HUMAN:PTPRJ

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	PTPRJ (synonyms: DEP1)
Protein Name(s)	Receptor-type tyrosine-protein phosphatase eta Protein-tyrosine phosphatase eta R-PTP-eta Density-enhanced phosphatase 1 DEP-1 HPTP eta Protein-tyrosine phosphatase receptor type J R-PTP-J
External Links
UniProt	Q12913
EMBL	U10886 D37781 AC026975 AC103828 BC063417 AH011675
CCDS	CCDS44596.1 CCDS7945.1
PIR	I38670
RefSeq	NP_001091973.1 NP_002834.3
UniGene	Hs.318547
PDB	2CFV 2DLE 2NZ6
PDBsum	2CFV 2DLE 2NZ6
ProteinModelPortal	Q12913
SMR	Q12913
BioGrid	111759
IntAct	Q12913
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 ENST00000440289
GeneID	5795
KEGG	hsa:5795
UCSC	uc001ngo.5
CTD	5795
DisGeNET	5795
GeneCards	PTPRJ
H-InvDB	HIX0035923
HGNC	HGNC:9673
HPA	HPA006026
MalaCards	PTPRJ
MIM	600925
neXtProt	NX_Q12913
OpenTargets	ENSG00000149177
PharmGKB	PA34018
eggNOG	KOG0791 COG5599
GeneTree	ENSGT00770000120452
HOGENOM	HOG000232054
HOVERGEN	HBG053761
InParanoid	Q12913
KO	K05698
PhylomeDB	Q12913
TreeFam	TF351926
BioCyc	ZFISH:HS07590-MONOMER
BRENDA	3.1.3.48
Reactome	[www.reactome.org/content/detail/R-HSA-202427 R-HSA-202427] [www.reactome.org/content/detail/R-HSA-6798695 R-HSA-6798695] [www.reactome.org/content/detail/R-HSA-6807004 R-HSA-6807004]
SignaLink	Q12913
SIGNOR	Q12913
ChiTaRS	PTPRJ
EvolutionaryTrace	Q12913
GeneWiki	PTPRJ
GenomeRNAi	5795
PRO	PR:Q12913
Proteomes	UP000005640
Bgee	ENSG00000149177
CleanEx	HS_PTPRJ
ExpressionAtlas	Q12913
Genevisible	Q12913
GO	GO:0009986 GO:0005911 GO:0070062 GO:0001772 GO:0005887 GO:0005886 GO:0032587 GO:0008013 GO:0070097 GO:0045295 GO:0051019 GO:0016791 GO:0005161 GO:0019901 GO:0004725 GO:0060242 GO:0030308 GO:0030336 GO:0008285 GO:0042059 GO:0043407 GO:0010642 GO:0051898 GO:0050860 GO:0043116 GO:0035335 GO:0048008 GO:0050918 GO:0045785 GO:0051894 GO:0051897 GO:0030155 GO:0050852
CDD	cd00063
Gene3D	2.60.40.10 3.90.190.10
InterPro	IPR003961 IPR013783 IPR029021 IPR000242 IPR016130 IPR003595 IPR000387
Pfam	PF00041 PF00102
PRINTS	PR00700
SMART	SM00060 SM00194 SM00404
SUPFAM	SSF49265 SSF52799
PROSITE	PS50853 PS00383 PS50056 PS50055

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:1905451	positive regulation of Fc-gamma receptor signaling pathway involved in phagocytosis	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q64455	P	occurs_in:(CL:0002476) regulates_o_occurs_in:(CL:0002476)	Seeded From UniProt	complete
involved_in	GO:0050731	positive regulation of peptidyl-tyrosine phosphorylation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q64455	P	has_regulation_target:(UniProtKB:P07948)	Seeded From UniProt	complete
involved_in	GO:0043410	positive regulation of MAPK cascade	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q64455	P		Seeded From UniProt	complete
involved_in	GO:0035584	calcium-mediated signaling using intracellular calcium source	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q64455	P	occurs_in:(CL:0000236) occurs_in:(UBERON:0000029)	Seeded From UniProt	complete
involved_in	GO:0032760	positive regulation of tumor necrosis factor production	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q64455	P	occurs_in:(CL:0002476) regulates_o_occurs_in:(CL:0002476)	Seeded From UniProt	complete
involved_in	GO:0030183	B cell differentiation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q64455	P	causally_upstream_of:(GO:0050853)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[1]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
enables	GO:0070097	delta-catenin binding	PMID:19332538^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60716	F		Seeded From UniProt	complete
enables	GO:0070097	delta-catenin binding	PMID:12370829^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O60716	F		Seeded From UniProt	complete
involved_in	GO:0060242	contact inhibition	PMID:7937872^[5]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051898	negative regulation of protein kinase B signaling	PMID:19922411^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051897	positive regulation of protein kinase B signaling	PMID:18936167^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051894	positive regulation of focal adhesion assembly	PMID:21091576^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051019	mitogen-activated protein kinase binding	PMID:19494114^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P28482	F		Seeded From UniProt	complete
involved_in	GO:0050918	positive chemotaxis	PMID:14709717^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050860	negative regulation of T cell receptor signaling pathway	PMID:11259588^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050860	negative regulation of T cell receptor signaling pathway	PMID:9780142^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0050860	negative regulation of T cell receptor signaling pathway	PMID:12913111^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048008	platelet-derived growth factor receptor signaling pathway	PMID:21091576^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045785	positive regulation of cell adhesion	PMID:21091576^[8]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0045295	gamma-catenin binding	PMID:12370829^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P14923	F		Seeded From UniProt	complete
involved_in	GO:0043407	negative regulation of MAP kinase activity	PMID:19494114^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043116	negative regulation of vascular permeability	PMID:19332538^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
Colocalizes with	GO:0005899	insulin receptor complex	PMID:26063811^[14]	ECO:0000314			C		Figure 3C: Ptprj is shown by immunostaining to colocalize with the IR at the cell surface in HEK293T cells.	complete CACAO 12256
involved_in	GO:0042059	negative regulation of epidermal growth factor receptor signaling pathway	PMID:19836242^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035335	peptidyl-tyrosine dephosphorylation	PMID:9780142^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035335	peptidyl-tyrosine dephosphorylation	PMID:12475979^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035335	peptidyl-tyrosine dephosphorylation	PMID:10821867^[17]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035335	peptidyl-tyrosine dephosphorylation	PMID:9531590^[18]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035335	peptidyl-tyrosine dephosphorylation	PMID:12913111^[13]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035335	peptidyl-tyrosine dephosphorylation	PMID:18348712^[19]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035335	peptidyl-tyrosine dephosphorylation	PMID:18936167^[7]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035335	peptidyl-tyrosine dephosphorylation	PMID:19332538^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030336	negative regulation of cell migration	PMID:16682945^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030308	negative regulation of cell growth	PMID:14709717^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030155	regulation of cell adhesion	PMID:12370829^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	PMID:19332538^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P12931	F		Seeded From UniProt	complete
enables	GO:0016791	phosphatase activity	PMID:11259588^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016791	phosphatase activity	PMID:19836242^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016791	phosphatase activity	PMID:12370829^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016791	phosphatase activity	PMID:19494114^[9]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0016791	phosphatase activity	PMID:12062403^[21]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0010642	negative regulation of platelet-derived growth factor receptor signaling pathway	PMID:14709717^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0009986	cell surface	PMID:12913111^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0008285	negative regulation of cell population proliferation	PMID:14709717^[10]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0008285	negative regulation of cell population proliferation	PMID:16682945^[20]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008013	beta-catenin binding	PMID:12370829^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P35222	F		Seeded From UniProt	complete
part_of	GO:0005911	cell-cell junction	PMID:12370829^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005911	cell-cell junction	PMID:19332538^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:9531590^[18]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:18348712^[19]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:19836242^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005161	platelet-derived growth factor receptor binding	PMID:10821867^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P09619	F		Seeded From UniProt	complete
enables	GO:0004725	protein tyrosine phosphatase activity	PMID:9780142^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004725	protein tyrosine phosphatase activity	PMID:12475979^[16]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004725	protein tyrosine phosphatase activity	PMID:10821867^[17]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004725	protein tyrosine phosphatase activity	PMID:9531590^[18]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004725	protein tyrosine phosphatase activity	PMID:12913111^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004725	protein tyrosine phosphatase activity	PMID:18348712^[19]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004725	protein tyrosine phosphatase activity	PMID:19332538^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004725	protein tyrosine phosphatase activity	PMID:18936167^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0001772	immunological synapse	PMID:12913111^[13]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004725	protein tyrosine phosphatase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000242 InterPro:IPR016130	F		Seeded From UniProt	complete
involved_in	GO:0006470	protein dephosphorylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000242	P		Seeded From UniProt	complete
involved_in	GO:0016311	dephosphorylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000387 InterPro:IPR016130	P		Seeded From UniProt	complete
enables	GO:0016791	phosphatase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000387	F		Seeded From UniProt	complete
enables	GO:0004725	protein tyrosine phosphatase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:3.1.3.48	F		Seeded From UniProt	complete
part_of	GO:0005887	integral component of plasma membrane	PMID:7937872^[5]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0050852	T cell receptor signaling pathway	Reactome:R-HSA-202403	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0043312	neutrophil degranulation	Reactome:R-HSA-6798695	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0035579	specific granule membrane	Reactome:R-HSA-6799350	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	Reactome:R-HSA-6807008 Reactome:R-HSA-6799350 Reactome:R-HSA-202214	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004725	protein tyrosine phosphatase activity	Reactome:R-HSA-6807008	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-1003 UniProtKB-SubCell:SL-0039	C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0472	C		Seeded From UniProt	complete
part_of	GO:0016021	integral component of membrane	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0812	C		Seeded From UniProt	complete
part_of	GO:0030054	cell junction	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0965 UniProtKB-SubCell:SL-0038	C		Seeded From UniProt	complete
part_of	GO:0042995	cell projection	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0966	C		Seeded From UniProt	complete
enables	GO:0004721	phosphoprotein phosphatase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0904	F		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
part_of	GO:0032587	ruffle membrane	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0301	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Sallee, JL & Burridge, K (2009) Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells. J. Biol. Chem. 284 14997-5006 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 Holsinger, LJ et al. (2002) The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn). Oncogene 21 7067-76 PubMed GONUTS page
↑ ^5.0 ^5.1 Ostman, A et al. (1994) Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density. Proc. Natl. Acad. Sci. U.S.A. 91 9680-4 PubMed GONUTS page
↑ Omerovic, J et al. (2010) 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 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 Chabot, C et al. (2009) New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival. Mol. Cell. Biol. 29 241-53 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 Petermann, A et al. (2011) Loss of the protein-tyrosine phosphatase DEP-1/PTPRJ drives meningioma cell motility. Brain Pathol. 21 405-18 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 Sacco, F et al. (2009) Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the RAS pathway by direct dephosphorylation of ERK1/2 kinases. J. Biol. Chem. 284 22048-58 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 Kellie, S et al. (2004) The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation. J. Cell. Sci. 117 609-18 PubMed GONUTS page
↑ ^11.0 ^11.1 Baker, JE et al. (2001) 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 2393-403 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 Tangye, SG et al. (1998) Negative regulation of human T cell activation by the receptor-type protein tyrosine phosphatase CD148. J. Immunol. 161 3803-7 PubMed GONUTS page
↑ ^13.0 ^13.1 ^13.2 ^13.3 ^13.4 Lin, J & Weiss, A (2003) The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling. J. Cell Biol. 162 673-82 PubMed GONUTS page
↑ Shintani, T et al. (2015) The R3 receptor-like protein tyrosine phosphatase subfamily inhibits insulin signalling by dephosphorylating the insulin receptor at specific sites. J. Biochem. 158 235-43 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 Tarcic, G et al. (2009) An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase controlling EGFR endocytosis. Curr. Biol. 19 1788-98 PubMed GONUTS page
↑ ^16.0 ^16.1 Palka, HL et al. (2003) Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1. J. Biol. Chem. 278 5728-35 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 Kovalenko, M et al. (2000) Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1. J. Biol. Chem. 275 16219-26 PubMed GONUTS page
↑ ^18.0 ^18.1 ^18.2 de la Fuente-García, MA et al. (1998) CD148 is a membrane protein tyrosine phosphatase present in all hematopoietic lineages and is involved in signal transduction on lymphocytes. Blood 91 2800-9 PubMed GONUTS page
↑ ^19.0 ^19.1 ^19.2 Tsuboi, N et al. (2008) The tyrosine phosphatase CD148 interacts with the p85 regulatory subunit of phosphoinositide 3-kinase. Biochem. J. 413 193-200 PubMed GONUTS page
↑ ^20.0 ^20.1 Balavenkatraman, KK et al. (2006) DEP-1 protein tyrosine phosphatase inhibits proliferation and migration of colon carcinoma cells and is upregulated by protective nutrients. Oncogene 25 6319-24 PubMed GONUTS page
↑ Persson, C et al. (2002) 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 PubMed GONUTS page

[PMID:23533145-1] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19056867-2] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:19332538-3] 3.0 ^3.1 ^3.2 ^3.3 ^3.4 ^3.5 Sallee, JL & Burridge, K (2009) Density-enhanced phosphatase 1 regulates phosphorylation of tight junction proteins and enhances barrier function of epithelial cells. J. Biol. Chem. 284 14997-5006 PubMed GONUTS page

[PMID:12370829-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 Holsinger, LJ et al. (2002) The transmembrane receptor protein tyrosine phosphatase DEP1 interacts with p120(ctn). Oncogene 21 7067-76 PubMed GONUTS page

[PMID:7937872-5] 5.0 ^5.1 Ostman, A et al. (1994) Expression of DEP-1, a receptor-like protein-tyrosine-phosphatase, is enhanced with increasing cell density. Proc. Natl. Acad. Sci. U.S.A. 91 9680-4 PubMed GONUTS page

[PMID:19922411-6] Omerovic, J et al. (2010) 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 PubMed GONUTS page

[PMID:18936167-7] 7.0 ^7.1 ^7.2 Chabot, C et al. (2009) New role for the protein tyrosine phosphatase DEP-1 in Akt activation and endothelial cell survival. Mol. Cell. Biol. 29 241-53 PubMed GONUTS page

[PMID:21091576-8] 8.0 ^8.1 ^8.2 Petermann, A et al. (2011) Loss of the protein-tyrosine phosphatase DEP-1/PTPRJ drives meningioma cell motility. Brain Pathol. 21 405-18 PubMed GONUTS page

[PMID:19494114-9] 9.0 ^9.1 ^9.2 Sacco, F et al. (2009) Tumor suppressor density-enhanced phosphatase-1 (DEP-1) inhibits the RAS pathway by direct dephosphorylation of ERK1/2 kinases. J. Biol. Chem. 284 22048-58 PubMed GONUTS page

[PMID:14709717-10] 10.0 ^10.1 ^10.2 ^10.3 Kellie, S et al. (2004) The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation. J. Cell. Sci. 117 609-18 PubMed GONUTS page

[PMID:11259588-11] 11.0 ^11.1 Baker, JE et al. (2001) 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 2393-403 PubMed GONUTS page

[PMID:9780142-12] 12.0 ^12.1 ^12.2 Tangye, SG et al. (1998) Negative regulation of human T cell activation by the receptor-type protein tyrosine phosphatase CD148. J. Immunol. 161 3803-7 PubMed GONUTS page

[PMID:12913111-13] 13.0 ^13.1 ^13.2 ^13.3 ^13.4 Lin, J & Weiss, A (2003) The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling. J. Cell Biol. 162 673-82 PubMed GONUTS page

[PMID:26063811-14] Shintani, T et al. (2015) The R3 receptor-like protein tyrosine phosphatase subfamily inhibits insulin signalling by dephosphorylating the insulin receptor at specific sites. J. Biochem. 158 235-43 PubMed GONUTS page

[PMID:19836242-15] 15.0 ^15.1 ^15.2 Tarcic, G et al. (2009) An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase controlling EGFR endocytosis. Curr. Biol. 19 1788-98 PubMed GONUTS page

[PMID:12475979-16] 16.0 ^16.1 Palka, HL et al. (2003) Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1. J. Biol. Chem. 278 5728-35 PubMed GONUTS page

[PMID:10821867-17] 17.0 ^17.1 ^17.2 Kovalenko, M et al. (2000) Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1. J. Biol. Chem. 275 16219-26 PubMed GONUTS page

[PMID:9531590-18] 18.0 ^18.1 ^18.2 de la Fuente-García, MA et al. (1998) CD148 is a membrane protein tyrosine phosphatase present in all hematopoietic lineages and is involved in signal transduction on lymphocytes. Blood 91 2800-9 PubMed GONUTS page

[PMID:18348712-19] 19.0 ^19.1 ^19.2 Tsuboi, N et al. (2008) The tyrosine phosphatase CD148 interacts with the p85 regulatory subunit of phosphoinositide 3-kinase. Biochem. J. 413 193-200 PubMed GONUTS page

[PMID:16682945-20] 20.0 ^20.1 Balavenkatraman, KK et al. (2006) DEP-1 protein tyrosine phosphatase inhibits proliferation and migration of colon carcinoma cells and is upregulated by protective nutrients. Oncogene 25 6319-24 PubMed GONUTS page

[PMID:12062403-21] Persson, C et al. (2002) 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 PubMed GONUTS page

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HUMAN:PTPRJ

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