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{{Infobox_gene}}
'''Tyrosine-protein phosphatase non-receptor type 9''' is an [[enzyme]] that in humans is encoded by the ''PTPN9'' [[gene]].<ref name="pmid1557404">{{cite journal | vauthors = Gu M, Warshawsky I, Majerus PW | title = Cloning and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to retinaldehyde-binding protein and yeast SEC14p | journal = Proc Natl Acad Sci U S A | volume = 89 | issue = 7 | pages = 2980–4 |date=May 1992 | pmid = 1557404 | pmc = 48787 | doi =10.1073/pnas.89.7.2980  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PTPN9 protein tyrosine phosphatase, non-receptor type 9| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5780| accessdate = }}</ref>
== Function ==
The protein encoded by this gene is a member of the protein tyrosine phosphatase ([[protein tyrosine phosphatase|PTP]]) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including [[cell growth]], [[cellular differentiation|differentiation]], [[cell cycle|mitotic cycle]], and [[oncogenesis|oncogenic]] transformation. This PTP contains an [[N-terminus|N-terminal]] domain that shares a significant similarity with yeast SEC14, which is a protein that has phosphatidylinositol transfer activity and is required for protein secretion through the [[Golgi apparatus|Golgi complex]] in yeast. This PTP was found to be activated by poly-[[inositol phosphates|phosphoinositide]], and is thought to be involved in signaling events regulating [[phagocytosis]].<ref name="entrez" />
== References ==
{{reflist}}
== Further reading ==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  |vauthors=Kruger JM, Fukushima T, Cherepanov V, etal |title=Protein-tyrosine phosphatase MEG2 is expressed by human neutrophils. Localization to the phagosome and activation by polyphosphoinositides |journal=J. Biol. Chem. |volume=277 |issue= 4 |pages= 2620–8 |year= 2002 |pmid= 11711529 |doi= 10.1074/jbc.M104550200 }}
*{{cite journal  |vauthors=Qi Y, Zhao R, Cao H, etal |title=Purification and characterization of protein tyrosine phosphatase PTP-MEG2 |journal=J. Cell. Biochem. |volume=86 |issue= 1 |pages= 79–89 |year= 2002 |pmid= 12112018 |doi= 10.1002/jcb.10195 }}
*{{cite journal  |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 }}
*{{cite journal  |vauthors=Pasquali C, Curchod ML, Wälchli S, etal |title=Identification of protein tyrosine phosphatases with specificity for the ligand-activated growth hormone receptor |journal=Mol. Endocrinol. |volume=17 |issue= 11 |pages= 2228–39 |year= 2004 |pmid= 12907755 |doi= 10.1210/me.2003-0011 }}
*{{cite journal  |vauthors=Xu MJ, Sui X, Zhao R, etal |title=PTP-MEG2 is activated in polycythemia vera erythroid progenitor cells and is required for growth and expansion of erythroid cells |journal=Blood |volume=102 |issue= 13 |pages= 4354–60 |year= 2004 |pmid= 12920026 |doi= 10.1182/blood-2003-04-1308 }}
*{{cite journal  |vauthors=Huynh H, Wang X, Li W, etal |title=Homotypic secretory vesicle fusion induced by the protein tyrosine phosphatase MEG2 depends on polyphosphoinositides in T cells |journal=J. Immunol. |volume=171 |issue= 12 |pages= 6661–71 |year= 2004 |pmid= 14662869 |doi=  10.4049/jimmunol.171.12.6661}}
*{{cite journal  |vauthors=Huynh H, Bottini N, Williams S, etal |title=Control of vesicle fusion by a tyrosine phosphatase |journal=Nat. Cell Biol. |volume=6 |issue= 9 |pages= 831–9 |year= 2004 |pmid= 15322554 |doi= 10.1038/ncb1164 }}
*{{cite journal  |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
*{{cite journal  |vauthors=Rual JF, Venkatesan K, Hao T, etal |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  |vauthors=Cho CY, Koo SH, Wang Y, etal |title=Identification of the tyrosine phosphatase PTP-MEG2 as an antagonist of hepatic insulin signaling |journal=Cell Metab. |volume=3 |issue= 5 |pages= 367–78 |year= 2007 |pmid= 16679294 |doi= 10.1016/j.cmet.2006.03.006 }}
*{{cite journal  |vauthors=Saito K, Williams S, Bulankina A, etal |title=Association of protein-tyrosine phosphatase MEG2 via its Sec14p homology domain with vesicle-trafficking proteins |journal=J. Biol. Chem. |volume=282 |issue= 20 |pages= 15170–8 |year= 2007 |pmid= 17387180 |doi= 10.1074/jbc.M608682200 }}
}}
{{refend}}
{{PDB Gallery|geneid=5780}}
{{Protein tyrosine phosphatases}}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PTPN9_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2pa5.
| PDB = {{PDB2|2pa5}}
| Name = Protein tyrosine phosphatase, non-receptor type 9
| HGNCid = 9661
| Symbol = PTPN9
| AltSymbols =; MEG2
| OMIM = 600768
| ECnumber = 
| Homologene = 2121
| MGIid = 1928376
| GeneAtlas_image1 = PBB_GE_PTPN9_202958_at_tn.png
| Function = {{GNF_GO|id=GO:0004726 |text = non-membrane spanning protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}} {{GNF_GO|id=GO:0006810 |text = transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5780
    | Hs_Ensembl = ENSG00000169410
    | Hs_RefseqProtein = XP_001128975
    | Hs_RefseqmRNA = XM_001128975
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 15
    | Hs_GenLoc_start = 73546515
    | Hs_GenLoc_end = 73658680
    | Hs_Uniprot = P43378
    | Mm_EntrezGene = 56294
    | Mm_Ensembl = ENSMUSG00000032290
    | Mm_RefseqmRNA = NM_019651
    | Mm_RefseqProtein = NP_062625
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 56793105
    | Mm_GenLoc_end = 56860945
    | Mm_Uniprot = Q2M4G8
  }}
}}
'''Protein tyrosine phosphatase, non-receptor type 9''', also known as '''PTPN9''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTPN9 protein tyrosine phosphatase, non-receptor type 9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5780| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an N-terminal domain that shares a significant similarity with yeast SEC14, which is a protein that has phosphatidylinositol transfer activity and is required for protein secretion through the Golgi complex in yeast. This PTP was found to be activated by polyphosphoinositide, and is thought to be involved in signaling events regulating phagocytosis.<ref name="entrez">{{cite web | title = Entrez Gene: PTPN9 protein tyrosine phosphatase, non-receptor type 9| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5780| accessdate = }}</ref>
}}
==References==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal  | author=Gu M, Warshawsky I, Majerus PW |title=Cloning and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to retinaldehyde-binding protein and yeast SEC14p. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 7 |pages= 2980-4 |year= 1992 |pmid= 1557404 |doi=  }}
*{{cite journal  | author=Kruger JM, Fukushima T, Cherepanov V, ''et al.'' |title=Protein-tyrosine phosphatase MEG2 is expressed by human neutrophils. Localization to the phagosome and activation by polyphosphoinositides. |journal=J. Biol. Chem. |volume=277 |issue= 4 |pages= 2620-8 |year= 2002 |pmid= 11711529 |doi= 10.1074/jbc.M104550200 }}
*{{cite journal  | author=Qi Y, Zhao R, Cao H, ''et al.'' |title=Purification and characterization of protein tyrosine phosphatase PTP-MEG2. |journal=J. Cell. Biochem. |volume=86 |issue= 1 |pages= 79-89 |year= 2002 |pmid= 12112018 |doi= 10.1002/jcb.10195 }}
*{{cite journal  | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Pasquali C, Curchod ML, Wälchli S, ''et al.'' |title=Identification of protein tyrosine phosphatases with specificity for the ligand-activated growth hormone receptor. |journal=Mol. Endocrinol. |volume=17 |issue= 11 |pages= 2228-39 |year= 2004 |pmid= 12907755 |doi= 10.1210/me.2003-0011 }}
*{{cite journal  | author=Xu MJ, Sui X, Zhao R, ''et al.'' |title=PTP-MEG2 is activated in polycythemia vera erythroid progenitor cells and is required for growth and expansion of erythroid cells. |journal=Blood |volume=102 |issue= 13 |pages= 4354-60 |year= 2004 |pmid= 12920026 |doi= 10.1182/blood-2003-04-1308 }}
*{{cite journal  | author=Huynh H, Wang X, Li W, ''et al.'' |title=Homotypic secretory vesicle fusion induced by the protein tyrosine phosphatase MEG2 depends on polyphosphoinositides in T cells. |journal=J. Immunol. |volume=171 |issue= 12 |pages= 6661-71 |year= 2004 |pmid= 14662869 |doi=  }}
*{{cite journal  | author=Huynh H, Bottini N, Williams S, ''et al.'' |title=Control of vesicle fusion by a tyrosine phosphatase. |journal=Nat. Cell Biol. |volume=6 |issue= 9 |pages= 831-9 |year= 2004 |pmid= 15322554 |doi= 10.1038/ncb1164 }}
*{{cite journal  | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal  | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  | author=Cho CY, Koo SH, Wang Y, ''et al.'' |title=Identification of the tyrosine phosphatase PTP-MEG2 as an antagonist of hepatic insulin signaling. |journal=Cell Metab. |volume=3 |issue= 5 |pages= 367-78 |year= 2007 |pmid= 16679294 |doi= 10.1016/j.cmet.2006.03.006 }}
*{{cite journal  | author=Saito K, Williams S, Bulankina A, ''et al.'' |title=Association of protein-tyrosine phosphatase MEG2 via its Sec14p homology domain with vesicle-trafficking proteins. |journal=J. Biol. Chem. |volume=282 |issue= 20 |pages= 15170-8 |year= 2007 |pmid= 17387180 |doi= 10.1074/jbc.M608682200 }}
}}
{{refend}}


{{protein-stub}}
{{gene-15-stub}}
{{WikiDoc Sources}}

Latest revision as of 18:57, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

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UniProt

n/a

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RefSeq (mRNA)

n/a

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Tyrosine-protein phosphatase non-receptor type 9 is an enzyme that in humans is encoded by the PTPN9 gene.[1][2]

Function

The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP contains an N-terminal domain that shares a significant similarity with yeast SEC14, which is a protein that has phosphatidylinositol transfer activity and is required for protein secretion through the Golgi complex in yeast. This PTP was found to be activated by poly-phosphoinositide, and is thought to be involved in signaling events regulating phagocytosis.[2]

References

  1. ↑ Gu M, Warshawsky I, Majerus PW (May 1992). "Cloning and expression of a cytosolic megakaryocyte protein-tyrosine-phosphatase with sequence homology to retinaldehyde-binding protein and yeast SEC14p". Proc Natl Acad Sci U S A. 89 (7): 2980–4. doi:10.1073/pnas.89.7.2980. PMC 48787. PMID 1557404.
  2. ↑ 2.0 2.1 "Entrez Gene: PTPN9 protein tyrosine phosphatase, non-receptor type 9".

Further reading



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