CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002100
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Receptor-type tyrosine-protein phosphatase C 
Protein Synonyms/Alias
 Leukocyte common antigen; L-CA; T200; CD45 
Gene Name
 Ptprc 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
612DLLLETYKRKIADEGacetylation[1]
639VFSKFPIKDARKSQNacetylation[1]
756VVTINDHKRCPDYIIubiquitination[2]
938IGNQEENKKKNRSSNacetylation[1]
1060GDMEVMLKDTNKSSAacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
Functional 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). 
Sequence Annotation
 DOMAIN 361 449 Fibronectin type-III 1.
 DOMAIN 454 541 Fibronectin type-III 2.
 DOMAIN 622 881 Tyrosine-protein phosphatase 1.
 DOMAIN 913 1196 Tyrosine-protein phosphatase 2.
 REGION 822 828 Substrate binding (By similarity).
 ACT_SITE 822 822 Phosphocysteine intermediate (By
 ACT_SITE 1137 1137 Phosphocysteine intermediate (By
 BINDING 790 790 Substrate (By similarity).
 BINDING 866 866 Substrate (By similarity).
 MOD_RES 922 922 Phosphoserine (By similarity).
 MOD_RES 944 944 Phosphoserine (By similarity).
 MOD_RES 1266 1266 Phosphoserine (By similarity).
 CARBOHYD 62 62 N-linked (GlcNAc...) (Potential).
 CARBOHYD 142 142 N-linked (GlcNAc...) (Potential).
 CARBOHYD 153 153 N-linked (GlcNAc...) (Potential).
 CARBOHYD 164 164 N-linked (GlcNAc...) (Potential).
 CARBOHYD 178 178 N-linked (GlcNAc...) (Potential).
 CARBOHYD 200 200 N-linked (GlcNAc...) (Potential).
 CARBOHYD 245 245 N-linked (GlcNAc...) (Potential).
 CARBOHYD 250 250 N-linked (GlcNAc...) (Potential).
 CARBOHYD 271 271 N-linked (GlcNAc...) (Potential).
 CARBOHYD 282 282 N-linked (GlcNAc...) (Potential).
 CARBOHYD 327 327 N-linked (GlcNAc...) (Potential).
 CARBOHYD 333 333 N-linked (GlcNAc...) (Potential).
 CARBOHYD 371 371 N-linked (GlcNAc...) (Potential).
 CARBOHYD 374 374 N-linked (GlcNAc...) (Potential).
 CARBOHYD 471 471 N-linked (GlcNAc...) (Potential).
 CARBOHYD 502 502 N-linked (GlcNAc...) (Potential).  
Keyword
 Alternative splicing; Complete proteome; Glycoprotein; Hydrolase; Membrane; Phosphoprotein; Protein phosphatase; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1273 AA 
Protein Sequence
MYLWLKLLAF SLALLGPEVF VTGQGTTDDG LDTTEIVLLP QTDPLPARTT EFTPPSISER 60
GNGSSETTYL PGFSSTLMPH LTPQPDSQTP SARGADTQTL SSQADLTTLT AAPSGETDPP 120
GVPEESTVPE TFPGGTPILA RNSTAPSPTH TSNVSTTDIS SGANLTTPAP STLGFASNTT 180
TSTEIATPQT KPSCDEKFGN VTVRYIYDDS SKNFNANLEG DKKPKCEYTD CEKELKNLPE 240
CSQKNVTLSN GSCTPDKIIN LDVPPGTHNF NLTNCTPDIE ANTSICLEWK IKNKFTCDIQ 300
KISYNFRCTP EMKTFALDKH GTLWLHNLTV RTNYTCAAEV LYNNVILLKQ DRRVQTDFGT 360
PEMLPHVQCK NSTNSTTLVS WAEPASKHHG YILCYKKTPS EKCENLANDV NSFEVKNLRP 420
YTEYTVSLFA YVIGRVQRNG PAKDCNFRTK AARPGKVNGM KTSRASDNSI NVTCNSPYEI 480
NGPEARYILE VKSGGSLVKT FNQSTCKFVV DNLYYSTDYE FLVYFYNGEY LGDPEIKPQS 540
TSYNSKALII FLVFLIIVTS IALLVVLYKI YDLRKKRSSN LDEQQELVER DEEKQLINVD 600
PIHSDLLLET YKRKIADEGR LFLAEFQSIP RVFSKFPIKD ARKSQNQNKN RYVDILPYDY 660
NRVELSEING DAGSTYINAS YIDGFKEPRK YIAAQGPRDE TVDDFWKMIW EQKATVIVMV 720
TRCEEGNRNK CAEYWPCMEE GTRTFRDVVV TINDHKRCPD YIIQKLSIAH KKEKATGREV 780
THIQFTSWPD HGVPEDPHLL LKLRRRVNAF SNFFSGPIVV HCSAGVGRTG TYIGIDAMLE 840
SLEAEGKVDV YGYVVNLRRQ RCLMVQVEAQ YILIHQALVE YNQFGETEVN LSELHSCLQN 900
LKKRDPPSDP SPLEAEYQRL PSYRSWRTQH IGNQEENKKK NRSSNVVPYD FNRVPLKHEL 960
EMSKESEAES DESSDEDSDS EETSKYINAS FVMSYWKPEM MIAAQGPLKE TIGDFWQMIF 1020
QRKVKVIVML TELMSGDQEV CAQYWGEGKQ TYGDMEVMLK DTNKSSAYIL RAFELRHSKR 1080
KEPRTVYQYQ CTTWKGEELP AEPKDLVTLI QNIKQKLPKS GSEGMKYHKH ASILVHCRDG 1140
SQQTGLFCAL FNLLESAETE DVVDVFQVVK SLRKARPGMV GSFEQYQFLY DIMASIYPTQ 1200
NGQVKKANSQ DKIEFHNEVD GAKQDANCVQ PADPLNKAQE DSKEVGASEP ASGSEEPEHS 1260
ANGPMSPALT PSS 1273 
Gene Ontology
 GO:0009986; C:cell surface; IDA:RGD.
 GO:0009897; C:external side of plasma membrane; IEA:Compara.
 GO:0005925; C:focal adhesion; ISS:UniProtKB.
 GO:0005887; C:integral to plasma membrane; IDA:UniProtKB.
 GO:0009898; C:internal side of plasma membrane; TAS:RGD.
 GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
 GO:0008201; F:heparin binding; IEA:Compara.
 GO:0019901; F:protein kinase binding; ISS:UniProtKB.
 GO:0019887; F:protein kinase regulator activity; TAS:RGD.
 GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:RGD.
 GO:0000187; P:activation of MAPK activity; IEA:Compara.
 GO:0030183; P:B cell differentiation; IEA:Compara.
 GO:0042100; P:B cell proliferation; ISS:UniProtKB.
 GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB.
 GO:0048539; P:bone marrow development; IEA:Compara.
 GO:0051607; P:defense response to virus; ISS:UniProtKB.
 GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Compara.
 GO:0034113; P:heterotypic cell-cell adhesion; IEA:Compara.
 GO:0002378; P:immunoglobulin biosynthetic process; IEA:Compara.
 GO:0007159; P:leukocyte cell-cell adhesion; IEA:Compara.
 GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; IEA:Compara.
 GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; ISS:UniProtKB.
 GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; IEA:Compara.
 GO:0031953; P:negative regulation of protein autophosphorylation; IEA:Compara.
 GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
 GO:0001915; P:negative regulation of T cell mediated cytotoxicity; ISS:UniProtKB.
 GO:0045060; P:negative thymic T cell selection; IEA:Compara.
 GO:0046641; P:positive regulation of alpha-beta T cell proliferation; IEA:Compara.
 GO:0050857; P:positive regulation of antigen receptor-mediated signaling pathway; ISS:UniProtKB.
 GO:0043065; P:positive regulation of apoptotic process; IEA:Compara.
 GO:0030890; P:positive regulation of B cell proliferation; IEA:Compara.
 GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IEA:Compara.
 GO:2000473; P:positive regulation of hematopoietic stem cell migration; IEA:Compara.
 GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; IEA:Compara.
 GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IEA:Compara.
 GO:2000648; P:positive regulation of stem cell proliferation; IEA:Compara.
 GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IEA:Compara.
 GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
 GO:0045059; P:positive thymic T cell selection; IEA:Compara.
 GO:0045577; P:regulation of B cell differentiation; IEA:Compara.
 GO:0050855; P:regulation of B cell receptor signaling pathway; IEA:Compara.
 GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
 GO:0033261; P:regulation of S phase; IEA:Compara.
 GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
 GO:0010332; P:response to gamma radiation; IDA:RGD.
 GO:0048864; P:stem cell development; IEA:Compara.
 GO:0030217; P:T cell differentiation; ISS:UniProtKB.
 GO:0042098; P:T cell proliferation; IEA:Compara.
 GO:0050852; P:T cell receptor signaling pathway; ISS:UniProtKB. 
Interpro
 IPR003961; Fibronectin_type3.
 IPR013783; Ig-like_fold.
 IPR016335; Leukocyte_common_ag.
 IPR024739; PTP_recept_N.
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS.
 IPR000242; Tyr_Pase_rcpt/non-rcpt. 
Pfam
 PF12567; CD45
 PF00041; fn3
 PF12453; PTP_N
 PF00102; Y_phosphatase 
SMART
 SM00060; FN3
 SM00194; PTPc 
PROSITE
 PS50853; FN3
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50055; TYR_PHOSPHATASE_PTP 
PRINTS
 PR00700; PRTYPHPHTASE.