FRS2_MOUSE - dbPTM
FRS2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FRS2_MOUSE
UniProt AC Q8C180
Protein Name Fibroblast growth factor receptor substrate 2
Gene Name Frs2
Organism Mus musculus (Mouse).
Sequence Length 508
Subcellular Localization Membrane
Lipid-anchor .
Protein Description Adapter protein that links activated FGR and NGF receptors to downstream signaling pathways. Plays an important role in the activation of MAP kinases and in the phosphorylation of PIK3R1, the regulatory subunit of phosphatidylinositol 3-kinase, in response to ligand-mediated activation of FGFR1. Modulates signaling via SHC1 by competing for a common binding site on NTRK1..
Protein Sequence MGSCCSCPDKDTVPDNHRNKFKVINVDDDGNELGSGVMELTDTELILYTRKRDSVKWHYLCLRRYGYDSNLFSFESGRRCQTGQGIFAFKCARAEELFNMLQEIMQNNSINVVEEPVVERSSHQTELEVPRTPRTPTTPGLGAQNLPNGYPRYPSFGDASSHPSSRHPSVGSARLPSVGEESTHPLLVAEEQVHTYVNTTGVQEERKNRASVHVPPEARVSNAESNTPKEEPSNPEDRDPQVLLKPEGVRFVLGPTPVQKQLMEKEKLEQLGKDPVSGSGAGNTEWDTGYDSDERRDVPPVNKLVYENINGLSIPSASGVRRGRLTSTSTSDTQNINNSAQRRPALLNYENLPSLPPVWEARKLSRDEDDNLGPKTPSLNGYHNNLDPMHNYVNTENVTVPASAHKIDYSKRRDCTPTVFNFDIRRPSLEHRQLNYIQVDLEGGSDSDNPQTPKTPTTPLPQTPTRRTELYAVIDIERTAAMSNLQKALPRDDGTSRKTRHNSTDLPM
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------MGSCCSCPD
------CCCCCCCCC		29.419182757
2N-myristoyl glycine------MGSCCSCPD
------CCCCCCCCC		29.41-
35PhosphorylationDDGNELGSGVMELTD
CCCCEECCCEEEECC		40.6225338131
121PhosphorylationEEPVVERSSHQTELE
ECCEEECCCCCCEEE		20.7529550500
122PhosphorylationEPVVERSSHQTELEV
CCEEECCCCCCEEEC		26.3229550500
125PhosphorylationVERSSHQTELEVPRT
EECCCCCCEEECCCC		36.7929550500
132PhosphorylationTELEVPRTPRTPTTP
CEEECCCCCCCCCCC		15.8528418008
135PhosphorylationEVPRTPRTPTTPGLG
ECCCCCCCCCCCCCC		26.6221659605
137PhosphorylationPRTPRTPTTPGLGAQ
CCCCCCCCCCCCCCC		45.0427087446
138PhosphorylationRTPRTPTTPGLGAQN
CCCCCCCCCCCCCCC		19.3027087446
150PhosphorylationAQNLPNGYPRYPSFG
CCCCCCCCCCCCCCC		7.38-
153PhosphorylationLPNGYPRYPSFGDAS
CCCCCCCCCCCCCCC		9.9525619855
155PhosphorylationNGYPRYPSFGDASSH
CCCCCCCCCCCCCCC		32.6925619855
160PhosphorylationYPSFGDASSHPSSRH
CCCCCCCCCCCCCCC		33.6425619855
161PhosphorylationPSFGDASSHPSSRHP
CCCCCCCCCCCCCCC		40.9325619855
164PhosphorylationGDASSHPSSRHPSVG
CCCCCCCCCCCCCCC		34.2825619855
165PhosphorylationDASSHPSSRHPSVGS
CCCCCCCCCCCCCCC		38.7725619855
169PhosphorylationHPSSRHPSVGSARLP
CCCCCCCCCCCCCCC		32.7425521595
172PhosphorylationSRHPSVGSARLPSVG
CCCCCCCCCCCCCCC		14.2025521595
177PhosphorylationVGSARLPSVGEESTH
CCCCCCCCCCCCCCC		47.5524068923
182PhosphorylationLPSVGEESTHPLLVA
CCCCCCCCCCCEEEE		27.9325293948
183PhosphorylationPSVGEESTHPLLVAE
CCCCCCCCCCEEEEE		30.6925293948
195PhosphorylationVAEEQVHTYVNTTGV
EEEEEEHHHCCCCCC		30.2424068923
196PhosphorylationAEEQVHTYVNTTGVQ
EEEEEHHHCCCCCCH		4.109632781
199PhosphorylationQVHTYVNTTGVQEER
EEHHHCCCCCCHHHH		18.1924068923
200PhosphorylationVHTYVNTTGVQEERK
EHHHCCCCCCHHHHH		30.1024068923
211PhosphorylationEERKNRASVHVPPEA
HHHHCCCCCCCCHHH		14.9826824392
221PhosphorylationVPPEARVSNAESNTP
CCHHHHCCCCCCCCC		25.4325619855
225PhosphorylationARVSNAESNTPKEEP
HHCCCCCCCCCCCCC		43.5225619855
227PhosphorylationVSNAESNTPKEEPSN
CCCCCCCCCCCCCCC		45.0425619855
233PhosphorylationNTPKEEPSNPEDRDP
CCCCCCCCCCCCCCC		69.1925619855
277PhosphorylationQLGKDPVSGSGAGNT
HHCCCCCCCCCCCCC		32.4125338131
279PhosphorylationGKDPVSGSGAGNTEW
CCCCCCCCCCCCCCC		20.2629899451
284PhosphorylationSGSGAGNTEWDTGYD
CCCCCCCCCCCCCCC		37.2228066266
288PhosphorylationAGNTEWDTGYDSDER
CCCCCCCCCCCCCCC		38.4211390647
290PhosphorylationNTEWDTGYDSDERRD
CCCCCCCCCCCCCCC		17.8629550500
292PhosphorylationEWDTGYDSDERRDVP
CCCCCCCCCCCCCCC		32.6525521595
306PhosphorylationPPVNKLVYENINGLS
CCCHHHHEECCCCCC		17.4420116462
316PhosphorylationINGLSIPSASGVRRG
CCCCCCCCCCCCCCC		33.1422499769
326PhosphorylationGVRRGRLTSTSTSDT
CCCCCCCCCCCCCCC		28.7025619855
327PhosphorylationVRRGRLTSTSTSDTQ
CCCCCCCCCCCCCCC		25.5925619855
328PhosphorylationRRGRLTSTSTSDTQN
CCCCCCCCCCCCCCC		30.6825619855
329PhosphorylationRGRLTSTSTSDTQNI
CCCCCCCCCCCCCCC		26.1925619855
330PhosphorylationGRLTSTSTSDTQNIN
CCCCCCCCCCCCCCC		30.6125619855
331PhosphorylationRLTSTSTSDTQNINN
CCCCCCCCCCCCCCC		38.1325619855
333PhosphorylationTSTSTSDTQNINNSA
CCCCCCCCCCCCCHH		24.2325619855
339PhosphorylationDTQNINNSAQRRPAL
CCCCCCCHHHHCCCH		22.6925619855
349PhosphorylationRRPALLNYENLPSLP
HCCCHHCCCCCCCCC		13.2318515860
354PhosphorylationLNYENLPSLPPVWEA
HCCCCCCCCCCHHHH		57.5922499769
365PhosphorylationVWEARKLSRDEDDNL
HHHHHHCCCCCCCCC		40.4926824392
376PhosphorylationDDNLGPKTPSLNGYH
CCCCCCCCCCCCCCC		22.6522499769
378PhosphorylationNLGPKTPSLNGYHNN
CCCCCCCCCCCCCCC		39.4322499769
382PhosphorylationKTPSLNGYHNNLDPM
CCCCCCCCCCCCCCC		10.5722499769
392PhosphorylationNLDPMHNYVNTENVT
CCCCCCCCCCCCCCE		4.7622499769
395PhosphorylationPMHNYVNTENVTVPA
CCCCCCCCCCCEEEC		20.9222499769
403PhosphorylationENVTVPASAHKIDYS
CCCEEECCCCCCCCH		25.49-
428PhosphorylationNFDIRRPSLEHRQLN
EEECCCCCCCCCCCC		44.5725521595
436PhosphorylationLEHRQLNYIQVDLEG
CCCCCCCEEEEECCC		11.009632781
445PhosphorylationQVDLEGGSDSDNPQT
EEECCCCCCCCCCCC		44.8121183079
447PhosphorylationDLEGGSDSDNPQTPK
ECCCCCCCCCCCCCC		40.7721183079
455PhosphorylationDNPQTPKTPTTPLPQ
CCCCCCCCCCCCCCC		27.3725619855
457PhosphorylationPQTPKTPTTPLPQTP
CCCCCCCCCCCCCCC		46.4025619855
458PhosphorylationQTPKTPTTPLPQTPT
CCCCCCCCCCCCCCC		24.8328066266
463PhosphorylationPTTPLPQTPTRRTEL
CCCCCCCCCCCCCEE		25.3725619855
465PhosphorylationTPLPQTPTRRTELYA
CCCCCCCCCCCEEEE		35.8525619855
471PhosphorylationPTRRTELYAVIDIER
CCCCCEEEEEEEHHH		7.819632781
499PhosphorylationDDGTSRKTRHNSTDL
CCCCCCCCCCCCCCC		35.7329472430
503PhosphorylationSRKTRHNSTDLPM--
CCCCCCCCCCCCC--		19.7126824392
504PhosphorylationRKTRHNSTDLPM---
CCCCCCCCCCCC---		47.0424068923
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
196YPhosphorylationKinaseFGFR1P16092
Uniprot
306YPhosphorylationKinaseFGFR1P16092
Uniprot
349YPhosphorylationKinaseFGFR1P16092
Uniprot
392YPhosphorylationKinaseFGFR1P16092
Uniprot
436YPhosphorylationKinaseFGFR1P16092
Uniprot
471YPhosphorylationKinaseFGFR1P16092
Uniprot
-KUbiquitinationE3 ubiquitin ligaseCblP22682
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FRS2_MOUSE !!
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 FRS2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KPCI_HUMANPRKCIphysical
10383403
PTN11_MOUSEPtpn11physical
15870281
GRB2_MOUSEGrb2physical
15870281
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FRS2_MOUSE

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"A lipid-anchored Grb2-binding protein that links FGF-receptoractivation to the Ras/MAPK signaling pathway.";
Kouhara H., Hadari Y.R., Spivak-Kroizman T., Schilling J.,Bar-Sagi D., Lax I., Schlessinger J.;
Cell 89:693-702(1997).
Cited for: PROTEIN SEQUENCE OF 251-260; 305-320; 344-361 AND 468-480, FUNCTION,INTERACTION WITH GRB2, IDENTIFICATION IN A COMPLEX WITH GRB2 AND SOS1,MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2; TYR-196; TYR-306;TYR-349 AND TYR-392, PHOSPHORYLATION AT TYROSINE RESIDUES, AND TISSUESPECIFICITY.
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169; SER-172 ANDSER-211, AND MASS SPECTROMETRY.
"Docking protein FRS2 links the protein tyrosine kinase RET and itsoncogenic forms with the mitogen-activated protein kinase signalingcascade.";
Melillo R.M., Santoro M., Ong S.-H., Billaud M., Fusco A.,Hadari Y.R., Schlessinger J., Lax I.;
Mol. Cell. Biol. 21:4177-4187(2001).
Cited for: FUNCTION, INTERACTION WITH RET, AND PHOSPHORYLATION AT TYROSINERESIDUES.
"Suc1-associated neurotrophic factor target (SNT) protein is a majorFGF-stimulated tyrosine phosphorylated 90-kDa protein which binds tothe SH2 domain of GRB2.";
Ong S.-H., Goh K.C., Lim Y.P., Low B.C., Klint P., Claesson-Welsh L.,Cao X., Tan Y.H., Guy G.R.;
Biochem. Biophys. Res. Commun. 225:1021-1026(1996).
Cited for: INTERACTION WITH SUC1 AND GRB2, PHOSPHORYLATION AT TYROSINE RESIDUES,AND SUBCELLULAR LOCATION.
"A lipid-anchored Grb2-binding protein that links FGF-receptoractivation to the Ras/MAPK signaling pathway.";
Kouhara H., Hadari Y.R., Spivak-Kroizman T., Schilling J.,Bar-Sagi D., Lax I., Schlessinger J.;
Cell 89:693-702(1997).
Cited for: PROTEIN SEQUENCE OF 251-260; 305-320; 344-361 AND 468-480, FUNCTION,INTERACTION WITH GRB2, IDENTIFICATION IN A COMPLEX WITH GRB2 AND SOS1,MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2; TYR-196; TYR-306;TYR-349 AND TYR-392, PHOSPHORYLATION AT TYROSINE RESIDUES, AND TISSUESPECIFICITY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-288, AND MASSSPECTROMETRY.
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-349, AND MASSSPECTROMETRY.
"Stimulation of phosphatidylinositol 3-kinase by fibroblast growthfactor receptors is mediated by coordinated recruitment of multipledocking proteins.";
Ong S.H., Hadari Y.R., Gotoh N., Guy G.R., Schlessinger J., Lax I.;
Proc. Natl. Acad. Sci. U.S.A. 98:6074-6079(2001).
Cited for: FUNCTION, INTERACTION WITH GRB2 AND GAB1, AND PHOSPHORYLATION ATTYR-196; TYR-306; TYR-349; TYR-392; TYR-436 AND TYR-471.
"Binding of Shp2 tyrosine phosphatase to FRS2 is essential forfibroblast growth factor-induced PC12 cell differentiation.";
Hadari Y.R., Kouhara H., Lax I., Schlessinger J.;
Mol. Cell. Biol. 18:3966-3973(1998).
Cited for: INTERACTION WITH PTPN11, FUNCTION, PHOSPHORYLATION AT TYR-196;TYR-306; TYR-349; TYR-392 AND TYR-436, AND MUTAGENESIS OF TYR-436.

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