ID PTPRJ_HUMAN Reviewed; 1337 AA. AC Q12913; Q15255; Q8NHM2; Q9UDA9; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 3. DT 19-JAN-2010, entry version 104. DE RecName: Full=Receptor-type tyrosine-protein phosphatase eta; DE Short=Protein-tyrosine phosphatase eta; DE Short=R-PTP-eta; DE EC=3.1.3.48; DE AltName: Full=HPTP eta; DE AltName: Full=Protein-tyrosine phosphatase receptor type J; DE AltName: Full=Density-enhanced phosphatase 1; DE Short=DEP-1; DE AltName: CD_antigen=CD148; DE Flags: Precursor; GN Name=PTPRJ; Synonyms=DEP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-872. RX MEDLINE=95024024; PubMed=7937872; DOI=10.1073/pnas.91.21.9680; RA Oestman A., Yang Q., Tonks N.K.; RT "Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is RT enhanced with increasing cell density."; RL Proc. Natl. Acad. Sci. U.S.A. 91:9680-9684(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASP-872. RX MEDLINE=95086212; PubMed=7994032; RA Honda H., Inazawa J., Nishida J., Yazaki Y., Hirai H.; RT "Molecular cloning, characterization, and chromosomal localization of RT a novel protein-tyrosine phosphatase, HPTP eta."; RL Blood 84:4186-4194(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., RA Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., RA FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S., RA Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., RA Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., RA Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-1337, VARIANTS COLON CANCER RP CYS-214 AND PRO-276, AND VARIANT ASP-872. RC TISSUE=Colon; RX MEDLINE=22084388; PubMed=12089527; DOI=10.1038/ng903; RA Ruivenkamp C.A.L., van Wezel T., Zanon C., Stassen A.P.M., Vlcek C., RA Csikos T., Klous A.M., Tripodis N., Perrakis A., Boerrigter L., RA Groot P.C., Lindeman J., Mooi W.J., Meijjer G.A., Scholten G., RA Dauwerse H., Paces V., van Zandwijk N., van Ommen G.J.B., Demant P.; RT "Ptprj is a candidate for the mouse colon-cancer susceptibility locus RT Scc1 and is frequently deleted in human cancers."; RL Nat. Genet. 31:295-300(2002). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1124-1245, AND TISSUE SPECIFICITY. RC TISSUE=Leukemia; RX MEDLINE=93247293; PubMed=8483328; RA Honda H., Shibuya M., Chiba S., Yazaki Y., Hirai H.; RT "Identification of novel protein-tyrosine phosphatases in a human RT leukemia cell line, F-36P."; RL Leukemia 7:742-746(1993). RN [6] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-342; ASN-351; ASN-391 AND RP ASN-396, AND MASS SPECTROMETRY. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [7] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-413 AND ASN-937, AND MASS RP SPECTROMETRY. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [8] RP STRUCTURE BY NMR OF 366-456. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the fourth FN3 domain of human receptor-type RT tyrosine-protein phosphatase eta."; RL Submitted (OCT-2006) to the PDB data bank. CC -!- FUNCTION: May contribute to the mechanism of contact inhibition of CC cell growth. CC -!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein CC tyrosine + phosphate. CC -!- INTERACTION: CC Q9UM73:ALK; NbExp=1; IntAct=EBI-2264500, EBI-357361; CC P22681:CBL; NbExp=1; IntAct=EBI-2264500, EBI-518228; CC P19022:CDH2; NbExp=1; IntAct=EBI-2264500, EBI-2256711; CC P41240:CSK; NbExp=1; IntAct=EBI-2264500, EBI-1380630; CC P35222:CTNNB1; NbExp=1; IntAct=EBI-2264500, EBI-491549; CC P00533:EGFR; NbExp=1; IntAct=EBI-2264500, EBI-297353; CC P19235:EPOR; NbExp=1; IntAct=EBI-2264500, EBI-617321; CC P04626:ERBB2; NbExp=1; IntAct=EBI-2264500, EBI-641062; CC Q13480:GAB1; NbExp=1; IntAct=EBI-2264500, EBI-517684; CC P10912:GHR; NbExp=1; IntAct=EBI-2264500, EBI-286316; CC Q13224:GRIN2B; NbExp=1; IntAct=EBI-2264500, EBI-2256942; CC P06213:INSR; NbExp=1; IntAct=EBI-2264500, EBI-475899; CC O60674:JAK2; NbExp=1; IntAct=EBI-2264500, EBI-518647; CC P10721:KIT; NbExp=1; IntAct=EBI-2264500, EBI-1379503; CC P06239:LCK; NbExp=1; IntAct=EBI-2264500, EBI-1348; CC P48357:LEPR; NbExp=1; IntAct=EBI-2264500, EBI-518596; CC P48356:Lepr (xeno); NbExp=1; IntAct=EBI-2264500, EBI-2257257; CC P27361:MAPK3; NbExp=1; IntAct=EBI-2264500, EBI-73995; CC P08581:MET; NbExp=1; IntAct=EBI-2264500, EBI-1039152; CC P46459:NSF; NbExp=1; IntAct=EBI-2264500, EBI-712251; CC P04629:NTRK1; NbExp=1; IntAct=EBI-2264500, EBI-1028226; CC P09619:PDGFRB; NbExp=1; IntAct=EBI-2264500, EBI-641237; CC O15530:PDPK1; NbExp=1; IntAct=EBI-2264500, EBI-717097; CC Q99569:PKP4; NbExp=1; IntAct=EBI-2264500, EBI-726447; CC O14974:PPP1R12A; NbExp=1; IntAct=EBI-2264500, EBI-351726; CC P49023:PXN; NbExp=1; IntAct=EBI-2264500, EBI-702209; CC P42680:TEC; NbExp=1; IntAct=EBI-2264500, EBI-1383480; CC Q02763:TEK; NbExp=1; IntAct=EBI-2264500, EBI-2257090; CC P35590:TIE1; NbExp=1; IntAct=EBI-2264500, EBI-2256865; CC Q07912:TNK2; NbExp=1; IntAct=EBI-2264500, EBI-603457; CC P42768:WAS; NbExp=1; IntAct=EBI-2264500, EBI-346375; CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- TISSUE SPECIFICITY: Expressed in the promyelocytic cell line HL60, CC the granulocyte-macrophage colony-stimulating factor-dependent CC leukemic cell line F-36P, and the interleukin-3 and CC erythropoietin-dependent leukemic cell line F-36E. CC -!- PTM: N- and O-glycosylated. CC -!- DISEASE: Defects in PTPRJ are found in cancers of colon, lung, and CC breast. CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. CC Receptor class 3 subfamily. CC -!- SIMILARITY: Contains 9 fibronectin type-III domains. CC -!- SIMILARITY: Contains 1 tyrosine-protein phosphatase domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U10886; AAB36687.1; -; mRNA. DR EMBL; D37781; BAA07035.1; -; mRNA. DR EMBL; AC103828; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC026975; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF387844; AAM69432.1; -; Genomic_DNA. DR EMBL; AF387823; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387824; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387825; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387826; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387827; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387828; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387829; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387830; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387831; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387832; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387833; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387834; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387835; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387836; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387837; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387838; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387839; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387840; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387841; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387842; AAM69432.1; JOINED; Genomic_DNA. DR EMBL; AF387843; AAM69432.1; JOINED; Genomic_DNA. DR IPI; IPI00290328; -. DR PIR; I38670; I38670. DR RefSeq; NP_002834.3; -. DR UniGene; Hs.318547; -. DR PDB; 2CFV; X-ray; 2.50 A; A=1019-1311. DR PDB; 2DLE; NMR; -; A=366-456. DR PDB; 2NZ6; X-ray; 2.30 A; A=1019-1311. DR PDBsum; 2CFV; -. DR PDBsum; 2DLE; -. DR PDBsum; 2NZ6; -. DR SMR; Q12913; 330-615, 591-704, 777-853. DR IntAct; Q12913; 31. DR STRING; Q12913; -. DR PhosphoSite; Q12913; -. DR PRIDE; Q12913; -. DR Ensembl; ENST00000418331; ENSP00000400010; ENSG00000149177; Homo sapiens. DR GeneID; 5795; -. DR UCSC; uc001ngp.2; human. DR CTD; 5795; -. DR GeneCards; GC11P047958; -. DR H-InvDB; HIX0035923; -. DR HGNC; HGNC:9673; PTPRJ. DR HPA; HPA006026; -. DR MIM; 600925; gene. DR PharmGKB; PA34018; -. DR eggNOG; prNOG07391; -. DR HOGENOM; HBG282919; -. DR HOVERGEN; Q12913; -. DR InParanoid; Q12913; -. DR OMA; YTYEDFK; -. DR OrthoDB; EOG9DNHQ0; -. DR PhylomeDB; Q12913; -. DR BRENDA; 3.1.3.48; 247. DR Pathway_Interaction_DB; pdgfrbpathway; PDGFR-beta signaling pathway. DR Pathway_Interaction_DB; met_pathway; Signaling events activated by Hepatocyte Growth Factor Receptor (c-Met). DR NextBio; 22564; -. DR ArrayExpress; Q12913; -. DR Bgee; Q12913; -. DR CleanEx; HS_PTPRJ; -. DR Genevestigator; Q12913; -. DR GermOnline; ENSG00000149177; Homo sapiens. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0005887; C:integral to plasma membrane; TAS:ProtInc. DR GO; GO:0005634; C:nucleus; IDA:HPA. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0005001; F:transmembrane receptor protein tyrosine pho...; TAS:ProtInc. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0006470; P:protein amino acid dephosphorylation; TAS:ProtInc. DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kin...; TAS:ProtInc. DR InterPro; IPR000387; Dual-sp/Tyr_phosphatase. DR InterPro; IPR008957; Fibronectin_typ-III-like_fold. DR InterPro; IPR003961; FN_III. DR InterPro; IPR016130; Tyr_Pase_AS. DR InterPro; IPR000242; Tyr_Pase_rcpt/non-rcpt. DR Gene3D; G3DSA:2.60.40.30; FN_III-like; 4. DR Pfam; PF00041; fn3; 4. DR Pfam; PF00102; Y_phosphatase; 1. DR PRINTS; PR00700; PRTYPHPHTASE. DR SMART; SM00060; FN3; 8. DR SMART; SM00194; PTPc; 1. DR PROSITE; PS50853; FN3; 9. DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Disease mutation; Glycoprotein; KW Hydrolase; Membrane; Phosphoprotein; Polymorphism; KW Protein phosphatase; Repeat; Signal; Transmembrane. FT SIGNAL 1 35 Potential. FT CHAIN 36 1337 Receptor-type tyrosine-protein FT phosphatase eta. FT /FTId=PRO_0000025444. FT TOPO_DOM 36 975 Extracellular (Potential). FT TRANSMEM 976 996 Potential. FT TOPO_DOM 997 1337 Cytoplasmic (Potential). FT DOMAIN 119 205 Fibronectin type-III 1. FT DOMAIN 207 291 Fibronectin type-III 2. FT DOMAIN 271 364 Fibronectin type-III 3. FT DOMAIN 365 452 Fibronectin type-III 4. FT DOMAIN 453 538 Fibronectin type-III 5. FT DOMAIN 540 620 Fibronectin type-III 6. FT DOMAIN 622 717 Fibronectin type-III 7. FT DOMAIN 720 811 Fibronectin type-III 8. FT DOMAIN 816 902 Fibronectin type-III 9. FT DOMAIN 1041 1298 Tyrosine-protein phosphatase. FT ACT_SITE 1239 1239 Phosphocysteine intermediate (By FT similarity). FT MOD_RES 1011 1011 Phosphoserine (By similarity). FT CARBOHYD 72 72 N-linked (GlcNAc...) (Potential). FT CARBOHYD 82 82 N-linked (GlcNAc...) (Potential). FT CARBOHYD 93 93 N-linked (GlcNAc...) (Potential). FT CARBOHYD 104 104 N-linked (GlcNAc...) (Potential). FT CARBOHYD 142 142 N-linked (GlcNAc...) (Potential). FT CARBOHYD 172 172 N-linked (GlcNAc...) (Potential). FT CARBOHYD 192 192 N-linked (GlcNAc...) (Potential). FT CARBOHYD 231 231 N-linked (GlcNAc...) (Potential). FT CARBOHYD 258 258 N-linked (GlcNAc...) (Potential). FT CARBOHYD 278 278 N-linked (GlcNAc...) (Potential). FT CARBOHYD 342 342 N-linked (GlcNAc...). FT CARBOHYD 351 351 N-linked (GlcNAc...). FT CARBOHYD 376 376 N-linked (GlcNAc...) (Potential). FT CARBOHYD 391 391 N-linked (GlcNAc...). FT CARBOHYD 396 396 N-linked (GlcNAc...). FT CARBOHYD 413 413 N-linked (GlcNAc...). FT CARBOHYD 431 431 N-linked (GlcNAc...) (Potential). FT CARBOHYD 501 501 N-linked (GlcNAc...) (Potential). FT CARBOHYD 525 525 N-linked (GlcNAc...) (Potential). FT CARBOHYD 536 536 N-linked (GlcNAc...) (Potential). FT CARBOHYD 582 582 N-linked (GlcNAc...) (Potential). FT CARBOHYD 603 603 N-linked (GlcNAc...) (Potential). FT CARBOHYD 618 618 N-linked (GlcNAc...) (Potential). FT CARBOHYD 628 628 N-linked (GlcNAc...) (Potential). FT CARBOHYD 637 637 N-linked (GlcNAc...) (Potential). FT CARBOHYD 666 666 N-linked (GlcNAc...) (Potential). FT CARBOHYD 669 669 N-linked (GlcNAc...) (Potential). FT CARBOHYD 761 761 N-linked (GlcNAc...) (Potential). FT CARBOHYD 772 772 N-linked (GlcNAc...) (Potential). FT CARBOHYD 784 784 N-linked (GlcNAc...) (Potential). FT CARBOHYD 790 790 N-linked (GlcNAc...) (Potential). FT CARBOHYD 824 824 N-linked (GlcNAc...) (Potential). FT CARBOHYD 910 910 N-linked (GlcNAc...) (Potential). FT CARBOHYD 937 937 N-linked (GlcNAc...). FT VARIANT 214 214 R -> C (in colon cancer; somatic FT mutation). FT /FTId=VAR_015905. FT VARIANT 276 276 Q -> P (in colon cancer; somatic FT mutation; dbSNP:rs1566734). FT /FTId=VAR_015906. FT VARIANT 293 293 A -> T (in dbSNP:rs2229701). FT /FTId=VAR_038414. FT VARIANT 326 326 R -> Q (in dbSNP:rs1503185). FT /FTId=VAR_024582. FT VARIANT 372 372 V -> I (in dbSNP:rs2229703). FT /FTId=VAR_038415. FT VARIANT 872 872 E -> D (in dbSNP:rs4752904). FT /FTId=VAR_038416. FT VARIANT 1235 1235 I -> T (in dbSNP:rs11039554). FT /FTId=VAR_038417. FT CONFLICT 261 261 G -> D (in Ref. 1; AAB36687). FT CONFLICT 918 929 YNGKLEPLGSYR -> LQWEAGTSGLLP (in Ref. 2; FT BAA07035). FT CONFLICT 1130 1130 K -> Q (in Ref. 5). FT CONFLICT 1234 1234 P -> E (in Ref. 5). FT CONFLICT 1243 1243 V -> I (in Ref. 5). FT HELIX 1023 1047 FT TURN 1048 1054 FT TURN 1058 1061 FT HELIX 1063 1068 FT TURN 1078 1080 FT STRAND 1087 1089 FT HELIX 1090 1093 FT STRAND 1096 1100 FT STRAND 1108 1113 FT TURN 1117 1119 FT HELIX 1120 1129 FT STRAND 1134 1138 FT STRAND 1155 1157 FT STRAND 1159 1161 FT STRAND 1164 1173 FT STRAND 1175 1186 FT TURN 1187 1189 FT STRAND 1192 1200 FT HELIX 1212 1225 FT STRAND 1235 1243 FT HELIX 1244 1261 FT STRAND 1262 1265 FT HELIX 1267 1275 FT HELIX 1285 1302 SQ SEQUENCE 1337 AA; 145941 MW; B44F4343FC8FD1B4 CRC64; MKPAAREARL PPRSPGLRWA LPLLLLLLRL GQILCAGGTP SPIPDPSVAT VATGENGITQ ISSTAESFHK QNGTGTPQVE TNTSEDGESS GANDSLRTPE QGSNGTDGAS QKTPSSTGPS PVFDIKAVSI SPTNVILTWK SNDTAASEYK YVVKHKMENE KTITVVHQPW CNITGLRPAT SYVFSITPGI GNETWGDPRV IKVITEPIPV SDLRVALTGV RKAALSWSNG NGTASCRVLL ESIGSHEELT QDSRLQVNIS GLKPGVQYNI NPYLLQSNKT KGDPLGTEGG LDASNTERSR AGSPTAPVHD ESLVGPVDPS SGQQSRDTEV LLVGLEPGTR YNATVYSQAA NGTEGQPQAI EFRTNAIQVF DVTAVNISAT SLTLIWKVSD NESSSNYTYK IHVAGETDSS NLNVSEPRAV IPGLRSSTFY NITVCPVLGD IEGTPGFLQV HTPPVPVSDF RVTVVSTTEI GLAWSSHDAE SFQMHITQEG AGNSRVEITT NQSIIIGGLF PGTKYCFEIV PKGPNGTEGA SRTVCNRTVP SAVFDIHVVY VTTTEMWLDW KSPDGASEYV YHLVIESKHG SNHTSTYDKA ITLQGLIPGT LYNITISPEV DHVWGDPNST AQYTRPSNVS NIDVSTNTTA ATLSWQNFDD ASPTYSYCLL IEKAGNSSNA TQVVTDIGIT DATVTELIPG SSYTVEIFAQ VGDGIKSLEP GRKSFCTDPA SMASFDCEVV PKEPALVLKW TCPPGANAGF ELEVSSGAWN NATHLESCSS ENGTEYRTEV TYLNFSTSYN ISITTVSCGK MAAPTRNTCT TGITDPPPPD GSPNITSVSH NSVKVKFSGF EASHGPIKAY AVILTTGEAG HPSADVLKYT YEDFKKGASD TYVTYLIRTE EKGRSQSLSE VLKYEIDVGN ESTTLGYYNG KLEPLGSYRA CVAGFTNITF HPQNKGLIDG AESYVSFSRY SDAVSLPQDP GVICGAVFGC IFGALVIVTV GGFIFWRKKR KDAKNNEVSF SQIKPKKSKL IRVENFEAYF KKQQADSNCG FAEEYEDLKL VGISQPKYAA ELAENRGKNR YNNVLPYDIS RVKLSVQTHS TDDYINANYM PGYHSKKDFI ATQGPLPNTL KDFWRMVWEK NVYAIIMLTK CVEQGRTKCE EYWPSKQAQD YGDITVAMTS EIVLPEWTIR DFTVKNIQTS ESHPLRQFHF TSWPDHGVPD TTDLLINFRY LVRDYMKQSP PESPILVHCS AGVGRTGTFI AIDRLIYQIE NENTVDVYGI VYDLRMHRPL MVQTEDQYVF LNQCVLDIVR SQKDSKVDLI YQNTTAMTIY ENLAPVTTFG KTNGYIA //