FES_HUMAN - dbPTM
FES_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FES_HUMAN
UniProt AC P07332
Protein Name Tyrosine-protein kinase Fes/Fps
Gene Name FES
Organism Homo sapiens (Human).
Sequence Length 822
Subcellular Localization Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Cell membrane
Peripheral membrane protein
Cytoplasmic side. Cytoplasmic vesicle. Golgi apparatus. Cell junction, focal adhesion. Distributed throughout the cytosol when the kinase is not activated. Assoc
Protein Description Tyrosine-protein kinase that acts downstream of cell surface receptors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, cell attachment and cell spreading. Plays a role in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Acts down-stream of the activated FCER1 receptor and the mast/stem cell growth factor receptor KIT. Plays a role in the regulation of mast cell degranulation. Plays a role in the regulation of cell differentiation and promotes neurite outgrowth in response to NGF signaling. Plays a role in cell scattering and cell migration in response to HGF-induced activation of EZR. Phosphorylates BCR and down-regulates BCR kinase activity. Phosphorylates HCLS1/HS1, PECAM1, STAT3 and TRIM28..
Protein Sequence MGFSSELCSPQGHGVLQQMQEAELRLLEGMRKWMAQRVKSDREYAGLLHHMSLQDSGGQSRAISPDSPISQSWAEITSQTEGLSRLLRQHAEDLNSGPLSKLSLLIRERQQLRKTYSEQWQQLQQELTKTHSQDIEKLKSQYRALARDSAQAKRKYQEASKDKDRDKAKDKYVRSLWKLFAHHNRYVLGVRAAQLHHQHHHQLLLPGLLRSLQDLHEEMACILKEILQEYLEISSLVQDEVVAIHREMAAAAARIQPEAEYQGFLRQYGSAPDVPPCVTFDESLLEEGEPLEPGELQLNELTVESVQHTLTSVTDELAVATEMVFRRQEMVTQLQQELRNEEENTHPRERVQLLGKRQVLQEALQGLQVALCSQAKLQAQQELLQTKLEHLGPGEPPPVLLLQDDRHSTSSSEQEREGGRTPTLEILKSHISGIFRPKFSLPPPLQLIPEVQKPLHEQLWYHGAIPRAEVAELLVHSGDFLVRESQGKQEYVLSVLWDGLPRHFIIQSLDNLYRLEGEGFPSIPLLIDHLLSTQQPLTKKSGVVLHRAVPKDKWVLNHEDLVLGEQIGRGNFGEVFSGRLRADNTLVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTFLRTEGARLRVKTLLQMVGDAAAGMEYLESKCCIHRDLAARNCLVTEKNVLKISDFGMSREEADGVYAASGGLRQVPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGASPYPNLSNQQTREFVEKGGRLPCPELCPDAVFRLMEQCWAYEPGQRPSFSTIYQELQSIRKRHR
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
64PhosphorylationGGQSRAISPDSPISQ
CCCCCCCCCCCCCCH		22.9728450419
67PhosphorylationSRAISPDSPISQSWA
CCCCCCCCCCCHHHH		27.7628450419
70PhosphorylationISPDSPISQSWAEIT
CCCCCCCCHHHHHHH		22.8828450419
72PhosphorylationPDSPISQSWAEITSQ
CCCCCCHHHHHHHHH		22.8228450419
77PhosphorylationSQSWAEITSQTEGLS
CHHHHHHHHHCHHHH		13.2928450419
100PhosphorylationDLNSGPLSKLSLLIR
HHHCCCCHHHHHHHH		34.38-
115PhosphorylationERQQLRKTYSEQWQQ
HHHHHHHHHHHHHHH		26.3319845377
116PhosphorylationRQQLRKTYSEQWQQL
HHHHHHHHHHHHHHH		17.1619845377
117PhosphorylationQQLRKTYSEQWQQLQ
HHHHHHHHHHHHHHH		28.6627251275
149PhosphorylationYRALARDSAQAKRKY
HHHHHHHHHHHHHHH		19.4127251275
156PhosphorylationSAQAKRKYQEASKDK
HHHHHHHHHHHHHCC		18.6722817900
261PhosphorylationRIQPEAEYQGFLRQY
HHCCHHHHHHHHHHH		22.4521253578
332PhosphorylationFRRQEMVTQLQQELR
HHHHHHHHHHHHHHH		23.4224043423
373PhosphorylationGLQVALCSQAKLQAQ
HHHHHHHHHHHHHHH		33.74-
408PhosphorylationLLQDDRHSTSSSEQE
EEECCCCCCCCHHHH		30.7723401153
409PhosphorylationLQDDRHSTSSSEQER
EECCCCCCCCHHHHH		26.8828450419
410PhosphorylationQDDRHSTSSSEQERE
ECCCCCCCCHHHHHC		34.5826657352
411PhosphorylationDDRHSTSSSEQEREG
CCCCCCCCHHHHHCC		37.6726657352
412PhosphorylationDRHSTSSSEQEREGG
CCCCCCCHHHHHCCC		42.9628450419
421PhosphorylationQEREGGRTPTLEILK
HHHCCCCCCHHHHHH		24.7329978859
423PhosphorylationREGGRTPTLEILKSH
HCCCCCCHHHHHHHH		36.0929978859
432PhosphorylationEILKSHISGIFRPKF
HHHHHHHCCCCCCCC		22.0324275569
440PhosphorylationGIFRPKFSLPPPLQL
CCCCCCCCCCCCCHH		46.2022210691
461PhosphorylationPLHEQLWYHGAIPRA
CHHHHHHHCCCCCHH		10.0420860994
477PhosphorylationVAELLVHSGDFLVRE
HHHHHHHCCCEEEEE		32.36-
491PhosphorylationESQGKQEYVLSVLWD
ECCCCCEEHHHHHHC		12.2824825855
513PhosphorylationIQSLDNLYRLEGEGF
ECCHHHHHHCCCCCC		21.2923532336
595PhosphorylationAVKSCRETLPPDLKA
EEECHHHHCCCCHHH		25.80-
597UbiquitinationKSCRETLPPDLKAKF
ECHHHHCCCCHHHHH		27.9821890473
597UbiquitinationKSCRETLPPDLKAKF
ECHHHHCCCCHHHHH		27.9821890473
614PhosphorylationEARILKQYSHPNIVR
HHHHHHHCCCCCHHH		13.8322817900
655UbiquitinationLRTEGARLRVKTLLQ
HCCCCHHHHHHHHHH		7.9721890473
667UbiquitinationLLQMVGDAAAGMEYL
HHHHHHHHHHHHHHH		8.0321890473
698UbiquitinationVTEKNVLKISDFGMS
ECCCCEEEHHHCCCC		35.56-
700PhosphorylationEKNVLKISDFGMSRE
CCCEEEHHHCCCCHH		25.8729978859
705PhosphorylationKISDFGMSREEADGV
EHHHCCCCHHHHCCE		36.6029978859
713PhosphorylationREEADGVYAASGGLR
HHHHCCEEECCCCCC		11.2815485904
716PhosphorylationADGVYAASGGLRQVP
HCCEEECCCCCCCCC		25.8115485904
725UbiquitinationGLRQVPVKWTAPEAL
CCCCCCEEECCCCHH		32.5321890473
734PhosphorylationTAPEALNYGRYSSES
CCCCHHHCCCCCCHH		12.1127273156
775UbiquitinationQTREFVEKGGRLPCP
HHHHHHHCCCCCCCC		62.45-
811PhosphorylationRPSFSTIYQELQSIR
CCCHHHHHHHHHHHH		8.9522817900
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
713YPhosphorylationKinaseFESP07332
PSP
811YPhosphorylationKinaseFESP07332
PSP
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:20804422
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FES_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 FES_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCR_HUMANBCRphysical
10706130
HS90A_HUMANHSP90AA1physical
9222609
HSP74_HUMANHSPA4physical
9222609
FKBP4_HUMANFKBP4physical
9222609
FKBP5_HUMANFKBP5physical
9222609
TEBP_HUMANPTGES3physical
9222609
PPID_HUMANPPIDphysical
9222609
STAT3_HUMANSTAT3physical
9714332
HSH2D_HUMANHSH2Dphysical
11700021
BCR_HUMANBCRphysical
7529874
MYOME_HUMANPDE4DIPphysical
21900206
ZN775_HUMANZNF775physical
21900206
ZN746_HUMANZNF746physical
21900206
TIF1B_HUMANTRIM28physical
16792528
MDFI_HUMANMDFIphysical
19060904
DESP_HUMANDSPphysical
25852190
BCAR1_MOUSEBcar1physical
8999909
FES_HUMANFESphysical
26702831
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 FES_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-67; TYR-261;SER-408; THR-409; SER-410; SER-411; SER-412; THR-421; THR-423;TYR-614; TYR-713 AND SER-716, AND MASS SPECTROMETRY.
"Structural coupling of SH2-kinase domains links Fes and Abl substraterecognition and kinase activation.";
Filippakopoulos P., Kofler M., Hantschel O., Gish G.D., Grebien F.,Salah E., Neudecker P., Kay L.E., Turk B.E., Superti-Furga G.,Pawson T., Knapp S.;
Cell 134:793-803(2008).
Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 448-822 OF UNPHOSPHORYLATEDAPOPROTEIN AND IN COMPLEX WITH STAUROSPORINE AND A SUBSTRATE PEPTIDE,CATALYTIC ACTIVITY, ENZYME REGULATION, PHOSPHORYLATION AT TYR-713, NMRSPECTROSCOPY, AND MUTAGENESIS OF GLY-463 AND ARG-483.
"Bimolecular fluorescence complementation demonstrates that the c-Fesprotein-tyrosine kinase forms constitutive oligomers in livingcells.";
Shaffer J.M., Hellwig S., Smithgall T.E.;
Biochemistry 48:4780-4788(2009).
Cited for: SUBUNIT, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-713,PHOSPHORYLATION BY HCK, AND DOMAIN.
"Spatial recruitment and activation of the Fes kinase by ezrinpromotes HGF-induced cell scattering.";
Naba A., Reverdy C., Louvard D., Arpin M.;
EMBO J. 27:38-50(2008).
Cited for: FUNCTION IN CYTOSKELETON REORGANIZATION, INTERACTION WITH EZR,PHOSPHORYLATION AT TYR-713, AND SUBCELLULAR LOCATION.
"The human c-Fes tyrosine kinase binds tubulin and microtubulesthrough separate domains and promotes microtubule assembly.";
Laurent C.E., Delfino F.J., Cheng H.Y., Smithgall T.E.;
Mol. Cell. Biol. 24:9351-9358(2004).
Cited for: FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH TUBULIN ANDMICROTUBULES, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-713,PHOSPHORYLATION BY HCK, AND MUTAGENESIS OF LEU-145; ARG-483 ANDLYS-590.
"Regulation of the human c-fes protein tyrosine kinase (p93c-fes) byits src homology 2 domain and major autophosphorylation site (Tyr-713).";
Hjermstad S.J., Peters K.L., Briggs S.D., Glazer R.I., Smithgall T.E.;
Oncogene 8:2283-2292(1993).
Cited for: PHOSPHORYLATION AT TYR-713, CATALYTIC ACTIVITY, AND MUTAGENESIS OFTYR-713.

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