PTPRS_HUMAN - dbPTM
PTPRS_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTPRS_HUMAN
UniProt AC Q13332
Protein Name Receptor-type tyrosine-protein phosphatase S
Gene Name PTPRS
Organism Homo sapiens (Human).
Sequence Length 1948
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Cell projection, axon . Perikaryon . Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane . Cell junction, synapse, synaptosome . Cell junction, synapse, postsynaptic cell membrane, postsy
Protein Description Cell surface receptor that binds to glycosaminoglycans, including chondroitin sulfate proteoglycans and heparan sulfate proteoglycan. [PubMed: 21454754 Binding to chondroitin sulfate and heparan sulfate proteoglycans has opposite effects on PTPRS oligomerization and regulation of neurite outgrowth. Contributes to the inhibition of neurite and axonal outgrowth by chondroitin sulfate proteoglycans, also after nerve transection. Plays a role in stimulating neurite outgrowth in response to the heparan sulfate proteoglycan GPC2. Required for normal brain development, especially for normal development of the pituitary gland and the olfactory bulb. Functions as tyrosine phosphatase]
Protein Sequence MAPTWGPGMVSVVGPMGLLVVLLVGGCAAEEPPRFIKEPKDQIGVSGGVASFVCQATGDPKPRVTWNKKGKKVNSQRFETIEFDESAGAVLRIQPLRTPRDENVYECVAQNSVGEITVHAKLTVLREDQLPSGFPNIDMGPQLKVVERTRTATMLCAASGNPDPEITWFKDFLPVDPSASNGRIKQLRSETFESTPIRGALQIESSEETDQGKYECVATNSAGVRYSSPANLYVRELREVRRVAPRFSILPMSHEIMPGGNVNITCVAVGSPMPYVKWMQGAEDLTPEDDMPVGRNVLELTDVKDSANYTCVAMSSLGVIEAVAQITVKSLPKAPGTPMVTENTATSITITWDSGNPDPVSYYVIEYKSKSQDGPYQIKEDITTTRYSIGGLSPNSEYEIWVSAVNSIGQGPPSESVVTRTGEQAPASAPRNVQARMLSATTMIVQWEEPVEPNGLIRGYRVYYTMEPEHPVGNWQKHNVDDSLLTTVGSLLEDETYTVRVLAFTSVGDGPLSDPIQVKTQQGVPGQPMNLRAEARSETSITLSWSPPRQESIIKYELLFREGDHGREVGRTFDPTTSYVVEDLKPNTEYAFRLAARSPQGLGAFTPVVRQRTLQSKPSAPPQDVKCVSVRSTAILVSWRPPPPETHNGALVGYSVRYRPLGSEDPEPKEVNGIPPTTTQILLEALEKWTQYRITTVAHTEVGPGPESSPVVVRTDEDVPSAPPRKVEAEALNATAIRVLWRSPAPGRQHGQIRGYQVHYVRMEGAEARGPPRIKDVMLADAQWETDDTAEYEMVITNLQPETAYSITVAAYTMKGDGARSKPKVVVTKGAVLGRPTLSVQQTPEGSLLARWEPPAGTAEDQVLGYRLQFGREDSTPLATLEFPPSEDRYTASGVHKGATYVFRLAARSRGGLGEEAAEVLSIPEDTPRGHPQILEAAGNASAGTVLLRWLPPVPAERNGAIVKYTVAVREAGALGPARETELPAAAEPGAENALTLQGLKPDTAYDLQVRAHTRRGPGPFSPPVRYRTFLRDQVSPKNFKVKMIMKTSVLLSWEFPDNYNSPTPYKIQYNGLTLDVDGRTTKKLITHLKPHTFYNFVLTNRGSSLGGLQQTVTAWTAFNLLNGKPSVAPKPDADGFIMVYLPDGQSPVPVQSYFIVMVPLRKSRGGQFLTPLGSPEDMDLEELIQDISRLQRRSLRHSRQLEVPRPYIAARFSVLPPTFHPGDQKQYGGFDNRGLEPGHRYVLFVLAVLQKSEPTFAASPFSDPFQLDNPDPQPIVDGEEGLIWVIGPVLAVVFIICIVIAILLYKNKPDSKRKDSEPRTKCLLNNADLAPHHPKDPVEMRRINFQTPDSGLRSPLREPGFHFESMLSHPPIPIADMAEHTERLKANDSLKLSQEYESIDPGQQFTWEHSNLEVNKPKNRYANVIAYDHSRVILQPIEGIMGSDYINANYVDGYRCQNAYIATQGPLPETFGDFWRMVWEQRSATIVMMTRLEEKSRIKCDQYWPNRGTETYGFIQVTLLDTIELATFCVRTFSLHKNGSSEKREVRQFQFTAWPDHGVPEYPTPFLAFLRRVKTCNPPDAGPIVVHCSAGVGRTGCFIVIDAMLERIKPEKTVDVYGHVTLMRSQRNYMVQTEDQYSFIHEALLEAVGCGNTEVPARSLYAYIQKLAQVEPGEHVTGMELEFKRLANSKAHTSRFISANLPCNKFKNRLVNIMPYESTRVCLQPIRGVEGSDYINASFIDGYRQQKAYIATQGPLAETTEDFWRMLWENNSTIVVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTVRQFQFTDWPEQGVPKSGEGFIDFIGQVHKTKEQFGQDGPISVHCSAGVGRTGVFITLSIVLERMRYEGVVDIFQTVKMLRTQRPAMVQTEDEYQFCYQAALEYLGSFDHYAT
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
214PhosphorylationEETDQGKYECVATNS
CCCCCCEEEEEEECC		22.7630576142
219PhosphorylationGKYECVATNSAGVRY
CEEEEEEECCCCCCC		14.8730576142
221PhosphorylationYECVATNSAGVRYSS
EEEEEECCCCCCCCC		23.2630576142
263N-linked_GlycosylationIMPGGNVNITCVAVG
CCCCCCEEEEEEECC		28.0525385546
308N-linked_GlycosylationTDVKDSANYTCVAMS
CCCCCCCCCEEEEEC		36.2825385546
383 (in isoform 6)Phosphorylation-34.14-
383 (in isoform 7)Phosphorylation-34.14-
387PhosphorylationEDITTTRYSIGGLSP
ECEECCEEEECCCCC		11.5320068231
388PhosphorylationDITTTRYSIGGLSPN
CEECCEEEECCCCCC		16.0920068231
393PhosphorylationRYSIGGLSPNSEYEI
EEEECCCCCCCCEEE		25.8820068231
396PhosphorylationIGGLSPNSEYEIWVS
ECCCCCCCCEEEEEE		44.9620068231
398PhosphorylationGLSPNSEYEIWVSAV
CCCCCCCEEEEEEEH		16.7320068231
403PhosphorylationSEYEIWVSAVNSIGQ
CCEEEEEEEHHHCCC		16.1120068231
407PhosphorylationIWVSAVNSIGQGPPS
EEEEEHHHCCCCCCC		22.8420068231
414PhosphorylationSIGQGPPSESVVTRT
HCCCCCCCCCEEECC		45.7120068231
416PhosphorylationGQGPPSESVVTRTGE
CCCCCCCCEEECCCC		26.6520068231
419PhosphorylationPPSESVVTRTGEQAP
CCCCCEEECCCCCCC		21.9820068231
483PhosphorylationQKHNVDDSLLTTVGS
HHCCCCHHHHHHHHH		22.3326074081
486PhosphorylationNVDDSLLTTVGSLLE
CCCHHHHHHHHHHHC		25.4026074081
487PhosphorylationVDDSLLTTVGSLLED
CCHHHHHHHHHHHCC		23.8826074081
490PhosphorylationSLLTTVGSLLEDETY
HHHHHHHHHHCCCCE		25.9926074081
537PhosphorylationNLRAEARSETSITLS
CCCEEECCCCEEEEE		52.8823403867
544PhosphorylationSETSITLSWSPPRQE
CCCEEEEECCCCCCH		19.5023403867
546PhosphorylationTSITLSWSPPRQESI
CEEEEECCCCCCHHE		22.9623403867
552PhosphorylationWSPPRQESIIKYELL
CCCCCCHHEEEEEEE		22.6724719451
556PhosphorylationRQESIIKYELLFREG
CCHHEEEEEEEEECC		11.0321406692
610DimethylationGAFTPVVRQRTLQSK
CCCCHHHHHHHCCCC		22.09-
610MethylationGAFTPVVRQRTLQSK
CCCCHHHHHHHCCCC		22.0930762979
696PhosphorylationWTQYRITTVAHTEVG
HHCCEEEEEEECCCC		17.2119690332
700O-linked_GlycosylationRITTVAHTEVGPGPE
EEEEEEECCCCCCCC		23.72OGP
700PhosphorylationRITTVAHTEVGPGPE
EEEEEEECCCCCCCC		23.7219690332
708PhosphorylationEVGPGPESSPVVVRT
CCCCCCCCCCEEEEC		42.9719690332
709PhosphorylationVGPGPESSPVVVRTD
CCCCCCCCCEEEECC		21.7619690332
720 (in isoform 6)N-linked_Glycosylation-36.78-
733N-linked_GlycosylationKVEAEALNATAIRVL
CHHHHHHCCCEEHHH		42.1519159218
733N-linked_GlycosylationKVEAEALNATAIRVL
CHHHHHHCCCEEHHH		42.1516335952
756PhosphorylationQHGQIRGYQVHYVRM
CCCEECCEEEEEEEE		9.4924043423
760PhosphorylationIRGYQVHYVRMEGAE
ECCEEEEEEEECCHH		7.3024043423
803PhosphorylationITNLQPETAYSITVA
EECCCCCCCEEEEEE		37.26-
812PhosphorylationYSITVAAYTMKGDGA
EEEEEEEEEECCCCC		9.53-
813PhosphorylationSITVAAYTMKGDGAR
EEEEEEEEECCCCCC		14.00-
837O-linked_GlycosylationGAVLGRPTLSVQQTP
CCCCCCCEEEEEECC		30.24OGP
843O-linked_GlycosylationPTLSVQQTPEGSLLA
CEEEEEECCCCCEEE		13.25OGP
843PhosphorylationPTLSVQQTPEGSLLA
CEEEEEECCCCCEEE		13.2525159151
858PhosphorylationRWEPPAGTAEDQVLG
EECCCCCCHHHHCCE		29.0426074081
866PhosphorylationAEDQVLGYRLQFGRE
HHHHCCEEEEECCCC		12.1826074081
875PhosphorylationLQFGREDSTPLATLE
EECCCCCCCCCEEEE		27.4626074081
876PhosphorylationQFGREDSTPLATLEF
ECCCCCCCCCEEEEC		34.3426074081
880PhosphorylationEDSTPLATLEFPPSE
CCCCCCEEEECCCCC		34.2126074081
891PhosphorylationPPSEDRYTASGVHKG
CCCCCCCCCCCCCCC		18.42-
893PhosphorylationSEDRYTASGVHKGAT
CCCCCCCCCCCCCCC		33.28-
900PhosphorylationSGVHKGATYVFRLAA
CCCCCCCCHHHHHHH		28.9624144214
901PhosphorylationGVHKGATYVFRLAAR
CCCCCCCHHHHHHHH		9.3224144214
917 (in isoform 7)Phosphorylation-12.4827251275
922 (in isoform 7)Phosphorylation-41.0727251275
940N-linked_GlycosylationQILEAAGNASAGTVL
HHHHHHCCCCCCEEE		26.45UniProtKB CARBOHYD
965PhosphorylationRNGAIVKYTVAVREA
CCCEEEEEEEEEHHC		8.7822210691
966PhosphorylationNGAIVKYTVAVREAG
CCEEEEEEEEEHHCC		9.0322210691
996PhosphorylationPGAENALTLQGLKPD
CCCCCCEEECCCCCC		18.0222210691
1022PhosphorylationRRGPGPFSPPVRYRT
CCCCCCCCCCCCHHH		31.2828674419
1027PhosphorylationPFSPPVRYRTFLRDQ
CCCCCCCHHHHCCCC		17.7824719451
1036PhosphorylationTFLRDQVSPKNFKVK
HHCCCCCCCCCCEEE		25.2324719451
1062PhosphorylationEFPDNYNSPTPYKIQ
ECCCCCCCCCCEEEE		21.5723312004
1219PhosphorylationRFSVLPPTFHPGDQK
EEEECCCCCCCCCCC		32.4124719451
1228PhosphorylationHPGDQKQYGGFDNRG
CCCCCCCCCCCCCCC		26.6724719451
1317PhosphorylationPDSKRKDSEPRTKCL
CCCCCCCCCCCHHHH		53.1626699800
1322UbiquitinationKDSEPRTKCLLNNAD
CCCCCCHHHHHCCCC		24.94-
1326 (in isoform 6)Phosphorylation-28.7927251275
1331 (in isoform 6)Phosphorylation-11.2627251275
1344 (in isoform 3)Phosphorylation-4.2327251275
1349 (in isoform 3)Phosphorylation-24.0027251275
1366PhosphorylationEPGFHFESMLSHPPI
CCCCCHHHHHCCCCC		24.8727251275
1382PhosphorylationIADMAEHTERLKAND
HHHHHHHHHHHHHCC		17.8227251275
1386UbiquitinationAEHTERLKANDSLKL
HHHHHHHHHCCCCHH		51.90-
1392UbiquitinationLKANDSLKLSQEYES
HHHCCCCHHHHHHHC		50.47-
1397PhosphorylationSLKLSQEYESIDPGQ
CCHHHHHHHCCCCCC		13.82-
1417UbiquitinationHSNLEVNKPKNRYAN
CCCCEECCCCCCEEE		63.6521906983
1422PhosphorylationVNKPKNRYANVIAYD
ECCCCCCEEEEEEEC		16.3621945579
1428PhosphorylationRYANVIAYDHSRVIL
CEEEEEEECCCCEEE		11.7628796482
1431PhosphorylationNVIAYDHSRVILQPI
EEEEECCCCEEEEEC		25.9128796482
1484PhosphorylationRMVWEQRSATIVMMT
HHHHHHHCCEEEEEE		29.47-
1486PhosphorylationVWEQRSATIVMMTRL
HHHHHCCEEEEEECC		18.49-
1492DimethylationATIVMMTRLEEKSRI
CEEEEEECCHHHHCC		23.39-
1492MethylationATIVMMTRLEEKSRI
CEEEEEECCHHHHCC		23.3924377377
1662PhosphorylationEVPARSLYAYIQKLA
CCCHHHHHHHHHHHC		9.9028796482
1685UbiquitinationTGMELEFKRLANSKA
CCCEEEHHHHHCCCC		36.81-
1694PhosphorylationLANSKAHTSRFISAN
HHCCCCCHHHHHHCC		26.85-
1695PhosphorylationANSKAHTSRFISANL
HCCCCCHHHHHHCCC		18.48-
1706UbiquitinationSANLPCNKFKNRLVN
HCCCCCHHHCCCCEE		65.51-
1717PhosphorylationRLVNIMPYESTRVCL
CCEEECCCCCCEEEE		12.72-
1720PhosphorylationNIMPYESTRVCLQPI
EECCCCCCEEEEEEC		18.38-
1733PhosphorylationPIRGVEGSDYINASF
ECCCCCCCCCCCHHH		17.4621945579
1735PhosphorylationRGVEGSDYINASFID
CCCCCCCCCCHHHCC		9.5821945579
1793PhosphorylationGREKCHQYWPAERSA
CHHHHHHHCCCCHHC		6.95-
1818PhosphorylationAEYNMPQYILREFKV
HHCCCCHHHHEEEEE		8.96-
1824UbiquitinationQYILREFKVTDARDG
HHHHEEEEEECCCCC		39.20-
1826PhosphorylationILREFKVTDARDGQS
HHEEEEEECCCCCCC		25.24-
1833PhosphorylationTDARDGQSRTVRQFQ
ECCCCCCCEEEEEEE		35.13-
1835PhosphorylationARDGQSRTVRQFQFT
CCCCCCEEEEEEEEC		25.86-
1851UbiquitinationWPEQGVPKSGEGFID
CCCCCCCCCCCCHHH		69.55-
1902PhosphorylationIVLERMRYEGVVDIF
HHHHHHCCCCHHHHH		14.0027762562
1911PhosphorylationGVVDIFQTVKMLRTQ
CHHHHHHHHHHHHCC		16.0227762562
1939PhosphorylationCYQAALEYLGSFDHY
HHHHHHHHHCCCCCC		19.74-
1942PhosphorylationAALEYLGSFDHYAT-
HHHHHHCCCCCCCC-		25.5528176443
1946PhosphorylationYLGSFDHYAT-----
HHCCCCCCCC-----		17.4928796482
1948PhosphorylationGSFDHYAT-------
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

Oops, there are no upstream regulatory protein records of PTPRS_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTPRS_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 PTPRS_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHD3_HUMANCHD3physical
16169070
FEZ1_HUMANFEZ1physical
16169070
PROF2_HUMANPFN2physical
16169070
UT14A_HUMANUTP14Aphysical
16169070
SETB1_HUMANSETDB1physical
16169070
KAT5_HUMANKAT5physical
16169070
TBB2A_HUMANTUBB2Aphysical
16169070
UBR1_HUMANUBR1physical
16169070
PTN_HUMANPTNphysical
16169070
EF1G_HUMANEEF1Gphysical
16169070
CE126_HUMANKIAA1377physical
16169070
U119A_HUMANUNC119physical
16169070
LIPA1_HUMANPPFIA1physical
8524829
PTPRD_HUMANPTPRDphysical
9566880
LIPA1_HUMANPPFIA1physical
9624153
LIPA2_HUMANPPFIA2physical
9624153
LIPA3_HUMANPPFIA3physical
9624153
TRIO_HUMANTRIOphysical
27880917
LIPA1_HUMANPPFIA1physical
27880917
PTPRF_HUMANPTPRFphysical
27880917
CSKI2_HUMANCASKIN2physical
27880917
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 PTPRS_HUMAN

loading...

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-733, AND MASSSPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-733, 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-733, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory