PTN12_MOUSE - dbPTM
PTN12_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTN12_MOUSE
UniProt AC P35831
Protein Name Tyrosine-protein phosphatase non-receptor type 12
Gene Name Ptpn12
Organism Mus musculus (Mouse).
Sequence Length 775
Subcellular Localization Cytoplasm . Cell junction, focal adhesion . Cell projection, podosome . Partial translocation to focal adhesion sites might be mediated by interaction with SORBS2.
Protein Description Dephosphorylates a range of proteins, and thereby regulates cellular signaling cascades. [PubMed: 17070019 Dephosphorylates cellular tyrosine kinases, such as ERBB2 and PTK2B/PYK2, and thereby regulates signaling via ERBB2 and PTK2B/PYK2. Selectively dephosphorylates ERBB2 phosphorylated at 'Tyr-1112', 'Tyr-1196', and/or 'Tyr-1248' (By similarity]
Protein Sequence MEQVEILRRFIQRVQAMKSPDHNGEDNFARDFMRLRRLSTKYRTEKIYPTATGEKEENVKKNRYKDILPFDHSRVKLTLKTPSQDSDYINANFIKGVYGPKAYVATQGPLANTVIDFWRMIWEYNVVIIVMACREFEMGRKKCERYWPLYGEDPITFAPFKISCENEQARTDYFIRTLLLEFQNESRRLYQFHYVNWPDHDVPSSFDSILDMISLMRKYQEHEDVPICIHCSAGCGRTGAICAIDYTWNLLKAGKIPEEFNVFNLIQEMRTQRHSAVQTKEQYELVHRAIAQLFEKQLQLYEIHGAQKIADGNEITTGTMVSSIDSEKQDSPPPKPPRTRSCLVEGDAKEEILQPPEPHPVPPILTPSPPSAFPTVTTVWQDSDRYHPKPVLHMASPEQHPADLNRSYDKSADPMGKSESAIEHIDKKLERNLSFEIKKVPLQEGPKSFDGNTLLNRGHAIKIKSASSSVVDRTSKPQELSAGALKVDDVSQNSCADCSAAHSHRAAESSEESQSNSHTPPRPDCLPLDKKGHVTWSLHGPENATPVPDSPDGKSPDNHSQTLKTVSSTPNSTAEEEAHDLTEHHNSSPLLKAPLSFTNPLHSDDSDSDGGSSDGAVTRNKTSISTASATVSPASSAESACTRRVLPMSIARQEVAGTPHSGAEKDADVSEESPPPLPERTPESFVLADMPVRPEWHELPNQEWSEQRESEGLTTSGNEKHDAGGIHTEASADSPPAFSDKKDQITKSPAEVTDIGFGNRCGKPKGPREPPSEWT
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
1Acetylation-------MEQVEILR
-------CHHHHHHH		7.99-
19PhosphorylationQRVQAMKSPDHNGED
HHHHHHCCCCCCCCC		23.6025521595
39PhosphorylationFMRLRRLSTKYRTEK
HHHHHHHHHHHCCCE		22.50-
64PhosphorylationENVKKNRYKDILPFD
HHHCCCCCCCCCCCC		23.5425159016
81PhosphorylationRVKLTLKTPSQDSDY
EEEEEEECCCCCCCC		31.1426643407
83PhosphorylationKLTLKTPSQDSDYIN
EEEEECCCCCCCCCC		52.4226643407
171PhosphorylationCENEQARTDYFIRTL
CCCHHHHHHHHHHHH		37.7617203969
173PhosphorylationNEQARTDYFIRTLLL
CHHHHHHHHHHHHHH		10.5717203969
186PhosphorylationLLEFQNESRRLYQFH
HHHHCCCCCCEEEEE		30.1917203969
296UbiquitinationAIAQLFEKQLQLYEI
HHHHHHHHHHHHHEC		49.3122790023
301PhosphorylationFEKQLQLYEIHGAQK
HHHHHHHHECCCCCE		10.4029514104
316PhosphorylationIADGNEITTGTMVSS
ECCCCCCCCCCEEEC		17.0025619855
317PhosphorylationADGNEITTGTMVSSI
CCCCCCCCCCEEECC		35.9925619855
319PhosphorylationGNEITTGTMVSSIDS
CCCCCCCCEEECCCC		16.5925619855
322PhosphorylationITTGTMVSSIDSEKQ
CCCCCEEECCCCCCC		15.6827742792
323PhosphorylationTTGTMVSSIDSEKQD
CCCCEEECCCCCCCC		21.0027087446
326PhosphorylationTMVSSIDSEKQDSPP
CEEECCCCCCCCCCC		45.0527087446
331PhosphorylationIDSEKQDSPPPKPPR
CCCCCCCCCCCCCCC		36.4925521595
339PhosphorylationPPPKPPRTRSCLVEG
CCCCCCCCCEEEEEC		32.4829550500
341PhosphorylationPKPPRTRSCLVEGDA
CCCCCCCEEEEECCC		15.9325521595
366PhosphorylationHPVPPILTPSPPSAF
CCCCCCCCCCCCCCC		23.5725619855
368PhosphorylationVPPILTPSPPSAFPT
CCCCCCCCCCCCCCC		44.1825619855
371PhosphorylationILTPSPPSAFPTVTT
CCCCCCCCCCCCCEE		46.0225619855
375PhosphorylationSPPSAFPTVTTVWQD
CCCCCCCCCEEEECC		24.8325619855
377PhosphorylationPSAFPTVTTVWQDSD
CCCCCCCEEEECCCC		20.3626643407
378PhosphorylationSAFPTVTTVWQDSDR
CCCCCCEEEECCCCC		18.5326643407
383PhosphorylationVTTVWQDSDRYHPKP
CEEEECCCCCCCCCC		14.6423649490
386PhosphorylationVWQDSDRYHPKPVLH
EECCCCCCCCCCEEE		27.7126643407
396PhosphorylationKPVLHMASPEQHPAD
CCEEEECCCCCCCCH		22.7626824392
407PhosphorylationHPADLNRSYDKSADP
CCCHHCCCCCCCCCC		36.2919854140
434PhosphorylationKKLERNLSFEIKKVP
HHHHHHCCEEEEECC		25.1227087446
448PhosphorylationPLQEGPKSFDGNTLL
CCCCCCCCCCCCCCC		31.5326824392
453PhosphorylationPKSFDGNTLLNRGHA
CCCCCCCCCCCCCCE		37.8526643407
465PhosphorylationGHAIKIKSASSSVVD
CCEEEEEECCCCCCC		36.5425338131
467PhosphorylationAIKIKSASSSVVDRT
EEEEEECCCCCCCCC		30.18-
474PhosphorylationSSSVVDRTSKPQELS
CCCCCCCCCCCCCCC		36.3225338131
475PhosphorylationSSVVDRTSKPQELSA
CCCCCCCCCCCCCCC		43.1425338131
509PhosphorylationHSHRAAESSEESQSN
HHHHHHHCCHHHHCC		38.0225159016
510PhosphorylationSHRAAESSEESQSNS
HHHHHHCCHHHHCCC		36.5725159016
513PhosphorylationAAESSEESQSNSHTP
HHHCCHHHHCCCCCC		34.5525159016
515PhosphorylationESSEESQSNSHTPPR
HCCHHHHCCCCCCCC		49.9725159016
517PhosphorylationSEESQSNSHTPPRPD
CHHHHCCCCCCCCCC		33.7025159016
519PhosphorylationESQSNSHTPPRPDCL
HHHCCCCCCCCCCCE		34.5127087446
535PhosphorylationLDKKGHVTWSLHGPE
CCCCCCEEEEEECCC		12.0321743459
537PhosphorylationKKGHVTWSLHGPENA
CCCCEEEEEECCCCC		10.9221743459
545PhosphorylationLHGPENATPVPDSPD
EECCCCCCCCCCCCC		36.0827087446
550PhosphorylationNATPVPDSPDGKSPD
CCCCCCCCCCCCCCC		20.8627087446
555PhosphorylationPDSPDGKSPDNHSQT
CCCCCCCCCCCCCCE		42.9126824392
560PhosphorylationGKSPDNHSQTLKTVS
CCCCCCCCCEEEECC		30.9926745281
562PhosphorylationSPDNHSQTLKTVSST
CCCCCCCEEEECCCC		32.9826745281
565PhosphorylationNHSQTLKTVSSTPNS
CCCCEEEECCCCCCC		28.8226060331
567PhosphorylationSQTLKTVSSTPNSTA
CCEEEECCCCCCCCH		33.4525777480
568PhosphorylationQTLKTVSSTPNSTAE
CEEEECCCCCCCCHH		43.4721743459
569PhosphorylationTLKTVSSTPNSTAEE
EEEECCCCCCCCHHH		20.9821743459
572PhosphorylationTVSSTPNSTAEEEAH
ECCCCCCCCHHHHHH		30.1425777480
573PhosphorylationVSSTPNSTAEEEAHD
CCCCCCCCHHHHHHH		44.7426643407
582PhosphorylationEEEAHDLTEHHNSSP
HHHHHHHHHCCCCCC		39.0526239621
587PhosphorylationDLTEHHNSSPLLKAP
HHHHCCCCCCCCCCC		29.0426239621
588PhosphorylationLTEHHNSSPLLKAPL
HHHCCCCCCCCCCCC		25.5327149854
596PhosphorylationPLLKAPLSFTNPLHS
CCCCCCCCCCCCCCC		29.0320531401
598PhosphorylationLKAPLSFTNPLHSDD
CCCCCCCCCCCCCCC		32.3321082442
603PhosphorylationSFTNPLHSDDSDSDG
CCCCCCCCCCCCCCC		51.2821082442
606PhosphorylationNPLHSDDSDSDGGSS
CCCCCCCCCCCCCCC		43.9621082442
608PhosphorylationLHSDDSDSDGGSSDG
CCCCCCCCCCCCCCC		41.9521082442
612PhosphorylationDSDSDGGSSDGAVTR
CCCCCCCCCCCCCCC		30.6821082442
613PhosphorylationSDSDGGSSDGAVTRN
CCCCCCCCCCCCCCC		43.2525619855
618PhosphorylationGSSDGAVTRNKTSIS
CCCCCCCCCCCCCCE		28.1725619855
622PhosphorylationGAVTRNKTSISTASA
CCCCCCCCCCEEEEE		34.5425619855
623PhosphorylationAVTRNKTSISTASAT
CCCCCCCCCEEEEEE		19.0225619855
625PhosphorylationTRNKTSISTASATVS
CCCCCCCEEEEEEEC		20.0725619855
626PhosphorylationRNKTSISTASATVSP
CCCCCCEEEEEEECC		23.9825619855
628PhosphorylationKTSISTASATVSPAS
CCCCEEEEEEECCCC		25.2625619855
630PhosphorylationSISTASATVSPASSA
CCEEEEEEECCCCCC		21.0125619855
632PhosphorylationSTASATVSPASSAES
EEEEEEECCCCCCHH		15.4725619855
635PhosphorylationSATVSPASSAESACT
EEEECCCCCCHHHHH		33.2025619855
636PhosphorylationATVSPASSAESACTR
EEECCCCCCHHHHHH		37.8625619855
639PhosphorylationSPASSAESACTRRVL
CCCCCCHHHHHHCCC		28.4925619855
642PhosphorylationSSAESACTRRVLPMS
CCCHHHHHHCCCCCC		22.6425619855
658PhosphorylationARQEVAGTPHSGAEK
HHHHHCCCCCCCCCC		14.2125777480
661PhosphorylationEVAGTPHSGAEKDAD
HHCCCCCCCCCCCCC		40.6825777480
670PhosphorylationAEKDADVSEESPPPL
CCCCCCCCCCCCCCC		35.8725521595
673PhosphorylationDADVSEESPPPLPER
CCCCCCCCCCCCCCC		38.3625521595
705PhosphorylationELPNQEWSEQRESEG
CCCCHHHHHHHHHCC		24.0929514104
714PhosphorylationQRESEGLTTSGNEKH
HHHHCCCCCCCCCCC		29.7626824392
715PhosphorylationRESEGLTTSGNEKHD
HHHCCCCCCCCCCCC		39.4129233185
716PhosphorylationESEGLTTSGNEKHDA
HHCCCCCCCCCCCCC		34.0929233185
728PhosphorylationHDAGGIHTEASADSP
CCCCCCCCCCCCCCC		31.1825619855
731PhosphorylationGGIHTEASADSPPAF
CCCCCCCCCCCCCCC		26.7827087446
734PhosphorylationHTEASADSPPAFSDK
CCCCCCCCCCCCCCC		32.2826824392
739PhosphorylationADSPPAFSDKKDQIT
CCCCCCCCCCCHHCC		51.1025619855
746PhosphorylationSDKKDQITKSPAEVT
CCCCHHCCCCCCCCE		21.6025619855
748PhosphorylationKKDQITKSPAEVTDI
CCHHCCCCCCCCEEC		22.2325521595
753PhosphorylationTKSPAEVTDIGFGNR
CCCCCCCEECCCCCC		17.2625619855
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 PTN12_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTN12_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 PTN12_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SHC1_MOUSEShc1physical
12052829
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PTN12_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 SER-331, AND MASSSPECTROMETRY.
"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-434, AND MASSSPECTROMETRY.
"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 SER-596; THR-598; SER-603AND SER-608, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND SER-673, ANDMASS SPECTROMETRY.
"Phosphoproteomic analysis of the developing mouse brain.";
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
Mol. Cell. Proteomics 3:1093-1101(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-748, AND MASSSPECTROMETRY.

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