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Entry version 184 (13 Nov 2019)
Sequence version 4 (20 Dec 2005)
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Protein

Tyrosine-protein phosphatase non-receptor type 11

Gene

Ptpn11

Organism
Rattus norvegicus (Rat)
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

Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Positively regulates MAPK signal transduction pathway. Dephosphorylates GAB1, ARHGAP35 and EGFR. Dephosphorylates ROCK2 at 'Tyr-722' resulting in stimulatation of its RhoA binding activity. Dephosphorylates CDC73.By similarity

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by orthovanadate, molybdate and spermidine.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=15 mM for pNPP1 Publication
  2. KM=13 µM for nAChR1 Publication
  3. KM=67 nM for MBP1 Publication
  1. Vmax=16 µmol/min/mg enzyme toward pNPP1 Publication
  2. Vmax=98 nmol/min/mg enzyme toward nAChR1 Publication
  3. Vmax=15 µmol/min/mg enzyme toward MBP1 Publication

pH dependencei

Optimum pH is 8.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei429SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei463Phosphocysteine intermediatePROSITE-ProRule annotation1
Binding sitei510SubstrateBy 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

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1059683 Interleukin-6 signaling
R-RNO-109704 PI3K Cascade
R-RNO-110056 MAPK3 (ERK1) activation
R-RNO-112411 MAPK1 (ERK2) activation
R-RNO-114604 GPVI-mediated activation cascade
R-RNO-1257604 PIP3 activates AKT signaling
R-RNO-1295596 Spry regulation of FGF signaling
R-RNO-1433557 Signaling by SCF-KIT
R-RNO-180292 GAB1 signalosome
R-RNO-186763 Downstream signal transduction
R-RNO-210993 Tie2 Signaling
R-RNO-388841 Costimulation by the CD28 family
R-RNO-389513 CTLA4 inhibitory signaling
R-RNO-389948 PD-1 signaling
R-RNO-512988 Interleukin-3, Interleukin-5 and GM-CSF signaling
R-RNO-5654689 PI-3K cascade:FGFR1
R-RNO-5654693 FRS-mediated FGFR1 signaling
R-RNO-5654695 PI-3K cascade:FGFR2
R-RNO-5654700 FRS-mediated FGFR2 signaling
R-RNO-5654706 FRS-mediated FGFR3 signaling
R-RNO-5654710 PI-3K cascade:FGFR3
R-RNO-5654712 FRS-mediated FGFR4 signaling
R-RNO-5654720 PI-3K cascade:FGFR4
R-RNO-5654726 Negative regulation of FGFR1 signaling
R-RNO-5654727 Negative regulation of FGFR2 signaling
R-RNO-5654732 Negative regulation of FGFR3 signaling
R-RNO-5654733 Negative regulation of FGFR4 signaling
R-RNO-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-RNO-8853659 RET signaling
R-RNO-8854691 Interleukin-20 family signaling
R-RNO-8865999 MET activates PTPN11
R-RNO-8934593 Regulation of RUNX1 Expression and Activity
R-RNO-909733 Interferon alpha/beta signaling
R-RNO-912694 Regulation of IFNA signaling
R-RNO-936964 Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon

<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:
Tyrosine-protein phosphatase non-receptor type 11 (EC:3.1.3.48By similarity)
Alternative name(s):
Protein-tyrosine phosphatase 1D
Short name:
PTP-1D
Protein-tyrosine phosphatase SYP
SH-PTP2
Short name:
SHP-2
Short name:
Shp2
<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:Ptpn11
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 12

Organism-specific databases

Rat genome database

More...
RGDi
3447 Ptpn11

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

<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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<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_00000947692 – 597Tyrosine-protein phosphatase non-receptor type 11Add BLAST596

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei2N-acetylthreonineBy similarity1
Modified residuei62PhosphotyrosineCombined sources1
Modified residuei66PhosphotyrosineBy similarity1
Modified residuei546Phosphotyrosine; by PDGFRBy similarity1
Modified residuei584Phosphotyrosine; by PDGFRBy similarity1

<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

Phosphorylated on Tyr-546 and Tyr-584 upon receptor protein tyrosine kinase activation; which creates a binding site for GRB2 and other SH2-containing proteins. Phosphorylated upon activation of the receptor-type kinase FLT3. Phosphorylated upon activation of the receptor-type kinase PDGFRA. Phosphorylated by activated PDGFRB (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P41499

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

More...
PaxDbi
P41499

PRoteomics IDEntifications database

More...
PRIDEi
P41499

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P41499

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

More...
PhosphoSitePlusi
P41499

<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 brain, muscle and lung.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000030124 Expressed in 9 organ(s), highest expression level in Ammon's horn

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P41499 RN

<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

Interacts with phosphorylated SIT1, LIME1, BCAR3 and MZPL1.

Interacts with FCRL4, FCRL6, ANKHD1, SHB, INPP5D/SHIP1 and CD84 (By similarity).

Interacts with MILR1 (tyrosine-phosphorylated).

Interacts with FLT1 (tyrosine-phosphorylated), FLT3 (tyrosine-phosphorylated), FLT4 (tyrosine-phosphorylated), KIT and GRB2 (By similarity).

Interacts with PTPNS1.

Interacts with KIR2DL1; the interaction is enhanced by ARRB2.

Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated) (By similarity).

Interacts with GAB2 (By similarity).

Interacts with TERT; the interaction retains TERT in the nucleus.

Interacts with PECAM1 and FER.

Interacts with EPHA2 (activated); participates in PTK2/FAK1 dephosphorylation in EPHA2 downstream signaling.

Interacts with PDGFRA (tyrosine phosphorylated).

Interacts with PDGFRB (tyrosine phosphorylated); this interaction increases the PTPN11 phosphatase activity (By similarity).

Interacts with ROS1; this mediates PTPN11 phosphorylation.

Interacts with CEACAM1 (via cytoplasmic domain); this interaction depends on the monomer/dimer equilibrium and is phosphorylation-dependent (By similarity).

Interacts with MPIG6B (via ITIM motif) (By similarity).

Interacts with SIGLEC10 (By similarity).

By similarity3 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)

More...
BioGridi
247651, 5 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
P41499

Database of interacting proteins

More...
DIPi
DIP-47397N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P41499

Protein interaction database and analysis system

More...
IntActi
P41499, 11 interactors

Molecular INTeraction database

More...
MINTi
P41499

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000041842

<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

3D structure databases

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

More...
SMRi
P41499

Database of comparative protein structure models

More...
ModBasei
Search...

<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>Domaini6 – 102SH2 1PROSITE-ProRule annotationAdd BLAST97
Domaini112 – 216SH2 2PROSITE-ProRule annotationAdd BLAST105
Domaini247 – 521Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST275

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>Regioni463 – 469Substrate bindingBy similarity7

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The SH2 domains repress phosphatase activity. Binding of these domains to phosphotyrosine-containing proteins relieves this auto-inhibition, possibly by inducing a conformational change in the enzyme.

<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, SH2 domain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0790 Eukaryota
COG5599 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153876

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000273907

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P41499

KEGG Orthology (KO)

More...
KOi
K07293

Identification of Orthologs from Complete Genome Data

More...
OMAi
GKPKVTH

Database of Orthologous Groups

More...
OrthoDBi
411281at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P41499

TreeFam database of animal gene trees

More...
TreeFami
TF351632

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.505.10, 2 hits
3.90.190.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029021 Prot-tyrosine_phosphatase-like
IPR000242 PTPase_domain
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR016130 Tyr_Pase_AS
IPR003595 Tyr_Pase_cat
IPR012152 Tyr_Pase_non-rcpt_typ-6/11
IPR000387 TYR_PHOSPHATASE_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00017 SH2, 2 hits
PF00102 Y_phosphatase, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000929 Tyr-Ptase_nr_6, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00700 PRTYPHPHTASE
PR00401 SH2DOMAIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00194 PTPc, 1 hit
SM00404 PTPc_motif, 1 hit
SM00252 SH2, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52799 SSF52799, 1 hit
SSF55550 SSF55550, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50001 SH2, 2 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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
Isoform 1 (identifier: P41499-1) [UniParc]FASTAAdd to basket
Also known as: PTP1Di

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
        10         20         30         40         50
MTSRRWFHPN ITGVEAENLL LTRGVDGSFL ARPSKSNPGD FTLSVRRNGA
60 70 80 90 100
VTHIKIQNTG DYYDLYGGEK FATLAELVQY YMEHHGQLKE KNGDVIELKY
110 120 130 140 150
PLNCADPTSE RWFHGHLSGK EAEKLLTEKG KHGSFLVRES QSHPGDFVLS
160 170 180 190 200
VRTGDDKGES NDSKSKVTHV MIRCQELKYD VGGGERFDSL TDLVEHYKKN
210 220 230 240 250
PMVETLGTVL QLKQPLNTTR INAAEIESRV RELSKLAETT DKVKQGFWEE
260 270 280 290 300
FETLQQQECK LLYSRKEGQR QENKNKNRYK NILPFDHTRV VLHDGDPNEP
310 320 330 340 350
VSDYINANII MPEFETKCNN SKPKKSYIAT QGCLQNTVND FWRMVFQENS
360 370 380 390 400
RVIVMTTKEV ERGKSKCVKY WPDECALKEY GVMRVRNVRE SAAHDYTLRE
410 420 430 440 450
LKLSKVGQAL LQGNTERTVW QYHFRTWPDH GVPSDPGGVL DFLEEVHHKQ
460 470 480 490 500
ESIVDAGPVV VHCSAGIGRT GTFIVIDILI DIIREKGVDC DIDVPKTIQM
510 520 530 540 550
VRSQRSGMVQ TEAQYRFIYM AVQHYIETLQ RRIEEEQKSK RKGHEYTNIK
560 570 580 590
YSLVDQTSGD QSPLPPCTPT PPCAEMREDS ARVYENVGLM QQQRSFR
Length:597
Mass (Da):68,458
Last modified:December 20, 2005 - v4
<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:i7155D1E99161F5C2
GO
Isoform 2 (identifier: P41499-2) [UniParc]FASTAAdd to basket
Also known as: PTP1D

The sequence of this isoform differs from the canonical sequence as follows:
     409-412: Missing.

Note: Much higher phosphatase activity than isoform 1, optimum pH is 7.
Show »
Length:593
Mass (Da):68,033
Checksum:i3329F10F0F60AF48
GO

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 conflicti75A → P in AAA20543 (PubMed:8048963).Curated1
Sequence conflicti551Y → S in AAA19133 (PubMed:7512964).Curated1

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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_016676409 – 412Missing in isoform 2. 2 Publications4

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U09307 mRNA Translation: AAA20543.1
U05963 mRNA Translation: AAA19133.1

Protein sequence database of the Protein Information Resource

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PIRi
A53593

NCBI Reference Sequences

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RefSeqi
NP_001171064.1, NM_001177593.1 [P41499-1]
NP_037220.2, NM_013088.2 [P41499-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSRNOT00000046323; ENSRNOP00000041842; ENSRNOG00000030124 [P41499-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
25622

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
rno:25622

UCSC genome browser

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UCSCi
RGD:3447 rat [P41499-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09307 mRNA Translation: AAA20543.1
U05963 mRNA Translation: AAA19133.1
PIRiA53593
RefSeqiNP_001171064.1, NM_001177593.1 [P41499-1]
NP_037220.2, NM_013088.2 [P41499-2]

3D structure databases

SMRiP41499
ModBaseiSearch...

Protein-protein interaction databases

BioGridi247651, 5 interactors
CORUMiP41499
DIPiDIP-47397N
ELMiP41499
IntActiP41499, 11 interactors
MINTiP41499
STRINGi10116.ENSRNOP00000041842

PTM databases

iPTMnetiP41499
PhosphoSitePlusiP41499

Proteomic databases

jPOSTiP41499
PaxDbiP41499
PRIDEiP41499

Genome annotation databases

EnsembliENSRNOT00000046323; ENSRNOP00000041842; ENSRNOG00000030124 [P41499-1]
GeneIDi25622
KEGGirno:25622
UCSCiRGD:3447 rat [P41499-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5781
RGDi3447 Ptpn11

Phylogenomic databases

eggNOGiKOG0790 Eukaryota
COG5599 LUCA
GeneTreeiENSGT00940000153876
HOGENOMiHOG000273907
InParanoidiP41499
KOiK07293
OMAiGKPKVTH
OrthoDBi411281at2759
PhylomeDBiP41499
TreeFamiTF351632

Enzyme and pathway databases

ReactomeiR-RNO-1059683 Interleukin-6 signaling
R-RNO-109704 PI3K Cascade
R-RNO-110056 MAPK3 (ERK1) activation
R-RNO-112411 MAPK1 (ERK2) activation
R-RNO-114604 GPVI-mediated activation cascade
R-RNO-1257604 PIP3 activates AKT signaling
R-RNO-1295596 Spry regulation of FGF signaling
R-RNO-1433557 Signaling by SCF-KIT
R-RNO-180292 GAB1 signalosome
R-RNO-186763 Downstream signal transduction
R-RNO-210993 Tie2 Signaling
R-RNO-388841 Costimulation by the CD28 family
R-RNO-389513 CTLA4 inhibitory signaling
R-RNO-389948 PD-1 signaling
R-RNO-512988 Interleukin-3, Interleukin-5 and GM-CSF signaling
R-RNO-5654689 PI-3K cascade:FGFR1
R-RNO-5654693 FRS-mediated FGFR1 signaling
R-RNO-5654695 PI-3K cascade:FGFR2
R-RNO-5654700 FRS-mediated FGFR2 signaling
R-RNO-5654706 FRS-mediated FGFR3 signaling
R-RNO-5654710 PI-3K cascade:FGFR3
R-RNO-5654712 FRS-mediated FGFR4 signaling
R-RNO-5654720 PI-3K cascade:FGFR4
R-RNO-5654726 Negative regulation of FGFR1 signaling
R-RNO-5654727 Negative regulation of FGFR2 signaling
R-RNO-5654732 Negative regulation of FGFR3 signaling
R-RNO-5654733 Negative regulation of FGFR4 signaling
R-RNO-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-RNO-8853659 RET signaling
R-RNO-8854691 Interleukin-20 family signaling
R-RNO-8865999 MET activates PTPN11
R-RNO-8934593 Regulation of RUNX1 Expression and Activity
R-RNO-909733 Interferon alpha/beta signaling
R-RNO-912694 Regulation of IFNA signaling
R-RNO-936964 Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon

Miscellaneous databases

Protein Ontology

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PROi
PR:P41499

Gene expression databases

BgeeiENSRNOG00000030124 Expressed in 9 organ(s), highest expression level in Ammon's horn
GenevisibleiP41499 RN

Family and domain databases

Gene3Di3.30.505.10, 2 hits
3.90.190.10, 1 hit
InterProiView protein in InterPro
IPR029021 Prot-tyrosine_phosphatase-like
IPR000242 PTPase_domain
IPR000980 SH2
IPR036860 SH2_dom_sf
IPR016130 Tyr_Pase_AS
IPR003595 Tyr_Pase_cat
IPR012152 Tyr_Pase_non-rcpt_typ-6/11
IPR000387 TYR_PHOSPHATASE_dom
PfamiView protein in Pfam
PF00017 SH2, 2 hits
PF00102 Y_phosphatase, 1 hit
PIRSFiPIRSF000929 Tyr-Ptase_nr_6, 1 hit
PRINTSiPR00700 PRTYPHPHTASE
PR00401 SH2DOMAIN
SMARTiView protein in SMART
SM00194 PTPc, 1 hit
SM00404 PTPc_motif, 1 hit
SM00252 SH2, 2 hits
SUPFAMiSSF52799 SSF52799, 1 hit
SSF55550 SSF55550, 2 hits
PROSITEiView protein in PROSITE
PS50001 SH2, 2 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

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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 nameiPTN11_RAT
<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: P41499
Secondary accession number(s): Q62626
<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, 1995
Last sequence update: December 20, 2005
Last modified: November 13, 2019
This is version 184 of the entry and version 4 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

<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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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