UniProtKB - Q06124 (PTN11_HUMAN)
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- BLAST>sp|Q06124|PTN11_HUMAN Tyrosine-protein phosphatase non-receptor type 11 OS=Homo sapiens OX=9606 GN=PTPN11 PE=1 SV=2 MTSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTHIKIQNTG DYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKYPLNCADPTSERWFHGHLSGK EAEKLLTEKGKHGSFLVRESQSHPGDFVLSVRTGDDKGESNDGKSKVTHVMIRCQELKYD VGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPLNTTRINAAEIESRVRELSKLAETT DKVKQGFWEEFETLQQQECKLLYSRKEGQRQENKNKNRYKNILPFDHTRVVLHDGDPNEP VSDYINANIIMPEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEV ERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYTLRELKLSKVGQALLQGNTERTVW QYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILI DIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETLQRRIEEEQKSK RKGHEYTNIKYSLADQTSGDQSPLPPCTPTPPCAEMREDSARVYENVGLMQQQKSFR
- Align
Tyrosine-protein phosphatase non-receptor type 11
PTPN11
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>Select a section on the left to see content.
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation."
Miao H., Burnett E., Kinch M., Simon E., Wang B.
Nat. Cell Biol. 2:62-69(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH EPHA2. - Ref.31"Nuclear protein tyrosine phosphatase Shp-2 is one important negative regulator of nuclear export of telomerase reverse transcriptase."
Jakob S., Schroeder P., Lukosz M., Buchner N., Spyridopoulos I., Altschmied J., Haendeler J.
J. Biol. Chem. 283:33155-33161(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TERT, FUNCTION. - Ref.32"Regulation of RhoA-dependent ROCKII activation by Shp2."
Lee H.H., Chang Z.F.
J. Cell Biol. 181:999-1012(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.71"Determination of the catalytic activity of LEOPARD syndrome-associated SHP2 mutants toward parafibromin, a bona fide SHP2 substrate involved in Wnt signaling."
Noda S., Takahashi A., Hayashi T., Tanuma S., Hatakeyama M.
Biochem. Biophys. Res. Commun. 469:1133-1139(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT JMML LYS-76, CHARACTERIZATION OF VARIANT JMML LYS-76, VARIANTS LPRD1 CYS-279; MET-472; PRO-510 AND GLU-514, CHARACTERIZATION OF VARIANTS LPRD1 CYS-279; MET-472; PRO-510 AND GLU-514, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CDC73, SUBCELLULAR LOCATION. - Ref.72"Structural, Functional, and Clinical Characterization of a Novel PTPN11 Mutation Cluster Underlying Noonan Syndrome."
Pannone L., Bocchinfuso G., Flex E., Rossi C., Baldassarre G., Lissewski C., Pantaleoni F., Consoli F., Lepri F., Magliozzi M., Anselmi M., Delle Vigne S., Sorge G., Karaer K., Cuturilo G., Sartorio A., Tinschert S., Accadia M. , Digilio M.C., Zampino G., De Luca A., Cav e H., Zenker M., Gelb B.D., Dallapiccola B., Stella L., Ferrero G.B., Martinelli S., Tartaglia M.
Hum. Mutat. 38:451-459(2017) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NS1 HIS-261; PHE-261; ARG-262; PHE-262 AND GLN-265, CHARACTERIZATION VARIANTS NS1 HIS-261; PHE-261; ARG-262; PHE-262 AND GLN-265, FUNCTION, CATALYTIC ACTIVITY.
<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. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
3 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.48"Salicylic acid based small molecule inhibitor for the oncogenic Src homology-2 domain containing protein tyrosine phosphatase-2 (SHP2)."
Zhang X., He Y., Liu S., Yu Z., Jiang Z.X., Yang Z., Dong Y., Nabinger S.C., Wu L., Gunawan A.M., Wang L., Chan R.J., Zhang Z.Y.
J. Med. Chem. 53:2482-2493(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 262-532 IN COMPLEX WITH INHIBITOR, CATALYTIC ACTIVITY. - Ref.71"Determination of the catalytic activity of LEOPARD syndrome-associated SHP2 mutants toward parafibromin, a bona fide SHP2 substrate involved in Wnt signaling."
Noda S., Takahashi A., Hayashi T., Tanuma S., Hatakeyama M.
Biochem. Biophys. Res. Commun. 469:1133-1139(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT JMML LYS-76, CHARACTERIZATION OF VARIANT JMML LYS-76, VARIANTS LPRD1 CYS-279; MET-472; PRO-510 AND GLU-514, CHARACTERIZATION OF VARIANTS LPRD1 CYS-279; MET-472; PRO-510 AND GLU-514, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CDC73, SUBCELLULAR LOCATION. - Ref.72"Structural, Functional, and Clinical Characterization of a Novel PTPN11 Mutation Cluster Underlying Noonan Syndrome."
Pannone L., Bocchinfuso G., Flex E., Rossi C., Baldassarre G., Lissewski C., Pantaleoni F., Consoli F., Lepri F., Magliozzi M., Anselmi M., Delle Vigne S., Sorge G., Karaer K., Cuturilo G., Sartorio A., Tinschert S., Accadia M. , Digilio M.C., Zampino G., De Luca A., Cav e H., Zenker M., Gelb B.D., Dallapiccola B., Stella L., Ferrero G.B., Martinelli S., Tartaglia M.
Hum. Mutat. 38:451-459(2017) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NS1 HIS-261; PHE-261; ARG-262; PHE-262 AND GLN-265, CHARACTERIZATION VARIANTS NS1 HIS-261; PHE-261; ARG-262; PHE-262 AND GLN-265, FUNCTION, CATALYTIC ACTIVITY.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 429 | SubstrateBy similarity | 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 463 | Phosphocysteine intermediate | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 510 | SubstrateBy similarity | 1 |
<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
- 1-phosphatidylinositol-3-kinase activity Source: Reactome
- cell adhesion molecule binding Source: Ensembl
- D1 dopamine receptor binding Source: Ensembl
- insulin receptor binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- insulin receptor substrate binding Source: Ensembl
- non-membrane spanning protein tyrosine phosphatase activity Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- peptide hormone receptor binding Source: Ensembl
- phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: Reactome
- phospholipase binding Source: Ensembl
- phosphoprotein phosphatase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- phosphotyrosine residue binding Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- protein domain specific binding Source: Ensembl
- protein tyrosine phosphatase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- receptor tyrosine kinase binding Source: Ensembl
- SH3/SH2 adaptor activity Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
<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 - Biological processi
- abortive mitotic cell cycle Source: Ensembl
- activation of MAPK activity Source: Ensembl
- atrioventricular canal development Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- axon guidance Source: Reactome
- Bergmann glial cell differentiation Source: Ensembl
- brain development Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- cellular response to cytokine stimulus Source: Reactome
- cellular response to epidermal growth factor stimulus Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- cellular response to mechanical stimulus Source: Ensembl
- cerebellar cortex formation Source: Ensembl
- cytokine-mediated signaling pathway Source: Reactome
- DNA damage checkpoint Source: Ensembl
- ephrin receptor signaling pathway Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- epidermal growth factor receptor signaling pathway Source: Reactome
- ERBB signaling pathway Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- face morphogenesis Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- fibroblast growth factor receptor signaling pathway Source: Reactome
- genitalia development Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- glucose homeostasis Source: Ensembl
- heart development Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- homeostasis of number of cells within a tissue Source: Ensembl
- hormone-mediated signaling pathway Source: Ensembl
- hormone metabolic process Source: Ensembl
- inner ear development Source: BHF-UCL <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- integrin-mediated signaling pathway Source: Ensembl
- interleukin-6-mediated signaling pathway Source: Reactome
- intestinal epithelial cell migration Source: Ensembl
- leukocyte migration Source: Reactome
- megakaryocyte development Source: Ensembl
- microvillus organization Source: Ensembl
- multicellular organismal reproductive process Source: Ensembl
- multicellular organism growth Source: Ensembl
- negative regulation of cell adhesion mediated by integrin Source: Ensembl
- negative regulation of cortisol secretion Source: Ensembl
- negative regulation of growth hormone secretion Source: Ensembl
- negative regulation of insulin secretion Source: Ensembl
- neurotrophin TRK receptor signaling pathway Source: Ensembl
- organ growth Source: Ensembl
- peptidyl-tyrosine dephosphorylation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- platelet activation Source: Reactome
- platelet-derived growth factor receptor signaling pathway Source: Ensembl
- platelet formation Source: Ensembl
- positive regulation of ERK1 and ERK2 cascade Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of glucose import in response to insulin stimulus Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of hormone secretion Source: Ensembl
- positive regulation of mitotic cell cycle Source: Ensembl
- positive regulation of protein kinase B signaling Source: Reactome
- regulation of cell adhesion mediated by integrin Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of multicellular organism growth Source: Ensembl
- regulation of protein complex assembly Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of protein export from nucleus Source: Ensembl
- regulation of type I interferon-mediated signaling pathway Source: Reactome
- T cell costimulation Source: Reactome
- triglyceride metabolic process Source: Ensembl
<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 function | Hydrolase, Protein phosphatase |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.1.3.48 2681 |
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, 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 |
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_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:3.1.3.482 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
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_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 Synonyms:PTP2C, SHPTP2 |
| <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>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [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 lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <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 |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000179295.16 |
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 |
<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
Nucleus
- Nucleus 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.71"Determination of the catalytic activity of LEOPARD syndrome-associated SHP2 mutants toward parafibromin, a bona fide SHP2 substrate involved in Wnt signaling."
Noda S., Takahashi A., Hayashi T., Tanuma S., Hatakeyama M.
Biochem. Biophys. Res. Commun. 469:1133-1139(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT JMML LYS-76, CHARACTERIZATION OF VARIANT JMML LYS-76, VARIANTS LPRD1 CYS-279; MET-472; PRO-510 AND GLU-514, CHARACTERIZATION OF VARIANTS LPRD1 CYS-279; MET-472; PRO-510 AND GLU-514, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CDC73, SUBCELLULAR LOCATION.
- Nucleus 1 Publication
Other locations
- Cytoplasm 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.71"Determination of the catalytic activity of LEOPARD syndrome-associated SHP2 mutants toward parafibromin, a bona fide SHP2 substrate involved in Wnt signaling."
Noda S., Takahashi A., Hayashi T., Tanuma S., Hatakeyama M.
Biochem. Biophys. Res. Commun. 469:1133-1139(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT JMML LYS-76, CHARACTERIZATION OF VARIANT JMML LYS-76, VARIANTS LPRD1 CYS-279; MET-472; PRO-510 AND GLU-514, CHARACTERIZATION OF VARIANTS LPRD1 CYS-279; MET-472; PRO-510 AND GLU-514, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CDC73, SUBCELLULAR LOCATION.
- Cytoplasm 1 Publication
Cytosol
- cytosol Source: Reactome
Mitochondrion
- mitochondrion Source: Ensembl
Nucleus
- nucleoplasm Source: Reactome
- nucleus Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
- cytoplasm Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein-containing complex Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
<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>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
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.51"Grouping of multiple-lentigines/LEOPARD and Noonan syndromes on the PTPN11 gene."
Digilio M.C., Conti E., Sarkozy A., Mingarelli R., Dottorini T., Marino B., Pizzuti A., Dallapiccola B.
Am. J. Hum. Genet. 71:389-394(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LPRD1 CYS-279 AND MET-472. - Ref.57"A novel PTPN11 mutation in LEOPARD syndrome."
Conti E., Dottorini T., Sarkozy A., Tiller G.E., Esposito G., Pizzuti A., Dallapiccola B.
Hum. Mutat. 21:654-654(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT LPRD1 PRO-510. - Ref.61"Two novel and one recurrent PTPN11 mutations in LEOPARD syndrome."
Yoshida R., Nagai T., Hasegawa T., Kinoshita E., Tanaka T., Ogata T.
Am. J. Med. Genet. A 130:432-434(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LPRD1 THR-465 AND ALA-468. - Ref.62"PTPN11 mutations in patients with LEOPARD syndrome: a French multicentric experience."
French collaborative Noonan study group
Keren B., Hadchouel A., Saba S., Sznajer Y., Bonneau D., Leheup B., Boute O., Gaillard D., Lacombe D., Layet V., Marlin S., Mortier G., Toutain A., Beylot C., Baumann C., Verloes A., Cave H.
J. Med. Genet. 41:E117-E117(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LPRD1 CYS-279; SER-279; MET-472 AND PRO-514. - Ref.63"Clinical and molecular analysis of 30 patients with multiple lentigines LEOPARD syndrome."
Sarkozy A., Conti E., Digilio M.C., Marino B., Morini E., Pacileo G., Wilson M., Calabro R., Pizzuti A., Dallapiccola B.
J. Med. Genet. 41:E68-E68(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LPRD1 CYS-279; SER-279; ALA-468; MET-472; TRP-502; LEU-502 AND PRO-510. - Ref.66"Genetic heterogeneity in LEOPARD syndrome: two families with no mutations in PTPN11."
Kalidas K., Shaw A.C., Crosby A.H., Newbury-Ecob R., Greenhalgh L., Temple I.K., Law C., Patel A., Patton M.A., Jeffery S.
J. Hum. Genet. 50:21-25(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT LPRD1 PRO-510. - Ref.67"PTPN11 gene mutations: linking the Gln510Glu mutation to the 'LEOPARD syndrome phenotype'."
Digilio M.C., Sarkozy A., Pacileo G., Limongelli G., Marino B., Dallapiccola B.
Eur. J. Pediatr. 165:803-805(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT LPRD1 GLU-514. - Ref.68"Acute myelomonocytic leukemia in a boy with LEOPARD syndrome (PTPN11 gene mutation positive)."
Ucar C., Calyskan U., Martini S., Heinritz W.
J. Pediatr. Hematol. Oncol. 28:123-125(2006) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT LPRD1 CYS-279. - Ref.70"A PTPN11 allele encoding a catalytically impaired SHP2 protein in a patient with a Noonan syndrome phenotype."
Edwards J.J., Martinelli S., Pannone L., Lo I.F., Shi L., Edelmann L., Tartaglia M., Luk H.M., Gelb B.D.
Am. J. Med. Genet. A 164:2351-2355(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT NS1 SER-495, VARIANT LPRD1 TRP-502, CHARACTERIZATION OF VARIANTS NS1 SER-495, CHARACTERIZATION OF VARIANT LPRD1 TRP-502. - Ref.71"Determination of the catalytic activity of LEOPARD syndrome-associated SHP2 mutants toward parafibromin, a bona fide SHP2 substrate involved in Wnt signaling."
Noda S., Takahashi A., Hayashi T., Tanuma S., Hatakeyama M.
Biochem. Biophys. Res. Commun. 469:1133-1139(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT JMML LYS-76, CHARACTERIZATION OF VARIANT JMML LYS-76, VARIANTS LPRD1 CYS-279; MET-472; PRO-510 AND GLU-514, CHARACTERIZATION OF VARIANTS LPRD1 CYS-279; MET-472; PRO-510 AND GLU-514, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CDC73, SUBCELLULAR LOCATION.
Digilio M.C., Conti E., Sarkozy A., Mingarelli R., Dottorini T., Marino B., Pizzuti A., Dallapiccola B.
Am. J. Hum. Genet. 71:389-394(2002) [PubMed] [Europe PMC] [Abstract]
Conti E., Dottorini T., Sarkozy A., Tiller G.E., Esposito G., Pizzuti A., Dallapiccola B.
Hum. Mutat. 21:654-654(2003) [PubMed] [Europe PMC] [Abstract]
Yoshida R., Nagai T., Hasegawa T., Kinoshita E., Tanaka T., Ogata T.
Am. J. Med. Genet. A 130:432-434(2004) [PubMed] [Europe PMC] [Abstract]
French collaborative Noonan study group
Keren B., Hadchouel A., Saba S., Sznajer Y., Bonneau D., Leheup B., Boute O., Gaillard D., Lacombe D., Layet V., Marlin S., Mortier G., Toutain A., Beylot C., Baumann C., Verloes A., Cave H.
J. Med. Genet. 41:E117-E117(2004) [PubMed] [Europe PMC] [Abstract]
Sarkozy A., Conti E., Digilio M.C., Marino B., Morini E., Pacileo G., Wilson M., Calabro R., Pizzuti A., Dallapiccola B.
J. Med. Genet. 41:E68-E68(2004) [PubMed] [Europe PMC] [Abstract]
Kalidas K., Shaw A.C., Crosby A.H., Newbury-Ecob R., Greenhalgh L., Temple I.K., Law C., Patel A., Patton M.A., Jeffery S.
J. Hum. Genet. 50:21-25(2005) [PubMed] [Europe PMC] [Abstract]
Digilio M.C., Sarkozy A., Pacileo G., Limongelli G., Marino B., Dallapiccola B.
Eur. J. Pediatr. 165:803-805(2006) [PubMed] [Europe PMC] [Abstract]
Ucar C., Calyskan U., Martini S., Heinritz W.
J. Pediatr. Hematol. Oncol. 28:123-125(2006) [PubMed] [Europe PMC] [Abstract]
Edwards J.J., Martinelli S., Pannone L., Lo I.F., Shi L., Edelmann L., Tartaglia M., Luk H.M., Gelb B.D.
Am. J. Med. Genet. A 164:2351-2355(2014) [PubMed] [Europe PMC] [Abstract]
Noda S., Takahashi A., Hayashi T., Tanuma S., Hatakeyama M.
Biochem. Biophys. Res. Commun. 469:1133-1139(2016) [PubMed] [Europe PMC] [Abstract]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_027188 | 279 | Y → S in LPRD1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_027190 | 465 | A → T in LPRD1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_027191 | 468 | G → A in LPRD1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015621 | 472 | T → M in LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73. 5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_027192 | 502 | R → L in LPRD1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_027193 | 502 | R → W in LPRD1; reduced phosphatase activity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_027194 | 510 | Q → P in LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_027196 | 514 | Q → P in LPRD1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Noonan syndrome 1 (NS1)15 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.49"Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome."
Tartaglia M., Mehler E.L., Goldberg R., Zampino G., Brunner H.G., Kremer H., van der Burgt I., Crosby A.H., Ion A., Jeffery S., Kalidas K., Patton M.A., Kucherlapati R.S., Gelb B.D.
Nat. Genet. 29:465-468(2001) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NS1 GLY-61; CYS-63; GLY-72; SER-72; ASP-76; ARG-79; VAL-282; ASP-308 AND VAL-508. - Ref.50"PTPN11 mutations in Noonan syndrome: molecular spectrum, genotype-phenotype correlation, and phenotypic heterogeneity."
Tartaglia M., Kalidas K., Shaw A., Song X., Musat D.L., van der Burgt I., Brunner H.G., Bertola D.R., Crosby A.H., Ion A., Kucherlapati R.S., Jeffery S., Patton M.A., Gelb B.D.
Am. J. Hum. Genet. 70:1555-1563(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NS1 ALA-42; ALA-60; ASN-61; GLY-61; ASP-62; CYS-63; GLY-72; ILE-73; ASP-76; ARG-79; ALA-106; ASP-139; CYS-279; VAL-282; LEU-285; SER-285; ASP-308; SER-308; VAL-309; LYS-505 AND VAL-508. - Ref.52"PTPN11 mutations in Noonan syndrome type I: detection of recurrent mutations in exons 3 and 13."
Maheshwari M., Belmont J., Fernbach S., Ho T., Molinari L., Yakub I., Yu F., Combes A., Towbin J.A., Craigen W.J., Gibbs R.A.
Hum. Mutat. 20:298-304(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NS1 ASP-62; CYS-63 AND THR-506. - Ref.53"PTPN11 (protein-tyrosine phosphatase, nonreceptor-type 11) mutations in seven Japanese patients with Noonan syndrome."
Kosaki K., Suzuki T., Muroya K., Hasegawa T., Sato S., Matsuo N., Kosaki R., Nagai T., Hasegawa Y., Ogata T.
J. Clin. Endocrinol. Metab. 87:3529-3533(2002) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NS1 GLY-61; CYS-63; SER-72; ILE-73; SER-285 AND ASP-308. - Ref.54"PTPN11 mutation in a large family with Noonan syndrome and dizygous twinning."
Schollen E., Matthijs G., Gewillig M., Fryns J.-P., Legius E.
Eur. J. Hum. Genet. 11:85-88(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT NS1 ARG-79. - Ref.55"Spectrum of mutations in PTPN11 and genotype-phenotype correlation in 96 patients with Noonan syndrome and five patients with cardio-facio-cutaneous syndrome."
Musante L., Kehl H.G., Majewski F., Meinecke P., Schweiger S., Gillessen-Kaesbach G., Wieczorek D., Hinkel G.K., Tinschert S., Hoeltzenbein M., Ropers H.-H., Kalscheuer V.M.
Eur. J. Hum. Genet. 11:201-206(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NS1 LYS-58; ASN-61; GLY-61; CYS-63; GLN-69; LEU-71; SER-72; ILE-73; ASP-76; ARG-79; ASP-139; ARG-256; VAL-282 AND ASP-308. - Ref.56"Noonan syndrome with leukaemoid reaction and overproduction of catecholamines: a case report."
Kondoh T., Ishii E., Aoki Y., Shimizu T., Zaitsu M., Matsubara Y., Moriuchi H.
Eur. J. Pediatr. 162:548-549(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT NS1 THR-506. - Ref.58"Correlation between PTPN11 gene mutations and congenital heart defects in Noonan and LEOPARD syndromes."
Sarkozy A., Conti E., Seripa D., Digilio M.C., Grifone N., Tandoi C., Fazio V.M., Di Ciommo V., Marino B., Pizzuti A., Dallapiccola B.
J. Med. Genet. 40:704-708(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NS1 ILE-2; ALA-42; ASP-62; CYS-63; GLY-72; PRO-79; ALA-106; CYS-279; ASP-308; SER-308; MET-472; ARG-507; VAL-508 AND PHE-564. - Ref.59"Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia, myelodysplastic syndromes and acute myeloid leukemia."
Tartaglia M., Niemeyer C.M., Fragale A., Song X., Buechner J., Jung A., Haehlen K., Hasle H., Licht J.D., Gelb B.D.
Nat. Genet. 34:148-150(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS JMML TYR-61; VAL-61; LYS-69; THR-72; VAL-72; ALA-76; GLY-76; LYS-76; VAL-76; ALA-507 AND ARG-507, VARIANTS MYELODYSPLASTIC SYNDROME VAL-60; VAL-61; LYS-69; LEU-71 AND ALA-76, VARIANTS NS1 ASP-62 AND ILE-73, VARIANT ACUTE MYELOID LEUKEMIA LYS-71. - Ref.60"Clinical variability in a Noonan syndrome family with a new PTPN11 gene mutation."
Bertola D.R., Pereira A.C., de Oliveira P.S.L., Kim C.A., Krieger J.E.
Am. J. Med. Genet. A 130:378-383(2004) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT NS1 MET-415. - Ref.64"Neurofibromatosis-Noonan syndrome: molecular evidence of the concurrence of both disorders in a patient."
Bertola D.R., Pereira A.C., Passetti F., de Oliveira P.S.L., Messiaen L., Gelb B.D., Kim C.A., Krieger J.E.
Am. J. Med. Genet. A 136:242-245(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT NS1 ARG-510. - Ref.65"A novel mutation in the PTPN11 gene in a patient with Noonan syndrome and rapidly progressive hypertrophic cardiomyopathy."
Takahashi K., Kogaki S., Kurotobi S., Nasuno S., Ohta M., Okabe H., Wada K., Sakai N., Taniike M., Ozono K.
Eur. J. Pediatr. 164:497-500(2005) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT NS1 GLU-514. - Ref.69"PTPN11, SOS1, KRAS, and RAF1 gene analysis, and genotype-phenotype correlation in Korean patients with Noonan syndrome."
Ko J.M., Kim J.M., Kim G.H., Yoo H.W.
J. Hum. Genet. 53:999-1006(2008) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT NS1 ALA-59. - Ref.70"A PTPN11 allele encoding a catalytically impaired SHP2 protein in a patient with a Noonan syndrome phenotype."
Edwards J.J., Martinelli S., Pannone L., Lo I.F., Shi L., Edelmann L., Tartaglia M., Luk H.M., Gelb B.D.
Am. J. Med. Genet. A 164:2351-2355(2014) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT NS1 SER-495, VARIANT LPRD1 TRP-502, CHARACTERIZATION OF VARIANTS NS1 SER-495, CHARACTERIZATION OF VARIANT LPRD1 TRP-502. - Ref.72"Structural, Functional, and Clinical Characterization of a Novel PTPN11 Mutation Cluster Underlying Noonan Syndrome."
Pannone L., Bocchinfuso G., Flex E., Rossi C., Baldassarre G., Lissewski C., Pantaleoni F., Consoli F., Lepri F., Magliozzi M., Anselmi M., Delle Vigne S., Sorge G., Karaer K., Cuturilo G., Sartorio A., Tinschert S., Accadia M. , Digilio M.C., Zampino G., De Luca A., Cav e H., Zenker M., Gelb B.D., Dallapiccola B., Stella L., Ferrero G.B., Martinelli S., Tartaglia M.
Hum. Mutat. 38:451-459(2017) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS NS1 HIS-261; PHE-261; ARG-262; PHE-262 AND GLN-265, CHARACTERIZATION VARIANTS NS1 HIS-261; PHE-261; ARG-262; PHE-262 AND GLN-265, FUNCTION, CATALYTIC ACTIVITY.
Tartaglia M., Mehler E.L., Goldberg R., Zampino G., Brunner H.G., Kremer H., van der Burgt I., Crosby A.H., Ion A., Jeffery S., Kalidas K., Patton M.A., Kucherlapati R.S., Gelb B.D.
Nat. Genet. 29:465-468(2001) [PubMed] [Europe PMC] [Abstract]
Tartaglia M., Kalidas K., Shaw A., Song X., Musat D.L., van der Burgt I., Brunner H.G., Bertola D.R., Crosby A.H., Ion A., Kucherlapati R.S., Jeffery S., Patton M.A., Gelb B.D.
Am. J. Hum. Genet. 70:1555-1563(2002) [PubMed] [Europe PMC] [Abstract]
Maheshwari M., Belmont J., Fernbach S., Ho T., Molinari L., Yakub I., Yu F., Combes A., Towbin J.A., Craigen W.J., Gibbs R.A.
Hum. Mutat. 20:298-304(2002) [PubMed] [Europe PMC] [Abstract]
Kosaki K., Suzuki T., Muroya K., Hasegawa T., Sato S., Matsuo N., Kosaki R., Nagai T., Hasegawa Y., Ogata T.
J. Clin. Endocrinol. Metab. 87:3529-3533(2002) [PubMed] [Europe PMC] [Abstract]
Schollen E., Matthijs G., Gewillig M., Fryns J.-P., Legius E.
Eur. J. Hum. Genet. 11:85-88(2003) [PubMed] [Europe PMC] [Abstract]
Musante L., Kehl H.G., Majewski F., Meinecke P., Schweiger S., Gillessen-Kaesbach G., Wieczorek D., Hinkel G.K., Tinschert S., Hoeltzenbein M., Ropers H.-H., Kalscheuer V.M.
Eur. J. Hum. Genet. 11:201-206(2003) [PubMed] [Europe PMC] [Abstract]
Kondoh T., Ishii E., Aoki Y., Shimizu T., Zaitsu M., Matsubara Y., Moriuchi H.
Eur. J. Pediatr. 162:548-549(2003) [PubMed] [Europe PMC] [Abstract]
Sarkozy A., Conti E., Seripa D., Digilio M.C., Grifone N., Tandoi C., Fazio V.M., Di Ciommo V., Marino B., Pizzuti A., Dallapiccola B.
J. Med. Genet. 40:704-708(2003) [PubMed] [Europe PMC] [Abstract]
Tartaglia M., Niemeyer C.M., Fragale A., Song X., Buechner J., Jung A., Haehlen K., Hasle H., Licht J.D., Gelb B.D.
Nat. Genet. 34:148-150(2003) [PubMed] [Europe PMC] [Abstract]
Bertola D.R., Pereira A.C., de Oliveira P.S.L., Kim C.A., Krieger J.E.
Am. J. Med. Genet. A 130:378-383(2004) [PubMed] [Europe PMC] [Abstract]
Bertola D.R., Pereira A.C., Passetti F., de Oliveira P.S.L., Messiaen L., Gelb B.D., Kim C.A., Krieger J.E.
Am. J. Med. Genet. A 136:242-245(2005) [PubMed] [Europe PMC] [Abstract]
Takahashi K., Kogaki S., Kurotobi S., Nasuno S., Ohta M., Okabe H., Wada K., Sakai N., Taniike M., Ozono K.
Eur. J. Pediatr. 164:497-500(2005) [PubMed] [Europe PMC] [Abstract]
Ko J.M., Kim J.M., Kim G.H., Yoo H.W.
J. Hum. Genet. 53:999-1006(2008) [PubMed] [Europe PMC] [Abstract]
Edwards J.J., Martinelli S., Pannone L., Lo I.F., Shi L., Edelmann L., Tartaglia M., Luk H.M., Gelb B.D.
Am. J. Med. Genet. A 164:2351-2355(2014) [PubMed] [Europe PMC] [Abstract]
Pannone L., Bocchinfuso G., Flex E., Rossi C., Baldassarre G., Lissewski C., Pantaleoni F., Consoli F., Lepri F., Magliozzi M., Anselmi M., Delle Vigne S., Sorge G., Karaer K., Cuturilo G., Sartorio A., Tinschert S., Accadia M. , Digilio M.C., Zampino G., De Luca A., Cav e H., Zenker M., Gelb B.D., Dallapiccola B., Stella L., Ferrero G.B., Martinelli S., Tartaglia M.
Hum. Mutat. 38:451-459(2017) [PubMed] [Europe PMC] [Abstract]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_027183 | 2 | T → I in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015601 | 42 | T → A in NS1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_027184 | 58 | N → K in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_066060 | 59 | T → A in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015602 | 60 | G → A in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015603 | 61 | D → G in NS1. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015604 | 61 | D → N in NS1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015605 | 62 | Y → D in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015606 | 63 | Y → C in NS1. 6 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_027185 | 69 | E → Q in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015607 | 72 | A → G in NS1. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015608 | 72 | A → S in NS1. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015609 | 73 | T → I in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015610 | 76 | E → D in NS1. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_027186 | 79 | Q → P in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015611 | 79 | Q → R in NS1. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015612 | 106 | D → A in NS1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015613 | 139 | E → D in NS1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_027187 | 256 | Q → R in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_078101 | 261 | L → F in NS1; increases MAPK signaling; increases protein tyrosine phosphatase activity; changed substrate selectivity for GAB1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_078102 | 261 | L → H in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_078103 | 262 | L → F in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_078104 | 262 | L → R in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_078105 | 265 | R → Q in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015615 | 282 | I → V in NS1. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015617 | 285 | F → L in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015616 | 285 | F → S in NS1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015619 | 308 | N → D in NS1; common mutation. 5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015618 | 308 | N → S in NS1; some patients also manifest giant cell lesions of bone and soft tissue. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015620 | 309 | I → V in NS1; unknown pathological significance. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_027189 | 415 | T → M in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_071706 | 495 | P → S in NS1; increased phosphatase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015622 | 505 | R → K in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015623 | 506 | S → T in NS1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015624 | 508 | M → V in NS1. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_027195 | 510 | Q → R in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_027197 | 564 | L → F in NS1; unknown pathological significance. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Leukemia, juvenile myelomonocytic (JMML)2 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.59"Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia, myelodysplastic syndromes and acute myeloid leukemia."
Tartaglia M., Niemeyer C.M., Fragale A., Song X., Buechner J., Jung A., Haehlen K., Hasle H., Licht J.D., Gelb B.D.
Nat. Genet. 34:148-150(2003) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS JMML TYR-61; VAL-61; LYS-69; THR-72; VAL-72; ALA-76; GLY-76; LYS-76; VAL-76; ALA-507 AND ARG-507, VARIANTS MYELODYSPLASTIC SYNDROME VAL-60; VAL-61; LYS-69; LEU-71 AND ALA-76, VARIANTS NS1 ASP-62 AND ILE-73, VARIANT ACUTE MYELOID LEUKEMIA LYS-71. - Ref.71"Determination of the catalytic activity of LEOPARD syndrome-associated SHP2 mutants toward parafibromin, a bona fide SHP2 substrate involved in Wnt signaling."
Noda S., Takahashi A., Hayashi T., Tanuma S., Hatakeyama M.
Biochem. Biophys. Res. Commun. 469:1133-1139(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT JMML LYS-76, CHARACTERIZATION OF VARIANT JMML LYS-76, VARIANTS LPRD1 CYS-279; MET-472; PRO-510 AND GLU-514, CHARACTERIZATION OF VARIANTS LPRD1 CYS-279; MET-472; PRO-510 AND GLU-514, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CDC73, SUBCELLULAR LOCATION.
Tartaglia M., Niemeyer C.M., Fragale A., Song X., Buechner J., Jung A., Haehlen K., Hasle H., Licht J.D., Gelb B.D.
Nat. Genet. 34:148-150(2003) [PubMed] [Europe PMC] [Abstract]
Noda S., Takahashi A., Hayashi T., Tanuma S., Hatakeyama M.
Biochem. Biophys. Res. Commun. 469:1133-1139(2016) [PubMed] [Europe PMC] [Abstract]
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_015991 | 61 | D → V in JMML; also in myelodysplastic syndrome. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015992 | 61 | D → Y in JMML. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015993 | 69 | E → K in JMML; also in myelodysplastic syndrome. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015996 | 72 | A → T in JMML. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015997 | 72 | A → V in JMML. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015998 | 76 | E → A in JMML; also in myelodysplastic syndrome. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015999 | 76 | E → G in JMML. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_016000 | 76 | E → K in JMML; increases protein tyrosine phosphatase activity against CDC73. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_016001 | 76 | E → V in JMML. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_016002 | 507 | G → A in JMML. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Metachondromatosis (MC)1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.40"Whole-genome sequencing of a single proband together with linkage analysis identifies a Mendelian disease gene."
Sobreira N.L., Cirulli E.T., Avramopoulos D., Wohler E., Oswald G.L., Stevens E.L., Ge D., Shianna K.V., Smith J.P., Maia J.M., Gumbs C.E., Pevsner J., Thomas G., Valle D., Hoover-Fong J.E., Goldstein D.B.
PLoS Genet. 6:E1000991-E1000991(2010) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN MC.
Sobreira N.L., Cirulli E.T., Avramopoulos D., Wohler E., Oswald G.L., Stevens E.L., Ge D., Shianna K.V., Smith J.P., Maia J.M., Gumbs C.E., Pevsner J., Thomas G., Valle D., Hoover-Fong J.E., Goldstein D.B.
PLoS Genet. 6:E1000991-E1000991(2010) [PubMed] [Europe PMC] [Abstract]
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 463 | C → S: Abolishes phosphatase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<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>Keywords - Diseasei
Deafness, Disease mutationOrganism-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 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 151100 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 500 LEOPARD syndrome 2499 Metachondromatosis 648 Noonan syndrome |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA33986 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL3864 |
Drug and drug target database More...DrugBanki | DB02779 Dodecane-Trimethylamine |
Polymorphism and mutation 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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 methioninei | RemovedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| |||
| <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_0000094767 | 2 – 597 | Tyrosine-protein phosphatase non-receptor type 11Add BLAST | 596 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 residuei | 2 | N-acetylthreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 62 | PhosphotyrosineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <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 residuei | 66 | PhosphotyrosineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <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 residuei | 546 | Phosphotyrosine; by PDGFRBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <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 residuei | 584 | Phosphotyrosine; by PDGFRCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.5"Activation of a phosphotyrosine phosphatase by tyrosine phosphorylation."
Vogel W., Lammers R., Huang J., Ullrich A.
Science 259:1611-1614(1993) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PHOSPHORYLATION. - Ref.10"Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor."
Lechleider R.J., Sugimoto S., Bennett A.M., Kashishian A.S., Cooper J.A., Shoelson S.E., Walsh C.T., Neel B.G.
J. Biol. Chem. 268:21478-21481(1993) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION, INTERACTION WITH PDGFRB. - Ref.11"Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras."
Bennett A.M., Tang T.L., Sugimoto S., Walsh C.T., Neel B.G.
Proc. Natl. Acad. Sci. U.S.A. 91:7335-7339(1994) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION BY PDGFRB. - Ref.39"Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell proliferation but not migration."
Wardega P., Heldin C.H., Lennartsson J.
Cell. Signal. 22:1363-1368(2010) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION, INTERACTION WITH PDGFRB.
<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>Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | 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 human proteome resource More...ProteomicsDBi | 58414 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 | Q06124 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | 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
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"Identification of a human src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrew."
Freeman R.M. Jr., Plutzky J., Neel B.G.
Proc. Natl. Acad. Sci. U.S.A. 89:11239-11243(1992) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY. - Ref.3"Cloning, expression and mutational analysis of SH-PTP2, human protein-tyrosine phosphatase."
Bastien L., Ramachandran C., Liu S., Adam M.
Biochem. Biophys. Res. Commun. 196:124-133(1993) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), MUTAGENESIS OF CYS-463, TISSUE SPECIFICITY. - Ref.4"A widely expressed human protein-tyrosine phosphatase containing src homology 2 domains."
Ahmad S., Banville D.L., Zhao Z., Fischer E.H., Shen S.H.
Proc. Natl. Acad. Sci. U.S.A. 90:2197-2201(1993) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000179295 |
CleanEx database of gene expression profiles More...CleanExi | HS_PTPN11 |
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 | CAB005377 |
<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
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
27 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor."
Lechleider R.J., Sugimoto S., Bennett A.M., Kashishian A.S., Cooper J.A., Shoelson S.E., Walsh C.T., Neel B.G.
J. Biol. Chem. 268:21478-21481(1993) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION, INTERACTION WITH PDGFRB. - Ref.12"Activation of protein-tyrosine phosphatase SH-PTP2 by a tyrosine-based activation motif of a novel brain molecule."
Ohnishi H., Kubota M., Ohtake A., Sato K., Sano S.
J. Biol. Chem. 271:25569-25574(1996) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PTPNS1. - Ref.13"A family of proteins that inhibit signalling through tyrosine kinase receptors."
Kharitonenkov A., Chen Z., Sures I., Wang H., Schilling J., Ullrich A.
Nature 386:181-186(1997) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PTPNS1. - Ref.14"Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2."
Igarashi K., Isohara T., Kato T., Shigeta K., Yamano T., Uno I.
Biochem. Biophys. Res. Commun. 246:95-99(1998) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FLT1. - Ref.15"Gab-family adapter proteins act downstream of cytokine and growth factor receptors and T- and B-cell antigen receptors."
Nishida K., Yoshida Y., Itoh M., Fukada T., Ohtani T., Shirogane T., Atsumi T., Takahashi-Tezuka M., Ishihara K., Hibi M., Hirano T.
Blood 93:1809-1816(1999) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GAB2. - Ref.16"SHP2-interacting transmembrane adaptor protein (SIT), a novel disulfide-linked dimer regulating human T-cell activation."
Marie-Cardine A., Kirchgessner H., Bruyns E., Shevchenko A., Mann M., Autschbach F., Ratnofsky S., Meuer S., Schraven B.
J. Exp. Med. 189:1181-1194(1999) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SIT1. - Ref.17"Activation of EphA2 kinase suppresses integrin function and causes focal-adhesion-kinase dephosphorylation."
Miao H., Burnett E., Kinch M., Simon E., Wang B.
Nat. Cell Biol. 2:62-69(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH EPHA2. - Ref.18"Dissecting the interaction of SHP-2 with PZR, an immunoglobulin family protein containing immunoreceptor tyrosine-based inhibitory motifs."
Zhao R., Zhao Z.J.
J. Biol. Chem. 275:5453-5459(2000) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MZPL1, DEPHOSPHORYLATION OF MZPL1. - Ref.19"Molecular cloning and characterization of SPAP1, an inhibitory receptor."
Xu M.-J., Zhao R., Zhao Z.J.
Biochem. Biophys. Res. Commun. 280:768-775(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FCRL3. - Ref.20"Cell surface receptors Ly-9 and CD84 recruit the X-linked lymphoproliferative disease gene product SAP."
Sayos J., Martin M., Chen A., Simarro M., Howie D., Morra M., Engel P., Terhorst C.
Blood 97:3867-3874(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CD84. - Ref.21"Distinct interactions of the X-linked lymphoproliferative syndrome gene product SAP with cytoplasmic domains of members of the CD2 receptor family."
Lewis J., Eiben L.J., Nelson D.L., Cohen J.I., Nichols K.E., Ochs H.D., Notarangelo L.D., Duckett C.S.
Clin. Immunol. 100:15-23(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CD84. - Ref.22"Structural and functional dissection of the cytoplasmic domain of the transmembrane adaptor protein SIT (SHP2-interacting transmembrane adaptor protein)."
Pfrepper K.-I., Marie-Cardine A., Simeoni L., Kuramitsu Y., Leo A., Spicka J., Hilgert I., Scherer J., Schraven B.
Eur. J. Immunol. 31:1825-1836(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SIT1. - Ref.23"Identification of Fer tyrosine kinase localized on microtubules as a platelet endothelial cell adhesion molecule-1 phosphorylating kinase in vascular endothelial cells."
Kogata N., Masuda M., Kamioka Y., Yamagishi A., Endo A., Okada M., Mochizuki N.
Mol. Biol. Cell 14:3553-3564(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FER AND PECAM1. - Ref.24"The inhibitory potential of Fc receptor homolog 4 on memory B cells."
Ehrhardt G.R.A., Davis R.S., Hsu J.T., Leu C.-M., Ehrhardt A., Cooper M.D.
Proc. Natl. Acad. Sci. U.S.A. 100:13489-13494(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FCRL4. - Ref.26"Activation of vascular endothelial growth factor receptor-3 and its downstream signaling promote cell survival under oxidative stress."
Wang J.F., Zhang X., Groopman J.E.
J. Biol. Chem. 279:27088-27097(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FLT4. - Ref.28"ANKHD1, ankyrin repeat and KH domain containing 1, is overexpressed in acute leukemias and is associated with SHP2 in K562 cells."
Traina F., Favaro P.M.B., Medina Sde S., Duarte Ada S., Winnischofer S.M., Costa F.F., Saad S.T.O.
Biochim. Biophys. Acta 1762:828-834(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ANKHD1. - Ref.29"ROS fusion tyrosine kinase activates a SH2 domain-containing phosphatase-2/phosphatidylinositol 3-kinase/mammalian target of rapamycin signaling axis to form glioblastoma in mice."
Charest A., Wilker E.W., McLaughlin M.E., Lane K., Gowda R., Coven S., McMahon K., Kovach S., Feng Y., Yaffe M.B., Jacks T., Housman D.
Cancer Res. 66:7473-7481(2006) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ROS1. - Ref.30"FcRL6, a new ITIM-bearing receptor on cytolytic cells, is broadly expressed by lymphocytes following HIV-1 infection."
Wilson T.J., Presti R.M., Tassi I., Overton E.T., Cella M., Colonna M.
Blood 109:3786-3793(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FCRL6. - Ref.31"Nuclear protein tyrosine phosphatase Shp-2 is one important negative regulator of nuclear export of telomerase reverse transcriptase."
Jakob S., Schroeder P., Lukosz M., Buchner N., Spyridopoulos I., Altschmied J., Haendeler J.
J. Biol. Chem. 283:33155-33161(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TERT, FUNCTION. - Ref.33"An essential function for beta-arrestin 2 in the inhibitory signaling of natural killer cells."
Yu M.-C., Su L.-L., Zou L., Liu Y., Wu N., Kong L., Zhuang Z.-H., Sun L., Liu H.P., Hu J.-H., Li D., Strominger J.L., Zang J.-W., Pei G., Ge B.-X.
Nat. Immunol. 9:898-907(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH KIR2DL1. - Ref.35"GAREM, a novel adaptor protein for growth factor receptor-bound protein 2, contributes to cellular transformation through the activation of extracellular signal-regulated kinase signaling."
Tashiro K., Tsunematsu T., Okubo H., Ohta T., Sano E., Yamauchi E., Taniguchi H., Konishi H.
J. Biol. Chem. 284:20206-20214(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GAREM1. - Ref.36"A novel and critical role for tyrosine 663 in platelet endothelial cell adhesion molecule-1 trafficking and transendothelial migration."
Dasgupta B., Dufour E., Mamdouh Z., Muller W.A.
J. Immunol. 182:5041-5051(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PECAM1. - Ref.37"FCRL3, an autoimmune susceptibility gene, has inhibitory potential on B-cell receptor-mediated signaling."
Kochi Y., Myouzen K., Yamada R., Suzuki A., Kurosaki T., Nakamura Y., Yamamoto K.
J. Immunol. 183:5502-5510(2009) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FCRL3. - Ref.39"Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell proliferation but not migration."
Wardega P., Heldin C.H., Lennartsson J.
Cell. Signal. 22:1363-1368(2010) [PubMed] [Europe PMC] [Abstract]Cited for: PHOSPHORYLATION, INTERACTION WITH PDGFRB. - Ref.43"Mice lacking the ITIM-containing receptor G6b-B exhibit macrothrombocytopenia and aberrant platelet function."
Mazharian A., Wang Y.J., Mori J., Bem D., Finney B., Heising S., Gissen P., White J.G., Berndt M.C., Gardiner E.E., Nieswandt B., Douglas M.R., Campbell R.D., Watson S.P., Senis Y.A.
Sci. Signal. 5:RA78-RA78(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MPIG6B. - Ref.48"Salicylic acid based small molecule inhibitor for the oncogenic Src homology-2 domain containing protein tyrosine phosphatase-2 (SHP2)."
Zhang X., He Y., Liu S., Yu Z., Jiang Z.X., Yang Z., Dong Y., Nabinger S.C., Wu L., Gunawan A.M., Wang L., Chan R.J., Zhang Z.Y.
J. Med. Chem. 53:2482-2493(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 262-532 IN COMPLEX WITH INHIBITOR, CATALYTIC ACTIVITY. - Ref.71"Determination of the catalytic activity of LEOPARD syndrome-associated SHP2 mutants toward parafibromin, a bona fide SHP2 substrate involved in Wnt signaling."
Noda S., Takahashi A., Hayashi T., Tanuma S., Hatakeyama M.
Biochem. Biophys. Res. Commun. 469:1133-1139(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT JMML LYS-76, CHARACTERIZATION OF VARIANT JMML LYS-76, VARIANTS LPRD1 CYS-279; MET-472; PRO-510 AND GLU-514, CHARACTERIZATION OF VARIANTS LPRD1 CYS-279; MET-472; PRO-510 AND GLU-514, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH CDC73, SUBCELLULAR LOCATION.
<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
<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
- cell adhesion molecule binding Source: Ensembl
- D1 dopamine receptor binding Source: Ensembl
- insulin receptor binding Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- insulin receptor substrate binding Source: Ensembl
- peptide hormone receptor binding Source: Ensembl
- phospholipase binding Source: Ensembl
- phosphotyrosine residue binding Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- protein domain specific binding Source: Ensembl
- receptor tyrosine kinase binding Source: Ensembl
- SH3/SH2 adaptor activity Source: BHF-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 111745, 172 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, 75 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 |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 4 – 6 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 13 – 23 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 28 – 33 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 35 – 37 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 41 – 47 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 50 – 57 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 59 – 61 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 63 – 65 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 70 – 73 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 74 – 82 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 83 – 85 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 87 – 90 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 91 – 93 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 107 – 109 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 113 – 116 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 119 – 129 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 134 – 139 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 141 – 143 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 147 – 153 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 154 – 156 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 166 – 175 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 178 – 184 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 187 – 189 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 190 – 199 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 202 – 204 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 205 – 207 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 208 – 210 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 218 – 222 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 223 – 225 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 226 – 234 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 251 – 253 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 256 – 258 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 259 – 262 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 266 – 269 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 271 – 276 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 277 – 279 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 286 – 288 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 289 – 291 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 304 – 310 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 319 – 321 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 323 – 325 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 327 – 331 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 335 – 337 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 338 – 347 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 352 – 355 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 359 – 361 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 364 – 366 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 376 – 380 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 383 – 392 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 394 – 405 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 413 – 415 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 417 – 424 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 429 – 431 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 434 – 436 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 437 – 451 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 459 – 467 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 468 – 486 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 19 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 488 – 492 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 494 – 502 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 512 – 528 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 17 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 585 – 589 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | Q06124 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q06124 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | 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 key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Domaini | 6 – 102 | SH2 1PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 97 | |
| <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>Domaini | 112 – 216 | SH2 2PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 105 | |
| <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>Domaini | 247 – 521 | Tyrosine-protein phosphatasePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 275 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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>Regioni | 463 – 469 | Substrate bindingBy similarity | 7 |
<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
<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
<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>Keywords - Domaini
Repeat, SH2 domainPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG0790 Eukaryota COG5599 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000148980 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000273907 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG000223 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q06124 |
KEGG Orthology (KO) More...KOi | K07293 |
Identification of Orthologs from Complete Genome Data More...OMAi | KEYGAMR |
Database of Orthologous Groups More...OrthoDBi | EOG091G0VZ3 |
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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)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 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.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
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
ESIMDAGPVV VHCSAGIGRT GTFIVIDILI DIIREKGVDC DIDVPKTIQM
510 520 530 540 550
VRSQRSGMVQ TEAQYRFIYM AVQHYIETLQ RRIEEEQKSK RKGHEYTNIK
560 570 580 590
YSLADQTSGD QSPLPPCTPT PPCAEMREDS ARVYENVGLM QQQKSFR
The sequence of this isoform differs from the canonical sequence as follows:
408-411: Missing.
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
The sequence of this isoform differs from the canonical sequence as follows:
408-411: Missing.
464-464: S → R
465-597: Missing.
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
DAGPVVVHCR
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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 conflicti | 539 | S → R in BAA02740 (PubMed:8216283).Curated | 1 | |
| <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 conflicti | 552 | S → P in BAA02740 (PubMed:8216283).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <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_027183 | 2 | T → I in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015601 | 42 | T → A in NS1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_027184 | 58 | N → K in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_066060 | 59 | T → A in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015602 | 60 | G → A in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015990 | 60 | G → V in myelodysplastic syndrome. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015603 | 61 | D → G in NS1. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015604 | 61 | D → N in NS1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015991 | 61 | D → V in JMML; also in myelodysplastic syndrome. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015992 | 61 | D → Y in JMML. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015605 | 62 | Y → D in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015606 | 63 | Y → C in NS1. 6 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015993 | 69 | E → K in JMML; also in myelodysplastic syndrome. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_027185 | 69 | E → Q in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015994 | 71 | F → K in acute myeloid leukemia; requires 2 nucleotide substitutions. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015995 | 71 | F → L in myelodysplastic syndrome. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015607 | 72 | A → G in NS1. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015608 | 72 | A → S in NS1. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015996 | 72 | A → T in JMML. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015997 | 72 | A → V in JMML. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015609 | 73 | T → I in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015998 | 76 | E → A in JMML; also in myelodysplastic syndrome. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015610 | 76 | E → D in NS1. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015999 | 76 | E → G in JMML. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_016000 | 76 | E → K in JMML; increases protein tyrosine phosphatase activity against CDC73. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_016001 | 76 | E → V in JMML. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_027186 | 79 | Q → P in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015611 | 79 | Q → R in NS1. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015612 | 106 | D → A in NS1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015613 | 139 | E → D in NS1. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_027187 | 256 | Q → R in NS1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_078101 | 261 | L → F in NS1; increases MAPK signaling; increases protein tyrosine phosphatase activity; changed substrate selectivity for GAB1. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_078102 | 261 | L → H in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_078103 | 262 | L → F in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_078104 | 262 | L → R in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_078105 | 265 | R → Q in NS1; increases MAPK signaling; increased protein tyrosine phosphatase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <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_015614 | 279 | Y → C in NS1 and LPRD1; does not affect subcellular location; decreases protein tyrosine phosphatase activity against CDC73. 7 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
|