PTN18_HUMAN - dbPTM
PTN18_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTN18_HUMAN
UniProt AC Q99952
Protein Name Tyrosine-protein phosphatase non-receptor type 18
Gene Name PTPN18
Organism Homo sapiens (Human).
Sequence Length 460
Subcellular Localization Nucleus. Cytoplasm.
Protein Description Differentially dephosphorylate autophosphorylated tyrosine kinases which are known to be overexpressed in tumor tissues..
Protein Sequence MSRSLDSARSFLERLEARGGREGAVLAGEFSDIQACSAAWKADGVCSTVAGSRPENVRKNRYKDVLPYDQTRVILSLLQEEGHSDYINGNFIRGVDGSLAYIATQGPLPHTLLDFWRLVWEFGVKVILMACREIENGRKRCERYWAQEQEPLQTGLFCITLIKEKWLNEDIMLRTLKVTFQKESRSVYQLQYMSWPDRGVPSSPDHMLAMVEEARRLQGSGPEPLCVHCSAGCGRTGVLCTVDYVRQLLLTQMIPPDFSLFDVVLKMRKQRPAAVQTEEQYRFLYHTVAQMFCSTLQNASPHYQNIKENCAPLYDDALFLRTPQALLAIPRPPGGVLRSISVPGSPGHAMADTYAVVQKRGAPAGAGSGTQTGTGTGTGARSAEEAPLYSKVTPRAQRPGAHAEDARGTLPGRVPADQSPAGSGAYEDVAGGAQTGGLGFNLRIGRPKGPRDPPAEWTRV
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
10PhosphorylationRSLDSARSFLERLEA
CCHHHHHHHHHHHHH		33.6216094384
32 (in isoform 2)Ubiquitination-42.19-
76PhosphorylationDQTRVILSLLQEEGH
HHHHHHHHHHHHHCC		18.8622817900
86PhosphorylationQEEGHSDYINGNFIR
HHHCCCCCCCCCEEC		10.1727642862
281PhosphorylationAVQTEEQYRFLYHTV
CCCCHHHHHHHHHHH		13.4522817900
303PhosphorylationLQNASPHYQNIKENC
HHHCCHHHHHHHHHC		13.4622817900
314PhosphorylationKENCAPLYDDALFLR
HHHCCCCCCCCEECC		15.6621945579
322PhosphorylationDDALFLRTPQALLAI
CCCEECCCCHHHHCC		23.1522817900
339PhosphorylationPPGGVLRSISVPGSP
CCCCEEEEEECCCCC		18.3028450419
341PhosphorylationGGVLRSISVPGSPGH
CCEEEEEECCCCCCC		24.4123401153
345PhosphorylationRSISVPGSPGHAMAD
EEEECCCCCCCCCHH		22.9528450419
353PhosphorylationPGHAMADTYAVVQKR
CCCCCHHCEEEEEEC		12.1128060719
354PhosphorylationGHAMADTYAVVQKRG
CCCCHHCEEEEEECC		9.6529978859
370PhosphorylationPAGAGSGTQTGTGTG
CCCCCCCCCCCCCCC		25.3422817900
374PhosphorylationGSGTQTGTGTGTGAR
CCCCCCCCCCCCCCC		34.6528060719
376PhosphorylationGTQTGTGTGTGARSA
CCCCCCCCCCCCCCH		31.2628060719
378PhosphorylationQTGTGTGTGARSAEE
CCCCCCCCCCCCHHH		27.7528060719
382PhosphorylationGTGTGARSAEEAPLY
CCCCCCCCHHHCCCC		39.2321945579
387PhosphorylationARSAEEAPLYSKVTP
CCCHHHCCCCCCCCC		34.8015951569
389PhosphorylationSAEEAPLYSKVTPRA
CHHHCCCCCCCCCCC		12.8421945579
390PhosphorylationAEEAPLYSKVTPRAQ
HHHCCCCCCCCCCCC		28.4721945579
393PhosphorylationAPLYSKVTPRAQRPG
CCCCCCCCCCCCCCC		15.7023401153
409PhosphorylationHAEDARGTLPGRVPA
CHHHCCCCCCCCCCC		24.9928450419
419PhosphorylationGRVPADQSPAGSGAY
CCCCCCCCCCCCCCC		19.7728450419
423PhosphorylationADQSPAGSGAYEDVA
CCCCCCCCCCCCCCC		23.5028450419
426PhosphorylationSPAGSGAYEDVAGGA
CCCCCCCCCCCCCCC		19.0429978859
435PhosphorylationDVAGGAQTGGLGFNL
CCCCCCCCCCCCEEE		32.4629978859
458PhosphorylationRDPPAEWTRV-----
CCCCHHCCCC-----		17.04-
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
281YPhosphorylationKinaseTECP42680
PSP
303YPhosphorylationKinaseTECP42680
PSP
354YPhosphorylationKinaseTECP42680
PSP
389YPhosphorylationKinaseTECP42680
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTN18_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 PTN18_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PPIP1_HUMANPSTPIP1physical
9265651
AIFM1_HUMANAIFM1physical
27880917
AIP_HUMANAIPphysical
27880917
ATPA_HUMANATP5A1physical
27880917
ATX2_HUMANATXN2physical
27880917
BAG2_HUMANBAG2physical
27880917
BAG5_HUMANBAG5physical
27880917
DNJA2_HUMANDNAJA2physical
27880917
DNJB1_HUMANDNAJB1physical
27880917
DNJC7_HUMANDNAJC7physical
27880917
IRS4_HUMANIRS4physical
27880917
AF1Q_HUMANMLLT11physical
27880917
NU155_HUMANNUP155physical
27880917
PPIP2_HUMANPSTPIP2physical
27880917
CAB45_HUMANSDF4physical
27880917
STML2_HUMANSTOML2physical
27880917
SYTM_HUMANTARS2physical
27880917
TBB2A_HUMANTUBB2Aphysical
27880917
TBB6_HUMANTUBB6physical
27880917
PTN18_HUMANPTPN18physical
27432908
PPIP2_HUMANPSTPIP2physical
27432908
CBWD2_HUMANCBWD2physical
27432908
AGAL_HUMANGLAphysical
27432908
CATB_HUMANCTSBphysical
27432908
MAIP1_HUMANC2orf47physical
27432908
STIP1_HUMANSTIP1physical
27432908
CPVL_HUMANCPVLphysical
27432908
ARL1_HUMANARL1physical
27432908
CDIPT_HUMANCDIPTphysical
27432908
SSR4_HUMANSSTR4physical
27432908
TMX3_HUMANTMX3physical
27432908
MIRO1_HUMANRHOT1physical
27432908
ARF1_HUMANARF1physical
27432908
HAX1_HUMANHAX1physical
27432908
NDUS3_HUMANNDUFS3physical
27432908
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 PTN18_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, AND MASSSPECTROMETRY.
"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-389, 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-389, 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-389, AND MASSSPECTROMETRY.
"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-389, AND MASSSPECTROMETRY.

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