CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011947
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Receptor-type tyrosine-protein phosphatase eta 
Protein Synonyms/Alias
 Protein-tyrosine phosphatase eta; R-PTP-eta; Density-enhanced phosphatase 1; DEP-1; HPTP eta; Protein-tyrosine phosphatase receptor type J; R-PTP-J; CD148 
Gene Name
 PTPRJ 
Gene Synonyms/Alias
 DEP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1031ENFEAYFKKQQADSNubiquitination[1, 2]
1057LVGISQPKYAAELAEubiquitination[3]
Reference
 [1] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [2] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [3] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, RET (variant MEN2A), KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2. Plays a role in cell adhesion, migration, proliferation and differentiation. Involved in vascular development. Regulator of macrophage adhesion and spreading. Positively affects cell-matrix adhesion. Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation. Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR. Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation. Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation. Enhances the barrier function of epithelial junctions during reassembly. Negatively regulates T-cell receptor (TCR) signaling. Upon T-cell TCR activation, it is up-regulated and excluded from the immunological synapses, while upon T-cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling. 
Sequence Annotation
 DOMAIN 119 205 Fibronectin type-III 1.
 DOMAIN 207 291 Fibronectin type-III 2.
 DOMAIN 271 364 Fibronectin type-III 3.
 DOMAIN 365 452 Fibronectin type-III 4.
 DOMAIN 453 538 Fibronectin type-III 5.
 DOMAIN 540 620 Fibronectin type-III 6.
 DOMAIN 622 717 Fibronectin type-III 7.
 DOMAIN 720 811 Fibronectin type-III 8.
 DOMAIN 816 902 Fibronectin type-III 9.
 DOMAIN 1041 1298 Tyrosine-protein phosphatase.
 REGION 1239 1245 Substrate binding (By similarity).
 ACT_SITE 1239 1239 Phosphocysteine intermediate (By
 BINDING 1205 1205 Substrate (By similarity).
 BINDING 1283 1283 Substrate (By similarity).
 MOD_RES 1011 1011 Phosphoserine (By similarity).
 CARBOHYD 72 72 N-linked (GlcNAc...) (Potential).
 CARBOHYD 82 82 N-linked (GlcNAc...) (Potential).
 CARBOHYD 93 93 N-linked (GlcNAc...) (Potential).
 CARBOHYD 104 104 N-linked (GlcNAc...) (Potential).
 CARBOHYD 142 142 N-linked (GlcNAc...) (Potential).
 CARBOHYD 172 172 N-linked (GlcNAc...) (Potential).
 CARBOHYD 192 192 N-linked (GlcNAc...) (Potential).
 CARBOHYD 231 231 N-linked (GlcNAc...) (Potential).
 CARBOHYD 258 258 N-linked (GlcNAc...) (Potential).
 CARBOHYD 278 278 N-linked (GlcNAc...) (Potential).
 CARBOHYD 342 342 N-linked (GlcNAc...).
 CARBOHYD 351 351 N-linked (GlcNAc...).
 CARBOHYD 376 376 N-linked (GlcNAc...) (Potential).
 CARBOHYD 391 391 N-linked (GlcNAc...).
 CARBOHYD 396 396 N-linked (GlcNAc...).
 CARBOHYD 413 413 N-linked (GlcNAc...).
 CARBOHYD 431 431 N-linked (GlcNAc...) (Potential).
 CARBOHYD 501 501 N-linked (GlcNAc...) (Potential).
 CARBOHYD 525 525 N-linked (GlcNAc...) (Potential).
 CARBOHYD 536 536 N-linked (GlcNAc...) (Potential).
 CARBOHYD 582 582 N-linked (GlcNAc...) (Potential).
 CARBOHYD 603 603 N-linked (GlcNAc...) (Potential).
 CARBOHYD 618 618 N-linked (GlcNAc...) (Potential).
 CARBOHYD 628 628 N-linked (GlcNAc...) (Potential).
 CARBOHYD 637 637 N-linked (GlcNAc...) (Potential).
 CARBOHYD 666 666 N-linked (GlcNAc...) (Potential).
 CARBOHYD 669 669 N-linked (GlcNAc...) (Potential).
 CARBOHYD 761 761 N-linked (GlcNAc...) (Potential).
 CARBOHYD 772 772 N-linked (GlcNAc...) (Potential).
 CARBOHYD 784 784 N-linked (GlcNAc...) (Potential).
 CARBOHYD 790 790 N-linked (GlcNAc...) (Potential).
 CARBOHYD 824 824 N-linked (GlcNAc...) (Potential).
 CARBOHYD 910 910 N-linked (GlcNAc...) (Potential).
 CARBOHYD 937 937 N-linked (GlcNAc...).  
Keyword
 3D-structure; Alternative splicing; Cell junction; Cell membrane; Cell projection; Complete proteome; Direct protein sequencing; Glycoprotein; Hydrolase; Membrane; Phosphoprotein; Polymorphism; Protein phosphatase; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1337 AA 
Protein Sequence
MKPAAREARL PPRSPGLRWA LPLLLLLLRL GQILCAGGTP SPIPDPSVAT VATGENGITQ 60
ISSTAESFHK QNGTGTPQVE TNTSEDGESS GANDSLRTPE QGSNGTDGAS QKTPSSTGPS 120
PVFDIKAVSI SPTNVILTWK SNDTAASEYK YVVKHKMENE KTITVVHQPW CNITGLRPAT 180
SYVFSITPGI GNETWGDPRV IKVITEPIPV SDLRVALTGV RKAALSWSNG NGTASCRVLL 240
ESIGSHEELT QDSRLQVNIS GLKPGVQYNI NPYLLQSNKT KGDPLGTEGG LDASNTERSR 300
AGSPTAPVHD ESLVGPVDPS SGQQSRDTEV LLVGLEPGTR YNATVYSQAA NGTEGQPQAI 360
EFRTNAIQVF DVTAVNISAT SLTLIWKVSD NESSSNYTYK IHVAGETDSS NLNVSEPRAV 420
IPGLRSSTFY NITVCPVLGD IEGTPGFLQV HTPPVPVSDF RVTVVSTTEI GLAWSSHDAE 480
SFQMHITQEG AGNSRVEITT NQSIIIGGLF PGTKYCFEIV PKGPNGTEGA SRTVCNRTVP 540
SAVFDIHVVY VTTTEMWLDW KSPDGASEYV YHLVIESKHG SNHTSTYDKA ITLQGLIPGT 600
LYNITISPEV DHVWGDPNST AQYTRPSNVS NIDVSTNTTA ATLSWQNFDD ASPTYSYCLL 660
IEKAGNSSNA TQVVTDIGIT DATVTELIPG SSYTVEIFAQ VGDGIKSLEP GRKSFCTDPA 720
SMASFDCEVV PKEPALVLKW TCPPGANAGF ELEVSSGAWN NATHLESCSS ENGTEYRTEV 780
TYLNFSTSYN ISITTVSCGK MAAPTRNTCT TGITDPPPPD GSPNITSVSH NSVKVKFSGF 840
EASHGPIKAY AVILTTGEAG HPSADVLKYT YEDFKKGASD TYVTYLIRTE EKGRSQSLSE 900
VLKYEIDVGN ESTTLGYYNG KLEPLGSYRA CVAGFTNITF HPQNKGLIDG AESYVSFSRY 960
SDAVSLPQDP GVICGAVFGC IFGALVIVTV GGFIFWRKKR KDAKNNEVSF SQIKPKKSKL 1020
IRVENFEAYF KKQQADSNCG FAEEYEDLKL VGISQPKYAA ELAENRGKNR YNNVLPYDIS 1080
RVKLSVQTHS TDDYINANYM PGYHSKKDFI ATQGPLPNTL KDFWRMVWEK NVYAIIMLTK 1140
CVEQGRTKCE EYWPSKQAQD YGDITVAMTS EIVLPEWTIR DFTVKNIQTS ESHPLRQFHF 1200
TSWPDHGVPD TTDLLINFRY LVRDYMKQSP PESPILVHCS AGVGRTGTFI AIDRLIYQIE 1260
NENTVDVYGI VYDLRMHRPL MVQTEDQYVF LNQCVLDIVR SQKDSKVDLI YQNTTAMTIY 1320
ENLAPVTTFG KTNGYIA 1337 
Gene Ontology
 GO:0009986; C:cell surface; IDA:UniProtKB.
 GO:0005911; C:cell-cell junction; IDA:UniProtKB.
 GO:0001772; C:immunological synapse; IDA:UniProtKB.
 GO:0005887; C:integral to plasma membrane; TAS:ProtInc.
 GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
 GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
 GO:0007596; P:blood coagulation; IEA:Compara.
 GO:0060242; P:contact inhibition; NAS:UniProtKB.
 GO:0007507; P:heart development; IEA:Compara.
 GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
 GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
 GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
 GO:0043407; P:negative regulation of MAP kinase activity; IDA:UniProtKB.
 GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IDA:UniProtKB.
 GO:0051898; P:negative regulation of protein kinase B signaling cascade; IMP:UniProtKB.
 GO:2000272; P:negative regulation of receptor activity; IEA:Compara.
 GO:0050860; P:negative regulation of T cell receptor signaling pathway; IDA:UniProtKB.
 GO:0043116; P:negative regulation of vascular permeability; IDA:UniProtKB.
 GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:UniProtKB.
 GO:0050918; P:positive chemotaxis; IDA:UniProtKB.
 GO:0051894; P:positive regulation of focal adhesion assembly; IMP:UniProtKB.
 GO:0010759; P:positive regulation of macrophage chemotaxis; IEA:Compara.
 GO:0010572; P:positive regulation of platelet activation; IEA:Compara.
 GO:0051897; P:positive regulation of protein kinase B signaling cascade; IMP:UniProtKB.
 GO:0001570; P:vasculogenesis; IEA:Compara. 
Interpro
 IPR003961; Fibronectin_type3.
 IPR013783; Ig-like_fold.
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS.
 IPR000242; Tyr_Pase_rcpt/non-rcpt. 
Pfam
 PF00041; fn3
 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.