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Protein

Receptor-type tyrosine-protein phosphatase eta

Gene

PTPRJ

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.19 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei1205SubstrateBy similarity1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei1239Phosphocysteine intermediatePROSITE-ProRule annotation1
Binding sitei1283SubstrateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Protein phosphatase

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
3.1.3.48 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-202427 Phosphorylation of CD3 and TCR zeta chains
R-HSA-6798695 Neutrophil degranulation
R-HSA-6807004 Negative regulation of MET activity

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q12913

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q12913

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase eta (EC:3.1.3.48)
Short name:
Protein-tyrosine phosphatase eta
Short name:
R-PTP-eta
Alternative name(s):
Density-enhanced phosphatase 1
Short name:
DEP-1
HPTP eta
Protein-tyrosine phosphatase receptor type J
Short name:
R-PTP-J
CD_antigen: CD148
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PTPRJ
Synonyms:DEP1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 11

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000149177.12

Human Gene Nomenclature Database

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HGNCi
HGNC:9673 PTPRJ

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
600925 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q12913

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini36 – 975ExtracellularSequence analysisAdd BLAST940
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei976 – 996HelicalSequence analysisAdd BLAST21
Topological domaini997 – 1337CytoplasmicSequence analysisAdd BLAST341

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1016K → A: 80% decrease in interaction with MAPK1 and MAPK3. 1 Publication1
Mutagenesisi1205D → A: Substrate trapping with much higher affinity for substrate. 9 Publications1
Mutagenesisi1239C → S: Catalytically inactive and substrate trapping with higher affinity for substrate. 6 Publications1

Organism-specific databases

DisGeNET

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DisGeNETi
5795

MalaCards human disease database

More...
MalaCardsi
PTPRJ

Open Targets

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OpenTargetsi
ENSG00000149177

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34018

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3692

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PTPRJ

Domain mapping of disease mutations (DMDM)

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DMDMi
166899088

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 35Sequence analysisAdd BLAST35
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002544436 – 1337Receptor-type tyrosine-protein phosphatase etaAdd BLAST1302

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi72N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi82N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi93N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi104N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi142N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi172N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi192N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi231N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi258N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi278N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi342N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi351N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi376N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi391N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi396N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi413N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi431N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi501N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi525N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi536N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi582N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi603N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi618N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi628N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi637N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi666N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi669N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi761N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi772N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi784N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi790N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi824N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi910N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi937N-linked (GlcNAc...) asparagine1 Publication1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1009PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N- and O-glycosylated.3 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q12913

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q12913

MaxQB - The MaxQuant DataBase

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MaxQBi
Q12913

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q12913

PeptideAtlas

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PeptideAtlasi
Q12913

PRoteomics IDEntifications database

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PRIDEi
Q12913

ProteomicsDB human proteome resource

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ProteomicsDBi
59024
59025 [Q12913-2]

PTM databases

DEPOD human dephosphorylation database

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DEPODi
Q12913

GlyConnect protein glycosylation platform

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GlyConnecti
1707

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q12913

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q12913

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000149177 Expressed in 195 organ(s), highest expression level in blood

CleanEx database of gene expression profiles

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CleanExi
HS_PTPRJ

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q12913 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q12913 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA006026

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer. Interacts with CTNNB1 (phosphorylated) and JUP (phosphorylated). Interacts with FLT3 (phosphorylated). Interacts with GAB1 and GRB2.4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
111759, 30 interactors

Protein interaction database and analysis system

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IntActi
Q12913, 65 interactors

Molecular INTeraction database

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MINTi
Q12913

STRING: functional protein association networks

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STRINGi
9606.ENSP00000400010

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q12913

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11337
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CFVX-ray2.50A1019-1311[»]
2DLENMR-A366-456[»]
2NZ6X-ray2.30A1019-1311[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q12913

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q12913

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q12913

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini121 – 209Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST89
Domaini207 – 291Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST85
Domaini271 – 364Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST94
Domaini368 – 456Fibronectin type-III 4PROSITE-ProRule annotationAdd BLAST89
Domaini457 – 541Fibronectin type-III 5PROSITE-ProRule annotationAdd BLAST85
Domaini542 – 623Fibronectin type-III 6PROSITE-ProRule annotationAdd BLAST82
Domaini625 – 720Fibronectin type-III 7PROSITE-ProRule annotationAdd BLAST96
Domaini721 – 817Fibronectin type-III 8PROSITE-ProRule annotationAdd BLAST97
Domaini816 – 902Fibronectin type-III 9PROSITE-ProRule annotationAdd BLAST87
Domaini1041 – 1298Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST258

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1239 – 1245Substrate bindingBy similarity7

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0791 Eukaryota
COG5599 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156870

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000232054

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG062475

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q12913

KEGG Orthology (KO)

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KOi
K05698

Database of Orthologous Groups

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OrthoDBi
411281at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q12913

TreeFam database of animal gene trees

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TreeFami
TF351926

Family and domain databases

Conserved Domains Database

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CDDi
cd00063 FN3, 5 hits

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.10, 5 hits
3.90.190.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR013783 Ig-like_fold
IPR029021 Prot-tyrosine_phosphatase-like
IPR000242 PTPase_domain
IPR016130 Tyr_Pase_AS
IPR003595 Tyr_Pase_cat
IPR000387 TYR_PHOSPHATASE_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00041 fn3, 1 hit
PF00102 Y_phosphatase, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00700 PRTYPHPHTASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00060 FN3, 8 hits
SM00194 PTPc, 1 hit
SM00404 PTPc_motif, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF49265 SSF49265, 4 hits
SSF52799 SSF52799, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50853 FN3, 6 hits
PS00383 TYR_PHOSPHATASE_1, 1 hit
PS50056 TYR_PHOSPHATASE_2, 1 hit
PS50055 TYR_PHOSPHATASE_PTP, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q12913-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
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MKPAAREARL PPRSPGLRWA LPLLLLLLRL GQILCAGGTP SPIPDPSVAT
60 70 80 90 100
VATGENGITQ ISSTAESFHK QNGTGTPQVE TNTSEDGESS GANDSLRTPE
110 120 130 140 150
QGSNGTDGAS QKTPSSTGPS PVFDIKAVSI SPTNVILTWK SNDTAASEYK
160 170 180 190 200
YVVKHKMENE KTITVVHQPW CNITGLRPAT SYVFSITPGI GNETWGDPRV
210 220 230 240 250
IKVITEPIPV SDLRVALTGV RKAALSWSNG NGTASCRVLL ESIGSHEELT
260 270 280 290 300
QDSRLQVNIS GLKPGVQYNI NPYLLQSNKT KGDPLGTEGG LDASNTERSR
310 320 330 340 350
AGSPTAPVHD ESLVGPVDPS SGQQSRDTEV LLVGLEPGTR YNATVYSQAA
360 370 380 390 400
NGTEGQPQAI EFRTNAIQVF DVTAVNISAT SLTLIWKVSD NESSSNYTYK
410 420 430 440 450
IHVAGETDSS NLNVSEPRAV IPGLRSSTFY NITVCPVLGD IEGTPGFLQV
460 470 480 490 500
HTPPVPVSDF RVTVVSTTEI GLAWSSHDAE SFQMHITQEG AGNSRVEITT
510 520 530 540 550
NQSIIIGGLF PGTKYCFEIV PKGPNGTEGA SRTVCNRTVP SAVFDIHVVY
560 570 580 590 600
VTTTEMWLDW KSPDGASEYV YHLVIESKHG SNHTSTYDKA ITLQGLIPGT
610 620 630 640 650
LYNITISPEV DHVWGDPNST AQYTRPSNVS NIDVSTNTTA ATLSWQNFDD
660 670 680 690 700
ASPTYSYCLL IEKAGNSSNA TQVVTDIGIT DATVTELIPG SSYTVEIFAQ
710 720 730 740 750
VGDGIKSLEP GRKSFCTDPA SMASFDCEVV PKEPALVLKW TCPPGANAGF
760 770 780 790 800
ELEVSSGAWN NATHLESCSS ENGTEYRTEV TYLNFSTSYN ISITTVSCGK
810 820 830 840 850
MAAPTRNTCT TGITDPPPPD GSPNITSVSH NSVKVKFSGF EASHGPIKAY
860 870 880 890 900
AVILTTGEAG HPSADVLKYT YEDFKKGASD TYVTYLIRTE EKGRSQSLSE
910 920 930 940 950
VLKYEIDVGN ESTTLGYYNG KLEPLGSYRA CVAGFTNITF HPQNKGLIDG
960 970 980 990 1000
AESYVSFSRY SDAVSLPQDP GVICGAVFGC IFGALVIVTV GGFIFWRKKR
1010 1020 1030 1040 1050
KDAKNNEVSF SQIKPKKSKL IRVENFEAYF KKQQADSNCG FAEEYEDLKL
1060 1070 1080 1090 1100
VGISQPKYAA ELAENRGKNR YNNVLPYDIS RVKLSVQTHS TDDYINANYM
1110 1120 1130 1140 1150
PGYHSKKDFI ATQGPLPNTL KDFWRMVWEK NVYAIIMLTK CVEQGRTKCE
1160 1170 1180 1190 1200
EYWPSKQAQD YGDITVAMTS EIVLPEWTIR DFTVKNIQTS ESHPLRQFHF
1210 1220 1230 1240 1250
TSWPDHGVPD TTDLLINFRY LVRDYMKQSP PESPILVHCS AGVGRTGTFI
1260 1270 1280 1290 1300
AIDRLIYQIE NENTVDVYGI VYDLRMHRPL MVQTEDQYVF LNQCVLDIVR
1310 1320 1330
SQKDSKVDLI YQNTTAMTIY ENLAPVTTFG KTNGYIA
Length:1,337
Mass (Da):145,941
Last modified:February 5, 2008 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB44F4343FC8FD1B4
GO
Isoform 2 (identifier: Q12913-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     539-539: V → G
     540-1337: Missing.

Note: No experimental confirmation available.
Show »
Length:539
Mass (Da):57,190
Checksum:iE970DA55A6B2E38D
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WTK0A0A087WTK0_HUMAN
Receptor-type tyrosine-protein phos...
PTPRJ
1,338Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A087WVC6A0A087WVC6_HUMAN
Receptor-type tyrosine-protein phos...
PTPRJ
1,342Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PPH3E9PPH3_HUMAN
Receptor-type tyrosine-protein phos...
PTPRJ
120Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PJ83E9PJ83_HUMAN
Receptor-type tyrosine-protein phos...
PTPRJ
146Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti261G → D in AAB36687 (PubMed:7937872).Curated1
Sequence conflicti918 – 929YNGKL…LGSYR → LQWEAGTSGLLP in BAA07035 (PubMed:7994032).CuratedAdd BLAST12
Sequence conflicti1130K → Q no nucleotide entry (PubMed:8483328).Curated1
Sequence conflicti1234P → E no nucleotide entry (PubMed:8483328).Curated1
Sequence conflicti1243V → I no nucleotide entry (PubMed:8483328).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_015905214R → C in a colon cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs121434507EnsemblClinVar.1
Natural variantiVAR_015906276Q → P in a colon cancer sample; somatic mutation. 2 PublicationsCorresponds to variant dbSNP:rs1566734EnsemblClinVar.1
Natural variantiVAR_038414293A → T. Corresponds to variant dbSNP:rs2229701Ensembl.1
Natural variantiVAR_024582326R → Q1 PublicationCorresponds to variant dbSNP:rs1503185Ensembl.1
Natural variantiVAR_038415372V → I. Corresponds to variant dbSNP:rs2229703Ensembl.1
Natural variantiVAR_038416872E → D4 PublicationsCorresponds to variant dbSNP:rs4752904Ensembl.1
Natural variantiVAR_0384171235I → T. Corresponds to variant dbSNP:rs11039554Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_043652539V → G in isoform 2. 1 Publication1
Alternative sequenceiVSP_043653540 – 1337Missing in isoform 2. 1 PublicationAdd BLAST798

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U10886 mRNA Translation: AAB36687.1
D37781 mRNA Translation: BAA07035.1
AC026975 Genomic DNA No translation available.
AC103828 Genomic DNA No translation available.
BC063417 mRNA Translation: AAH63417.1
AH011675 Genomic DNA Translation: AAM69432.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS44596.1 [Q12913-2]
CCDS7945.1 [Q12913-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
I38670

NCBI Reference Sequences

More...
RefSeqi
NP_001091973.1, NM_001098503.1 [Q12913-2]
NP_002834.3, NM_002843.3 [Q12913-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.318547

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000418331; ENSP00000400010; ENSG00000149177 [Q12913-1]
ENST00000440289; ENSP00000409733; ENSG00000149177 [Q12913-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
5795

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:5795

UCSC genome browser

More...
UCSCi
uc001ngo.5 human [Q12913-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U10886 mRNA Translation: AAB36687.1
D37781 mRNA Translation: BAA07035.1
AC026975 Genomic DNA No translation available.
AC103828 Genomic DNA No translation available.
BC063417 mRNA Translation: AAH63417.1
AH011675 Genomic DNA Translation: AAM69432.1
CCDSiCCDS44596.1 [Q12913-2]
CCDS7945.1 [Q12913-1]
PIRiI38670
RefSeqiNP_001091973.1, NM_001098503.1 [Q12913-2]
NP_002834.3, NM_002843.3 [Q12913-1]
UniGeneiHs.318547

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CFVX-ray2.50A1019-1311[»]
2DLENMR-A366-456[»]
2NZ6X-ray2.30A1019-1311[»]
ProteinModelPortaliQ12913
SMRiQ12913
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111759, 30 interactors
IntActiQ12913, 65 interactors
MINTiQ12913
STRINGi9606.ENSP00000400010

Chemistry databases

BindingDBiQ12913
ChEMBLiCHEMBL3692

PTM databases

DEPODiQ12913
GlyConnecti1707
iPTMnetiQ12913
PhosphoSitePlusiQ12913

Polymorphism and mutation databases

BioMutaiPTPRJ
DMDMi166899088

Proteomic databases

EPDiQ12913
jPOSTiQ12913
MaxQBiQ12913
PaxDbiQ12913
PeptideAtlasiQ12913
PRIDEiQ12913
ProteomicsDBi59024
59025 [Q12913-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
5795
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000418331; ENSP00000400010; ENSG00000149177 [Q12913-1]
ENST00000440289; ENSP00000409733; ENSG00000149177 [Q12913-2]
GeneIDi5795
KEGGihsa:5795
UCSCiuc001ngo.5 human [Q12913-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5795
DisGeNETi5795
EuPathDBiHostDB:ENSG00000149177.12

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PTPRJ

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0035923
HGNCiHGNC:9673 PTPRJ
HPAiHPA006026
MalaCardsiPTPRJ
MIMi600925 gene
neXtProtiNX_Q12913
OpenTargetsiENSG00000149177
PharmGKBiPA34018

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0791 Eukaryota
COG5599 LUCA
GeneTreeiENSGT00940000156870
HOGENOMiHOG000232054
HOVERGENiHBG062475
InParanoidiQ12913
KOiK05698
OrthoDBi411281at2759
PhylomeDBiQ12913
TreeFamiTF351926

Enzyme and pathway databases

BRENDAi3.1.3.48 2681
ReactomeiR-HSA-202427 Phosphorylation of CD3 and TCR zeta chains
R-HSA-6798695 Neutrophil degranulation
R-HSA-6807004 Negative regulation of MET activity
SignaLinkiQ12913
SIGNORiQ12913

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
PTPRJ human
EvolutionaryTraceiQ12913

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PTPRJ

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
5795

Protein Ontology

More...
PROi
PR:Q12913

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000149177 Expressed in 195 organ(s), highest expression level in blood
CleanExiHS_PTPRJ
ExpressionAtlasiQ12913 baseline and differential
GenevisibleiQ12913 HS

Family and domain databases

CDDicd00063 FN3, 5 hits
Gene3Di2.60.40.10, 5 hits
3.90.190.10, 1 hit
InterProiView protein in InterPro
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR013783 Ig-like_fold
IPR029021 Prot-tyrosine_phosphatase-like
IPR000242 PTPase_domain
IPR016130 Tyr_Pase_AS
IPR003595 Tyr_Pase_cat
IPR000387 TYR_PHOSPHATASE_dom
PfamiView protein in Pfam
PF00041 fn3, 1 hit
PF00102 Y_phosphatase, 1 hit
PRINTSiPR00700 PRTYPHPHTASE
SMARTiView protein in SMART
SM00060 FN3, 8 hits
SM00194 PTPc, 1 hit
SM00404 PTPc_motif, 1 hit
SUPFAMiSSF49265 SSF49265, 4 hits
SSF52799 SSF52799, 1 hit
PROSITEiView protein in PROSITE
PS50853 FN3, 6 hits
PS00383 TYR_PHOSPHATASE_1, 1 hit
PS50056 TYR_PHOSPHATASE_2, 1 hit
PS50055 TYR_PHOSPHATASE_PTP, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPTPRJ_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q12913
Secondary accession number(s): Q15255
, Q6P4H4, Q8NHM2, Q9UDA9
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 5, 2008
Last modified: January 16, 2019
This is version 196 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
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