PTPRA_HUMAN - dbPTM
PTPRA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTPRA_HUMAN
UniProt AC P18433
Protein Name Receptor-type tyrosine-protein phosphatase alpha
Gene Name PTPRA
Organism Homo sapiens (Human).
Sequence Length 802
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description
Protein Sequence MDSWFILVLLGSGLICVSANNATTVAPSVGITRLINSSTAEPVKEEAKTSNPTSSLTSLSVAPTFSPNITLGPTYLTTVNSSDSDNGTTRTASTNSIGITISPNGTWLPDNQFTDARTEPWEGNSSTAATTPETFPPSGNSDSKDRRDETPIIAVMVALSSLLVIVFIIIVLYMLRFKKYKQAGSHSNSFRLSNGRTEDVEPQSVPLLARSPSTNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWTYGNIRVSVEDVTVLVDYTVRKFCIQQVGDMTNRKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKACNPQYAGAIVVHCSAGVGRTGTFVVIDAMLDMMHTERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTELEVTSLETHLQKIYNKIPGTSNNGLEEEFKKLTSIKIQNDKMRTGNLPANMKKNRVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDGYRQKDSYIASQGPLLHTIEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMISIIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLERVKAEGILDVFQTVKSLRLQRPHMVQTLEQYEFCYKVVQEYIDAFSDYANFK
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
18PhosphorylationGSGLICVSANNATTV
CCCEEEEECCCCCCC		22.37-
21N-linked_GlycosylationLICVSANNATTVAPS
EEEEECCCCCCCCCC		38.08UniProtKB CARBOHYD
36N-linked_GlycosylationVGITRLINSSTAEPV
CCHHHHCCCCCCCCC		34.20UniProtKB CARBOHYD
38O-linked_GlycosylationITRLINSSTAEPVKE
HHHHCCCCCCCCCCH		27.44OGP
39O-linked_GlycosylationTRLINSSTAEPVKEE
HHHCCCCCCCCCCHH		34.56OGP
68N-linked_GlycosylationVAPTFSPNITLGPTY
ECCCCCCCEEECCEE		38.38UniProtKB CARBOHYD
80N-linked_GlycosylationPTYLTTVNSSDSDNG
CEEEEEECCCCCCCC		33.43UniProtKB CARBOHYD
86N-linked_GlycosylationVNSSDSDNGTTRTAS
ECCCCCCCCCEEEEE		54.37UniProtKB CARBOHYD
104N-linked_GlycosylationIGITISPNGTWLPDN
EEEEECCCCCCCCCC		54.45UniProtKB CARBOHYD
124N-linked_GlycosylationRTEPWEGNSSTAATT
CCCCCCCCCCCCCCC		22.67UniProtKB CARBOHYD
171PhosphorylationVIVFIIIVLYMLRFK
HHHHHHHHHHHHHHH		14.6630622161
176 (in isoform 4)Phosphorylation-27.1029743597
176PhosphorylationIIVLYMLRFKKYKQA
HHHHHHHHHHHHHHC		27.1030622161
178 (in isoform 4)Phosphorylation-44.4917081983
178PhosphorylationVLYMLRFKKYKQAGS
HHHHHHHHHHHHCCC		44.4917081983
180 (in isoform 4)Phosphorylation-29.2029743597
180PhosphorylationYMLRFKKYKQAGSHS
HHHHHHHHHHCCCCC		29.2011676480
185 (in isoform 3)Phosphorylation-27.1029743597
185PhosphorylationKKYKQAGSHSNSFRL
HHHHHCCCCCCCEEC		27.1029978859
187PhosphorylationYKQAGSHSNSFRLSN
HHHCCCCCCCEECCC		35.5530266825
187 (in isoform 3)Phosphorylation-35.5517081983
189PhosphorylationQAGSHSNSFRLSNGR
HCCCCCCCEECCCCC		18.1130266825
189 (in isoform 3)Phosphorylation-18.1129743597
193PhosphorylationHSNSFRLSNGRTEDV
CCCCEECCCCCCCCC		32.7426074081
197PhosphorylationFRLSNGRTEDVEPQS
EECCCCCCCCCCCCC		37.6328450419
204PhosphorylationTEDVEPQSVPLLARS
CCCCCCCCCCEEECC		36.1011676480
208UbiquitinationEPQSVPLLARSPSTN
CCCCCCEEECCCCCC		2.8129967540
211O-linked_GlycosylationSVPLLARSPSTNRKY
CCCEEECCCCCCCCC		20.0029351928
211PhosphorylationSVPLLARSPSTNRKY
CCCEEECCCCCCCCC		20.0021712546
213PhosphorylationPLLARSPSTNRKYPP
CEEECCCCCCCCCCC		39.2921712546
214PhosphorylationLLARSPSTNRKYPPL
EEECCCCCCCCCCCC		42.2930108239
217UbiquitinationRSPSTNRKYPPLPVD
CCCCCCCCCCCCCHH		65.2729967540
218PhosphorylationSPSTNRKYPPLPVDK
CCCCCCCCCCCCHHH		13.5726074081
271PhosphorylationENKEKNRYVNILPYD
HHHHHCCEEEEEECC		13.7728152594
277PhosphorylationRYVNILPYDHSRVHL
CEEEEEECCCCCCCC		23.8928796482
280PhosphorylationNILPYDHSRVHLTPV
EEEECCCCCCCCEEC		32.8528796482
293PhosphorylationPVEGVPDSDYINASF
ECCCCCCHHHCCHHH		26.66-
407PhosphorylationITQFHFTSWPDFGVP
EEEEEECCCCCCCCC		35.35-
410UbiquitinationFHFTSWPDFGVPFTP
EEECCCCCCCCCCCC		46.8332015554
419UbiquitinationGVPFTPIGMLKFLKK
CCCCCCHHHHHHHHH		19.3032015554
421UbiquitinationPFTPIGMLKFLKKVK
CCCCHHHHHHHHHHH		2.7532015554
437UbiquitinationCNPQYAGAIVVHCSA
CCCCCCCEEEEECCC		5.3532015554
445UbiquitinationIVVHCSAGVGRTGTF
EEEECCCCCCCCCEE		13.2032015554
450UbiquitinationSAGVGRTGTFVVIDA
CCCCCCCCEEEEEHH		18.7832015554
459UbiquitinationFVVIDAMLDMMHTER
EEEEHHHHHHHCCCC		4.0132015554
461UbiquitinationVIDAMLDMMHTERKV
EEHHHHHHHCCCCCC		1.5432015554
522PhosphorylationETHLQKIYNKIPGTS
HHHHHHHHHCCCCCC		19.8928796482
542PhosphorylationEEFKKLTSIKIQNDK
HHHHHHHCCEECCCC		32.11-
551UbiquitinationKIQNDKMRTGNLPAN
EECCCCCCCCCCCCC		45.2624816145
552PhosphorylationIQNDKMRTGNLPANM
ECCCCCCCCCCCCCC		27.24-
560UbiquitinationGNLPANMKKNRVLQI
CCCCCCCCCCCEEEE		46.8624816145
562UbiquitinationLPANMKKNRVLQIIP
CCCCCCCCCEEEECC		33.5032015554
570PhosphorylationRVLQIIPYEFNRVII
CEEEECCCCCCEEEE		23.8128796482
571UbiquitinationVLQIIPYEFNRVIIP
EEEECCCCCCEEEEE		30.9632015554
586PhosphorylationVKRGEENTDYVNASF
ECCCCCCCCCCCHHH		31.8028796482
588PhosphorylationRGEENTDYVNASFID
CCCCCCCCCCHHHCC		8.1228796482
592PhosphorylationNTDYVNASFIDGYRQ
CCCCCCHHHCCCCCC		19.9629978859
602PhosphorylationDGYRQKDSYIASQGP
CCCCCCCCEEECCCC		26.0227732954
603PhosphorylationGYRQKDSYIASQGPL
CCCCCCCEEECCCCC		15.6127732954
606PhosphorylationQKDSYIASQGPLLHT
CCCCEEECCCCCHHH		26.5527732954
613PhosphorylationSQGPLLHTIEDFWRM
CCCCCHHHHHHHHHH		26.4927732954
670PhosphorylationKKEEECESYTVRDLL
ECHHHCCCCCHHHEE		37.4521406692
671PhosphorylationKEEECESYTVRDLLV
CHHHCCCCCHHHEEE		6.2221406692
672PhosphorylationEEECESYTVRDLLVT
HHHCCCCCHHHEEEE		20.5321406692
765AcetylationLDVFQTVKSLRLQRP
HHHHHHHHHHCCCCC		47.3530591675
766PhosphorylationDVFQTVKSLRLQRPH
HHHHHHHHHCCCCCC		17.8719764811
781PhosphorylationMVQTLEQYEFCYKVV
HHHHHHHHHHHHHHH		11.12-
785PhosphorylationLEQYEFCYKVVQEYI
HHHHHHHHHHHHHHH		16.49-
791PhosphorylationCYKVVQEYIDAFSDY
HHHHHHHHHHHHHHH		6.2428176443
796PhosphorylationQEYIDAFSDYANFK-
HHHHHHHHHHHCCC-		31.2827273156
798PhosphorylationYIDAFSDYANFK---
HHHHHHHHHCCC---		11.4029255136
798DephosphorylationYIDAFSDYANFK---
HHHHHHHHHCCC---		11.407518772
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
-KUbiquitinationE3 ubiquitin ligaseMARCHF9Q86YJ5
PMID:19457934
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTPRA_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 PTPRA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRB2_HUMANGRB2physical
8670803
ARL2_HUMANARL2physical
27880917
ATX2_HUMANATXN2physical
27880917
GRB2_HUMANGRB2physical
27880917
KCMA1_HUMANKCNMA1physical
27880917
NCBP1_HUMANNCBP1physical
27880917
SERC_HUMANPSAT1physical
27880917
PTPRE_HUMANPTPREphysical
27880917
VPS25_HUMANVPS25physical
27880917
TMM51_HUMANTMEM51physical
27880917
GRDN_HUMANCCDC88Aphysical
27880917
E41L1_HUMANEPB41L1physical
27880917
PSD3_HUMANPSD3physical
27880917
BASP1_HUMANBASP1physical
27880917
GRIN3_HUMANGPRIN3physical
27880917
EXOC3_HUMANEXOC3physical
27880917
BAIP2_HUMANBAIAP2physical
27880917
RAPH1_HUMANRAPH1physical
27880917
MERL_HUMANNF2physical
27880917
GAB1_HUMANGAB1physical
27880917
PTPRE_HUMANPTPREphysical
28514442
ASND1_HUMANASNSD1physical
28514442
GRB2_HUMANGRB2physical
28514442
MYCPP_HUMANDENND4Aphysical
28514442
TPC2_HUMANTPCN2physical
28514442
CY561_HUMANCYB561physical
28514442
GLT12_HUMANGALNT12physical
28514442
LEG1_HUMANLGALS1physical
28514442
PTPRA_HUMANPTPRAphysical
27432908
PTPRE_HUMANPTPREphysical
27432908
TXND5_HUMANTXNDC5physical
27432908
XPO5_HUMANXPO5physical
27432908
TNPO3_HUMANTNPO3physical
27432908
SAAL1_HUMANSAAL1physical
27432908
XPO4_HUMANXPO4physical
27432908
B4GA1_HUMANB4GAT1physical
27432908
XPO6_HUMANXPO6physical
27432908
PDIA6_HUMANPDIA6physical
27432908
NCDN_HUMANNCDNphysical
27432908
XPO2_HUMANCSE1Lphysical
27432908
TNPO1_HUMANTNPO1physical
27432908
XPOT_HUMANXPOTphysical
27432908
CALX_HUMANCANXphysical
27432908
GRB2_HUMANGRB2physical
23532252
SRC_HUMANSRCphysical
23532252
MBP_HUMANMBPphysical
23532252
PTPRG_HUMANPTPRGphysical
23532252
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 PTPRA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-798, AND MASSSPECTROMETRY.
"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 TYR-798, 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-798, 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-798, 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-798, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-798, 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-798, AND MASSSPECTROMETRY.

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