PTPRA: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Receptor-type tyrosine-protein phosphatase alpha''' is an [[enzyme]] that in humans is encoded by the ''PTPRA'' [[gene]].<ref name="pmid2172030">{{cite journal | vauthors = Jirik FR, Janzen NM, Melhado IG, Harder KW | title = Cloning and chromosomal assignment of a widely expressed human receptor-like protein-tyrosine phosphatase | journal = FEBS Lett | volume = 273 | issue = 1–2 | pages = 239–42 | date = December 1990 | pmid = 2172030 | pmc =  | doi = 10.1016/0014-5793(90)81094-5 }}</ref><ref name="pmid2169617">{{cite journal | vauthors = Kaplan R, Morse B, Huebner K, Croce C, Howk R, Ravera M, Ricca G, Jaye M, Schlessinger J | title = Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain | journal = Proc Natl Acad Sci U S A | volume = 87 | issue = 18 | pages = 7000–4 | date = October 1990 | pmid = 2169617 | pmc = 54670 | doi = 10.1073/pnas.87.18.7000 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PTPRA protein tyrosine phosphatase, receptor type, A| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5786| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_PTPRA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1p15.
| PDB = {{PDB2|1p15}}, {{PDB2|1yfo}}
| Name = Protein tyrosine phosphatase, receptor type, A
| HGNCid = 9664
| Symbol = PTPRA
| AltSymbols =; LRP; PTPA; HEPTP; HLPR; HPTPA; HPTPalpha; PTPRL2; R-PTP-alpha; RPTPA
| OMIM = 176884
| ECnumber = 
| Homologene = 20621
| MGIid = 97808
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005001 |text = transmembrane receptor protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5786
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_002827
    | Hs_RefseqmRNA = NM_002836
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 19262
    | Mm_Ensembl = ENSMUSG00000027303
    | Mm_RefseqmRNA = NM_008980
    | Mm_RefseqProtein = NP_033006
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 2
    | Mm_GenLoc_start = 130141723
    | Mm_GenLoc_end = 130245741
    | Mm_Uniprot = Q3TRY9
  }}
}}
'''Protein tyrosine phosphatase, receptor type, A''', also known as '''PTPRA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PTPRA protein tyrosine phosphatase, receptor type, A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5786| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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 extracellular domain, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. This PTP has been shown to dephosphorylate and activate Src family tyrosine kinases, and is implicated in the regulation of integrin signaling, cell adhesion and proliferation. Three alternatively spliced variants of this gene, which encode two distinct isoforms, have been reported.<ref name="entrez" />
{{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 extracellular domain, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. This PTP has been shown to dephosphorylate and activate Src family tyrosine kinases, and is implicated in the regulation of integrin signaling, cell adhesion and proliferation. Three alternatively spliced variants of this gene, which encode two distinct isoforms, have been reported.<ref name="entrez">{{cite web | title = Entrez Gene: PTPRA protein tyrosine phosphatase, receptor type, A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5786| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
PTPRA has been shown to [[Protein-protein interaction|interact]] with [[Grb2]]<ref name=pmid8670803>{{cite journal | vauthors = den Hertog J, Hunter T | title = Tight association of GRB2 with receptor protein-tyrosine phosphatase alpha is mediated by the SH2 and C-terminal SH3 domains | journal = EMBO J. | volume = 15 | issue = 12 | pages = 3016–27 | date = June 1996 | pmid = 8670803 | pmc = 450243 }}</ref><ref name=pmid7518772>{{cite journal | vauthors = den Hertog J, Tracy S, Hunter T | title = Phosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo | journal = EMBO J. | volume = 13 | issue = 13 | pages = 3020–32 | date = July 1994 | pmid = 7518772 | pmc = 395191 }}</ref><ref name=pmid11923305>{{cite journal | vauthors = Zheng XM, Resnick RJ, Shalloway D | title = Mitotic activation of protein-tyrosine phosphatase alpha and regulation of its Src-mediated transforming activity by its sites of protein kinase C phosphorylation | journal = J. Biol. Chem. | volume = 277 | issue = 24 | pages = 21922–9 | date = June 2002 | pmid = 11923305 | doi = 10.1074/jbc.M201394200 }}</ref> and [[KCNA2]].<ref name=pmid9878055>{{cite journal | vauthors = Tsai W, Morielli AD, Cachero TG, Peralta EG | title = Receptor protein tyrosine phosphatase alpha participates in the m1 muscarinic acetylcholine receptor-dependent regulation of Kv1.2 channel activity | journal = EMBO J. | volume = 18 | issue = 1 | pages = 109–18 | date = January 1999 | pmid = 9878055 | pmc = 1171107 | doi = 10.1093/emboj/18.1.109 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Mustelin T, Hunter T | title = Meeting at mitosis: cell cycle-specific regulation of c-Src by RPTPalpha | journal = Sci. STKE | volume = 2002 | issue = 115 | pages = PE3 | year = 2002 | pmid = 11796915 | doi = 10.1126/stke.2002.115.pe3 }}
| citations =
* {{cite journal | vauthors = Zheng XM, Wang Y, Pallen CJ | title = Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase | journal = Nature | volume = 359 | issue = 6393 | pages = 336–9 | year = 1992 | pmid = 1383828 | doi = 10.1038/359336a0 }}
*{{cite journal | author=Mustelin T, Hunter T |title=Meeting at mitosis: cell cycle-specific regulation of c-Src by RPTPalpha. |journal=Sci. STKE |volume=2002 |issue= 115 |pages= PE3 |year= 2002 |pmid= 11796915 |doi= 10.1126/stke.2002.115.pe3 }}
* {{cite journal | vauthors = Jirik FR, Anderson LL, Duncan AM | title = The human protein-tyrosine phosphatase PTP alpha/LRP gene (PTPA) is assigned to chromosome 20p13 | journal = Cytogenet. Cell Genet. | volume = 60 | issue = 2 | pages = 117–8 | year = 1992 | pmid = 1611910 | doi = 10.1159/000133317 }}
*{{cite journal | author=Zheng XM, Wang Y, Pallen CJ |title=Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase. |journal=Nature |volume=359 |issue= 6393 |pages= 336-9 |year= 1992 |pmid= 1383828 |doi= 10.1038/359336a0 }}
* {{cite journal | vauthors = Rao VV, Löffler C, Sap J, Schlessinger J, Hansmann I | title = The gene for receptor-linked protein-tyrosine-phosphatase (PTPA) is assigned to human chromosome 20p12-pter by in situ hybridization (ISH and FISH) | journal = Genomics | volume = 13 | issue = 3 | pages = 906–7 | year = 1992 | pmid = 1639427 | doi = 10.1016/0888-7543(92)90186-V }}
*{{cite journal | author=Jirik FR, Anderson LL, Duncan AM |title=The human protein-tyrosine phosphatase PTP alpha/LRP gene (PTPA) is assigned to chromosome 20p13. |journal=Cytogenet. Cell Genet. |volume=60 |issue= 2 |pages= 117-8 |year= 1992 |pmid= 1611910 |doi= }}
* {{cite journal | vauthors = Sap J, D'Eustachio P, Givol D, Schlessinger J | title = Cloning and expression of a widely expressed receptor tyrosine phosphatase | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 87 | issue = 16 | pages = 6112–6 | year = 1990 | pmid = 2166945 | pmc = 54482 | doi = 10.1073/pnas.87.16.6112 }}
*{{cite journal | author=Rao VV, Löffler C, Sap J, ''et al.'' |title=The gene for receptor-linked protein-tyrosine-phosphatase (PTPA) is assigned to human chromosome 20p12-pter by in situ hybridization (ISH and FISH). |journal=Genomics |volume=13 |issue= 3 |pages= 906-7 |year= 1992 |pmid= 1639427 |doi= }}
* {{cite journal | vauthors = Krueger NX, Streuli M, Saito H | title = Structural diversity and evolution of human receptor-like protein tyrosine phosphatases | journal = EMBO J. | volume = 9 | issue = 10 | pages = 3241–52 | year = 1990 | pmid = 2170109 | pmc = 552056 | doi =  }}
*{{cite journal | author=Sap J, D'Eustachio P, Givol D, Schlessinger J |title=Cloning and expression of a widely expressed receptor tyrosine phosphatase. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 16 |pages= 6112-6 |year= 1990 |pmid= 2166945 |doi= }}
* {{cite journal | vauthors = Ohagi S, Nishi M, Steiner DF | title = Sequence of a cDNA encoding human LRP (leukocyte common antigen-related peptide) | journal = Nucleic Acids Res. | volume = 18 | issue = 23 | pages = 7159 | year = 1991 | pmid = 2175890 | pmc = 332805 | doi = 10.1093/nar/18.23.7159 }}
*{{cite journal | author=Kaplan R, Morse B, Huebner K, ''et al.'' |title=Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=87 |issue= 18 |pages= 7000-4 |year= 1990 |pmid= 2169617 |doi=  }}
* {{cite journal | vauthors = den Hertog J, Tracy S, Hunter T | title = Phosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo | journal = EMBO J. | volume = 13 | issue = 13 | pages = 3020–32 | year = 1994 | pmid = 7518772 | pmc = 395191 | doi =  }}
*{{cite journal | author=Krueger NX, Streuli M, Saito H |title=Structural diversity and evolution of human receptor-like protein tyrosine phosphatases. |journal=EMBO J. |volume=9 |issue= 10 |pages= 3241-52 |year= 1990 |pmid= 2170109 |doi= }}
* {{cite journal | vauthors = den Hertog J, Pals CE, Peppelenbosch MP, Tertoolen LG, de Laat SW, Kruijer W | title = Receptor protein tyrosine phosphatase alpha activates pp60c-src and is involved in neuronal differentiation | journal = EMBO J. | volume = 12 | issue = 10 | pages = 3789–98 | year = 1993 | pmid = 7691597 | pmc = 413662 | doi =  }}
*{{cite journal | author=Jirik FR, Janzen NM, Melhado IG, Harder KW |title=Cloning and chromosomal assignment of a widely expressed human receptor-like protein-tyrosine phosphatase. |journal=FEBS Lett. |volume=273 |issue= 1-2 |pages= 239-42 |year= 1990 |pmid= 2172030 |doi=  }}
* {{cite journal | vauthors = Stover DR, Furet P, Lydon NB | title = Modulation of the SH2 binding specificity and kinase activity of Src by tyrosine phosphorylation within its SH2 domain | journal = J. Biol. Chem. | volume = 271 | issue = 21 | pages = 12481–7 | year = 1996 | pmid = 8647855 | doi = 10.1074/jbc.271.21.12481 }}
*{{cite journal | author=Ohagi S, Nishi M, Steiner DF |title=Sequence of a cDNA encoding human LRP (leukocyte common antigen-related peptide). |journal=Nucleic Acids Res. |volume=18 |issue= 23 |pages= 7159 |year= 1991 |pmid= 2175890 |doi=  }}
* {{cite journal | vauthors = den Hertog J, Hunter T | title = Tight association of GRB2 with receptor protein-tyrosine phosphatase alpha is mediated by the SH2 and C-terminal SH3 domains | journal = EMBO J. | volume = 15 | issue = 12 | pages = 3016–27 | year = 1996 | pmid = 8670803 | pmc = 450243 | doi =  }}
*{{cite journal | author=den Hertog J, Tracy S, Hunter T |title=Phosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo. |journal=EMBO J. |volume=13 |issue= 13 |pages= 3020-32 |year= 1994 |pmid= 7518772 |doi= }}
* {{cite journal | vauthors = Shimizu Y, Sugiyama H, Fujii Y, Sasaki K, Inoue K, Ogawa H, Tamaki H, Miyake S, Oji Y, Soma T, Yamagami T, Hirata M, Ikeda K, Monden T, Kishimoto T | title = Lineage- and differentiation stage-specific expression of LSM-1 (LPAP), a possible substrate for CD45, in human hematopoietic cells | journal = Am. J. Hematol. | volume = 54 | issue = 1 | pages = 1–11 | year = 1997 | pmid = 8980254 | doi = 10.1002/(SICI)1096-8652(199701)54:1<1::AID-AJH1>3.0.CO;2-1 }}
*{{cite journal | author=den Hertog J, Pals CE, Peppelenbosch MP, ''et al.'' |title=Receptor protein tyrosine phosphatase alpha activates pp60c-src and is involved in neuronal differentiation. |journal=EMBO J. |volume=12 |issue= 10 |pages= 3789-98 |year= 1993 |pmid= 7691597 |doi=  }}
* {{cite journal | vauthors = Lim KL, Lai DS, Kalousek MB, Wang Y, Pallen CJ | title = Kinetic analysis of two closely related receptor-like protein-tyrosine-phosphatases, PTP alpha and PTP epsilon | journal = Eur. J. Biochem. | volume = 245 | issue = 3 | pages = 693–700 | year = 1997 | pmid = 9183007 | doi = 10.1111/j.1432-1033.1997.00693.x }}
*{{cite journal | author=Stover DR, Furet P, Lydon NB |title=Modulation of the SH2 binding specificity and kinase activity of Src by tyrosine phosphorylation within its SH2 domain. |journal=J. Biol. Chem. |volume=271 |issue= 21 |pages= 12481-7 |year= 1996 |pmid= 8647855 |doi= }}
* {{cite journal | vauthors = Somani AK, Bignon JS, Mills GB, Siminovitch KA, Branch DR | title = Src kinase activity is regulated by the SHP-1 protein-tyrosine phosphatase | journal = J. Biol. Chem. | volume = 272 | issue = 34 | pages = 21113–9 | year = 1997 | pmid = 9261115 | doi = 10.1074/jbc.272.34.21113 }}
*{{cite journal | author=den Hertog J, Hunter T |title=Tight association of GRB2 with receptor protein-tyrosine phosphatase alpha is mediated by the SH2 and C-terminal SH3 domains. |journal=EMBO J. |volume=15 |issue= 12 |pages= 3016-27 |year= 1996 |pmid= 8670803 |doi= }}
* {{cite journal | vauthors = Feito MJ, Bragardo M, Buonfiglio D, Bonissoni S, Bottarel F, Malavasi F, Dianzani U | title = gp 120s derived from four syncytium-inducing HIV-1 strains induce different patterns of CD4 association with lymphocyte surface molecules | journal = Int. Immunol. | volume = 9 | issue = 8 | pages = 1141–7 | year = 1997 | pmid = 9263011 | doi = 10.1093/intimm/9.8.1141 }}
*{{cite journal | author=Shimizu Y, Sugiyama H, Fujii Y, ''et al.'' |title=Lineage- and differentiation stage-specific expression of LSM-1 (LPAP), a possible substrate for CD45, in human hematopoietic cells. |journal=Am. J. Hematol. |volume=54 |issue= 1 |pages= 1-11 |year= 1997 |pmid= 8980254 |doi= }}
* {{cite journal | vauthors = Norris K, Norris F, Kono DH, Vestergaard H, Pedersen O, Theofilopoulos AN, Møller NP | title = Expression of protein-tyrosine phosphatases in the major insulin target tissues | journal = FEBS Lett. | volume = 415 | issue = 3 | pages = 243–8 | year = 1997 | pmid = 9357975 | doi = 10.1016/S0014-5793(97)01133-2 }}
*{{cite journal | author=Lim KL, Lai DS, Kalousek MB, ''et al.'' |title=Kinetic analysis of two closely related receptor-like protein-tyrosine-phosphatases, PTP alpha and PTP epsilon. |journal=Eur. J. Biochem. |volume=245 |issue= 3 |pages= 693-700 |year= 1997 |pmid= 9183007 |doi= }}
* {{cite journal | vauthors = Bhandari V, Lim KL, Pallen CJ | title = Physical and functional interactions between receptor-like protein-tyrosine phosphatase alpha and p59fyn | journal = J. Biol. Chem. | volume = 273 | issue = 15 | pages = 8691–8 | year = 1998 | pmid = 9535845 | doi = 10.1074/jbc.273.15.8691 }}
*{{cite journal | author=Somani AK, Bignon JS, Mills GB, ''et al.'' |title=Src kinase activity is regulated by the SHP-1 protein-tyrosine phosphatase. |journal=J. Biol. Chem. |volume=272 |issue= 34 |pages= 21113-9 |year= 1997 |pmid= 9261115 |doi= }}
* {{cite journal | vauthors = Harder KW, Moller NP, Peacock JW, Jirik FR | title = Protein-tyrosine phosphatase alpha regulates Src family kinases and alters cell-substratum adhesion | journal = J. Biol. Chem. | volume = 273 | issue = 48 | pages = 31890–900 | year = 1998 | pmid = 9822658 | doi = 10.1074/jbc.273.48.31890 }}
*{{cite journal | author=Feito MJ, Bragardo M, Buonfiglio D, ''et al.'' |title=gp 120s derived from four syncytium-inducing HIV-1 strains induce different patterns of CD4 association with lymphocyte surface molecules. |journal=Int. Immunol. |volume=9 |issue= 8 |pages= 1141-7 |year= 1997 |pmid= 9263011 |doi= }}
*{{cite journal | author=Norris K, Norris F, Kono DH, ''et al.'' |title=Expression of protein-tyrosine phosphatases in the major insulin target tissues. |journal=FEBS Lett. |volume=415 |issue= 3 |pages= 243-8 |year= 1997 |pmid= 9357975 |doi= }}
*{{cite journal  | author=Bhandari V, Lim KL, Pallen CJ |title=Physical and functional interactions between receptor-like protein-tyrosine phosphatase alpha and p59fyn. |journal=J. Biol. Chem. |volume=273 |issue= 15 |pages= 8691-8 |year= 1998 |pmid= 9535845 |doi=  }}
*{{cite journal  | author=Harder KW, Moller NP, Peacock JW, Jirik FR |title=Protein-tyrosine phosphatase alpha regulates Src family kinases and alters cell-substratum adhesion. |journal=J. Biol. Chem. |volume=273 |issue= 48 |pages= 31890-900 |year= 1998 |pmid= 9822658 |doi=  }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=5786}}
{{Protein tyrosine phosphatases}}


{{protein-stub}}
{{protein-stub}}
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Latest revision as of 18:58, 7 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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

Receptor-type tyrosine-protein phosphatase alpha is an enzyme that in humans is encoded by the PTPRA gene.[1][2][3]

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 extracellular domain, a single transmembrane segment and two tandem intracytoplasmic catalytic domains, and thus represents a receptor-type PTP. This PTP has been shown to dephosphorylate and activate Src family tyrosine kinases, and is implicated in the regulation of integrin signaling, cell adhesion and proliferation. Three alternatively spliced variants of this gene, which encode two distinct isoforms, have been reported.[3]

Interactions

PTPRA has been shown to interact with Grb2[4][5][6] and KCNA2.[7]

References

  1. ↑ Jirik FR, Janzen NM, Melhado IG, Harder KW (December 1990). "Cloning and chromosomal assignment of a widely expressed human receptor-like protein-tyrosine phosphatase". FEBS Lett. 273 (1–2): 239–42. doi:10.1016/0014-5793(90)81094-5. PMID 2172030.
  2. ↑ Kaplan R, Morse B, Huebner K, Croce C, Howk R, Ravera M, Ricca G, Jaye M, Schlessinger J (October 1990). "Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain". Proc Natl Acad Sci U S A. 87 (18): 7000–4. doi:10.1073/pnas.87.18.7000. PMC 54670. PMID 2169617.
  3. ↑ 3.0 3.1 "Entrez Gene: PTPRA protein tyrosine phosphatase, receptor type, A".
  4. ↑ den Hertog J, Hunter T (June 1996). "Tight association of GRB2 with receptor protein-tyrosine phosphatase alpha is mediated by the SH2 and C-terminal SH3 domains". EMBO J. 15 (12): 3016–27. PMC 450243. PMID 8670803.
  5. ↑ den Hertog J, Tracy S, Hunter T (July 1994). "Phosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo". EMBO J. 13 (13): 3020–32. PMC 395191. PMID 7518772.
  6. ↑ Zheng XM, Resnick RJ, Shalloway D (June 2002). "Mitotic activation of protein-tyrosine phosphatase alpha and regulation of its Src-mediated transforming activity by its sites of protein kinase C phosphorylation". J. Biol. Chem. 277 (24): 21922–9. doi:10.1074/jbc.M201394200. PMID 11923305.
  7. ↑ Tsai W, Morielli AD, Cachero TG, Peralta EG (January 1999). "Receptor protein tyrosine phosphatase alpha participates in the m1 muscarinic acetylcholine receptor-dependent regulation of Kv1.2 channel activity". EMBO J. 18 (1): 109–18. doi:10.1093/emboj/18.1.109. PMC 1171107. PMID 9878055.

Further reading


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