PTPRA_MOUSE - dbPTM
PTPRA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTPRA_MOUSE
UniProt AC P18052
Protein Name Receptor-type tyrosine-protein phosphatase alpha
Gene Name Ptpra
Organism Mus musculus (Mouse).
Sequence Length 829
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description
Protein Sequence MDSWFILVLFGSGLIHVSANNATTVSPSLGTTRLIKTSTTELAKEENKTSNSTSSVISLSVAPTFSPNLTLEPTYVTTVNSSHSDNGTRRAASTESGGTTISPNGSWLIENQFTDAITEPWEGNSSTAATTPETFPPADETPIIAVMVALSSLLVIVFIIIVLYMLRFKKYKQAGSHSNSFRLSNGRTEDVEPQSVPLLARSPSTNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPFLSLAVSKDAVKALNKTTPLLERRFIGKSNSRGCLSDDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNVRVSVEDVTVLVDYTVRKFCIQQVGDVTNRKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKACNPQYAGAIVVHCSAGVGRTGTFVVIDAMLDMMHSERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTELEVTSLETHLQKIYNKIPGTSNNGLEEEFKKLTSIKIQNDKMRTGNLPANMKKNRVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLLHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQEYIDAFSDYANFK
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
21N-linked_GlycosylationLIHVSANNATTVSPS
EEEEECCCCCCCCCC
38.08-
47N-linked_GlycosylationTELAKEENKTSNSTS
HHHHHHHCCCCCCCC
54.73-
51N-linked_GlycosylationKEENKTSNSTSSVIS
HHHCCCCCCCCCEEE
55.31-
68N-linked_GlycosylationVAPTFSPNLTLEPTY
ECCCCCCCCEEECEE
44.45-
80N-linked_GlycosylationPTYVTTVNSSHSDNG
CEEEEEECCCCCCCC
35.38-
86N-linked_GlycosylationVNSSHSDNGTRRAAS
ECCCCCCCCCEEEEE
57.67-
104N-linked_GlycosylationGGTTISPNGSWLIEN
CCEEECCCCCEEEEE
50.79-
124N-linked_GlycosylationITEPWEGNSSTAATT
CCCCCCCCCCCCCCC
22.67-
176PhosphorylationKKYKQAGSHSNSFRL
HHHHHCCCCCCCEEC
27.1025521595
178PhosphorylationYKQAGSHSNSFRLSN
HHHCCCCCCCEECCC
35.5525159016
180PhosphorylationQAGSHSNSFRLSNGR
HCCCCCCCEECCCCC
18.1125521595
184PhosphorylationHSNSFRLSNGRTEDV
CCCCEECCCCCCCCC
32.7420531401
188PhosphorylationFRLSNGRTEDVEPQS
EECCCCCCCCCCCCC
37.6325777480
195PhosphorylationTEDVEPQSVPLLARS
CCCCCCCCCCEEECC
36.1026026062
202PhosphorylationSVPLLARSPSTNRKY
CCCEEECCCCCCCCC
20.0025521595
204PhosphorylationPLLARSPSTNRKYPP
CEEECCCCCCCCCCC
39.297537734
205PhosphorylationLLARSPSTNRKYPPL
EEECCCCCCCCCCCC
42.2919060867
262 (in isoform 2)Phosphorylation-13.7725195567
279AcetylationAVSKDAVKALNKTTP
HCCHHHHHHHCCCCH
49.2122902405
334UbiquitinationFINGYQEKNKFIAAQ
HCCCHHHCCCEEEEC
50.3322790023
409AcetylationLVDYTVRKFCIQQVG
EEEHHHHHHHHHHHC
40.0122826441
476PhosphorylationCSAGVGRTGTFVVID
CCCCCCCCCEEEEEH
34.34-
478PhosphorylationAGVGRTGTFVVIDAM
CCCCCCCEEEEEHHH
16.79-
549PhosphorylationETHLQKIYNKIPGTS
HHHHHHHHHCCCCCC
19.8925367039
818PhosphorylationCYKVVQEYIDAFSDY
HHHHHHHHHHHHHHH
6.2425619855
823PhosphorylationQEYIDAFSDYANFK-
HHHHHHHHHHHCCC-
31.2822942356
825PhosphorylationYIDAFSDYANFK---
HHHHHHHHHCCC---
11.4026824392

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
180SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
180SPhosphorylationKinaseCAMK2AP11798
PSP
180SPhosphorylationKinasePRKCAP17252
GPS
180SPhosphorylationKinaseKPCAP20444
PhosphoELM
180SPhosphorylationKinasePKCAP05696
PSP
180SPhosphorylationKinasePKC-FAMILY-GPS
204SPhosphorylationKinaseCAMK2AQ9UQM7
PSP
204SPhosphorylationKinaseCAMK2AP11798
PSP
204SPhosphorylationKinasePRKCAP17252
GPS
204SPhosphorylationKinaseKPCAP20444
PhosphoELM
204SPhosphorylationKinasePKCAP05696
PSP
204SPhosphorylationKinasePKC-FAMILY-GPS
825YPhosphorylationKinaseSRCP05480
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTPRA_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 PTPRA_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
2AAA_MOUSEPpp2r1aphysical
12952889

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PTPRA_MOUSE

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Related Literatures of Post-Translational Modification
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-180; SER-204 ANDTYR-825, AND MASS SPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-825, AND MASSSPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-825, AND MASSSPECTROMETRY.

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