FRK_HUMAN - dbPTM
FRK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FRK_HUMAN
UniProt AC P42685
Protein Name Tyrosine-protein kinase FRK
Gene Name FRK
Organism Homo sapiens (Human).
Sequence Length 505
Subcellular Localization Cytoplasm . Nucleus . Predominantly found in the nucleus, with a small fraction found in the cell periphery.
Protein Description Non-receptor tyrosine-protein kinase that negatively regulates cell proliferation. Positively regulates PTEN protein stability through phosphorylation of PTEN on 'Tyr-336', which in turn prevents its ubiquitination and degradation, possibly by reducing its binding to NEDD4. May function as a tumor suppressor..
Protein Sequence MSNICQRLWEYLEPYLPCLSTEADKSTVIENPGALCSPQSQRHGHYFVALFDYQARTAEDLSFRAGDKLQVLDTLHEGWWFARHLEKRRDGSSQQLQGYIPSNYVAEDRSLQAEPWFFGAIGRSDAEKQLLYSENKTGSFLIRESESQKGEFSLSVLDGAVVKHYRIKRLDEGGFFLTRRRIFSTLNEFVSHYTKTSDGLCVKLGKPCLKIQVPAPFDLSYKTVDQWEIDRNSIQLLKRLGSGQFGEVWEGLWNNTTPVAVKTLKPGSMDPNDFLREAQIMKNLRHPKLIQLYAVCTLEDPIYIITELMRHGSLQEYLQNDTGSKIHLTQQVDMAAQVASGMAYLESRNYIHRDLAARNVLVGEHNIYKVADFGLARVFKVDNEDIYESRHEIKLPVKWTAPEAIRSNKFSIKSDVWSFGILLYEIITYGKMPYSGMTGAQVIQMLAQNYRLPQPSNCPQQFYNIMLECWNAEPKERPTFETLRWKLEDYFETDSSYSDANNFIR
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
3 (in isoform 2)Phosphorylation-37.4426270265
4 (in isoform 2)Phosphorylation-1.3326270265
5 (in isoform 2)Phosphorylation-1.9426270265
26PhosphorylationLSTEADKSTVIENPG
CCCCCCCCCCCCCCC		28.5828102081
27PhosphorylationSTEADKSTVIENPGA
CCCCCCCCCCCCCCC		31.1025159151
37PhosphorylationENPGALCSPQSQRHG
CCCCCCCCCCHHHCC		27.1625159151
40PhosphorylationGALCSPQSQRHGHYF
CCCCCCCHHHCCEEE		32.3426657352
46PhosphorylationQSQRHGHYFVALFDY
CHHHCCEEEEEEEEC		12.3522322096
53PhosphorylationYFVALFDYQARTAED
EEEEEEECCCCCHHH		9.2022322096
57PhosphorylationLFDYQARTAEDLSFR
EEECCCCCHHHHCCC		37.1020071362
62PhosphorylationARTAEDLSFRAGDKL
CCCHHHHCCCCCCEE		25.6328348404
92PhosphorylationLEKRRDGSSQQLQGY
HHHHCCCCCHHHEEC		29.3028857561
93PhosphorylationEKRRDGSSQQLQGYI
HHHCCCCCHHHEECC		27.7228857561
99PhosphorylationSSQQLQGYIPSNYVA
CCHHHEECCCCCCEE		9.1928152594
102PhosphorylationQLQGYIPSNYVAEDR
HHEECCCCCCEECCC		31.1027642862
104PhosphorylationQGYIPSNYVAEDRSL
EECCCCCCEECCCCC		12.8429759185
132PhosphorylationDAEKQLLYSENKTGS
HHHHHHHHEECCCCC		23.6428152594
133PhosphorylationAEKQLLYSENKTGSF
HHHHHHHEECCCCCE		34.3628152594
137PhosphorylationLLYSENKTGSFLIRE
HHHEECCCCCEEEEC		50.0328152594
139PhosphorylationYSENKTGSFLIRESE
HEECCCCCEEEECCC		23.3126356563
145PhosphorylationGSFLIRESESQKGEF
CCEEEECCCCCCCEE		32.4729083192
147PhosphorylationFLIRESESQKGEFSL
EEEECCCCCCCEEEE		46.6129083192
178PhosphorylationDEGGFFLTRRRIFST
CCCCCEEHHHHHHHH		19.5729759185
184PhosphorylationLTRRRIFSTLNEFVS
EHHHHHHHHHHHHHH		29.61-
193PhosphorylationLNEFVSHYTKTSDGL
HHHHHHHHCCCCCCE		11.4826356563
194PhosphorylationNEFVSHYTKTSDGLC
HHHHHHHCCCCCCEE		23.5626356563
221PhosphorylationPAPFDLSYKTVDQWE
CCCCCCCCCCCCCCE		20.2719060867
233PhosphorylationQWEIDRNSIQLLKRL
CCEECHHHHHHHHHH		16.7724719451
242PhosphorylationQLLKRLGSGQFGEVW
HHHHHHCCCCCHHHH		33.7323898821
303PhosphorylationCTLEDPIYIITELMR
EECCCHHHHHHHHHH		7.52-
317PhosphorylationRHGSLQEYLQNDTGS
HCCCHHHHHHCCCCC		10.7119060867
322PhosphorylationQEYLQNDTGSKIHLT
HHHHHCCCCCCEEEH		51.4025332170
368PhosphorylationLVGEHNIYKVADFGL
EECCCCHHHECCCCE		12.5321253578
387PhosphorylationKVDNEDIYESRHEIK
EECCHHHHHCCCEEE		21.8525159151
389PhosphorylationDNEDIYESRHEIKLP
CCHHHHHCCCEEECC		23.2026356563
407PhosphorylationTAPEAIRSNKFSIKS
CCCHHHHCCCCCCCC		37.9520071362
409AcetylationPEAIRSNKFSIKSDV
CHHHHCCCCCCCCHH		41.5619811639
493PhosphorylationKLEDYFETDSSYSDA
HHHHHHCCCCCCHHC		31.1426356563
495PhosphorylationEDYFETDSSYSDANN
HHHHCCCCCCHHCCC		38.3026356563
496PhosphorylationDYFETDSSYSDANNF
HHHCCCCCCHHCCCC		31.3127273156
497PhosphorylationYFETDSSYSDANNFI
HHCCCCCCHHCCCCC		17.9622322096
498PhosphorylationFETDSSYSDANNFIR
HCCCCCCHHCCCCCC		31.9927259358
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 FRK_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FRK_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 FRK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RB_HUMANRB1physical
7664264
PTEN_HUMANPTENphysical
19345329
SF3B4_HUMANSF3B4physical
25416956
BNIP2_HUMANBNIP2physical
21516116
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
DB08896Regorafenib
Regulatory Network of FRK_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-37; SER-62 AND TYR-387,AND MASS 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-46, AND MASSSPECTROMETRY.
"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-46 AND TYR-497, 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-46; TYR-387 AND TYR-497,AND MASS SPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-497, AND MASSSPECTROMETRY.

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