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Entry version 208 (05 Jun 2019)
Sequence version 2 (20 Dec 2005)
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Protein

Tyrosine-protein phosphatase non-receptor type 11

Gene

Ptpn11

Organism
Mus musculus (Mouse)
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 similarity1 Publication

<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 <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-MMU-1059683 Interleukin-6 signaling
R-MMU-109704 PI3K Cascade
R-MMU-110056 MAPK3 (ERK1) activation
R-MMU-112411 MAPK1 (ERK2) activation
R-MMU-114604 GPVI-mediated activation cascade
R-MMU-1257604 PIP3 activates AKT signaling
R-MMU-1433557 Signaling by SCF-KIT
R-MMU-180292 GAB1 signalosome
R-MMU-186763 Downstream signal transduction
R-MMU-210990 PECAM1 interactions
R-MMU-210993 Tie2 Signaling
R-MMU-388841 Costimulation by the CD28 family
R-MMU-389513 CTLA4 inhibitory signaling
R-MMU-389948 PD-1 signaling
R-MMU-432142 Platelet sensitization by LDL
R-MMU-512988 Interleukin-3, Interleukin-5 and GM-CSF signaling
R-MMU-5654689 PI-3K cascade:FGFR1
R-MMU-5654693 FRS-mediated FGFR1 signaling
R-MMU-5654695 PI-3K cascade:FGFR2
R-MMU-5654700 FRS-mediated FGFR2 signaling
R-MMU-5654706 FRS-mediated FGFR3 signaling
R-MMU-5654710 PI-3K cascade:FGFR3
R-MMU-5654712 FRS-mediated FGFR4 signaling
R-MMU-5654720 PI-3K cascade:FGFR4
R-MMU-5654726 Negative regulation of FGFR1 signaling
R-MMU-5654727 Negative regulation of FGFR2 signaling
R-MMU-5654732 Negative regulation of FGFR3 signaling
R-MMU-5654733 Negative regulation of FGFR4 signaling
R-MMU-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-MMU-8853659 RET signaling
R-MMU-8854691 Interleukin-20 family signaling
R-MMU-8865999 MET activates PTPN11
R-MMU-8934593 Regulation of RUNX1 Expression and Activity
R-MMU-909733 Interferon alpha/beta signaling
R-MMU-912694 Regulation of IFNA signaling
R-MMU-936964 Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P35235

<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 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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 5

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:99511 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 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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2620

<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_00000947682 – 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 residuei66PhosphotyrosineCombined sources1
Modified residuei546Phosphotyrosine; by PDGFR1 Publication1
Modified residuei584Phosphotyrosine; by PDGFR1 Publication1

<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 by activated PDGFRB (By similarity). Phosphorylated upon activation of the receptor-type kinase PDGFRA.By similarity3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P35235

MaxQB - The MaxQuant DataBase

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MaxQBi
P35235

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

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PaxDbi
P35235

PeptideAtlas

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PeptideAtlasi
P35235

PRoteomics IDEntifications database

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PRIDEi
P35235

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P35235

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

More...
PhosphoSitePlusi
P35235

<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

Highly expressed in brain, heart and kidney.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000043733 Expressed in 276 organ(s), highest expression level in lens of camera-type eye

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P35235 MM

<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 CD84 and with phosphorylated SIT1 and MZPL1.

Interacts with FCRL4, FCRL6 and ANKHD1.

Interacts with GAREM1 (tyrosine phosphorylated); the interaction increases MAPK/ERK activity and does not affect the GRB2/SOS complex formation (By similarity).

Interacts with PTPNS1 and BCAR3.

Interacts with phosphorylated LIME1.

Interacts with SHB and INPP5D/SHIP1.

Interacts with KIR2DL1; the interaction is enhanced by ARRB2 (By similarity).

Interacts with GAB2.

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 (By similarity).

Interacts with MILR1 (tyrosine phosphorylated).

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

Interacts with ROS1; mediates PTPN11 phosphorylation.

Interacts with PDGFRA (tyrosine phosphorylated).

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

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

Interacts with CEACAM1 (via cytoplasmic domain); this interaction depends on the monomer/dimer equilibrium and is phosphorylation-dependent (PubMed:19948503, PubMed:9867848).

Interacts with MPIG6B (via ITIM motif) (PubMed:23112346).

Interacts with SIGLEC10 (PubMed:23374343).

By similarity20 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
202477, 28 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P35235

Database of interacting proteins

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DIPi
DIP-29669N

Protein interaction database and analysis system

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IntActi
P35235, 34 interactors

Molecular INTeraction database

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MINTi
P35235

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000098333

<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

1597
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P35235

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P35235

<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 – 525Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST279

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

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eggNOGi
KOG0790 Eukaryota
COG5599 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153876

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000273907

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P35235

KEGG Orthology (KO)

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KOi
K07293

Identification of Orthologs from Complete Genome Data

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OMAi
KEYGAMR

Database of Orthologous Groups

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OrthoDBi
411281at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P35235

TreeFam database of animal gene trees

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TreeFami
TF351632

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.505.10, 2 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
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

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

PIRSF; a whole-protein classification database

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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

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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

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SUPFAMi
SSF52799 SSF52799, 1 hit
SSF55550 SSF55550, 2 hits

PROSITE; a protein domain and family database

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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: P35235-1) [UniParc]FASTAAdd to basket

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 NDGKSKVTHV 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 WPDEYALKEY GVMRVRNVKE 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):68,460
Last modified:December 20, 2005 - v2
<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:iC742BED37E39EA23
GO
Isoform 2 (identifier: P35235-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     408-411: Missing.

Show »
Length:593
Mass (Da):68,035
Checksum:i6C71EEEECCF7F159
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 conflicti390E → G in BAE37500 (PubMed:16141072).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_016675408 – 411Missing 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
D84372 mRNA Translation: BAA12328.1
AK159501 mRNA Translation: BAE35134.1
AK159587 mRNA Translation: BAE35207.1
AK163809 mRNA Translation: BAE37500.1
BC057398 mRNA Translation: AAH57398.1
BC059278 mRNA Translation: AAH59278.1
L08663 mRNA No translation available.

The Consensus CDS (CCDS) project

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CCDSi
CCDS39247.1 [P35235-1]
CCDS51637.1 [P35235-2]

Protein sequence database of the Protein Information Resource

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PIRi
A46209

NCBI Reference Sequences

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RefSeqi
NP_001103462.1, NM_001109992.1 [P35235-2]
NP_035332.1, NM_011202.3 [P35235-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000054547; ENSMUSP00000058757; ENSMUSG00000043733 [P35235-1]
ENSMUST00000100770; ENSMUSP00000098333; ENSMUSG00000043733 [P35235-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
19247

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:19247

UCSC genome browser

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UCSCi
uc008zio.2 mouse [P35235-1]
uc008zip.2 mouse [P35235-2]

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
D84372 mRNA Translation: BAA12328.1
AK159501 mRNA Translation: BAE35134.1
AK159587 mRNA Translation: BAE35207.1
AK163809 mRNA Translation: BAE37500.1
BC057398 mRNA Translation: AAH57398.1
BC059278 mRNA Translation: AAH59278.1
L08663 mRNA No translation available.
CCDSiCCDS39247.1 [P35235-1]
CCDS51637.1 [P35235-2]
PIRiA46209
RefSeqiNP_001103462.1, NM_001109992.1 [P35235-2]
NP_035332.1, NM_011202.3 [P35235-1]

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
1AYAX-ray2.05A/B4-103[»]
1AYBX-ray3.00A4-103[»]
1AYCX-ray2.30A4-103[»]
1AYDX-ray2.20A4-103[»]
SMRiP35235
ModBaseiSearch...

Protein-protein interaction databases

BioGridi202477, 28 interactors
CORUMiP35235
DIPiDIP-29669N
IntActiP35235, 34 interactors
MINTiP35235
STRINGi10090.ENSMUSP00000098333

Chemistry databases

ChEMBLiCHEMBL2620

PTM databases

iPTMnetiP35235
PhosphoSitePlusiP35235

Proteomic databases

EPDiP35235
MaxQBiP35235
PaxDbiP35235
PeptideAtlasiP35235
PRIDEiP35235

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000054547; ENSMUSP00000058757; ENSMUSG00000043733 [P35235-1]
ENSMUST00000100770; ENSMUSP00000098333; ENSMUSG00000043733 [P35235-2]
GeneIDi19247
KEGGimmu:19247
UCSCiuc008zio.2 mouse [P35235-1]
uc008zip.2 mouse [P35235-2]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
5781
MGIiMGI:99511 Ptpn11

Phylogenomic databases

eggNOGiKOG0790 Eukaryota
COG5599 LUCA
GeneTreeiENSGT00940000153876
HOGENOMiHOG000273907
InParanoidiP35235
KOiK07293
OMAiKEYGAMR
OrthoDBi411281at2759
PhylomeDBiP35235
TreeFamiTF351632

Enzyme and pathway databases

ReactomeiR-MMU-1059683 Interleukin-6 signaling
R-MMU-109704 PI3K Cascade
R-MMU-110056 MAPK3 (ERK1) activation
R-MMU-112411 MAPK1 (ERK2) activation
R-MMU-114604 GPVI-mediated activation cascade
R-MMU-1257604 PIP3 activates AKT signaling
R-MMU-1433557 Signaling by SCF-KIT
R-MMU-180292 GAB1 signalosome
R-MMU-186763 Downstream signal transduction
R-MMU-210990 PECAM1 interactions
R-MMU-210993 Tie2 Signaling
R-MMU-388841 Costimulation by the CD28 family
R-MMU-389513 CTLA4 inhibitory signaling
R-MMU-389948 PD-1 signaling
R-MMU-432142 Platelet sensitization by LDL
R-MMU-512988 Interleukin-3, Interleukin-5 and GM-CSF signaling
R-MMU-5654689 PI-3K cascade:FGFR1
R-MMU-5654693 FRS-mediated FGFR1 signaling
R-MMU-5654695 PI-3K cascade:FGFR2
R-MMU-5654700 FRS-mediated FGFR2 signaling
R-MMU-5654706 FRS-mediated FGFR3 signaling
R-MMU-5654710 PI-3K cascade:FGFR3
R-MMU-5654712 FRS-mediated FGFR4 signaling
R-MMU-5654720 PI-3K cascade:FGFR4
R-MMU-5654726 Negative regulation of FGFR1 signaling
R-MMU-5654727 Negative regulation of FGFR2 signaling
R-MMU-5654732 Negative regulation of FGFR3 signaling
R-MMU-5654733 Negative regulation of FGFR4 signaling
R-MMU-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-MMU-8853659 RET signaling
R-MMU-8854691 Interleukin-20 family signaling
R-MMU-8865999 MET activates PTPN11
R-MMU-8934593 Regulation of RUNX1 Expression and Activity
R-MMU-909733 Interferon alpha/beta signaling
R-MMU-912694 Regulation of IFNA signaling
R-MMU-936964 Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon
SABIO-RKiP35235

Miscellaneous databases

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

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ChiTaRSi
Ptpn11 mouse
EvolutionaryTraceiP35235

Protein Ontology

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PROi
PR:P35235

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000043733 Expressed in 276 organ(s), highest expression level in lens of camera-type eye
GenevisibleiP35235 MM

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
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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 nameiPTN11_MOUSE
<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: P35235
Secondary accession number(s): Q3TQ84, Q64509, Q6PCL5
<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: February 1, 1994
Last sequence update: December 20, 2005
Last modified: June 5, 2019
This is version 208 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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