PTPRC_HUMAN - dbPTM
PTPRC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTPRC_HUMAN
UniProt AC P08575
Protein Name Receptor-type tyrosine-protein phosphatase C {ECO:0000305}
Gene Name PTPRC {ECO:0000312|HGNC:HGNC:9666}
Organism Homo sapiens (Human).
Sequence Length 1306
Subcellular Localization Membrane
Single-pass type I membrane protein . Membrane raft . Colocalized with DPP4 in membrane rafts.
Protein Description Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-cell activation, recruits and dephosphorylates SKAP1 and FYN. Dephosphorylates LYN, and thereby modulates LYN activity (By similarity)..
Protein Sequence MTMYLWLKLLAFGFAFLDTEVFVTGQSPTPSPTGLTTAKMPSVPLSSDPLPTHTTAFSPASTFERENDFSETTTSLSPDNTSTQVSPDSLDNASAFNTTGVSSVQTPHLPTHADSQTPSAGTDTQTFSGSAANAKLNPTPGSNAISDVPGERSTASTFPTDPVSPLTTTLSLAHHSSAALPARTSNTTITANTSDAYLNASETTTLSPSGSAVISTTTIATTPSKPTCDEKYANITVDYLYNKETKLFTAKLNVNENVECGNNTCTNNEVHNLTECKNASVSISHNSCTAPDKTLILDVPPGVEKFQLHDCTQVEKADTTICLKWKNIETFTCDTQNITYRFQCGNMIFDNKEIKLENLEPEHEYKCDSEILYNNHKFTNASKIIKTDFGSPGEPQIIFCRSEAAHQGVITWNPPQRSFHNFTLCYIKETEKDCLNLDKNLIKYDLQNLKPYTKYVLSLHAYIIAKVQRNGSAAMCHFTTKSAPPSQVWNMTVSMTSDNSMHVKCRPPRDRNGPHERYHLEVEAGNTLVRNESHKNCDFRVKDLQYSTDYTFKAYFHNGDYPGEPFILHHSTSYNSKALIAFLAFLIIVTSIALLVVLYKIYDLHKKRSCNLDEQQELVERDDEKQLMNVEPIHADILLETYKRKIADEGRLFLAEFQSIPRVFSKFPIKEARKPFNQNKNRYVDILPYDYNRVELSEINGDAGSNYINASYIDGFKEPRKYIAAQGPRDETVDDFWRMIWEQKATVIVMVTRCEEGNRNKCAEYWPSMEEGTRAFGDVVVKINQHKRCPDYIIQKLNIVNKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLEGLEAENKVDVYGYVVKLRRQRCLMVQVEAQYILIHQALVEYNQFGETEVNLSELHPYLHNMKKRDPPSEPSPLEAEFQRLPSYRSWRTQHIGNQEENKSKNRNSNVIPYDYNRVPLKHELEMSKESEHDSDESSDDDSDSEEPSKYINASFIMSYWKPEVMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELKHGDQEICAQYWGEGKQTYGDIEVDLKDTDKSSTYTLRVFELRHSKRKDSRTVYQYQYTNWSVEQLPAEPKELISMIQVVKQKLPQKNSSEGNKHHKSTPLLIHCRDGSQQTGIFCALLNLLESAETEEVVDIFQVVKALRKARPGMVSTFEQYQFLYDVIASTYPAQNGQVKKNNHQEDKIEFDNEVDKVKQDANCVNPLGAPEKLPEAKEQAEGSEPTSGTEGPEHSVNGPASPALNQGS
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
54O-linked_GlycosylationSDPLPTHTTAFSPAS
CCCCCCCCCCCCCCH
12.22OGP
78N-linked_GlycosylationETTTSLSPDNTSTQV
CCCCCCCCCCCCCCC
39.04UniProtKB CARBOHYD
80N-linked_GlycosylationTTSLSPDNTSTQVSP
CCCCCCCCCCCCCCH
24.09-
90N-linked_GlycosylationTQVSPDSLDNASAFN
CCCCHHHCCCCCCCC
40.88UniProtKB CARBOHYD
92N-linked_GlycosylationVSPDSLDNASAFNTT
CCHHHCCCCCCCCCC
39.38-
95N-linked_GlycosylationDSLDNASAFNTTGVS
HHCCCCCCCCCCCCC
36.13UniProtKB CARBOHYD
97N-linked_GlycosylationLDNASAFNTTGVSSV
CCCCCCCCCCCCCCC
36.37-
106O-linked_GlycosylationTGVSSVQTPHLPTHA
CCCCCCCCCCCCCCC
48.07OGP
119O-linked_GlycosylationHADSQTPSAGTDTQT
CCCCCCCCCCCCCCC
28.58OGP
126O-linked_GlycosylationSAGTDTQTFSGSAAN
CCCCCCCCCCCCHHC
34.91OGP
139O-linked_GlycosylationANAKLNPTPGSNAIS
HCCCCCCCCCCCCCC
35.69OGP
151PhosphorylationAISDVPGERSTASTF
CCCCCCCCCCCCCCC
24.8319690332
154PhosphorylationDVPGERSTASTFPTD
CCCCCCCCCCCCCCC
30.5719690332
162PhosphorylationASTFPTDPVSPLTTT
CCCCCCCCCCCCHHH
21.4119690332
167O-linked_GlycosylationTDPVSPLTTTLSLAH
CCCCCCCHHHHHHHC
14.76OGP
176O-linked_GlycosylationTLSLAHHSSAALPAR
HHHHHCCCCCCCCCC
18.94OGP
177O-linked_GlycosylationLSLAHHSSAALPART
HHHHCCCCCCCCCCC
18.94OGP
184N-linked_GlycosylationSAALPARTSNTTITA
CCCCCCCCCCCEEEE
40.40UniProtKB CARBOHYD
185O-linked_GlycosylationAALPARTSNTTITAN
CCCCCCCCCCEEEEC
21.2427655845
186N-linked_GlycosylationALPARTSNTTITANT
CCCCCCCCCEEEECC
22.15-
187O-linked_GlycosylationLPARTSNTTITANTS
CCCCCCCCEEEECCC
3.0127655845
190N-linked_GlycosylationRTSNTTITANTSDAY
CCCCCEEEECCCCCC
31.31UniProtKB CARBOHYD
192N-linked_GlycosylationSNTTITANTSDAYLN
CCCEEEECCCCCCCC
21.76-
193O-linked_GlycosylationNTTITANTSDAYLNA
CCEEEECCCCCCCCC
36.8727655845
194O-linked_GlycosylationTTITANTSDAYLNAS
CEEEECCCCCCCCCC
15.5227655845
197N-linked_GlycosylationTANTSDAYLNASETT
EECCCCCCCCCCCCE
28.83UniProtKB CARBOHYD
199N-linked_GlycosylationNTSDAYLNASETTTL
CCCCCCCCCCCCEEE
34.11-
217O-linked_GlycosylationGSAVISTTTIATTPS
CCEEEEEEEEECCCC
2.77OGP
218O-linked_GlycosylationSAVISTTTIATTPSK
CEEEEEEEEECCCCC
11.88OGP
221O-linked_GlycosylationISTTTIATTPSKPTC
EEEEEEECCCCCCCC
35.68OGP
222O-linked_GlycosylationSTTTIATTPSKPTCD
EEEEEECCCCCCCCC
49.53OGP
232N-linked_GlycosylationKPTCDEKYANITVDY
CCCCCHHHCCEEEEE
27.6319349973
234N-linked_GlycosylationTCDEKYANITVDYLY
CCCHHHCCEEEEEEE
13.7119349973
240N-linked_GlycosylationANITVDYLYNKETKL
CCEEEEEEECCCCCE
32.8519349973
260N-linked_GlycosylationNVNENVECGNNTCTN
CCCCCCCCCCCCCCC
52.90UniProtKB CARBOHYD
262N-linked_GlycosylationNENVECGNNTCTNNE
CCCCCCCCCCCCCCC
25.38-
270N-linked_GlycosylationNTCTNNEVHNLTECK
CCCCCCCEECCCCCC
54.56UniProtKB CARBOHYD
272N-linked_GlycosylationCTNNEVHNLTECKNA
CCCCCEECCCCCCCC
44.66-
276N-linked_GlycosylationEVHNLTECKNASVSI
CEECCCCCCCCEEEE
49.4519349973
278N-linked_GlycosylationHNLTECKNASVSISH
ECCCCCCCCEEEEEC
26.2819349973
278PhosphorylationHNLTECKNASVSISH
ECCCCCCCCEEEEEC
26.28-
284N-linked_GlycosylationKNASVSISHNSCTAP
CCCEEEEECCCCCCC
31.8019349973
286N-linked_GlycosylationASVSISHNSCTAPDK
CEEEEECCCCCCCCC
4.5819349973
314UbiquitinationQLHDCTQVEKADTTI
ECCCCCEEECCCEEE
53.35-
322UbiquitinationEKADTTICLKWKNIE
ECCCEEEEEEECCEE
52.27-
324UbiquitinationADTTICLKWKNIETF
CCEEEEEEECCEEEE
46.60-
335N-linked_GlycosylationIETFTCDTQNITYRF
EEEEEECCCCEEEEE
30.5719349973
337N-linked_GlycosylationTFTCDTQNITYRFQC
EEEECCCCEEEEEEE
19.0519349973
345SulfoxidationITYRFQCGNMIFDNK
EEEEEEECCEEECCC
1.6421406390
350UbiquitinationQCGNMIFDNKEIKLE
EECCEEECCCEEEEC
63.76-
364UbiquitinationENLEPEHEYKCDSEI
CCCCCCCCCCCCHHH
28.69-
378N-linked_GlycosylationILYNNHKFTNASKII
HHCCCCCCCCHHHHE
45.40UniProtKB CARBOHYD
380N-linked_GlycosylationYNNHKFTNASKIIKT
CCCCCCCCHHHHEEC
26.85-
381UbiquitinationNNHKFTNASKIIKTD
CCCCCCCHHHHEECC
46.14-
384UbiquitinationKFTNASKIIKTDFGS
CCCCHHHHEECCCCC
45.58-
419N-linked_GlycosylationWNPPQRSFHNFTLCY
CCCCCCCCCCEEEEE
29.5919349973
421N-linked_GlycosylationPPQRSFHNFTLCYIK
CCCCCCCCEEEEEEE
22.6419349973
430AcetylationTLCYIKETEKDCLNL
EEEEEECCHHHHHCC
62.2525953088
437AcetylationTEKDCLNLDKNLIKY
CHHHHHCCCCCHHHH
57.7420167786
437UbiquitinationTEKDCLNLDKNLIKY
CHHHHHCCCCCHHHH
57.74-
451PhosphorylationYDLQNLKPYTKYVLS
HHHHHCCCCCHHHHH
25.15-
453PhosphorylationLQNLKPYTKYVLSLH
HHHCCCCCHHHHHEE
9.98-
456PhosphorylationLKPYTKYVLSLHAYI
CCCCCHHHHHEEHHH
14.20-
468N-linked_GlycosylationAYIIAKVQRNGSAAM
HHHHHHHHHCCCEEE
31.51UniProtKB CARBOHYD
470N-linked_GlycosylationIIAKVQRNGSAAMCH
HHHHHHHCCCEEEEE
19.19-
470PhosphorylationIIAKVQRNGSAAMCH
HHHHHHHCCCEEEEE
19.1923401153
480PhosphorylationAAMCHFTTKSAPPSQ
EEEEEEECCCCCHHH
43.8723401153
484PhosphorylationHFTTKSAPPSQVWNM
EEECCCCCHHHEEEE
35.9923401153
488N-linked_GlycosylationKSAPPSQVWNMTVSM
CCCCHHHEEEEEEEE
19.8619349973
490N-linked_GlycosylationAPPSQVWNMTVSMTS
CCHHHEEEEEEEECC
13.2519349973
492O-linked_GlycosylationPSQVWNMTVSMTSDN
HHHEEEEEEEECCCC
13.74OGP
494PhosphorylationQVWNMTVSMTSDNSM
HEEEEEEEECCCCCC
25.9822210691
495PhosphorylationVWNMTVSMTSDNSMH
EEEEEEEECCCCCCE
26.5928787133
497N-linked_GlycosylationNMTVSMTSDNSMHVK
EEEEEECCCCCCEEE
40.7919349973
529N-linked_GlycosylationVEAGNTLVRNESHKN
EECCCEEECCCCCCC
47.87UniProtKB CARBOHYD
531N-linked_GlycosylationAGNTLVRNESHKNCD
CCCEEECCCCCCCCC
43.22-
540UbiquitinationSHKNCDFRVKDLQYS
CCCCCCCEEEECCCC
48.76-
544PhosphorylationCDFRVKDLQYSTDYT
CCCEEEECCCCCCEE
22.34-
546PhosphorylationFRVKDLQYSTDYTFK
CEEEECCCCCCEEEE
28.26-
548PhosphorylationVKDLQYSTDYTFKAY
EEECCCCCCEEEEEE
17.73-
559PhosphorylationFKAYFHNGDYPGEPF
EEEEEECCCCCCCCE
17.97-
607PhosphorylationKIYDLHKKRSCNLDE
HHHHHHHHCCCCCHH
19.0828122231
639PhosphorylationPIHADILLETYKRKI
CCCHHHHHHHHHHHH
34.0229978859
640PhosphorylationIHADILLETYKRKIA
CCHHHHHHHHHHHHH
10.2227642862
641AcetylationHADILLETYKRKIAD
CHHHHHHHHHHHHHH
55.4225953088
641UbiquitinationHADILLETYKRKIAD
CHHHHHHHHHHHHHH
55.42-
657PhosphorylationGRLFLAEFQSIPRVF
CCEEEEEHHCCCCHH
39.6229978859
663PhosphorylationEFQSIPRVFSKFPIK
EHHCCCCHHHCCCHH
30.4528450419
664AcetylationFQSIPRVFSKFPIKE
HHCCCCHHHCCCHHH
43.6325953088
664UbiquitinationFQSIPRVFSKFPIKE
HHCCCCHHHCCCHHH
43.632189047
668UbiquitinationPRVFSKFPIKEARKP
CCHHHCCCHHHHCCC
45.63-
681PhosphorylationKPFNQNKNRYVDILP
CCCCCCCCCCEEECC
16.3328796482
683PhosphorylationFNQNKNRYVDILPYD
CCCCCCCCEEECCCC
27.98-
687PhosphorylationKNRYVDILPYDYNRV
CCCCEEECCCCCCEE
27.8428796482
689PhosphorylationRYVDILPYDYNRVEL
CCEEECCCCCCEEEE
10.0628796482
703PhosphorylationLSEINGDAGSNYINA
EEECCCCCCCCCCCH
28.3429978859
705PhosphorylationEINGDAGSNYINASY
ECCCCCCCCCCCHHH
9.3929978859
709PhosphorylationDAGSNYINASYIDGF
CCCCCCCCHHHCCCC
20.3828796482
710PhosphorylationAGSNYINASYIDGFK
CCCCCCCHHHCCCCC
10.7128796482
715UbiquitinationINASYIDGFKEPRKY
CCHHHCCCCCCCHHH
72.79-
719UbiquitinationYIDGFKEPRKYIAAQ
HCCCCCCCHHHHEEC
52.29-
720PhosphorylationIDGFKEPRKYIAAQG
CCCCCCCHHHHEECC
9.3227642862
759UbiquitinationTRCEEGNRNKCAEYW
EECCCCCCCHHHHHC
31.42-
763PhosphorylationEGNRNKCAEYWPSME
CCCCCHHHHHCCCHH
12.2329978859
766PhosphorylationRNKCAEYWPSMEEGT
CCHHHHHCCCHHHHC
25.3629978859
780AcetylationTRAFGDVVVKINQHK
CEEECCEEEEECCCC
25.0825953088
780UbiquitinationTRAFGDVVVKINQHK
CEEECCEEEEECCCC
25.08-
790PhosphorylationINQHKRCPDYIIQKL
ECCCCCCCHHHHHHH
5.76-
800AcetylationIIQKLNIVNKKEKAT
HHHHHCCCCCCCCCC
51.9525953088
800UbiquitinationIIQKLNIVNKKEKAT
HHHHHCCCCCCCCCC
51.95-
801UbiquitinationIQKLNIVNKKEKATG
HHHHCCCCCCCCCCC
60.28-
831UbiquitinationVPEDPHLLLKLRRRV
CCCCHHHHHHHHHHH
39.66-
858PhosphorylationVHCSAGVGRTGTYIG
EECCCCCCCCCCEEE
28.13-
860PhosphorylationCSAGVGRTGTYIGID
CCCCCCCCCCEEEHH
16.02-
861PhosphorylationSAGVGRTGTYIGIDA
CCCCCCCCCEEEHHH
9.86-
880PhosphorylationLEAENKVDVYGYVVK
HHHHCCEEEEEEEEE
9.7728796482
882PhosphorylationAENKVDVYGYVVKLR
HHCCEEEEEEEEEEC
5.6028796482
900PhosphorylationCLMVQVEAQYILIHQ
EEEEEEEHHHHHHHH
12.54-
926PhosphorylationEVNLSELHPYLHNMK
CCCHHHHHHHHHHCC
15.17-
932UbiquitinationLHPYLHNMKKRDPPS
HHHHHHHCCCCCCCC
51.79-
937PhosphorylationHNMKKRDPPSEPSPL
HHCCCCCCCCCCCCH
68.4830576142
951PhosphorylationLEAEFQRLPSYRSWR
HHHHHHCCCCHHHHH
37.4626074081
952PhosphorylationEAEFQRLPSYRSWRT
HHHHHCCCCHHHHHH
13.5126074081
954PhosphorylationEFQRLPSYRSWRTQH
HHHCCCCHHHHHHCC
16.8126074081
957PhosphorylationRLPSYRSWRTQHIGN
CCCCHHHHHHCCCCC
20.4526074081
967UbiquitinationQHIGNQEENKSKNRN
CCCCCCCCCCCCCCC
67.11-
968PhosphorylationHIGNQEENKSKNRNS
CCCCCCCCCCCCCCC
46.9029978859
973PhosphorylationEENKSKNRNSNVIPY
CCCCCCCCCCCCCCC
29.2729970186
975PhosphorylationNKSKNRNSNVIPYDY
CCCCCCCCCCCCCCC
4.7120166139
978PhosphorylationKNRNSNVIPYDYNRV
CCCCCCCCCCCCCCC
21.6719690332
980PhosphorylationRNSNVIPYDYNRVPL
CCCCCCCCCCCCCCC
10.0628796482
992PhosphorylationVPLKHELEMSKESEH
CCCCCCHHCCCCCCC
24.7220164059
994PhosphorylationLKHELEMSKESEHDS
CCCCHHCCCCCCCCC
54.7923186163
995PhosphorylationKHELEMSKESEHDSD
CCCHHCCCCCCCCCC
43.9226552605
997PhosphorylationELEMSKESEHDSDES
CHHCCCCCCCCCCCC
49.5115302935
999PhosphorylationEMSKESEHDSDESSD
HCCCCCCCCCCCCCC
45.2230576142
1001PhosphorylationSKESEHDSDESSDDD
CCCCCCCCCCCCCCC
56.9710066810
1002PhosphorylationKESEHDSDESSDDDS
CCCCCCCCCCCCCCC
44.0230576142
1003PhosphorylationESEHDSDESSDDDSD
CCCCCCCCCCCCCCC
42.9123911959
1004PhosphorylationSEHDSDESSDDDSDS
CCCCCCCCCCCCCCC
73.3710066810
1005PhosphorylationEHDSDESSDDDSDSE
CCCCCCCCCCCCCCC
60.3010066810
1007PhosphorylationDSDESSDDDSDSEEP
CCCCCCCCCCCCCCH
50.4523401153
1009PhosphorylationDESSDDDSDSEEPSK
CCCCCCCCCCCCHHH
48.0526552605
1013PhosphorylationDDDSDSEEPSKYINA
CCCCCCCCHHHHHCH
41.1725072903
1019PhosphorylationEEPSKYINASFIMSY
CCHHHHHCHHHHHHH
15.7110066810
1058SulfoxidationFQRKVKVIVMLTELK
HHHHCEEEEEEEECC
2.3521406390
1063AcetylationKVIVMLTELKHGDQE
EEEEEEEECCCCCHH
39.0321466224
1089UbiquitinationTYGDIEVDLKDTDKS
EEEEEEEECCCCCCC
54.86-
1093AcetylationIEVDLKDTDKSSTYT
EEEECCCCCCCCEEE
48.69-
1093UbiquitinationIEVDLKDTDKSSTYT
EEEECCCCCCCCEEE
48.69-
1097PhosphorylationLKDTDKSSTYTLRVF
CCCCCCCCEEEEEEE
13.0124719451
1098PhosphorylationKDTDKSSTYTLRVFE
CCCCCCCEEEEEEEE
14.2624719451
1107PhosphorylationTLRVFELRHSKRKDS
EEEEEEEECCCCCCC
27.9327135362
1112PhosphorylationELRHSKRKDSRTVYQ
EEECCCCCCCCEEEE
32.6527135362
1114PhosphorylationRHSKRKDSRTVYQYQ
ECCCCCCCCEEEEEE
27.7624719451
1116PhosphorylationSKRKDSRTVYQYQYT
CCCCCCCEEEEEEEC
10.8224719451
1124PhosphorylationVYQYQYTNWSVEQLP
EEEEEECCCCHHHCC
20.1824719451
1143UbiquitinationELISMIQVVKQKLPQ
HHHHHHHHHHHHCCC
42.74-
1216PhosphorylationPGMVSTFEQYQFLYD
CCCCCHHHHHHHHHH
8.277507203
1220PhosphorylationSTFEQYQFLYDVIAS
CHHHHHHHHHHHHHH
14.95-
1243UbiquitinationVKKNNHQEDKIEFDN
CCCCCCCCCCEECCH
43.30-
1268UbiquitinationCVNPLGAPEKLPEAK
CCCCCCCCCCCHHHH
69.18-
1279PhosphorylationPEAKEQAEGSEPTSG
HHHHHHHCCCCCCCC
31.7230108239
1281PhosphorylationAKEQAEGSEPTSGTE
HHHHHCCCCCCCCCC
33.3027251275
1282PhosphorylationKEQAEGSEPTSGTEG
HHHHCCCCCCCCCCC
35.4229970186
1283PhosphorylationEQAEGSEPTSGTEGP
HHHCCCCCCCCCCCC
55.2030576142
1285PhosphorylationAEGSEPTSGTEGPEH
HCCCCCCCCCCCCCC
37.2230576142
1291PhosphorylationTSGTEGPEHSVNGPA
CCCCCCCCCCCCCCC
18.6730108239
1297PhosphorylationPEHSVNGPASPALNQ
CCCCCCCCCCCCCCC
17.5323401153
1299PhosphorylationHSVNGPASPALNQGS
CCCCCCCCCCCCCCC
19.3619690332
1304PhosphorylationPASPALNQGS-----
CCCCCCCCCC-----
27.5628450419

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
999SPhosphorylationKinaseCSNK2A1P68400
GPS
999SPhosphorylationKinaseCK2-FAMILY-GPS
999SPhosphorylationKinaseCK2_GROUP-PhosphoELM
1002SPhosphorylationKinaseCSNK2A1P68400
GPS
1002SPhosphorylationKinaseCK2-FAMILY-GPS
1002SPhosphorylationKinaseCK2_GROUP-PhosphoELM
1003SPhosphorylationKinaseCSNK2A1P68400
GPS
1003SPhosphorylationKinaseCK2-FAMILY-GPS
1003SPhosphorylationKinaseCK2_GROUP-PhosphoELM
1007SPhosphorylationKinaseCSNK2A1P68400
GPS
1007SPhosphorylationKinasePKC-FAMILY-GPS
1007SPhosphorylationKinasePKC_GROUP-PhosphoELM
1216YPhosphorylationKinaseCSKP41240
PSP
1216YPhosphorylationKinaseLCKP06239
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTPRC_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 PTPRC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAEP_HUMANPAEPphysical
12556471
GANAB_HUMANGANABphysical
9148925
GLU2B_HUMANPRKCSHphysical
9148925
LCK_HUMANLCKphysical
8473339
PTCA_HUMANPTPRCAPphysical
8537410
PLK3_HUMANPLK3physical
11551930
LCK_HUMANLCKphysical
8576115
CD8A_HUMANCD8Aphysical
1834739
CD4_HUMANCD4physical
1834739
GANAB_HUMANGANABphysical
10921916
CD3Z_HUMANCD247physical
7526385
GANAB_HUMANGANABphysical
11564800
LYN_HUMANLYNphysical
7516335
CD79A_HUMANCD79Aphysical
7516335
CD79B_HUMANCD79Bphysical
7516335
SKAP1_HUMANSKAP1physical
11909961

Drug and Disease Associations
Kegg Disease
OMIM Disease
608971Severe combined immunodeficiency autosomal recessive T-cell-negative/B-cell-positive/NK-cell-positive (T(-)B(+)NK(+) SCID)
126200Multiple sclerosis (MS)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PTPRC_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-232; ASN-240; ASN-276;ASN-284; ASN-335; ASN-419; ASN-488 AND ASN-497, AND MASS SPECTROMETRY.
"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-232 AND ASN-335, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 SER-973 AND SER-1297, ANDMASS SPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-995; SER-1003 ANDSER-1007, AND MASS SPECTROMETRY.

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