PTPRC_RAT - dbPTM
PTPRC_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTPRC_RAT
UniProt AC P04157
Protein Name Receptor-type tyrosine-protein phosphatase C
Gene Name Ptprc
Organism Rattus norvegicus (Rat).
Sequence Length 1273
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 (By similarity). Dephosphorylates LYN, and thereby modulates LYN activity (By similarity)..
Protein Sequence MYLWLKLLAFSLALLGPEVFVTGQGTTDDGLDTTEIVLLPQTDPLPARTTEFTPPSISERGNGSSETTYLPGFSSTLMPHLTPQPDSQTPSARGADTQTLSSQADLTTLTAAPSGETDPPGVPEESTVPETFPGGTPILARNSTAPSPTHTSNVSTTDISSGANLTTPAPSTLGFASNTTTSTEIATPQTKPSCDEKFGNVTVRYIYDDSSKNFNANLEGDKKPKCEYTDCEKELKNLPECSQKNVTLSNGSCTPDKIINLDVPPGTHNFNLTNCTPDIEANTSICLEWKIKNKFTCDIQKISYNFRCTPEMKTFALDKHGTLWLHNLTVRTNYTCAAEVLYNNVILLKQDRRVQTDFGTPEMLPHVQCKNSTNSTTLVSWAEPASKHHGYILCYKKTPSEKCENLANDVNSFEVKNLRPYTEYTVSLFAYVIGRVQRNGPAKDCNFRTKAARPGKVNGMKTSRASDNSINVTCNSPYEINGPEARYILEVKSGGSLVKTFNQSTCKFVVDNLYYSTDYEFLVYFYNGEYLGDPEIKPQSTSYNSKALIIFLVFLIIVTSIALLVVLYKIYDLRKKRSSNLDEQQELVERDEEKQLINVDPIHSDLLLETYKRKIADEGRLFLAEFQSIPRVFSKFPIKDARKSQNQNKNRYVDILPYDYNRVELSEINGDAGSTYINASYIDGFKEPRKYIAAQGPRDETVDDFWKMIWEQKATVIVMVTRCEEGNRNKCAEYWPCMEEGTRTFRDVVVTINDHKRCPDYIIQKLSIAHKKEKATGREVTHIQFTSWPDHGVPEDPHLLLKLRRRVNAFSNFFSGPIVVHCSAGVGRTGTYIGIDAMLESLEAEGKVDVYGYVVNLRRQRCLMVQVEAQYILIHQALVEYNQFGETEVNLSELHSCLQNLKKRDPPSDPSPLEAEYQRLPSYRSWRTQHIGNQEENKKKNRSSNVVPYDFNRVPLKHELEMSKESEAESDESSDEDSDSEETSKYINASFVMSYWKPEMMIAAQGPLKETIGDFWQMIFQRKVKVIVMLTELMSGDQEVCAQYWGEGKQTYGDMEVMLKDTNKSSAYILRAFELRHSKRKEPRTVYQYQCTTWKGEELPAEPKDLVTLIQNIKQKLPKSGSEGMKYHKHASILVHCRDGSQQTGLFCALFNLLESAETEDVVDVFQVVKSLRKARPGMVGSFEQYQFLYDIMASIYPTQNGQVKKANSQDKIEFHNEVDGAKQDANCVQPADPLNKAQEDSKEVGASEPASGSEEPEHSANGPMSPALTPSS
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
62N-linked_GlycosylationPSISERGNGSSETTY
CCHHHCCCCCCCCCC
54.09-
142N-linked_GlycosylationGTPILARNSTAPSPT
CCEEEEECCCCCCCC
37.80-
153N-linked_GlycosylationPSPTHTSNVSTTDIS
CCCCCCCCCCCCCCC
32.68-
164N-linked_GlycosylationTDISSGANLTTPAPS
CCCCCCCCCCCCCCC
41.25-
178N-linked_GlycosylationSTLGFASNTTTSTEI
CCCCCCCCCCCCCCC
37.71-
200N-linked_GlycosylationSCDEKFGNVTVRYIY
CCCCCCCCEEEEEEE
29.44-
245N-linked_GlycosylationLPECSQKNVTLSNGS
CCHHHCCCEEECCCC
25.11-
250N-linked_GlycosylationQKNVTLSNGSCTPDK
CCCEEECCCCCCCCE
49.89-
271N-linked_GlycosylationPPGTHNFNLTNCTPD
CCCCCCCCCCCCCCC
51.80-
282N-linked_GlycosylationCTPDIEANTSICLEW
CCCCCCCCCEEEEEE
22.90-
327N-linked_GlycosylationHGTLWLHNLTVRTNY
CCEEEEEECEECCCC
34.93-
333N-linked_GlycosylationHNLTVRTNYTCAAEV
EECEECCCCEEHHHH
21.39-
371N-linked_GlycosylationLPHVQCKNSTNSTTL
CCCEEECCCCCCEEE
62.79-
374N-linked_GlycosylationVQCKNSTNSTTLVSW
EEECCCCCCEEEEEE
36.86-
471N-linked_GlycosylationRASDNSINVTCNSPY
CCCCCCEEEEECCCC
23.90-
502N-linked_GlycosylationGSLVKTFNQSTCKFV
CEEEEEECCCCCCEE
39.87-
578PhosphorylationYDLRKKRSSNLDEQQ
HHHHHHHCCCCHHHH
32.2430181290
579PhosphorylationDLRKKRSSNLDEQQE
HHHHHHCCCCHHHHH
45.5030181290
612AcetylationDLLLETYKRKIADEG
HHHHHHHHHHHHHCC
55.4222902405
639AcetylationVFSKFPIKDARKSQN
HHHCCCHHHHHHHCC
45.6422902405
652PhosphorylationQNQNKNRYVDILPYD
CCCCCCCEEEECCCC
16.3322673903
756UbiquitinationVVTINDHKRCPDYII
EEEECCCCCCCHHHH
59.57-
938AcetylationIGNQEENKKKNRSSN
CCCHHHHCCCCCCCC
69.2922902405
943PhosphorylationENKKKNRSSNVVPYD
HHCCCCCCCCCCCCC
35.3426437020
944PhosphorylationNKKKNRSSNVVPYDF
HCCCCCCCCCCCCCC
30.3329779826
949PhosphorylationRSSNVVPYDFNRVPL
CCCCCCCCCCCCCCC
22.8928689409
963PhosphorylationLKHELEMSKESEAES
CCHHHHHCCCCCCCC
24.7225532521
966PhosphorylationELEMSKESEAESDES
HHHHCCCCCCCCCCC
45.9322673903
970PhosphorylationSKESEAESDESSDED
CCCCCCCCCCCCCCC
54.4422673903
973PhosphorylationSEAESDESSDEDSDS
CCCCCCCCCCCCCCC
48.3422673903
974PhosphorylationEAESDESSDEDSDSE
CCCCCCCCCCCCCCH
42.8622673903
978PhosphorylationDESSDEDSDSEETSK
CCCCCCCCCCHHHHH
40.7722673903
980PhosphorylationSSDEDSDSEETSKYI
CCCCCCCCHHHHHHH
41.0822673903
1060AcetylationGDMEVMLKDTNKSSA
CCEEEEEECCCHHHH
44.4022902405
1209PhosphorylationGQVKKANSQDKIEFH
CCEEECCCCCCEEEE
44.6129779826
1248PhosphorylationDSKEVGASEPASGSE
HHCCCCCCCCCCCCC
37.8822673903
1252PhosphorylationVGASEPASGSEEPEH
CCCCCCCCCCCCCCC
54.2722673903
1254PhosphorylationASEPASGSEEPEHSA
CCCCCCCCCCCCCCC
35.9722673903
1260PhosphorylationGSEEPEHSANGPMSP
CCCCCCCCCCCCCCC
23.0522673903
1266PhosphorylationHSANGPMSPALTPSS
CCCCCCCCCCCCCCC
15.3422673903
1270PhosphorylationGPMSPALTPSS----
CCCCCCCCCCC----
24.1922673903
1272PhosphorylationMSPALTPSS------
CCCCCCCCC------
43.3722673903
1273PhosphorylationSPALTPSS-------
CCCCCCCC-------
45.5022673903

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 PTPRC_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTPRC_RAT !!

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PTPRC_RAT !!

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

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Related Literatures of Post-Translational Modification

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