PTPRF_HUMAN - dbPTM
PTPRF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTPRF_HUMAN
UniProt AC P10586
Protein Name Receptor-type tyrosine-protein phosphatase F
Gene Name PTPRF
Organism Homo sapiens (Human).
Sequence Length 1907
Subcellular Localization Membrane
Single-pass type I membrane protein.
Protein Description Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity.; The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one..
Protein Sequence MAPEPAPGRTMVPLVPALVMLGLVAGAHGDSKPVFIKVPEDQTGLSGGVASFVCQATGEPKPRITWMKKGKKVSSQRFEVIEFDDGAGSVLRIQPLRVQRDEAIYECTATNSLGEINTSAKLSVLEEEQLPPGFPSIDMGPQLKVVEKARTATMLCAAGGNPDPEISWFKDFLPVDPATSNGRIKQLRSGALQIESSEESDQGKYECVATNSAGTRYSAPANLYVRVRRVAPRFSIPPSSQEVMPGGSVNLTCVAVGAPMPYVKWMMGAEELTKEDEMPVGRNVLELSNVVRSANYTCVAISSLGMIEATAQVTVKALPKPPIDLVVTETTATSVTLTWDSGNSEPVTYYGIQYRAAGTEGPFQEVDGVATTRYSIGGLSPFSEYAFRVLAVNSIGRGPPSEAVRARTGEQAPSSPPRRVQARMLSASTMLVQWEPPEEPNGLVRGYRVYYTPDSRRPPNAWHKHNTDAGLLTTVGSLLPGITYSLRVLAFTAVGDGPPSPTIQVKTQQGVPAQPADFQAEVESDTRIQLSWLLPPQERIIMYELVYWAAEDEDQQHKVTFDPTSSYTLEDLKPDTLYRFQLAARSDMGVGVFTPTIEARTAQSTPSAPPQKVMCVSMGSTTVRVSWVPPPADSRNGVITQYSVAYEAVDGEDRGRHVVDGISREHSSWDLVGLEKWTEYRVWVRAHTDVGPGPESSPVLVRTDEDVPSGPPRKVEVEPLNSTAVHVYWKLPVPSKQHGQIRGYQVTYVRLENGEPRGLPIIQDVMLAEAQWRPEESEDYETTISGLTPETTYSVTVAAYTTKGDGARSKPKIVTTTGAVPGRPTMMISTTAMNTALLQWHPPKELPGELLGYRLQYCRADEARPNTIDFGKDDQHFTVTGLHKGTTYIFRLAAKNRAGLGEEFEKEIRTPEDLPSGFPQNLHVTGLTTSTTELAWDPPVLAERNGRIISYTVVFRDINSQQELQNITTDTRFTLTGLKPDTTYDIKVRAWTSKGSGPLSPSIQSRTMPVEQVFAKNFRVAAAMKTSVLLSWEVPDSYKSAVPFKILYNGQSVEVDGHSMRKLIADLQPNTEYSFVLMNRGSSAGGLQHLVSIRTAPDLLPHKPLPASAYIEDGRFDLSMPHVQDPSLVRWFYIVVVPIDRVGGSMLTPRWSTPEELELDELLEAIEQGGEEQRRRRRQAERLKPYVAAQLDVLPETFTLGDKKNYRGFYNRPLSPDLSYQCFVLASLKEPMDQKRYASSPYSDEIVVQVTPAQQQEEPEMLWVTGPVLAVILIILIVIAILLFKRKRTHSPSSKDEQSIGLKDSLLAHSSDPVEMRRLNYQTPGMRDHPPIPITDLADNIERLKANDGLKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSIDGVPGSDYINANYIDGYRKQNAYIATQGPLPETMGDFWRMVWEQRTATVVMMTRLEEKSRVKCDQYWPARGTETCGLIQVTLLDTVELATYTVRTFALHKSGSSEKRELRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPLDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYVFIHEALLEAATCGHTEVPARNLYAHIQKLGQVPPGESVTAMELEFKLLASSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFLDGYRQQKAYIATQGPLAESTEDFWRMLWEHNSTIIVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGSFDHYAT
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
117N-linked_GlycosylationTNSLGEINTSAKLSV
CCCCCCCCCCCCEEE		24.55UniProtKB CARBOHYD
144UbiquitinationIDMGPQLKVVEKART
CCCCCCEEHHHHHHH		38.7021906983
144 (in isoform 1)Ubiquitination-38.7021890473
144 (in isoform 2)Ubiquitination-38.7021890473
200O-linked_GlycosylationQIESSEESDQGKYEC
EEECCCCHHCCEEEE		31.05-
200O-linked_GlycosylationQIESSEESDQGKYEC
EEECCCCHHCCEEEE		31.059295285
205PhosphorylationEESDQGKYECVATNS
CCHHCCEEEEEEECC		22.7620068231
210PhosphorylationGKYECVATNSAGTRY
CEEEEEEECCCCCCE		14.8720068231
212PhosphorylationYECVATNSAGTRYSA
EEEEEECCCCCCEEC		24.5820068231
215PhosphorylationVATNSAGTRYSAPAN
EEECCCCCCEECCCE		26.5920068231
217PhosphorylationTNSAGTRYSAPANLY
ECCCCCCEECCCEEE		14.7130576142
218O-linked_GlycosylationNSAGTRYSAPANLYV
CCCCCCEECCCEEEE		25.20OGP
218PhosphorylationNSAGTRYSAPANLYV
CCCCCCEECCCEEEE		25.2030576142
224PhosphorylationYSAPANLYVRVRRVA
EECCCEEEEEEEEEC		5.9930576142
248PhosphorylationQEVMPGGSVNLTCVA
CCCCCCCCEEEEEEE		17.4723879269
250N-linked_GlycosylationVMPGGSVNLTCVAVG
CCCCCCEEEEEEEEC		31.18UniProtKB CARBOHYD
262PhosphorylationAVGAPMPYVKWMMGA
EECCCCCHHHHHHCC		14.3823879269
274UbiquitinationMGAEELTKEDEMPVG
HCCHHCCCCCCCCCC		75.6521906983
274 (in isoform 1)Ubiquitination-75.6521890473
274 (in isoform 2)Ubiquitination-75.6521890473
295N-linked_GlycosylationSNVVRSANYTCVAIS
HHHHHHCCCEEEEEE		33.61UniProtKB CARBOHYD
296PhosphorylationNVVRSANYTCVAISS
HHHHHCCCEEEEEEC		10.96-
348O-linked_GlycosylationSGNSEPVTYYGIQYR
CCCCCCEEEEEEEEE		23.03OGP
359O-linked_GlycosylationIQYRAAGTEGPFQEV
EEEEECCCCCCCCEE		32.80OGP
359PhosphorylationIQYRAAGTEGPFQEV
EEEEECCCCCCCCEE		32.8021406692
371PhosphorylationQEVDGVATTRYSIGG
CEECCEEEEEEECCC		14.9221406692
372PhosphorylationEVDGVATTRYSIGGL
EECCEEEEEEECCCC		20.1921406692
380PhosphorylationRYSIGGLSPFSEYAF
EEECCCCCCHHHHHH		27.46-
394PhosphorylationFRVLAVNSIGRGPPS
HHHHHHHCCCCCCCH		21.5921406692
447PhosphorylationPNGLVRGYRVYYTPD
CCCEECEEEEEECCC		6.0724043423
450PhosphorylationLVRGYRVYYTPDSRR
EECEEEEEECCCCCC		7.8224043423
451PhosphorylationVRGYRVYYTPDSRRP
ECEEEEEECCCCCCC		14.6724043423
452PhosphorylationRGYRVYYTPDSRRPP
CEEEEEECCCCCCCC		11.7024043423
455PhosphorylationRVYYTPDSRRPPNAW
EEEECCCCCCCCCCC		31.2424043423
485PhosphorylationLLPGITYSLRVLAFT
HCCCCCEEEEEEEEE		10.8924719451
507O-linked_GlycosylationSPTIQVKTQQGVPAQ
CCEEEEEECCCCCCC		27.54OGP
568O-linked_GlycosylationFDPTSSYTLEDLKPD
ECCCCCCCHHHCCCC		26.14OGP
594PhosphorylationDMGVGVFTPTIEART
CCCCCEECCCEEEEC		19.67-
596PhosphorylationGVGVFTPTIEARTAQ
CCCEECCCEEEECCC		28.52-
601PhosphorylationTPTIEARTAQSTPSA
CCCEEEECCCCCCCC		35.7823090842
604PhosphorylationIEARTAQSTPSAPPQ
EEEECCCCCCCCCCC		39.5623090842
605PhosphorylationEARTAQSTPSAPPQK
EEECCCCCCCCCCCE		14.8023090842
607PhosphorylationRTAQSTPSAPPQKVM
ECCCCCCCCCCCEEE		54.2023090842
617PhosphorylationPQKVMCVSMGSTTVR
CCEEEEEECCCCEEE		16.7023090842
620PhosphorylationVMCVSMGSTTVRVSW
EEEEECCCCEEEEEE		16.5623090842
621PhosphorylationMCVSMGSTTVRVSWV
EEEECCCCEEEEEEC		24.4723090842
622PhosphorylationCVSMGSTTVRVSWVP
EEECCCCEEEEEECC		14.1723090842
688PhosphorylationRVWVRAHTDVGPGPE
EEEEEECCCCCCCCC		31.2522210691
697PhosphorylationVGPGPESSPVLVRTD
CCCCCCCCCEEEECC		19.8422210691
703PhosphorylationSSPVLVRTDEDVPSG
CCCEEEECCCCCCCC		35.94-
709PhosphorylationRTDEDVPSGPPRKVE
ECCCCCCCCCCCEEE		64.87-
721N-linked_GlycosylationKVEVEPLNSTAVHVY
EEEEEECCCCEEEEE		48.29UniProtKB CARBOHYD
777PhosphorylationAQWRPEESEDYETTI
CCCCCCCCCCCEEEC		33.8230576142
788PhosphorylationETTISGLTPETTYSV
EEECCCCCCCCEEEE		23.7030576142
794PhosphorylationLTPETTYSVTVAAYT
CCCCCEEEEEEEEEE		14.8230576142
816PhosphorylationSKPKIVTTTGAVPGR
CCCEEEEECCCCCCC		16.61-
817PhosphorylationKPKIVTTTGAVPGRP
CCEEEEECCCCCCCC		17.49-
825PhosphorylationGAVPGRPTMMISTTA
CCCCCCCEEEEEECC		20.29-
830O-linked_GlycosylationRPTMMISTTAMNTAL
CCEEEEEECCHHHHH		13.98OGP
959N-linked_GlycosylationTVVFRDINSQQELQN
EEEEECCCCHHHHCC		37.7519349973
959N-linked_GlycosylationTVVFRDINSQQELQN
EEEEECCCCHHHHCC		37.7519349973
966N-linked_GlycosylationNSQQELQNITTDTRF
CCHHHHCCCCCCCCE		46.31UniProtKB CARBOHYD
966N-linked_GlycosylationNSQQELQNITTDTRF
CCHHHHCCCCCCCCE		46.3116335952
968PhosphorylationQQELQNITTDTRFTL
HHHHCCCCCCCCEEE		26.6026074081
969PhosphorylationQELQNITTDTRFTLT
HHHCCCCCCCCEEEC		31.4126074081
971PhosphorylationLQNITTDTRFTLTGL
HCCCCCCCCEEECCC		26.1226074081
974PhosphorylationITTDTRFTLTGLKPD
CCCCCCEEECCCCCC		21.8126074081
976PhosphorylationTDTRFTLTGLKPDTT
CCCCEEECCCCCCCE		37.0926074081
996PhosphorylationRAWTSKGSGPLSPSI
EEEECCCCCCCCCCH		40.7624719451
1000PhosphorylationSKGSGPLSPSIQSRT
CCCCCCCCCCHHCCC		21.53-
1007O-linked_GlycosylationSPSIQSRTMPVEQVF
CCCHHCCCCCHHHHH		30.95OGP
1025AcetylationFRVAAAMKTSVLLSW
HHHHHHHCEEEEEEE		32.6819820855
1026PhosphorylationRVAAAMKTSVLLSWE
HHHHHHCEEEEEEEE		15.81-
1027PhosphorylationVAAAMKTSVLLSWEV
HHHHHCEEEEEEEEC		12.78-
1031PhosphorylationMKTSVLLSWEVPDSY
HCEEEEEEEECCCCC		19.61-
1045AcetylationYKSAVPFKILYNGQS
CCCCCCEEEEECCEE		26.2319820861
1092PhosphorylationGGLQHLVSIRTAPDL
CCHHHHEEEEECCCC		16.8324719451
1108PhosphorylationPHKPLPASAYIEDGR
CCCCCCCCEEEECCC		21.4730257219
1110PhosphorylationKPLPASAYIEDGRFD
CCCCCCEEEECCCEE		11.4430257219
1286 (in isoform 2)Ubiquitination-26.7621890473
1289PhosphorylationLLFKRKRTHSPSSKD
HHHHHCCCCCCCCCC		29.7320873877
1291PhosphorylationFKRKRTHSPSSKDEQ
HHHCCCCCCCCCCHH		26.3420873877
1293PhosphorylationRKRTHSPSSKDEQSI
HCCCCCCCCCCHHCC		53.7020873877
1294PhosphorylationKRTHSPSSKDEQSIG
CCCCCCCCCCHHCCC		47.7325849741
1294 (in isoform 2)Ubiquitination-47.7321890473
1295UbiquitinationRTHSPSSKDEQSIGL
CCCCCCCCCHHCCCC		70.4021906983
1295 (in isoform 1)Ubiquitination-70.4021890473
1299PhosphorylationPSSKDEQSIGLKDSL
CCCCCHHCCCCCHHH		19.3130266825
1303UbiquitinationDEQSIGLKDSLLAHS
CHHCCCCCHHHHHCC		39.8121906983
1303 (in isoform 1)Ubiquitination-39.8121890473
1305PhosphorylationQSIGLKDSLLAHSSD
HCCCCCHHHHHCCCC		24.5630266825
1310PhosphorylationKDSLLAHSSDPVEMR
CHHHHHCCCCHHHHH		30.7225849741
1311PhosphorylationDSLLAHSSDPVEMRR
HHHHHCCCCHHHHHH		35.7525849741
1321PhosphorylationVEMRRLNYQTPGMRD
HHHHHCCCCCCCCCC		20.5321945579
1323PhosphorylationMRRLNYQTPGMRDHP
HHHCCCCCCCCCCCC		16.0821945579
1335PhosphorylationDHPPIPITDLADNIE
CCCCCCHHHHHHHHH		21.4324719451
13452-HydroxyisobutyrylationADNIERLKANDGLKF
HHHHHHHHHCCCCCC		51.90-
1345UbiquitinationADNIERLKANDGLKF
HHHHHHHHHCCCCCC		51.90-
1351UbiquitinationLKANDGLKFSQEYES
HHHCCCCCCCCCCCC		48.80-
1356PhosphorylationGLKFSQEYESIDPGQ
CCCCCCCCCCCCCCC		13.82-
1367 (in isoform 2)Ubiquitination-12.2221890473
1376UbiquitinationNSNLEVNKPKNRYAN
CCCCEECCCCCCEEE		63.6521906983
1376 (in isoform 1)Ubiquitination-63.6521890473
1381PhosphorylationVNKPKNRYANVIAYD
ECCCCCCEEEEEEEC		16.3621945579
1387PhosphorylationRYANVIAYDHSRVIL
CEEEEEEECCCEEEE		11.7628796482
1390PhosphorylationNVIAYDHSRVILTSI
EEEEECCCEEEEEEC		25.9128796482
1403PhosphorylationSIDGVPGSDYINANY
ECCCCCCCCCCCCEE		22.5927642862
1405PhosphorylationDGVPGSDYINANYID
CCCCCCCCCCCEECC		9.5827642862
1410PhosphorylationSDYINANYIDGYRKQ
CCCCCCEECCCCCCC		9.66-
1459MalonylationLEEKSRVKCDQYWPA
CHHHHCCCCCCCCCC		30.8626320211
1572UbiquitinationLERMKHEKTVDIYGH
HHHHCCCCCEEEEEE		54.27-
1573PhosphorylationERMKHEKTVDIYGHV
HHHCCCCCEEEEEEE		22.04-
1577PhosphorylationHEKTVDIYGHVTCMR
CCCCEEEEEEEEECC		9.1927642862
1621PhosphorylationEVPARNLYAHIQKLG
CCCHHHHHHHHHHHC		10.3221945579
16502-HydroxyisobutyrylationFKLLASSKAHTSRFI
EHHHHCCCCCHHHHH		41.51-
1650UbiquitinationFKLLASSKAHTSRFI
EHHHHCCCCCHHHHH		41.51-
1665UbiquitinationSANLPCNKFKNRLVN
HCCCCHHHHCCCCHH		65.51-
1676PhosphorylationRLVNIMPYELTRVCL
CCHHCCCHHHHHHHC		13.2421945579
1679PhosphorylationNIMPYELTRVCLQPI
HCCCHHHHHHHCCCC		14.7621945579
1692PhosphorylationPIRGVEGSDYINASF
CCCCCCCCCCCCHHH		17.4621945579
1694PhosphorylationRGVEGSDYINASFLD
CCCCCCCCCCHHHCC		9.5821945579
1698PhosphorylationGSDYINASFLDGYRQ
CCCCCCHHHCCCHHH		23.1227642862
1703PhosphorylationNASFLDGYRQQKAYI
CHHHCCCHHHCCEEE		12.6227642862
1707UbiquitinationLDGYRQQKAYIATQG
CCCHHHCCEEEEECC		34.51-
1709PhosphorylationGYRQQKAYIATQGPL
CHHHCCEEEEECCCC		9.7227642862
1748MalonylationLREMGREKCHQYWPA
HHHHCHHHHHHHCCC		35.3426320211
1752PhosphorylationGREKCHQYWPAERSA
CHHHHHHHCCCCHHC		6.95-
1777PhosphorylationAEYNMPQYILREFKV
HHCCCCHHHHHEEEE		8.96-
1783UbiquitinationQYILREFKVTDARDG
HHHHHEEEEECCCCC		39.20-
1785PhosphorylationILREFKVTDARDGQS
HHHEEEEECCCCCCC		25.24-
1792PhosphorylationTDARDGQSRTIRQFQ
ECCCCCCCEEEEEEE		36.60-
1801 (in isoform 2)Ubiquitination-26.7721890473
1810UbiquitinationWPEQGVPKTGEGFID
CCCCCCCCCCCCHHH		67.752190698
1810 (in isoform 1)Ubiquitination-67.7521890473
1824UbiquitinationDFIGQVHKTKEQFGQ
HHHHCEEECHHHHCC		63.54-
1861PhosphorylationIVLERMRYEGVVDMF
HHHHHHCCCCHHHHH		14.0012496362
1870PhosphorylationGVVDMFQTVKTLRTQ
CHHHHHHHHHHHHCC		16.8328509920
1888PhosphorylationMVQTEDQYQLCYRAA
CCCCHHHHHHHHHHH		18.7721945579
1892PhosphorylationEDQYQLCYRAALEYL
HHHHHHHHHHHHHHH		16.3321945579
1898PhosphorylationCYRAALEYLGSFDHY
HHHHHHHHHCCCCCC		19.74-
1901PhosphorylationAALEYLGSFDHYAT-
HHHHHHCCCCCCCC-		25.5528176443
1905PhosphorylationYLGSFDHYAT-----
HHCCCCCCCC-----		17.4928796482
1907PhosphorylationGSFDHYAT-------
CCCCCCCC-------		31.7928796482
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 PTPRF_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 PTPRF_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNB1_HUMANCTNNB1physical
11245482
LIPA1_HUMANPPFIA1physical
8524829
LIPA1_HUMANPPFIA1physical
7796809
RET_HUMANRETphysical
11121408
TRIO_HUMANTRIOphysical
8643598
CAV1_HUMANCAV1physical
12176037
CTNB1_HUMANCTNNB1physical
9245795
PLAK_HUMANJUPphysical
9245795
LIPA1_HUMANPPFIA1physical
9624153
LIPA3_HUMANPPFIA3physical
9624153
LIPA2_HUMANPPFIA2physical
9624153
ARBK1_HUMANADRBK1physical
26344197
DAAF5_HUMANDNAAF5physical
26344197
NAA50_HUMANNAA50physical
26344197
NPL4_HUMANNPLOC4physical
26344197
PFKAM_HUMANPFKMphysical
26344197
PICAL_HUMANPICALMphysical
26344197
PPWD1_HUMANPPWD1physical
26344197
SPS1_HUMANSEPHS1physical
26344197
FCL_HUMANTSTA3physical
26344197
UFD1_HUMANUFD1Lphysical
26344197
NUDC3_HUMANNUDCD3physical
27880917
NAA50_HUMANNAA50physical
27880917
TTI1_HUMANTTI1physical
27880917
F1712_HUMANFAM171A2physical
27880917
TRIO_HUMANTRIOphysical
27880917
SGT1_HUMANSUGT1physical
27880917
LIPA1_HUMANPPFIA1physical
27880917
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616001Aplasia or hypoplasia of the breasts and/or nipples 2 (BNAH2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PTPRF_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins.";
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.;
Nat. Biotechnol. 27:378-386(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-959 AND ASN-966, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-966, AND MASSSPECTROMETRY.

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