CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002678
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
 CD45 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
314HDCTQVEKADTTICLubiquitination[1]
322ADTTICLKWKNIETFubiquitination[1]
324TTICLKWKNIETFTCubiquitination[1]
350GNMIFDNKEIKLENLubiquitination[1]
364LEPEHEYKCDSEILYubiquitination[1]
381HKFTNASKIIKTDFGubiquitination[1]
384TNASKIIKTDFGSPGubiquitination[1]
437KDCLNLDKNLIKYDLacetylation[2]
437KDCLNLDKNLIKYDLubiquitination[1]
540KNCDFRVKDLQYSTDubiquitination[1]
641DILLETYKRKIADEGubiquitination[1]
664SIPRVFSKFPIKEARubiquitination[1, 3, 4, 5]
668VFSKFPIKEARKPFNubiquitination[1]
715ASYIDGFKEPRKYIAubiquitination[1, 4]
719DGFKEPRKYIAAQGPubiquitination[1]
759CEEGNRNKCAEYWPSubiquitination[1]
780AFGDVVVKINQHKRCubiquitination[1]
801KLNIVNKKEKATGREubiquitination[1]
831EDPHLLLKLRRRVNAubiquitination[1]
932PYLHNMKKRDPPSEPubiquitination[1]
1089GDIEVDLKDTDKSSTubiquitination[1]
1093VDLKDTDKSSTYTLRubiquitination[1]
1143ISMIQVVKQKLPQKNubiquitination[1]
1268NPLGAPEKLPEAKEQubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 
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. Dephosphorylates LYN, and thereby modulates LYN activity (By similarity). 
Sequence Annotation
 DOMAIN 390 478 Fibronectin type-III 1.
 DOMAIN 482 570 Fibronectin type-III 2.
 DOMAIN 651 910 Tyrosine-protein phosphatase 1.
 DOMAIN 942 1226 Tyrosine-protein phosphatase 2.
 REGION 851 857 Substrate binding (By similarity).
 ACT_SITE 851 851 Phosphocysteine intermediate.
 ACT_SITE 1167 1167 Phosphocysteine intermediate (By
 BINDING 819 819 Substrate (By similarity).
 BINDING 895 895 Substrate (By similarity).
 MOD_RES 951 951 Phosphoserine (By similarity).
 MOD_RES 973 973 Phosphoserine.
 MOD_RES 1297 1297 Phosphoserine.
 CARBOHYD 78 78 N-linked (GlcNAc...) (Potential).
 CARBOHYD 90 90 N-linked (GlcNAc...) (Potential).
 CARBOHYD 95 95 N-linked (GlcNAc...) (Potential).
 CARBOHYD 184 184 N-linked (GlcNAc...) (Potential).
 CARBOHYD 190 190 N-linked (GlcNAc...) (Potential).
 CARBOHYD 197 197 N-linked (GlcNAc...) (Potential).
 CARBOHYD 232 232 N-linked (GlcNAc...).
 CARBOHYD 240 240 N-linked (GlcNAc...); atypical.
 CARBOHYD 260 260 N-linked (GlcNAc...) (Potential).
 CARBOHYD 270 270 N-linked (GlcNAc...) (Potential).
 CARBOHYD 276 276 N-linked (GlcNAc...).
 CARBOHYD 284 284 N-linked (GlcNAc...); atypical.
 CARBOHYD 335 335 N-linked (GlcNAc...).
 CARBOHYD 378 378 N-linked (GlcNAc...) (Potential).
 CARBOHYD 419 419 N-linked (GlcNAc...).
 CARBOHYD 468 468 N-linked (GlcNAc...) (Potential).
 CARBOHYD 488 488 N-linked (GlcNAc...).
 CARBOHYD 497 497 N-linked (GlcNAc...); atypical.
 CARBOHYD 529 529 N-linked (GlcNAc...) (Potential).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Disease mutation; Glycoprotein; Hydrolase; Membrane; Phosphoprotein; Polymorphism; Protein phosphatase; Reference proteome; Repeat; SCID; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1304 AA 
Protein Sequence
MYLWLKLLAF GFAFLDTEVF VTGQSPTPSP TGLTTAKMPS VPLSSDPLPT HTTAFSPAST 60
FERENDFSET TTSLSPDNTS TQVSPDSLDN ASAFNTTGVS SVQTPHLPTH ADSQTPSAGT 120
DTQTFSGSAA NAKLNPTPGS NAISDVPGER STASTFPTDP VSPLTTTLSL AHHSSAALPA 180
RTSNTTITAN TSDAYLNASE TTTLSPSGSA VISTTTIATT PSKPTCDEKY ANITVDYLYN 240
KETKLFTAKL NVNENVECGN NTCTNNEVHN LTECKNASVS ISHNSCTAPD KTLILDVPPG 300
VEKFQLHDCT QVEKADTTIC LKWKNIETFT CDTQNITYRF QCGNMIFDNK EIKLENLEPE 360
HEYKCDSEIL YNNHKFTNAS KIIKTDFGSP GEPQIIFCRS EAAHQGVITW NPPQRSFHNF 420
TLCYIKETEK DCLNLDKNLI KYDLQNLKPY TKYVLSLHAY IIAKVQRNGS AAMCHFTTKS 480
APPSQVWNMT VSMTSDNSMH VKCRPPRDRN GPHERYHLEV EAGNTLVRNE SHKNCDFRVK 540
DLQYSTDYTF KAYFHNGDYP GEPFILHHST SYNSKALIAF LAFLIIVTSI ALLVVLYKIY 600
DLHKKRSCNL DEQQELVERD DEKQLMNVEP IHADILLETY KRKIADEGRL FLAEFQSIPR 660
VFSKFPIKEA RKPFNQNKNR YVDILPYDYN RVELSEINGD AGSNYINASY IDGFKEPRKY 720
IAAQGPRDET VDDFWRMIWE QKATVIVMVT RCEEGNRNKC AEYWPSMEEG TRAFGDVVVK 780
INQHKRCPDY IIQKLNIVNK KEKATGREVT HIQFTSWPDH GVPEDPHLLL KLRRRVNAFS 840
NFFSGPIVVH CSAGVGRTGT YIGIDAMLEG LEAENKVDVY GYVVKLRRQR CLMVQVEAQY 900
ILIHQALVEY NQFGETEVNL SELHPYLHNM KKRDPPSEPS PLEAEFQRLP SYRSWRTQHI 960
GNQEENKSKN RNSNVIPYDY NRVPLKHELE MSKESEHDSD ESSDDDSDSE EPSKYINASF 1020
IMSYWKPEVM IAAQGPLKET IGDFWQMIFQ RKVKVIVMLT ELKHGDQEIC AQYWGEGKQT 1080
YGDIEVDLKD TDKSSTYTLR VFELRHSKRK DSRTVYQYQY TNWSVEQLPA EPKELISMIQ 1140
VVKQKLPQKN SSEGNKHHKS TPLLIHCRDG SQQTGIFCAL LNLLESAETE EVVDIFQVVK 1200
ALRKARPGMV STFEQYQFLY DVIASTYPAQ NGQVKKNNHQ EDKIEFDNEV DKVKQDANCV 1260
NPLGAPEKLP EAKEQAEGSE PTSGTEGPEH SVNGPASPAL NQGS 1304 
Gene Ontology
 GO:0009897; C:external side of plasma membrane; IDA:MGI.
 GO:0005925; C:focal adhesion; ISS:UniProtKB.
 GO:0005887; C:integral to plasma membrane; ISS:UniProtKB.
 GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
 GO:0008201; F:heparin binding; IEA:Compara.
 GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
 GO:0000187; P:activation of MAPK activity; IEA:Compara.
 GO:0007411; P:axon guidance; TAS:Reactome.
 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; IMP:UniProtKB.
 GO:0051607; P:defense response to virus; ISS:UniProtKB.
 GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:UniProtKB.
 GO:0034113; P:heterotypic cell-cell adhesion; IEA:Compara.
 GO:0002378; P:immunoglobulin biosynthetic process; IMP:UniProtKB.
 GO:0007159; P:leukocyte cell-cell adhesion; IEA:Compara.
 GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; IMP:UniProtKB.
 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; IDA: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; IMP:UniProtKB.
 GO:0045588; P:positive regulation of gamma-delta T cell differentiation; IEA:Compara.
 GO:2000473; P:positive regulation of hematopoietic stem cell migration; IMP:UniProtKB.
 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:0045860; P:positive regulation of protein kinase activity; NAS:UniProtKB.
 GO:2000648; P:positive regulation of stem cell proliferation; IMP:UniProtKB.
 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:0033261; P:regulation of S phase; IMP:UniProtKB.
 GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
 GO:0010332; P:response to gamma radiation; IEA:Compara.
 GO:0048864; P:stem cell development; IMP:UniProtKB.
 GO:0030217; P:T cell differentiation; ISS:UniProtKB.
 GO:0042098; P:T cell proliferation; IEA:Compara.
 GO:0050852; P:T cell receptor signaling pathway; IDA: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.