G3BP2_HUMAN - dbPTM
G3BP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID G3BP2_HUMAN
UniProt AC Q9UN86
Protein Name Ras GTPase-activating protein-binding protein 2
Gene Name G3BP2
Organism Homo sapiens (Human).
Sequence Length 482
Subcellular Localization Cytoplasm.
Protein Description Probable scaffold protein that may be involved in mRNA transport..
Protein Sequence MVMEKPSPLLVGREFVRQYYTLLNKAPEYLHRFYGRNSSYVHGGVDASGKPQEAVYGQNDIHHKVLSLNFSECHTKIRHVDAHATLSDGVVVQVMGLLSNSGQPERKFMQTFVLAPEGSVPNKFYVHNDMFRYEDEVFGDSEPELDEESEDEVEEEQEERQPSPEPVQENANSGYYEAHPVTNGIEEPLEESSHEPEPEPESETKTEELKPQVEEKNLEELEEKSTTPPPAEPVSLPQEPPKAFSWASVTSKNLPPSGTVSSSGIPPHVKAPVSQPRVEAKPEVQSQPPRVREQRPRERPGFPPRGPRPGRGDMEQNDSDNRRIIRYPDSHQLFVGNLPHDIDENELKEFFMSFGNVVELRINTKGVGGKLPNFGFVVFDDSEPVQRILIAKPIMFRGEVRLNVEEKKTRAARERETRGGGDDRRDIRRNDRGPGGPRGIVGGGMMRDRDGRGPPPRGGMAQKLGSGRGTGQMEGRFTGQRR
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
3Sulfoxidation-----MVMEKPSPLL
-----CCCCCCCCCE		5.4528183972
5Ubiquitination---MVMEKPSPLLVG
---CCCCCCCCCEEC		32.4721890473
7Phosphorylation-MVMEKPSPLLVGRE
-CCCCCCCCCEECHH		38.9729255136
21PhosphorylationEFVRQYYTLLNKAPE
HHHHHHHHHHHHCHH		21.6028857561
25 (in isoform 2)Ubiquitination-66.3521890473
25UbiquitinationQYYTLLNKAPEYLHR
HHHHHHHHCHHHHHH		66.3521890473
25AcetylationQYYTLLNKAPEYLHR
HHHHHHHHCHHHHHH		66.3525953088
25 (in isoform 1)Ubiquitination-66.3521890473
29NitrationLLNKAPEYLHRFYGR
HHHHCHHHHHHHHCC		13.52-
29PhosphorylationLLNKAPEYLHRFYGR
HHHHCHHHHHHHHCC		13.5228102081
32MethylationKAPEYLHRFYGRNSS
HCHHHHHHHHCCCCC		24.72-
39PhosphorylationRFYGRNSSYVHGGVD
HHHCCCCCCCCCCCC		34.4228555341
48PhosphorylationVHGGVDASGKPQEAV
CCCCCCCCCCCCCCC		42.7728442448
50AcetylationGGVDASGKPQEAVYG
CCCCCCCCCCCCCCC		40.8226051181
50UbiquitinationGGVDASGKPQEAVYG
CCCCCCCCCCCCCCC		40.82-
56PhosphorylationGKPQEAVYGQNDIHH
CCCCCCCCCCCCHHH		21.7528152594
64UbiquitinationGQNDIHHKVLSLNFS
CCCCHHHHEEEECHH		30.61-
64AcetylationGQNDIHHKVLSLNFS
CCCCHHHHEEEECHH		30.6126051181
67PhosphorylationDIHHKVLSLNFSECH
CHHHHEEEECHHHHC		25.0128857561
71PhosphorylationKVLSLNFSECHTKIR
HEEEECHHHHCCEEE		37.9428857561
75PhosphorylationLNFSECHTKIRHVDA
ECHHHHCCEEEEEEC		39.5628857561
76UbiquitinationNFSECHTKIRHVDAH
CHHHHCCEEEEEECC		17.68-
76AcetylationNFSECHTKIRHVDAH
CHHHHCCEEEEEECC		17.6823749302
107 (in isoform 2)Ubiquitination-43.4521890473
107UbiquitinationNSGQPERKFMQTFVL
CCCCCCHHEEEEEEE		43.4521890473
107 (in isoform 1)Ubiquitination-43.4521890473
111PhosphorylationPERKFMQTFVLAPEG
CCHHEEEEEEECCCC		12.1520068231
119PhosphorylationFVLAPEGSVPNKFYV
EEECCCCCCCCEEEE		32.5121406692
123UbiquitinationPEGSVPNKFYVHNDM
CCCCCCCEEEEECCC		31.81-
133PhosphorylationVHNDMFRYEDEVFGD
EECCCEECCCCCCCC		19.2323663014
141PhosphorylationEDEVFGDSEPELDEE
CCCCCCCCCCCCCCC		56.2723927012
141 (in isoform 2)Phosphorylation-56.2718669648
149 (in isoform 2)Phosphorylation-48.5818669648
149PhosphorylationEPELDEESEDEVEEE
CCCCCCCCHHHHHHH		48.5823927012
163PhosphorylationEQEERQPSPEPVQEN
HHHHHCCCCCCCHHH		33.2928674151
173PhosphorylationPVQENANSGYYEAHP
CCHHHCCCCCCEECC		26.2625137130
175PhosphorylationQENANSGYYEAHPVT
HHHCCCCCCEECCCC		9.6526091039
176PhosphorylationENANSGYYEAHPVTN
HHCCCCCCEECCCCC		15.3426091039
182PhosphorylationYYEAHPVTNGIEEPL
CCEECCCCCCCCCCC		31.9826074081
192PhosphorylationIEEPLEESSHEPEPE
CCCCCCCCCCCCCCC		27.8526074081
193PhosphorylationEEPLEESSHEPEPEP
CCCCCCCCCCCCCCC		34.8426074081
202PhosphorylationEPEPEPESETKTEEL
CCCCCCCCCCCHHHC		62.3726074081
206PhosphorylationEPESETKTEELKPQV
CCCCCCCHHHCHHHH		41.9525159151
210AcetylationETKTEELKPQVEEKN
CCCHHHCHHHHHHHC		36.3626051181
216AcetylationLKPQVEEKNLEELEE
CHHHHHHHCHHHHHH		54.0126051181
225 (in isoform 2)Phosphorylation-40.5722167270
225PhosphorylationLEELEEKSTTPPPAE
HHHHHHHCCCCCCCC		40.5729255136
226PhosphorylationEELEEKSTTPPPAEP
HHHHHHCCCCCCCCC		55.1529255136
226 (in isoform 2)Phosphorylation-55.1522167270
227 (in isoform 2)Phosphorylation-40.6722167270
227PhosphorylationELEEKSTTPPPAEPV
HHHHHCCCCCCCCCC		40.6729255136
235PhosphorylationPPPAEPVSLPQEPPK
CCCCCCCCCCCCCCC		45.0817287340
235O-linked_GlycosylationPPPAEPVSLPQEPPK
CCCCCCCCCCCCCCC		45.0828657654
235 (in isoform 2)Phosphorylation-45.0823927012
245PhosphorylationQEPPKAFSWASVTSK
CCCCCCCCCEECCCC		26.9628857561
245O-linked_GlycosylationQEPPKAFSWASVTSK
CCCCCCCCCEECCCC		26.9628657654
248PhosphorylationPKAFSWASVTSKNLP
CCCCCCEECCCCCCC		21.4828857561
250PhosphorylationAFSWASVTSKNLPPS
CCCCEECCCCCCCCC		31.3328857561
251PhosphorylationFSWASVTSKNLPPSG
CCCEECCCCCCCCCC		19.8628857561
274PhosphorylationPHVKAPVSQPRVEAK
CCCCCCCCCCCCCCC		33.1528555341
281AcetylationSQPRVEAKPEVQSQP
CCCCCCCCCCHHCCC		28.3626051181
281SumoylationSQPRVEAKPEVQSQP
CCCCCCCCCCHHCCC		28.3628112733
281SumoylationSQPRVEAKPEVQSQP
CCCCCCCCCCHHCCC		28.36-
286PhosphorylationEAKPEVQSQPPRVRE
CCCCCHHCCCCCHHH		50.2428555341
337 (in isoform 2)Ubiquitination-45.1321890473
353PhosphorylationELKEFFMSFGNVVEL
HHHHHHHHCCCEEEE		25.50-
364PhosphorylationVVELRINTKGVGGKL
EEEEEEECCCCCCCC		27.14-
370AcetylationNTKGVGGKLPNFGFV
ECCCCCCCCCCCEEE		55.6426051181
370UbiquitinationNTKGVGGKLPNFGFV
ECCCCCCCCCCCEEE		55.642190698
370 (in isoform 1)Ubiquitination-55.6421890473
392SuccinylationVQRILIAKPIMFRGE
HHEEEEEECEEECCE		28.25-
392SuccinylationVQRILIAKPIMFRGE
HHEEEEEECEEECCE		28.25-
3922-HydroxyisobutyrylationVQRILIAKPIMFRGE
HHEEEEEECEEECCE		28.25-
392AcetylationVQRILIAKPIMFRGE
HHEEEEEECEEECCE		28.2525953088
392UbiquitinationVQRILIAKPIMFRGE
HHEEEEEECEEECCE		28.25-
424MethylationTRGGGDDRRDIRRND
HCCCCCCHHHHCCCC		42.80-
432MethylationRDIRRNDRGPGGPRG
HHHCCCCCCCCCCCC		57.67-
438MethylationDRGPGGPRGIVGGGM
CCCCCCCCCCCCCCC		51.23-
447MethylationIVGGGMMRDRDGRGP
CCCCCCCCCCCCCCC		27.24-
452MethylationMMRDRDGRGPPPRGG
CCCCCCCCCCCCCCC		59.75-
457DimethylationDGRGPPPRGGMAQKL
CCCCCCCCCCHHHCC		61.13-
457MethylationDGRGPPPRGGMAQKL
CCCCCCCCCCHHHCC		61.1324129315
466PhosphorylationGMAQKLGSGRGTGQM
CHHHCCCCCCCCCCC		35.4426434776
468MethylationAQKLGSGRGTGQMEG
HHCCCCCCCCCCCCC		40.9924129315
468DimethylationAQKLGSGRGTGQMEG
HHCCCCCCCCCCCCC		40.99-
470PhosphorylationKLGSGRGTGQMEGRF
CCCCCCCCCCCCCCC		23.9122210691
476MethylationGTGQMEGRFTGQRR-
CCCCCCCCCCCCCC-		16.79-
478PhosphorylationGQMEGRFTGQRR---
CCCCCCCCCCCC---		30.9222210691
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

Oops, there are no upstream regulatory protein records of G3BP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
457RMethylation

24129315
468RMethylation

24129315
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 G3BP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IKBA_HUMANNFKBIAphysical
10969074
DDX10_HUMANDDX10physical
19615732
RINI_HUMANRNH1physical
19615732
RL3L_HUMANRPL3Lphysical
19615732
NU214_HUMANNUP214physical
19615732
UBP10_HUMANUSP10physical
19615732
SYFM_HUMANFARS2physical
19615732
ASCC3_HUMANASCC3physical
19615732
ATX2L_HUMANATXN2Lphysical
19615732
NUP62_HUMANNUP62physical
19615732
NEPRO_HUMANC3orf17physical
19615732
NOG2_HUMANGNL2physical
19615732
UIMC1_HUMANUIMC1physical
19615732
UBAP2_HUMANUBAP2physical
19615732
DDX24_HUMANDDX24physical
19615732
NUFP2_HUMANNUFIP2physical
19615732
RPF2_HUMANRPF2physical
19615732
WDR36_HUMANWDR36physical
19615732
RL22L_HUMANRPL22L1physical
19615732
P53_HUMANTP53physical
17297477
G3BP1_HUMANG3BP1physical
26186194
NU214_HUMANNUP214physical
26186194
NUFP2_HUMANNUFIP2physical
26186194
P121A_HUMANPOM121physical
26186194
UBP10_HUMANUSP10physical
26186194
ATX2L_HUMANATXN2Lphysical
26186194
NU153_HUMANNUP153physical
26186194
NUP88_HUMANNUP88physical
26186194
NUP62_HUMANNUP62physical
26186194
PUR8_HUMANADSLphysical
26344197
NUFP2_HUMANNUFIP2physical
28514442
NU214_HUMANNUP214physical
28514442
ATX2L_HUMANATXN2Lphysical
28514442
TRI25_HUMANTRIM25physical
28514442
KLDC3_HUMANKLHDC3physical
28514442
G3BP1_HUMANG3BP1physical
28514442
P121A_HUMANPOM121physical
28514442
NU153_HUMANNUP153physical
28514442
NUP88_HUMANNUP88physical
28514442
UBP10_HUMANUSP10physical
27022092
CAPR1_HUMANCAPRIN1physical
27022092
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 G3BP2_HUMAN

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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC.";
Ong S.E., Mittler G., Mann M.;
Nat. Methods 1:119-126(2004).
Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-457 AND ARG-468, AND MASSSPECTROMETRY.
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-141; SER-149 ANDTHR-227, 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-225; THR-226 ANDTHR-227, 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-141; SER-149; SER-235AND THR-227, 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-141 AND SER-149, ANDMASS SPECTROMETRY.
"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-141; SER-149 ANDTHR-227, AND MASS SPECTROMETRY.

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