANAGAP1physical
27173435
MPIP2_HUMANCDC25Bphysical
27173435
CDK16_HUMANCDK16physical
27173435
F110B_HUMANFAM110Bphysical
27173435
UBP21_HUMANUSP21physical
27173435
AN34A_HUMANANKRD34Aphysical
27173435
FA53C_HUMANFAM53Cphysical
27173435
CING_HUMANCGNphysical
27173435
F110A_HUMANFAM110Aphysical
27173435
HDAC4_HUMANHDAC4physical
27173435
SIN1_HUMANMAPKAP1physical
27173435
TBC25_HUMANTBC1D25physical
27173435
NF1_HUMANNF1physical
27173435
NADK_HUMANNADKphysical
27173435
CBY1_HUMANCBY1physical
27173435
RAB3I_HUMANRAB3IPphysical
27173435
PTN11_HUMANPTPN11physical
16371368
GRB2_HUMANGRB2physical
16371368

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 GAB2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-404, AND MASSSPECTROMETRY.
"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-543, AND MASSSPECTROMETRY.
"Phosphorylation-dependent binding of 14-3-3 terminates signalling bythe Gab2 docking protein.";
Brummer T., Larance M., Herrera Abreu M.T., Lyons R.J., Timpson P.,Emmerich C.H., Fleuren E.D.G., Lehrbach G.M., Schramek D.,Guilhaus M., James D.E., Daly R.J.;
EMBO J. 27:2305-2316(2008).
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EGFR; GRB2; PTPN11;PI-3 KINASE; SFN; SHC1; YWHAB; YWHAE; YWHAG; YWHAH; YWHAQ AND YWHAZ,MUTAGENESIS OF SER-210 AND THR-391, AND PHOSPHORYLATION AT SER-133;SER-140; SER-141; SER-148; SER-149; SER-159; SER-164; SER-210;SER-218; SER-223; SER-264; THR-278; SER-281; THR-287; TYR-293;THR-331; THR-385; THR-391; SER-405; SER-480; SER-543; SER-622 ANDSER-623.
"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 THR-385, 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-266, AND MASSSPECTROMETRY.
"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-266, AND MASSSPECTROMETRY.

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