CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018800
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Receptor-type tyrosine-protein phosphatase U 
Protein Synonyms/Alias
 R-PTP-U; Pancreatic carcinoma phosphatase 2; PCP-2; Protein-tyrosine phosphatase J; PTP-J; hPTP-J; Protein-tyrosine phosphatase pi; PTP pi; Protein-tyrosine phosphatase receptor omicron; PTP-RO; Receptor-type protein-tyrosine phosphatase psi; R-PTP-psi 
Gene Name
 PTPRU 
Gene Synonyms/Alias
 FMI; PCP2; PTPRO 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
283NFAELIVKEPPTPIAubiquitination[1]
440QTIRECVKTEQGVSRubiquitination[2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] 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] 
Functional Description
 Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis. 
Sequence Annotation
 DOMAIN 25 188 MAM.
 DOMAIN 190 275 Ig-like C2-type.
 DOMAIN 285 377 Fibronectin type-III 1.
 DOMAIN 383 481 Fibronectin type-III 2.
 DOMAIN 482 585 Fibronectin type-III 3.
 DOMAIN 592 674 Fibronectin type-III 4.
 DOMAIN 888 1144 Tyrosine-protein phosphatase 1.
 DOMAIN 1176 1439 Tyrosine-protein phosphatase 2.
 REGION 771 887 Mediates interaction with CTNNB1 (By
 REGION 1085 1091 Substrate binding (By similarity).
 ACT_SITE 1085 1085 Phosphocysteine intermediate (By
 ACT_SITE 1380 1380 Phosphocysteine intermediate (By
 BINDING 1053 1053 Substrate (Potential).
 BINDING 1129 1129 Substrate (By similarity).
 MOD_RES 848 848 Phosphoserine.
 MOD_RES 853 853 Phosphoserine.
 CARBOHYD 75 75 N-linked (GlcNAc...) (Potential).
 CARBOHYD 410 410 N-linked (GlcNAc...) (Potential).
 CARBOHYD 685 685 N-linked (GlcNAc...) (Potential).
 DISULFID 210 264 Potential.  
Keyword
 Alternative splicing; Cell adhesion; Cell junction; Cell membrane; Complete proteome; Differentiation; Disulfide bond; Glycoprotein; Hydrolase; Immunoglobulin domain; Membrane; Phosphoprotein; Polymorphism; Protein phosphatase; Receptor; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1446 AA 
Protein Sequence
MARAQALVLA LTFQLCAPET ETPAAGCTFE EASDPAVPCE YSQAQYDDFQ WEQVRIHPGT 60
RAPADLPHGS YLMVNTSQHA PGQRAHVIFQ SLSENDTHCV QFSYFLYSRD GHSPGTLGVY 120
VRVNGGPLGS AVWNMTGSHG RQWHQAELAV STFWPNEYQV LFEALISPDR RGYMGLDDIL 180
LLSYPCAKAP HFSRLGDVEV NAGQNASFQC MAAGRAAEAE RFLLQRQSGA LVPAAGVRHI 240
SHRRFLATFP LAAVSRAEQD LYRCVSQAPR GAGVSNFAEL IVKEPPTPIA PPQLLRAGPT 300
YLIIQLNTNS IIGDGPIVRK EIEYRMARGP WAEVHAVSLQ TYKLWHLDPD TEYEISVLLT 360
RPGDGGTGRP GPPLISRTKC AEPMRAPKGL AFAEIQARQL TLQWEPLGYN VTRCHTYTVS 420
LCYHYTLGSS HNQTIRECVK TEQGVSRYTI KNLLPYRNVH VRLVLTNPEG RKEGKEVTFQ 480
TDEDVPSGIA AESLTFTPLE DMIFLKWEEP QEPNGLITQY EISYQSIESS DPAVNVPGPR 540
RTISKLRNET YHVFSNLHPG TTYLFSVRAR TGKGFGQAAL TEITTNISAP SFDYADMPSP 600
LGESENTITV LLRPAQGRGA PISVYQVIVE EERARRLRRE PGGQDCFPVP LTFEAALARG 660
LVHYFGAELA ASSLPEAMPF TVGDNQTYRG FWNPPLEPRK AYLIYFQAAS HLKGETRLNC 720
IRIARKAACK ESKRPLEVSQ RSEEMGLILG ICAGGLAVLI LLLGAIIVII RKGRDHYAYS 780
YYPKPVNMTK ATVNYRQEKT HMMSAVDRSF TDQSTLQEDE RLGLSFMDTH GYSTRGDQRS 840
GGVTEASSLL GGSPRRPCGR KGSPYHTGQL HPAVRVADLL QHINQMKTAE GYGFKQEYES 900
FFEGWDATKK KDKVKGSRQE PMPAYDRHRV KLHPMLGDPN ADYINANYID GYHRSNHFIA 960
TQGPKPEMVY DFWRMVWQEH CSSIVMITKL VEVGRVKCSR YWPEDSDTYG DIKIMLVKTE 1020
TLAEYVVRTF ALERRGYSAR HEVRQFHFTA WPEHGVPYHA TGLLAFIRRV KASTPPDAGP 1080
IVIHCSAGTG RTGCYIVLDV MLDMAECEGV VDIYNCVKTL CSRRVNMIQT EEQYIFIHDA 1140
ILEACLCGET TIPVSEFKAT YKEMIRIDPQ SNSSQLREEF QTLNSVTPPL DVEECSIALL 1200
PRNRDKNRSM DVLPPDRCLP FLISTDGDSN NYINAALTDS YTRSAAFIVT LHPLQSTTPD 1260
FWRLVYDYGC TSIVMLNQLN QSNSAWPCLQ YWPEPGRQQY GLMEVEFMSG TADEDLVARV 1320
FRVQNISRLQ EGHLLVRHFQ FLRWSAYRDT PDSKKAFLHL LAEVDKWQAE SGDGRTIVHC 1380
LNGGGRSGTF CACATVLEMI RCHNLVDVFF AAKTLRNYKP NMVETMDQYH FCYDVALEYL 1440
EGLESR 1446 
Gene Ontology
 GO:0005911; C:cell-cell junction; IDA:UniProtKB.
 GO:0005887; C:integral to plasma membrane; NAS:UniProtKB.
 GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; NAS:UniProtKB.
 GO:0060070; P:canonical Wnt receptor signaling pathway; IDA:UniProtKB.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0016337; P:cell-cell adhesion; IDA:UniProtKB.
 GO:0034109; P:homotypic cell-cell adhesion; IEA:Compara.
 GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
 GO:0034394; P:protein localization to cell surface; IDA:UniProtKB.
 GO:0007185; P:transmembrane receptor protein tyrosine phosphatase signaling pathway; NAS:UniProtKB. 
Interpro
 IPR008985; ConA-like_lec_gl_sf.
 IPR003961; Fibronectin_type3.
 IPR013783; Ig-like_fold.
 IPR003599; Ig_sub.
 IPR000998; MAM_dom.
 IPR000387; Tyr/Dual-sp_Pase.
 IPR016130; Tyr_Pase_AS.
 IPR000242; Tyr_Pase_rcpt/non-rcpt. 
Pfam
 PF00041; fn3
 PF00629; MAM
 PF00102; Y_phosphatase 
SMART
 SM00060; FN3
 SM00409; IG
 SM00137; MAM
 SM00194; PTPc 
PROSITE
 PS50853; FN3
 PS50835; IG_LIKE
 PS00740; MAM_1
 PS50060; MAM_2
 PS00383; TYR_PHOSPHATASE_1
 PS50056; TYR_PHOSPHATASE_2
 PS50055; TYR_PHOSPHATASE_PTP 
PRINTS
 PR00020; MAMDOMAIN.
 PR00700; PRTYPHPHTASE.