Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Receptor-type tyrosine-protein phosphatase eta (Protein-tyrosine phosphatase eta) (R-PTP-eta) (EC 3.1.3.48) (Density-enhanced phosphatase 1) (DEP-1) (HPTP eta) (Protein-tyrosine phosphatase receptor type J) (R-PTP-J) (CD antigen CD148)

 PTPRJ_HUMAN             Reviewed;        1337 AA.
Q12913; Q15255; Q6P4H4; Q8NHM2; Q9UDA9;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
05-FEB-2008, sequence version 3.
25-OCT-2017, entry version 185.
RecName: Full=Receptor-type tyrosine-protein phosphatase eta;
Short=Protein-tyrosine phosphatase eta;
Short=R-PTP-eta;
EC=3.1.3.48;
AltName: Full=Density-enhanced phosphatase 1;
Short=DEP-1;
AltName: Full=HPTP eta;
AltName: Full=Protein-tyrosine phosphatase receptor type J;
Short=R-PTP-J;
AltName: CD_antigen=CD148;
Flags: Precursor;
Name=PTPRJ; Synonyms=DEP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-872.
PubMed=7937872; DOI=10.1073/pnas.91.21.9680;
Oestman A., Yang Q., Tonks N.K.;
"Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is
enhanced with increasing cell density.";
Proc. Natl. Acad. Sci. U.S.A. 91:9680-9684(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ASP-872.
PubMed=7994032;
Honda H., Inazawa J., Nishida J., Yazaki Y., Hirai H.;
"Molecular cloning, characterization, and chromosomal localization of
a novel protein-tyrosine phosphatase, HPTP eta.";
Blood 84:4186-4194(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-1337, AND VARIANTS CYS-214;
PRO-276 AND ASP-872.
TISSUE=Colon;
PubMed=12089527; DOI=10.1038/ng903;
Ruivenkamp C.A.L., van Wezel T., Zanon C., Stassen A.P.M., Vlcek C.,
Csikos T., Klous A.M., Tripodis N., Perrakis A., Boerrigter L.,
Groot P.C., Lindeman J., Mooi W.J., Meijjer G.A., Scholten G.,
Dauwerse H., Paces V., van Zandwijk N., van Ommen G.J.B., Demant P.;
"Ptprj is a candidate for the mouse colon-cancer susceptibility locus
Scc1 and is frequently deleted in human cancers.";
Nat. Genet. 31:295-300(2002).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1124-1245 (ISOFORM 1), AND TISSUE
SPECIFICITY.
TISSUE=Leukemia;
PubMed=8483328;
Honda H., Shibuya M., Chiba S., Yazaki Y., Hirai H.;
"Identification of novel protein-tyrosine phosphatases in a human
leukemia cell line, F-36P.";
Leukemia 7:742-746(1993).
[7]
PROTEIN SEQUENCE OF 36-49; 485-502 AND 723-739, FUNCTION, TISSUE
SPECIFICITY, GLYCOSYLATION, AND SUBCELLULAR LOCATION.
PubMed=9531590;
de la Fuente-Garcia M.A., Nicolas J.M., Freed J.H., Palou E.,
Thomas A.P., Vilella R., Vives J., Gaya A.;
"CD148 is a membrane protein tyrosine phosphatase present in all
hematopoietic lineages and is involved in signal transduction on
lymphocytes.";
Blood 91:2800-2809(1998).
[8]
FUNCTION.
PubMed=9780142;
Tangye S.G., Wu J., Aversa G., de Vries J.E., Lanier L.L.,
Phillips J.H.;
"Negative regulation of human T cell activation by the receptor-type
protein tyrosine phosphatase CD148.";
J. Immunol. 161:3803-3807(1998).
[9]
FUNCTION.
PubMed=10821867; DOI=10.1074/jbc.275.21.16219;
Kovalenko M., Denner K., Sandstrom J., Persson C., Gross S., Jandt E.,
Vilella R., Bohmer F., Ostman A.;
"Site-selective dephosphorylation of the platelet-derived growth
factor beta-receptor by the receptor-like protein-tyrosine phosphatase
DEP-1.";
J. Biol. Chem. 275:16219-16226(2000).
[10]
FUNCTION.
PubMed=11259588; DOI=10.1128/MCB.21.7.2393-2403.2001;
Baker J.E., Majeti R., Tangye S.G., Weiss A.;
"Protein tyrosine phosphatase CD148-mediated inhibition of T-cell
receptor signal transduction is associated with reduced LAT and
phospholipase Cgamma1 phosphorylation.";
Mol. Cell. Biol. 21:2393-2403(2001).
[11]
FUNCTION.
PubMed=12062403; DOI=10.1016/S0014-5793(02)02570-X;
Persson C., Engstrom U., Mowbray S.L., Ostman A.;
"Primary sequence determinants responsible for site-selective
dephosphorylation of the PDGF beta-receptor by the receptor-like
protein tyrosine phosphatase DEP-1.";
FEBS Lett. 517:27-31(2002).
[12]
FUNCTION, INTERACTION WITH CTNNB1 AND JUP, MUTAGENESIS OF ASP-1205 AND
CYS-1239, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=12370829; DOI=10.1038/sj.onc.1205858;
Holsinger L.J., Ward K., Duffield B., Zachwieja J., Jallal B.;
"The transmembrane receptor protein tyrosine phosphatase DEP1
interacts with p120(ctn).";
Oncogene 21:7067-7076(2002).
[13]
FUNCTION, INTERACTION WITH CTNNB1; GRB2; GAB1 AND JUP, AND MUTAGENESIS
OF ASP-1205 AND CYS-1239.
PubMed=12475979; DOI=10.1074/jbc.M210656200;
Palka H.L., Park M., Tonks N.K.;
"Hepatocyte growth factor receptor tyrosine kinase met is a substrate
of the receptor protein-tyrosine phosphatase DEP-1.";
J. Biol. Chem. 278:5728-5735(2003).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12913111; DOI=10.1083/jcb.200303040;
Lin J., Weiss A.;
"The tyrosine phosphatase CD148 is excluded from the immunologic
synapse and down-regulates prolonged T cell signaling.";
J. Cell Biol. 162:673-682(2003).
[15]
FUNCTION.
PubMed=14709717; DOI=10.1242/jcs.00879;
Kellie S., Craggs G., Bird I.N., Jones G.E.;
"The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements,
aberrant cell-substratum interactions and a reduction in cell
proliferation.";
J. Cell Sci. 117:609-618(2004).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-342; ASN-351; ASN-391 AND
ASN-396.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[17]
FUNCTION, AND MUTAGENESIS OF ASP-1205.
PubMed=16778204; DOI=10.1158/0008-5472.CAN-06-0228;
Iervolino A., Iuliano R., Trapasso F., Viglietto G., Melillo R.M.,
Carlomagno F., Santoro M., Fusco A.;
"The receptor-type protein tyrosine phosphatase J antagonizes the
biochemical and biological effects of RET-derived oncoproteins.";
Cancer Res. 66:6280-6287(2006).
[18]
FUNCTION.
PubMed=16682945; DOI=10.1038/sj.onc.1209647;
Balavenkatraman K.K., Jandt E., Friedrich K., Kautenburger T.,
Pool-Zobel B.L., Ostman A., Bohmer F.D.;
"DEP-1 protein tyrosine phosphatase inhibits proliferation and
migration of colon carcinoma cells and is upregulated by protective
nutrients.";
Oncogene 25:6319-6324(2006).
[19]
FUNCTION, MUTAGENESIS OF ASP-1205, AND SUBCELLULAR LOCATION.
PubMed=18348712; DOI=10.1042/BJ20071317;
Tsuboi N., Utsunomiya T., Roberts R.L., Ito H., Takahashi K., Noda M.,
Takahashi T.;
"The tyrosine phosphatase CD148 interacts with the p85 regulatory
subunit of phosphoinositide 3-kinase.";
Biochem. J. 413:193-200(2008).
[20]
SUBUNIT.
PubMed=19246339; DOI=10.1182/blood-2008-08-174318;
Senis Y.A., Tomlinson M.G., Ellison S., Mazharian A., Lim J., Zhao Y.,
Kornerup K.N., Auger J.M., Thomas S.G., Dhanjal T., Kalia N.,
Zhu J.W., Weiss A., Watson S.P.;
"The tyrosine phosphatase CD148 is an essential positive regulator of
platelet activation and thrombosis.";
Blood 113:4942-4954(2009).
[21]
FUNCTION IN EGFR REGULATION, MUTAGENESIS OF ASP-1205 AND CYS-1239, AND
SUBCELLULAR LOCATION.
PubMed=19836242; DOI=10.1016/j.cub.2009.09.048;
Tarcic G., Boguslavsky S.K., Wakim J., Kiuchi T., Liu A., Reinitz F.,
Nathanson D., Takahashi T., Mischel P.S., Ng T., Yarden Y.;
"An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase
controlling EGFR endocytosis.";
Curr. Biol. 19:1788-1798(2009).
[22]
FUNCTION, MUTAGENESIS OF ASP-1205 AND CYS-1239, AND SUBCELLULAR
LOCATION.
PubMed=19332538; DOI=10.1074/jbc.M901901200;
Sallee J.L., Burridge K.;
"Density-enhanced phosphatase 1 regulates phosphorylation of tight
junction proteins and enhances barrier function of epithelial cells.";
J. Biol. Chem. 284:14997-15006(2009).
[23]
FUNCTION, AND MUTAGENESIS OF LYS-1016 AND ASP-1205.
PubMed=19494114; DOI=10.1074/jbc.M109.002758;
Sacco F., Tinti M., Palma A., Ferrari E., Nardozza A.P.,
Hooft van Huijsduijnen R., Takahashi T., Castagnoli L., Cesareni G.;
"Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the
RAS pathway by direct dephosphorylation of ERK1/2 kinases.";
J. Biol. Chem. 284:22048-22058(2009).
[24]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-413 AND ASN-937.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[25]
FUNCTION, AND MUTAGENESIS OF ASP-1205 AND CYS-1239.
PubMed=18936167; DOI=10.1128/MCB.01374-08;
Chabot C., Spring K., Gratton J.P., Elchebly M., Royal I.;
"New role for the protein tyrosine phosphatase DEP-1 in Akt activation
and endothelial cell survival.";
Mol. Cell. Biol. 29:241-253(2009).
[26]
FUNCTION.
PubMed=21091576; DOI=10.1111/j.1750-3639.2010.00464.x;
Petermann A., Haase D., Wetzel A., Balavenkatraman K.K., Tenev T.,
Guhrs K.H., Friedrich S., Nakamura M., Mawrin C., Bohmer F.D.;
"Loss of the protein-tyrosine phosphatase DEP-1/PTPRJ drives
meningioma cell motility.";
Brain Pathol. 21:405-418(2011).
[27]
FUNCTION.
PubMed=19922411; DOI=10.1042/BJ20091413;
Omerovic J., Clague M.J., Prior I.A.;
"Phosphatome profiling reveals PTPN2, PTPRJ and PTEN as potent
negative regulators of PKB/Akt activation in Ras-mutated cancer
cells.";
Biochem. J. 426:65-72(2010).
[28]
FUNCTION, INTERACTION WITH FLT3, AND MUTAGENESIS OF ASP-1205 AND
CYS-1239.
PubMed=21262971; DOI=10.1074/jbc.M110.205021;
Arora D., Stopp S., Bohmer S.A., Schons J., Godfrey R., Masson K.,
Razumovskaya E., Ronnstrand L., Tanzer S., Bauer R., Bohmer F.D.,
Muller J.P.;
"Protein-tyrosine phosphatase DEP-1 controls receptor tyrosine kinase
FLT3 signaling.";
J. Biol. Chem. 286:10918-10929(2011).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1009, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[30]
STRUCTURE BY NMR OF 366-456.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the fourth FN3 domain of human receptor-type
tyrosine-protein phosphatase eta.";
Submitted (OCT-2006) to the PDB data bank.
[31]
VARIANTS PRO-276; GLN-326 AND ASP-872.
PubMed=15378013; DOI=10.1038/sj.onc.1207766;
Iuliano R., Le Pera I., Cristofaro C., Baudi F., Arturi F.,
Pallante P., Martelli M.L., Trapasso F., Chiariotti L., Fusco A.;
"The tyrosine phosphatase PTPRJ/DEP-1 genotype affects thyroid
carcinogenesis.";
Oncogene 23:8432-8438(2004).
-!- FUNCTION: 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. {ECO:0000269|PubMed:10821867,
ECO:0000269|PubMed:11259588, ECO:0000269|PubMed:12062403,
ECO:0000269|PubMed:12370829, ECO:0000269|PubMed:12475979,
ECO:0000269|PubMed:12913111, ECO:0000269|PubMed:14709717,
ECO:0000269|PubMed:16682945, ECO:0000269|PubMed:16778204,
ECO:0000269|PubMed:18348712, ECO:0000269|PubMed:18936167,
ECO:0000269|PubMed:19332538, ECO:0000269|PubMed:19494114,
ECO:0000269|PubMed:19836242, ECO:0000269|PubMed:19922411,
ECO:0000269|PubMed:21091576, ECO:0000269|PubMed:21262971,
ECO:0000269|PubMed:9531590, ECO:0000269|PubMed:9780142}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- SUBUNIT: Monomer. Interacts with CTNNB1 (phosphorylated) and JUP
(phosphorylated). Interacts with FLT3 (phosphorylated). Interacts
with GAB1 and GRB2. {ECO:0000269|PubMed:12370829,
ECO:0000269|PubMed:12475979, ECO:0000269|PubMed:19246339,
ECO:0000269|PubMed:21262971}.
-!- INTERACTION:
P35222:CTNNB1; NbExp=2; IntAct=EBI-2264500, EBI-491549;
O60716:CTNND1; NbExp=5; IntAct=EBI-2264500, EBI-701927;
P04626:ERBB2; NbExp=2; IntAct=EBI-2264500, EBI-641062;
P17948:FLT1; NbExp=2; IntAct=EBI-2264500, EBI-1026718;
P36888:FLT3; NbExp=3; IntAct=EBI-2264500, EBI-3946257;
Q13480:GAB1; NbExp=2; IntAct=EBI-2264500, EBI-517684;
P10912:GHR; NbExp=2; IntAct=EBI-2264500, EBI-286316;
P35968:KDR; NbExp=4; IntAct=EBI-2264500, EBI-1005487;
P28482:MAPK1; NbExp=7; IntAct=EBI-2264500, EBI-959949;
P27361:MAPK3; NbExp=5; IntAct=EBI-2264500, EBI-73995;
P08581:MET; NbExp=5; IntAct=EBI-2264500, EBI-1039152;
P09619:PDGFRB; NbExp=4; IntAct=EBI-2264500, EBI-641237;
Q02763:TEK; NbExp=2; IntAct=EBI-2264500, EBI-2257090;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Cell projection, ruffle membrane {ECO:0000250}. Cell
junction. Note=After T-cell stimulation, it is temporarily
excluded from immunological synapses.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q12913-1; Sequence=Displayed;
Name=2;
IsoId=Q12913-2; Sequence=VSP_043652, VSP_043653;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in the promyelocytic cell line HL-
60, the granulocyte-macrophage colony-stimulating factor-dependent
leukemic cell line F-36P, and the IL3 and erythropoietin-dependent
leukemic cell line F-36E. Expressed predominantly in epithelial
cells and lymphocytes. Enhanced expression at high cell density.
{ECO:0000269|PubMed:12370829, ECO:0000269|PubMed:8483328,
ECO:0000269|PubMed:9531590}.
-!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:9531590}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Receptor class 3 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PTPRJID41932ch11p11.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U10886; AAB36687.1; -; mRNA.
EMBL; D37781; BAA07035.1; -; mRNA.
EMBL; AC026975; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC103828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC063417; AAH63417.1; -; mRNA.
EMBL; AH011675; AAM69432.1; -; Genomic_DNA.
CCDS; CCDS44596.1; -. [Q12913-2]
CCDS; CCDS7945.1; -. [Q12913-1]
PIR; I38670; I38670.
RefSeq; NP_001091973.1; NM_001098503.1. [Q12913-2]
RefSeq; NP_002834.3; NM_002843.3. [Q12913-1]
UniGene; Hs.318547; -.
PDB; 2CFV; X-ray; 2.50 A; A=1019-1311.
PDB; 2DLE; NMR; -; A=366-456.
PDB; 2NZ6; X-ray; 2.30 A; A=1019-1311.
PDBsum; 2CFV; -.
PDBsum; 2DLE; -.
PDBsum; 2NZ6; -.
ProteinModelPortal; Q12913; -.
SMR; Q12913; -.
BioGrid; 111759; 29.
IntAct; Q12913; 65.
MINT; MINT-1349281; -.
STRING; 9606.ENSP00000400010; -.
BindingDB; Q12913; -.
ChEMBL; CHEMBL3692; -.
DEPOD; Q12913; -.
iPTMnet; Q12913; -.
PhosphoSitePlus; Q12913; -.
BioMuta; PTPRJ; -.
DMDM; 166899088; -.
EPD; Q12913; -.
MaxQB; Q12913; -.
PaxDb; Q12913; -.
PeptideAtlas; Q12913; -.
PRIDE; Q12913; -.
DNASU; 5795; -.
Ensembl; ENST00000418331; ENSP00000400010; ENSG00000149177. [Q12913-1]
Ensembl; ENST00000440289; ENSP00000409733; ENSG00000149177. [Q12913-2]
GeneID; 5795; -.
KEGG; hsa:5795; -.
UCSC; uc001ngo.5; human. [Q12913-1]
CTD; 5795; -.
DisGeNET; 5795; -.
EuPathDB; HostDB:ENSG00000149177.12; -.
GeneCards; PTPRJ; -.
H-InvDB; HIX0035923; -.
HGNC; HGNC:9673; PTPRJ.
HPA; HPA006026; -.
MalaCards; PTPRJ; -.
MIM; 600925; gene.
neXtProt; NX_Q12913; -.
OpenTargets; ENSG00000149177; -.
PharmGKB; PA34018; -.
eggNOG; KOG0791; Eukaryota.
eggNOG; COG5599; LUCA.
GeneTree; ENSGT00900000140785; -.
HOGENOM; HOG000232054; -.
HOVERGEN; HBG053761; -.
InParanoid; Q12913; -.
KO; K05698; -.
PhylomeDB; Q12913; -.
TreeFam; TF351926; -.
BRENDA; 3.1.3.48; 2681.
Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6807004; Negative regulation of MET activity.
SignaLink; Q12913; -.
SIGNOR; Q12913; -.
ChiTaRS; PTPRJ; human.
EvolutionaryTrace; Q12913; -.
GeneWiki; PTPRJ; -.
GenomeRNAi; 5795; -.
PRO; PR:Q12913; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000149177; -.
CleanEx; HS_PTPRJ; -.
ExpressionAtlas; Q12913; baseline and differential.
Genevisible; Q12913; HS.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
GO; GO:0070097; F:delta-catenin binding; IPI:UniProtKB.
GO; GO:0045295; F:gamma-catenin binding; IPI:UniProtKB.
GO; GO:0051019; F:mitogen-activated protein kinase binding; IPI:UniProtKB.
GO; GO:0016791; F:phosphatase activity; IDA:UniProtKB.
GO; GO:0005161; F:platelet-derived growth factor receptor binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
GO; GO:0060242; P:contact inhibition; NAS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IMP:UniProtKB.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:0010642; P:negative regulation of platelet-derived growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IDA:UniProtKB.
GO; GO:0043116; P:negative regulation of vascular permeability; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:UniProtKB.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IMP:UniProtKB.
GO; GO:0050918; P:positive chemotaxis; IDA:UniProtKB.
GO; GO:0045785; P:positive regulation of cell adhesion; IMP:UniProtKB.
GO; GO:0051894; P:positive regulation of focal adhesion assembly; IMP:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:0030155; P:regulation of cell adhesion; IMP:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
CDD; cd00063; FN3; 5.
Gene3D; 1.20.5.100; -; 1.
Gene3D; 2.60.40.10; -; 8.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF00041; fn3; 2.
Pfam; PF00102; Y_phosphatase; 1.
PRINTS; PR00700; PRTYPHPHTASE.
SMART; SM00060; FN3; 8.
SMART; SM00194; PTPc; 1.
SMART; SM00404; PTPc_motif; 1.
SUPFAM; SSF49265; SSF49265; 4.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS50853; FN3; 6.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
1: Evidence at protein level;
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.
SIGNAL 1 35 {ECO:0000255}.
CHAIN 36 1337 Receptor-type tyrosine-protein
phosphatase eta.
/FTId=PRO_0000025444.
TOPO_DOM 36 975 Extracellular. {ECO:0000255}.
TRANSMEM 976 996 Helical. {ECO:0000255}.
TOPO_DOM 997 1337 Cytoplasmic. {ECO:0000255}.
DOMAIN 121 209 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 207 291 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 271 364 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 368 456 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 457 541 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 542 623 Fibronectin type-III 6.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 625 720 Fibronectin type-III 7.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 721 817 Fibronectin type-III 8.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 816 902 Fibronectin type-III 9.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1041 1298 Tyrosine-protein phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 1239 1245 Substrate binding. {ECO:0000250}.
ACT_SITE 1239 1239 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00160,
ECO:0000255|PROSITE-ProRule:PRU10044}.
BINDING 1205 1205 Substrate. {ECO:0000250}.
BINDING 1283 1283 Substrate. {ECO:0000250}.
MOD_RES 1009 1009 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 72 72 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 93 93 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 104 104 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 192 192 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 231 231 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 278 278 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 342 342 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 351 351 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 376 376 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 391 391 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 396 396 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 413 413 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
CARBOHYD 431 431 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 501 501 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 525 525 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 536 536 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 582 582 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 603 603 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 618 618 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 628 628 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 637 637 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 666 666 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 669 669 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 761 761 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 772 772 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 784 784 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 790 790 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 824 824 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 910 910 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 937 937 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
VAR_SEQ 539 539 V -> G (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043652.
VAR_SEQ 540 1337 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043653.
VARIANT 214 214 R -> C (in a colon cancer sample; somatic
mutation; dbSNP:rs121434507).
{ECO:0000269|PubMed:12089527}.
/FTId=VAR_015905.
VARIANT 276 276 Q -> P (in a colon cancer sample; somatic
mutation; dbSNP:rs1566734).
{ECO:0000269|PubMed:12089527,
ECO:0000269|PubMed:15378013}.
/FTId=VAR_015906.
VARIANT 293 293 A -> T (in dbSNP:rs2229701).
/FTId=VAR_038414.
VARIANT 326 326 R -> Q (in dbSNP:rs1503185).
{ECO:0000269|PubMed:15378013}.
/FTId=VAR_024582.
VARIANT 372 372 V -> I (in dbSNP:rs2229703).
/FTId=VAR_038415.
VARIANT 872 872 E -> D (in dbSNP:rs4752904).
{ECO:0000269|PubMed:12089527,
ECO:0000269|PubMed:15378013,
ECO:0000269|PubMed:7937872,
ECO:0000269|PubMed:7994032}.
/FTId=VAR_038416.
VARIANT 1235 1235 I -> T (in dbSNP:rs11039554).
/FTId=VAR_038417.
MUTAGEN 1016 1016 K->A: 80% decrease in interaction with
MAPK1 and MAPK3.
{ECO:0000269|PubMed:19494114}.
MUTAGEN 1205 1205 D->A: Substrate trapping with much higher
affinity for substrate.
{ECO:0000269|PubMed:12370829,
ECO:0000269|PubMed:12475979,
ECO:0000269|PubMed:16778204,
ECO:0000269|PubMed:18348712,
ECO:0000269|PubMed:18936167,
ECO:0000269|PubMed:19332538,
ECO:0000269|PubMed:19494114,
ECO:0000269|PubMed:19836242,
ECO:0000269|PubMed:21262971}.
MUTAGEN 1239 1239 C->S: Catalytically inactive and
substrate trapping with higher affinity
for substrate.
{ECO:0000269|PubMed:12370829,
ECO:0000269|PubMed:12475979,
ECO:0000269|PubMed:18936167,
ECO:0000269|PubMed:19332538,
ECO:0000269|PubMed:19836242,
ECO:0000269|PubMed:21262971}.
CONFLICT 261 261 G -> D (in Ref. 1; AAB36687).
{ECO:0000305}.
CONFLICT 918 929 YNGKLEPLGSYR -> LQWEAGTSGLLP (in Ref. 2;
BAA07035). {ECO:0000305}.
CONFLICT 1130 1130 K -> Q (in Ref. 6; no nucleotide entry).
{ECO:0000305}.
CONFLICT 1234 1234 P -> E (in Ref. 6; no nucleotide entry).
{ECO:0000305}.
CONFLICT 1243 1243 V -> I (in Ref. 6; no nucleotide entry).
{ECO:0000305}.
STRAND 368 377 {ECO:0000244|PDB:2DLE}.
STRAND 382 389 {ECO:0000244|PDB:2DLE}.
STRAND 398 404 {ECO:0000244|PDB:2DLE}.
STRAND 409 420 {ECO:0000244|PDB:2DLE}.
STRAND 429 440 {ECO:0000244|PDB:2DLE}.
STRAND 446 451 {ECO:0000244|PDB:2DLE}.
HELIX 1023 1047 {ECO:0000244|PDB:2NZ6}.
TURN 1048 1054 {ECO:0000244|PDB:2NZ6}.
TURN 1058 1061 {ECO:0000244|PDB:2NZ6}.
HELIX 1063 1068 {ECO:0000244|PDB:2NZ6}.
TURN 1078 1080 {ECO:0000244|PDB:2NZ6}.
STRAND 1087 1089 {ECO:0000244|PDB:2NZ6}.
HELIX 1090 1093 {ECO:0000244|PDB:2NZ6}.
STRAND 1096 1100 {ECO:0000244|PDB:2NZ6}.
STRAND 1108 1113 {ECO:0000244|PDB:2NZ6}.
TURN 1117 1119 {ECO:0000244|PDB:2NZ6}.
HELIX 1120 1129 {ECO:0000244|PDB:2NZ6}.
STRAND 1134 1138 {ECO:0000244|PDB:2NZ6}.
STRAND 1155 1157 {ECO:0000244|PDB:2NZ6}.
STRAND 1159 1161 {ECO:0000244|PDB:2NZ6}.
STRAND 1164 1173 {ECO:0000244|PDB:2NZ6}.
STRAND 1175 1186 {ECO:0000244|PDB:2NZ6}.
TURN 1187 1189 {ECO:0000244|PDB:2NZ6}.
STRAND 1192 1200 {ECO:0000244|PDB:2NZ6}.
HELIX 1212 1225 {ECO:0000244|PDB:2NZ6}.
STRAND 1235 1243 {ECO:0000244|PDB:2NZ6}.
HELIX 1244 1261 {ECO:0000244|PDB:2NZ6}.
STRAND 1262 1265 {ECO:0000244|PDB:2NZ6}.
HELIX 1267 1275 {ECO:0000244|PDB:2NZ6}.
HELIX 1285 1302 {ECO:0000244|PDB:2NZ6}.
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


Related products :

Catalog number Product name Quantity
10-054-165004 DEP1 (1024-1306) HUMAN - EC 3.1.3.48; Protein-tyrosine phosphatase eta; R-PTP-eta; HPTP eta; Protein-tyrosine phosphatase receptor type J; Density-enhanced phosphatase 1; DEP-1; CD148 antigen 0.02 mg
10-054-165001 PTPbeta (1675-1996) HUMAN - EC 3.1.3.48; Protein-tyrosine phosphatase eta; R-PTP-eta; HPTP eta; Protein-tyrosine phosphatase receptor type J; Density-enhanced phosphatase 1; DEP-1; CD148 antigen 0.02 mg
EIAAB33092 Density-enhanced phosphatase 1,DEP1,DEP-1,Homo sapiens,HPTP eta,Human,Protein-tyrosine phosphatase eta,Protein-tyrosine phosphatase receptor type J,PTPRJ,Receptor-type tyrosine-protein phosphatase eta
15-288-21475 Receptor-type tyrosine-protein phosphatase eta - EC 3.1.3.48; Protein-tyrosine phosphatase eta; R-PTP-eta; HPTP eta; Protein-tyrosine phosphatase receptor type J; Density-enhanced phosphatase 1; DEP-1 0.1 mg
15-288-21475B Receptor-type tyrosine-protein phosphatase eta - EC 3.1.3.48; Protein-tyrosine phosphatase eta; R-PTP-eta; HPTP eta; Protein-tyrosine phosphatase receptor type J; Density-enhanced phosphatase 1; DEP-1 0.05 mg
15-288-21475B Receptor-type tyrosine-protein phosphatase eta - EC 3.1.3.48; Protein-tyrosine phosphatase eta; R-PTP-eta; HPTP eta; Protein-tyrosine phosphatase receptor type J; Density-enhanced phosphatase 1; DEP-1 0.1 mg
15-288-21475 Receptor-type tyrosine-protein phosphatase eta - EC 3.1.3.48; Protein-tyrosine phosphatase eta; R-PTP-eta; HPTP eta; Protein-tyrosine phosphatase receptor type J; Density-enhanced phosphatase 1; DEP-1 0.05 mg
EIAAB33094 Byp,HPTP beta-like tyrosine phosphatase,Mouse,Mus musculus,Protein-tyrosine phosphatase eta,Protein-tyrosine phosphatase receptor type J,Ptprj,Receptor-type tyrosine-protein phosphatase eta,R-PTP-eta,
EIAAB33117 FMI,Homo sapiens,hPTP-J,Human,Pancreatic carcinoma phosphatase 2,PCP2,PCP-2,Protein-tyrosine phosphatase J,Protein-tyrosine phosphatase pi,Protein-tyrosine phosphatase receptor omicron,PTP pi,PTP-J,PT
EIAAB33093 Chicken,Gallus gallus,HPTP eta,Protein-tyrosine phosphatase eta,Protein-tyrosine phosphatase receptor type J,PTPRJ,Receptor-type tyrosine-protein phosphatase eta,R-PTP-eta,R-PTP-J,Supporting-cell anti
EIAAB33026 Mouse,Mus musculus,Protein tyrosine phosphatase DPZPTP,Protein tyrosine phosphatase PTP-BL,Protein-tyrosine phosphatase RIP,Ptp14,PTP36,Ptpn13,Tyrosine-protein phosphatase non-receptor type 13
EIAAB33112 LAR-PTP2,Leukocyte common antigen-related protein-tyrosine phosphatase 2,Ptprs,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase S,Receptor-type tyrosine-protein phosphatase sigma,R-PTP
EIAAB33022 Homo sapiens,Human,Protein-tyrosine phosphatase 1D,Protein-tyrosine phosphatase 2C,PTP-1D,PTP2C,PTP-2C,PTPN11,Shp2,SHP-2,SHPTP2,SH-PTP2,SH-PTP3,Tyrosine-protein phosphatase non-receptor type 11
EIAAB33050 Homo sapiens,Human,Neural-specific protein-tyrosine phosphatase,PTPN5,STEP,Striatum-enriched protein-tyrosine phosphatase,Tyrosine-protein phosphatase non-receptor type 5
EIAAB33049 Neural-specific protein-tyrosine phosphatase,Ptpn5,Rat,Rattus norvegicus,STEP,Striatum-enriched protein-tyrosine phosphatase,Tyrosine-protein phosphatase non-receptor type 5
EIAAB33048 Mouse,Mus musculus,Neural-specific protein-tyrosine phosphatase,Ptpn5,STEP,Striatum-enriched protein-tyrosine phosphatase,Tyrosine-protein phosphatase non-receptor type 5
EIAAB33091 Homo sapiens,Human,PTPRH,Receptor-type tyrosine-protein phosphatase H,R-PTP-H,SAP1,SAP-1,Stomach cancer-associated protein tyrosine phosphatase 1,Transmembrane-type protein-tyrosine phosphatase type H
10-782-55086 Tyrosine-protein phosphatase non-receptor type 6 - EC 3.1.3.48; Protein-tyrosine phosphatase 1C; PTP-1C; Hematopoietic cell protein-tyrosine phosphatase; SH-PTP1; Protein-tyrosine phosphatase SHP-1 N_ 0.001 mg
10-782-55086 Tyrosine-protein phosphatase non-receptor type 6 - EC 3.1.3.48; Protein-tyrosine phosphatase 1C; PTP-1C; Hematopoietic cell protein-tyrosine phosphatase; SH-PTP1; Protein-tyrosine phosphatase SHP-1 N_ 0.02 mg
10-782-55086 Tyrosine-protein phosphatase non-receptor type 6 - EC 3.1.3.48; Protein-tyrosine phosphatase 1C; PTP-1C; Hematopoietic cell protein-tyrosine phosphatase; SH-PTP1; Protein-tyrosine phosphatase SHP-1 N_ 0.005 mg
10-782-55086 Tyrosine-protein phosphatase non-receptor type 6 - EC 3.1.3.48; Protein-tyrosine phosphatase 1C; PTP-1C; Hematopoietic cell protein-tyrosine phosphatase; SH-PTP1; Protein-tyrosine phosphatase SHP-1 N_ 0.01 mg
PP-SHP1-020 SHP-1, Tyrosine-protein phosphatase non-receptor type 6, EC 3.1.3.48, Protein-tyrosine phosphatase 1C, PTP-1C, Hematopoietic cell protein-tyrosine phosphatase, SH-PTP1, Protein-tyrosine phosphatase SH 20
EIAAB33107 PC12-PTP1,Protein-tyrosine phosphatase PCPTP1,Ptp,Ptprr,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase R,R-PTP-R,Tyrosine phosphatase CBPTP
EIAAB33119 Embryonic stem cell protein-tyrosine phosphatase,ES cell phosphatase,Esp,Osteotesticular protein-tyrosine phosphatase,OST-PTP,Ptprv,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase V,R
EIAAB33056 Hematopoietic protein-tyrosine phosphatase,HEPTP,Lcptp,Protein-tyrosine phosphatase LC-PTP,Ptpn7,Rat,Rattus norvegicus,Tyrosine-protein phosphatase non-receptor type 7


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur