Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q06124 (PTN11_HUMAN)

Entry version 246 (07 Apr 2021)
Sequence version 3 (11 Dec 2019)
Previous versions | rss
Add a publicationFeedback
Protein

Tyrosine-protein phosphatase non-receptor type 11

Gene

PTPN11

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

Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus (PubMed:10655584, PubMed:18559669, PubMed:18829466, PubMed:26742426, PubMed:28074573). Positively regulates MAPK signal transduction pathway (PubMed:28074573). Dephosphorylates GAB1, ARHGAP35 and EGFR (PubMed:28074573). Dephosphorylates ROCK2 at 'Tyr-722' resulting in stimulation of its RhoA binding activity (PubMed:18559669). Dephosphorylates CDC73 (PubMed:26742426). Dephosphorylates SOX9 on tyrosine residues, leading to inactivate SOX9 and promote ossification (By similarity).By similarity5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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%5Fsection">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 sitei425SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei459Phosphocysteine intermediate1
Binding sitei506SubstrateBy 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

More...BRENDAi		3.1.3.48, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q06124

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1059683, Interleukin-6 signaling
R-HSA-109704, PI3K Cascade
R-HSA-110056, MAPK3 (ERK1) activation
R-HSA-112411, MAPK1 (ERK2) activation
R-HSA-114604, GPVI-mediated activation cascade
R-HSA-1170546, Prolactin receptor signaling
R-HSA-1257604, PIP3 activates AKT signaling
R-HSA-1295596, Spry regulation of FGF signaling
R-HSA-1433557, Signaling by SCF-KIT
R-HSA-180292, GAB1 signalosome
R-HSA-186763, Downstream signal transduction
R-HSA-210990, PECAM1 interactions
R-HSA-210993, Tie2 Signaling
R-HSA-2219530, Constitutive Signaling by Aberrant PI3K in Cancer
R-HSA-2586552, Signaling by Leptin
R-HSA-388841, Costimulation by the CD28 family
R-HSA-389513, CTLA4 inhibitory signaling
R-HSA-389948, PD-1 signaling
R-HSA-391160, Signal regulatory protein family interactions
R-HSA-418886, Netrin mediated repulsion signals
R-HSA-432142, Platelet sensitization by LDL
R-HSA-512988, Interleukin-3, Interleukin-5 and GM-CSF signaling
R-HSA-5654689, PI-3K cascade:FGFR1
R-HSA-5654693, FRS-mediated FGFR1 signaling
R-HSA-5654695, PI-3K cascade:FGFR2
R-HSA-5654700, FRS-mediated FGFR2 signaling
R-HSA-5654706, FRS-mediated FGFR3 signaling
R-HSA-5654710, PI-3K cascade:FGFR3
R-HSA-5654712, FRS-mediated FGFR4 signaling
R-HSA-5654720, PI-3K cascade:FGFR4
R-HSA-5654726, Negative regulation of FGFR1 signaling
R-HSA-5654727, Negative regulation of FGFR2 signaling
R-HSA-5654732, Negative regulation of FGFR3 signaling
R-HSA-5654733, Negative regulation of FGFR4 signaling
R-HSA-6811558, PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-877312, Regulation of IFNG signaling
R-HSA-8853659, RET signaling
R-HSA-8854691, Interleukin-20 family signaling
R-HSA-8865999, MET activates PTPN11
R-HSA-8934593, Regulation of RUNX1 Expression and Activity
R-HSA-9008059, Interleukin-37 signaling
R-HSA-9028731, Activated NTRK2 signals through FRS2 and FRS3
R-HSA-909733, Interferon alpha/beta signaling
R-HSA-912694, Regulation of IFNA signaling
R-HSA-936964, Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon
R-HSA-9607240, FLT3 Signaling
R-HSA-9645135, STAT5 Activation
R-HSA-9702518, STAT5 activation downstream of FLT3 ITD mutants
R-HSA-9703648, Signaling by FLT3 ITD and TKD mutants

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

More...SignaLinki		Q06124

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q06124

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...MoonDBi		Q06124, Predicted

<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%5Fand%5Ftaxonomy%5Fsection">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:3.1.3.482 Publications)
Alternative name(s):
Protein-tyrosine phosphatase 1D
Short name:
PTP-1D
Protein-tyrosine phosphatase 2C
Short name:
PTP-2C
SH-PTP2
Short name:
SHP-2
Short name:
Shp2
SH-PTP3
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
Synonyms:PTP2C, SHPTP2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

Human Gene Nomenclature Database

More...HGNCi		HGNC:9644, PTPN11

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		176876, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q06124

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000179295.16

<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

Keywords - Cellular componenti

Cytoplasm, Nucleus

<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

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

LEOPARD syndrome 1 (LPRD1)10 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA disorder characterized by lentigines, electrocardiographic conduction abnormalities, ocular hypertelorism, pulmonic stenosis, abnormalities of genitalia, retardation of growth, and sensorineural deafness.
Related information in OMIM
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_015614279Y → C in NS1 and LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73. 7 PublicationsCorresponds to variant dbSNP:rs121918456EnsemblClinVar.1
Natural variantiVAR_027188279Y → S in LPRD1. 2 PublicationsCorresponds to variant dbSNP:rs121918456EnsemblClinVar.1
Natural variantiVAR_027190461A → T in LPRD1. 1 PublicationCorresponds to variant dbSNP:rs121918468EnsemblClinVar.1
Natural variantiVAR_027191464G → A in LPRD1. 2 PublicationsCorresponds to variant dbSNP:rs121918469EnsemblClinVar.1
Natural variantiVAR_015621468T → M in LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73. 5 PublicationsCorresponds to variant dbSNP:rs121918457EnsemblClinVar.1
Natural variantiVAR_027192498R → L in LPRD1. 1 PublicationCorresponds to variant dbSNP:rs397507542EnsemblClinVar.1
Natural variantiVAR_027193498R → W in LPRD1; reduced phosphatase activity. 2 PublicationsCorresponds to variant dbSNP:rs397507541EnsemblClinVar.1
Natural variantiVAR_027194506Q → P in LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73. 4 PublicationsCorresponds to variant dbSNP:rs397509345EnsemblClinVar.1
Natural variantiVAR_076499510Q → E in NS1 and LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73. 3 PublicationsCorresponds to variant dbSNP:rs397507549EnsemblClinVar.1
Natural variantiVAR_027196510Q → P in LPRD1. 1 PublicationCorresponds to variant dbSNP:rs121918470EnsemblClinVar.1
Noonan syndrome 1 (NS1)15 Publications
The disease is caused by variants affecting the gene represented in this entry. Mutations in PTPN11 account for more than 50% of the cases.
Disease descriptionA form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells. Some patients with NS1 develop multiple giant cell lesions of the jaw or other bony or soft tissues, which are classified as pigmented villonodular synovitis (PVNS) when occurring in the jaw or joints.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0271832T → I in NS1. 1 PublicationCorresponds to variant dbSNP:rs267606990EnsemblClinVar.1
Natural variantiVAR_01560142T → A in NS1. 2 PublicationsCorresponds to variant dbSNP:rs397507501EnsemblClinVar.1
Natural variantiVAR_02718458N → K in NS1. 1 PublicationCorresponds to variant dbSNP:rs397507506EnsemblClinVar.1
Natural variantiVAR_06606059T → A in NS1. 1 PublicationCorresponds to variant dbSNP:rs886043790EnsemblClinVar.1
Natural variantiVAR_01560260G → A in NS1. 1 PublicationCorresponds to variant dbSNP:rs397507509EnsemblClinVar.1
Natural variantiVAR_01560361D → G in NS1. 4 PublicationsCorresponds to variant dbSNP:rs121918461EnsemblClinVar.1
Natural variantiVAR_01560461D → N in NS1. 2 PublicationsCorresponds to variant dbSNP:rs397507510EnsemblClinVar.1
Natural variantiVAR_01560562Y → D in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 PublicationsCorresponds to variant dbSNP:rs121918460EnsemblClinVar.1
Natural variantiVAR_01560663Y → C in NS1. 6 PublicationsCorresponds to variant dbSNP:rs121918459EnsemblClinVar.1
Natural variantiVAR_02718569E → Q in NS1. 1 PublicationCorresponds to variant dbSNP:rs397507511EnsemblClinVar.1
Natural variantiVAR_01599571F → L in NS1; also found in myelodysplastic syndrome. 2 PublicationsCorresponds to variant dbSNP:rs397507512EnsemblClinVar.1
Natural variantiVAR_01560772A → G in NS1. 3 PublicationsCorresponds to variant dbSNP:rs121918454EnsemblClinVar.1
Natural variantiVAR_01560872A → S in NS1. 3 PublicationsCorresponds to variant dbSNP:rs121918453EnsemblClinVar.1
Natural variantiVAR_01560973T → I in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 PublicationsCorresponds to variant dbSNP:rs121918462EnsemblClinVar.1
Natural variantiVAR_01561076E → D in NS1. 3 PublicationsCorresponds to variant dbSNP:rs397507514EnsemblClinVar.1
Natural variantiVAR_02718679Q → P in NS1. 1 Publication1
Natural variantiVAR_01561179Q → R in NS1. 4 PublicationsCorresponds to variant dbSNP:rs121918466EnsemblClinVar.1
Natural variantiVAR_015612106D → A in NS1. 2 PublicationsCorresponds to variant dbSNP:rs397507517EnsemblClinVar.1
Natural variantiVAR_015613139E → D in NS1. 2 PublicationsCorresponds to variant dbSNP:rs397507520EnsemblClinVar.1
Natural variantiVAR_027187256Q → R in NS1. 1 PublicationCorresponds to variant dbSNP:rs397507523EnsemblClinVar.1
Natural variantiVAR_078101261L → F in NS1; increases MAPK signaling; increases protein tyrosine phosphatase activity; changed substrate selectivity for GAB1. 1 PublicationCorresponds to variant dbSNP:rs397507525EnsemblClinVar.1
Natural variantiVAR_078102261L → H in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity. 1 PublicationCorresponds to variant dbSNP:rs765642157EnsemblClinVar.1
Natural variantiVAR_078103262L → F in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity. 1 Publication1
Natural variantiVAR_078104262L → R in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity. 1 PublicationCorresponds to variant dbSNP:rs397507526EnsemblClinVar.1
Natural variantiVAR_078105265R → Q in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity. 1 PublicationCorresponds to variant dbSNP:rs376607329EnsemblClinVar.1
Natural variantiVAR_015614279Y → C in NS1 and LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73. 7 PublicationsCorresponds to variant dbSNP:rs121918456EnsemblClinVar.1
Natural variantiVAR_015615282I → V in NS1. 3 PublicationsCorresponds to variant dbSNP:rs397507529EnsemblClinVar.1
Natural variantiVAR_015617285F → L in NS1. 1 PublicationCorresponds to variant dbSNP:rs397507531EnsemblClinVar.1
Natural variantiVAR_015616285F → S in NS1. 2 PublicationsCorresponds to variant dbSNP:rs121918463EnsemblClinVar.1
Natural variantiVAR_015619308N → D in NS1; common mutation. 5 PublicationsCorresponds to variant dbSNP:rs28933386EnsemblClinVar.1
Natural variantiVAR_015618308N → S in NS1; some patients also manifest giant cell lesions of bone and soft tissue. 2 PublicationsCorresponds to variant dbSNP:rs121918455EnsemblClinVar.1
Natural variantiVAR_015620309I → V in NS1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs201787206EnsemblClinVar.1
Natural variantiVAR_027189411T → M in NS1. 1 PublicationCorresponds to variant dbSNP:rs121918467EnsemblClinVar.1
Natural variantiVAR_071706491P → S in NS1; increased phosphatase activity. 1 PublicationCorresponds to variant dbSNP:rs397507539EnsemblClinVar.1
Natural variantiVAR_015622501R → K in NS1. 1 PublicationCorresponds to variant dbSNP:rs397507543EnsemblClinVar.1
Natural variantiVAR_015623502S → T in NS1. 2 PublicationsCorresponds to variant dbSNP:rs121918458EnsemblClinVar.1
Natural variantiVAR_016003503G → R in NS1 and JMML; JMML patient also shows growth retardation and pulmonic stenosis. 2 PublicationsCorresponds to variant dbSNP:rs397507545EnsemblClinVar.1
Natural variantiVAR_015624504M → V in NS1. 3 PublicationsCorresponds to variant dbSNP:rs397507547EnsemblClinVar.1
Natural variantiVAR_027195506Q → R in NS1. 1 Publication1
Natural variantiVAR_076499510Q → E in NS1 and LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73. 3 PublicationsCorresponds to variant dbSNP:rs397507549EnsemblClinVar.1
Natural variantiVAR_027197560L → F in NS1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs397516797EnsemblClinVar.1
Leukemia, juvenile myelomonocytic (JMML)2 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01599161D → V in JMML; also in myelodysplastic syndrome. 1 PublicationCorresponds to variant dbSNP:rs121918461EnsemblClinVar.1
Natural variantiVAR_01599261D → Y in JMML. 1 PublicationCorresponds to variant dbSNP:rs397507510EnsemblClinVar.1
Natural variantiVAR_01599369E → K in JMML; also in myelodysplastic syndrome. 1 PublicationCorresponds to variant dbSNP:rs397507511EnsemblClinVar.1
Natural variantiVAR_01599672A → T in JMML. 1 PublicationCorresponds to variant dbSNP:rs121918453EnsemblClinVar.1
Natural variantiVAR_01599772A → V in JMML. 1 PublicationCorresponds to variant dbSNP:rs121918454EnsemblClinVar.1
Natural variantiVAR_01599876E → A in JMML; also in myelodysplastic syndrome. 1 PublicationCorresponds to variant dbSNP:rs121918465EnsemblClinVar.1
Natural variantiVAR_01599976E → G in JMML. 1 PublicationCorresponds to variant dbSNP:rs121918465EnsemblClinVar.1
Natural variantiVAR_01600076E → K in JMML; increases protein tyrosine phosphatase activity against CDC73. 2 PublicationsCorresponds to variant dbSNP:rs121918464EnsemblClinVar.1
Natural variantiVAR_01600176E → V in JMML. 1 PublicationCorresponds to variant dbSNP:rs121918465EnsemblClinVar.1
Natural variantiVAR_016002503G → A in JMML. 1 PublicationCorresponds to variant dbSNP:rs397507546EnsemblClinVar.1
Natural variantiVAR_016003503G → R in NS1 and JMML; JMML patient also shows growth retardation and pulmonic stenosis. 2 PublicationsCorresponds to variant dbSNP:rs397507545EnsemblClinVar.1
Metachondromatosis (MC)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA skeletal disorder with radiologic features of both multiple exostoses and Ollier disease, characterized by the presence of exostoses, commonly of the bones of the hands and feet, and enchondromas of the metaphyses of long bones and iliac crest.
Related information in OMIM

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi459C → S: Abolishes phosphatase activity. 1 Publication1

Keywords - Diseasei

Deafness, Disease variant

Organism-specific databases

DisGeNET

More...DisGeNETi		5781

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		PTPN11

MalaCards human disease database

More...MalaCardsi		PTPN11
MIMi151100, phenotype
156250, phenotype
163950, phenotype
607785, phenotype

Open Targets

More...OpenTargetsi		ENSG00000179295

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		86834, Juvenile myelomonocytic leukemia
2499, Metachondromatosis
648, Noonan syndrome
500, Noonan syndrome with multiple lentigines

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33986

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q06124, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL3864

Drug and drug target database

More...DrugBanki		DB02779, Dodecyltrimethylammonium

DrugCentral

More...DrugCentrali		Q06124

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PTPN11

Domain mapping of disease mutations (DMDM)

More...DMDMi		84028248

<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%5Fprocessing%5Fsection">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 methionineiRemovedCombined sources
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000947672 – 593Tyrosine-protein phosphatase non-receptor type 11Add BLAST592

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-acetylthreonineCombined sources1
Modified residuei62PhosphotyrosineCombined sources1
Modified residuei66PhosphotyrosineBy similarity1
Modified residuei542Phosphotyrosine; by PDGFRBy similarity1
Modified residuei580Phosphotyrosine; by PDGFRCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-542 and Tyr-580 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 (By similarity). Phosphorylated by activated PDGFRB.By similarity4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-1556

Encyclopedia of Proteome Dynamics

More...EPDi		Q06124

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q06124

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q06124

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q06124

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

More...PaxDbi		Q06124

PeptideAtlas

More...PeptideAtlasi		Q06124

PRoteomics IDEntifications database

More...PRIDEi		Q06124

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		58414 [Q06124-1]
58415 [Q06124-2]
58416 [Q06124-3]

Consortium for Top Down Proteomics

More...TopDownProteomicsi		Q06124-2 [Q06124-2]

PTM databases

DEPOD human dephosphorylation database

More...DEPODi		PTPN11

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q06124

MetOSite database of methionine sulfoxide sites

More...MetOSitei		Q06124

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

More...PhosphoSitePlusi		Q06124

<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

Widely expressed, with highest levels in heart, brain, and skeletal muscle.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000179295, Expressed in substantia nigra and 254 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q06124, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q06124, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000179295, Low tissue specificity

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with phosphorylated LIME1 and BCAR3.

Interacts with SHB and INPP5D/SHIP1 (By similarity).

Interacts with MILR1 (tyrosine-phosphorylated).

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

Interacts with PDGFRA (tyrosine phosphorylated).

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

Interacts with PTPNS1 and CD84.

Interacts with phosphorylated SIT1 and MPZL1.

Interacts with FCRL4, FCRL6 and ANKHD1.

Interacts with KIR2DL1; the interaction is enhanced by ARRB2.

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.

Interacts with ROS1; mediates PTPN11 phosphorylation.

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

Interacts with GAREM1 isoform 1 (tyrosine phosphorylated); the interaction increases MAPK/ERK activity and does not affect the GRB2/SOS complex formation.

Interacts with CDC73 (PubMed:26742426).

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) (PubMed:23112346).

Interacts with SIGLEC10 (By similarity).

Interacts with FCRL3 (via phosphorylated ITIM motifs) (PubMed:11162587, PubMed:19843936).

By similarity27 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111745, 240 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q06124

Database of interacting proteins

More...DIPi		DIP-516N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q06124

Protein interaction database and analysis system

More...IntActi		Q06124, 176 interactors

Molecular INTeraction database

More...MINTi		Q06124

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000340944

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		Q06124

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q06124, protein

<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

1593
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Small Angle Scattering Biological Data Bank

More...SASBDBi		Q06124

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

More...SMRi		Q06124

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q06124

<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%5Fand%5Fdomains%5Fsection">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 – 517Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST271

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>Regioni459 – 465Substrate 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

Belongs to the protein-tyrosine phosphatase family. Non-receptor class 2 subfamily.Curated

Keywords - Domaini

Repeat, SH2 domain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0790, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000153876

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_001645_9_10_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q06124

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		Q06124

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

More...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%5Flength">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 (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 3 <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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q06124-2) [UniParc]FASTAAdd to basket
Also known as: PTP2C

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
LKLSKVGQGN TERTVWQYHF RTWPDHGVPS DPGGVLDFLE EVHHKQESIM 
       460        470        480        490        500
DAGPVVVHCS AGIGRTGTFI VIDILIDIIR EKGVDCDIDV PKTIQMVRSQ 
       510        520        530        540        550
RSGMVQTEAQ YRFIYMAVQH YIETLQRRIE EEQKSKRKGH EYTNIKYSLA 
       560        570        580        590 
DQTSGDQSPL PPCTPTPPCA EMREDSARVY ENVGLMQQQK SFR
Length:593
Mass (Da):68,011
Last modified:December 11, 2019 - 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:i9CDBEFFA5E6CCB45
GO
Isoform 2 (identifier: Q06124-1) [UniParc]FASTAAdd to basket
Also known as: PTP2Ci

The sequence of this isoform differs from the canonical sequence as follows:
     407-407: G → GQALL

Show »
Length:597
Mass (Da):68,436
Checksum:i37E8BFC7ECA2D03F
GO
Isoform 3 (identifier: Q06124-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     460-460: S → R
     461-593: Missing.

Show »
Length:460
Mass (Da):52,828
Checksum:iEB8E1553B37F1CC0
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 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0U1RRI0A0A0U1RRI0_HUMAN
Tyrosine-protein phosphatase non-re...
PTPN11
196Annotation 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>
H0YF12H0YF12_HUMAN
Tyrosine-protein phosphatase non-re...
PTPN11
108Annotation 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>
A0A1W2PPU4A0A1W2PPU4_HUMAN
Tyrosine-protein phosphatase non-re...
PTPN11
216Annotation 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 conflicti535S → R in BAA02740 (PubMed:8216283).Curated1
Sequence conflicti548S → P in BAA02740 (PubMed:8216283).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0271832T → I in NS1. 1 PublicationCorresponds to variant dbSNP:rs267606990EnsemblClinVar.1
Natural variantiVAR_01560142T → A in NS1. 2 PublicationsCorresponds to variant dbSNP:rs397507501EnsemblClinVar.1
Natural variantiVAR_02718458N → K in NS1. 1 PublicationCorresponds to variant dbSNP:rs397507506EnsemblClinVar.1
Natural variantiVAR_06606059T → A in NS1. 1 PublicationCorresponds to variant dbSNP:rs886043790EnsemblClinVar.1
Natural variantiVAR_01560260G → A in NS1. 1 PublicationCorresponds to variant dbSNP:rs397507509EnsemblClinVar.1
Natural variantiVAR_01599060G → V in myelodysplastic syndrome. 1 PublicationCorresponds to variant dbSNP:rs397507509EnsemblClinVar.1
Natural variantiVAR_01560361D → G in NS1. 4 PublicationsCorresponds to variant dbSNP:rs121918461EnsemblClinVar.1
Natural variantiVAR_01560461D → N in NS1. 2 PublicationsCorresponds to variant dbSNP:rs397507510EnsemblClinVar.1
Natural variantiVAR_01599161D → V in JMML; also in myelodysplastic syndrome. 1 PublicationCorresponds to variant dbSNP:rs121918461EnsemblClinVar.1
Natural variantiVAR_01599261D → Y in JMML. 1 PublicationCorresponds to variant dbSNP:rs397507510EnsemblClinVar.1
Natural variantiVAR_01560562Y → D in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 PublicationsCorresponds to variant dbSNP:rs121918460EnsemblClinVar.1
Natural variantiVAR_01560663Y → C in NS1. 6 PublicationsCorresponds to variant dbSNP:rs121918459EnsemblClinVar.1
Natural variantiVAR_01599369E → K in JMML; also in myelodysplastic syndrome. 1 PublicationCorresponds to variant dbSNP:rs397507511EnsemblClinVar.1
Natural variantiVAR_02718569E → Q in NS1. 1 PublicationCorresponds to variant dbSNP:rs397507511EnsemblClinVar.1
Natural variantiVAR_01599471F → K in acute myeloid leukemia; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_01599571F → L in NS1; also found in myelodysplastic syndrome. 2 PublicationsCorresponds to variant dbSNP:rs397507512EnsemblClinVar.1
Natural variantiVAR_01560772A → G in NS1. 3 PublicationsCorresponds to variant dbSNP:rs121918454EnsemblClinVar.1
Natural variantiVAR_01560872A → S in NS1. 3 PublicationsCorresponds to variant dbSNP:rs121918453EnsemblClinVar.1
Natural variantiVAR_01599672A → T in JMML. 1 PublicationCorresponds to variant dbSNP:rs121918453EnsemblClinVar.1
Natural variantiVAR_01599772A → V in JMML. 1 PublicationCorresponds to variant dbSNP:rs121918454EnsemblClinVar.1
Natural variantiVAR_01560973T → I in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 PublicationsCorresponds to variant dbSNP:rs121918462EnsemblClinVar.1
Natural variantiVAR_01599876E → A in JMML; also in myelodysplastic syndrome. 1 PublicationCorresponds to variant dbSNP:rs121918465EnsemblClinVar.1
Natural variantiVAR_01561076E → D in NS1. 3 PublicationsCorresponds to variant dbSNP:rs397507514EnsemblClinVar.1
Natural variantiVAR_01599976E → G in JMML. 1 PublicationCorresponds to variant dbSNP:rs121918465EnsemblClinVar.1
Natural variantiVAR_01600076E → K in JMML; increases protein tyrosine phosphatase activity against CDC73. 2 PublicationsCorresponds to variant dbSNP:rs121918464EnsemblClinVar.1
Natural variantiVAR_01600176E → V in JMML. 1 PublicationCorresponds to variant dbSNP:rs121918465EnsemblClinVar.1
Natural variantiVAR_02718679Q → P in NS1. 1 Publication1
Natural variantiVAR_01561179Q → R in NS1. 4 PublicationsCorresponds to variant dbSNP:rs121918466EnsemblClinVar.1
Natural variantiVAR_015612106D → A in NS1. 2 PublicationsCorresponds to variant dbSNP:rs397507517EnsemblClinVar.1
Natural variantiVAR_015613139E → D in NS1. 2 PublicationsCorresponds to variant dbSNP:rs397507520EnsemblClinVar.1
Natural variantiVAR_027187256Q → R in NS1. 1 Publication