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Tyrosine-protein phosphatase non-receptor type 11 (EC 3.1.3.48) (Protein-tyrosine phosphatase 1D) (PTP-1D) (Protein-tyrosine phosphatase 2C) (PTP-2C) (SH-PTP2) (SHP-2) (Shp2) (SH-PTP3)

 PTN11_HUMAN             Reviewed;         597 AA.
Q06124; A8K1D9; Q96HD7;
01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 2.
30-AUG-2017, entry version 213.
RecName: Full=Tyrosine-protein phosphatase non-receptor type 11;
EC=3.1.3.48 {ECO:0000269|PubMed:26742426, ECO:0000269|PubMed:28074573};
AltName: Full=Protein-tyrosine phosphatase 1D;
Short=PTP-1D;
AltName: Full=Protein-tyrosine phosphatase 2C;
Short=PTP-2C;
AltName: Full=SH-PTP2;
Short=SHP-2;
Short=Shp2;
AltName: Full=SH-PTP3;
Name=PTPN11; Synonyms=PTP2C, SHPTP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=T-cell;
PubMed=1281790; DOI=10.1016/0014-5793(92)81500-L;
Adachi M., Sekiya M., Miyachi T., Matsuno K., Hinoda Y., Imai K.,
Yachi A.;
"Molecular cloning of a novel protein-tyrosine phosphatase SH-PTP3
with sequence similarity to the src-homology region 2.";
FEBS Lett. 314:335-339(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=1280823; DOI=10.1073/pnas.89.23.11239;
Freeman R.M. Jr., Plutzky J., Neel B.G.;
"Identification of a human src homology 2-containing protein-tyrosine-
phosphatase: a putative homolog of Drosophila corkscrew.";
Proc. Natl. Acad. Sci. U.S.A. 89:11239-11243(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), MUTAGENESIS OF CYS-463, AND
TISSUE SPECIFICITY.
PubMed=8216283; DOI=10.1006/bbrc.1993.2224;
Bastien L., Ramachandran C., Liu S., Adam M.;
"Cloning, expression and mutational analysis of SH-PTP2, human
protein-tyrosine phosphatase.";
Biochem. Biophys. Res. Commun. 196:124-133(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
TISSUE=Umbilical cord;
PubMed=7681589; DOI=10.1073/pnas.90.6.2197;
Ahmad S., Banville D.L., Zhao Z., Fischer E.H., Shen S.H.;
"A widely expressed human protein-tyrosine phosphatase containing src
homology 2 domains.";
Proc. Natl. Acad. Sci. U.S.A. 90:2197-2201(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND PHOSPHORYLATION.
PubMed=7681217; DOI=10.1126/science.7681217;
Vogel W., Lammers R., Huang J., Ullrich A.;
"Activation of a phosphotyrosine phosphatase by tyrosine
phosphorylation.";
Science 259:1611-1614(1993).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[10]
PHOSPHORYLATION, AND INTERACTION WITH PDGFRB.
PubMed=7691811;
Lechleider R.J., Sugimoto S., Bennett A.M., Kashishian A.S.,
Cooper J.A., Shoelson S.E., Walsh C.T., Neel B.G.;
"Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2
by its binding site, phosphotyrosine 1009, on the human platelet-
derived growth factor receptor.";
J. Biol. Chem. 268:21478-21481(1993).
[11]
PHOSPHORYLATION BY PDGFRB.
PubMed=8041791; DOI=10.1073/pnas.91.15.7335;
Bennett A.M., Tang T.L., Sugimoto S., Walsh C.T., Neel B.G.;
"Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth
factor receptor beta to Ras.";
Proc. Natl. Acad. Sci. U.S.A. 91:7335-7339(1994).
[12]
INTERACTION WITH PTPNS1.
PubMed=8810330; DOI=10.1074/jbc.271.41.25569;
Ohnishi H., Kubota M., Ohtake A., Sato K., Sano S.;
"Activation of protein-tyrosine phosphatase SH-PTP2 by a tyrosine-
based activation motif of a novel brain molecule.";
J. Biol. Chem. 271:25569-25574(1996).
[13]
INTERACTION WITH PTPNS1.
PubMed=9062191; DOI=10.1038/386181a0;
Kharitonenkov A., Chen Z., Sures I., Wang H., Schilling J.,
Ullrich A.;
"A family of proteins that inhibit signalling through tyrosine kinase
receptors.";
Nature 386:181-186(1997).
[14]
INTERACTION WITH FLT1.
PubMed=9600074; DOI=10.1006/bbrc.1998.8578;
Igarashi K., Isohara T., Kato T., Shigeta K., Yamano T., Uno I.;
"Tyrosine 1213 of Flt-1 is a major binding site of Nck and SHP-2.";
Biochem. Biophys. Res. Commun. 246:95-99(1998).
[15]
INTERACTION WITH GAB2.
PubMed=10068651;
Nishida K., Yoshida Y., Itoh M., Fukada T., Ohtani T., Shirogane T.,
Atsumi T., Takahashi-Tezuka M., Ishihara K., Hibi M., Hirano T.;
"Gab-family adapter proteins act downstream of cytokine and growth
factor receptors and T- and B-cell antigen receptors.";
Blood 93:1809-1816(1999).
[16]
INTERACTION WITH SIT1.
PubMed=10209036; DOI=10.1084/jem.189.8.1181;
Marie-Cardine A., Kirchgessner H., Bruyns E., Shevchenko A., Mann M.,
Autschbach F., Ratnofsky S., Meuer S., Schraven B.;
"SHP2-interacting transmembrane adaptor protein (SIT), a novel
disulfide-linked dimer regulating human T-cell activation.";
J. Exp. Med. 189:1181-1194(1999).
[17]
FUNCTION, AND INTERACTION WITH EPHA2.
PubMed=10655584; DOI=10.1038/35000008;
Miao H., Burnett E., Kinch M., Simon E., Wang B.;
"Activation of EphA2 kinase suppresses integrin function and causes
focal-adhesion-kinase dephosphorylation.";
Nat. Cell Biol. 2:62-69(2000).
[18]
INTERACTION WITH MZPL1, AND DEPHOSPHORYLATION OF MZPL1.
PubMed=10681522; DOI=10.1074/jbc.275.8.5453;
Zhao R., Zhao Z.J.;
"Dissecting the interaction of SHP-2 with PZR, an immunoglobulin
family protein containing immunoreceptor tyrosine-based inhibitory
motifs.";
J. Biol. Chem. 275:5453-5459(2000).
[19]
INTERACTION WITH FCRL3.
PubMed=11162587; DOI=10.1006/bbrc.2000.4213;
Xu M.-J., Zhao R., Zhao Z.J.;
"Molecular cloning and characterization of SPAP1, an inhibitory
receptor.";
Biochem. Biophys. Res. Commun. 280:768-775(2001).
[20]
INTERACTION WITH CD84.
PubMed=11389028; DOI=10.1182/blood.V97.12.3867;
Sayos J., Martin M., Chen A., Simarro M., Howie D., Morra M.,
Engel P., Terhorst C.;
"Cell surface receptors Ly-9 and CD84 recruit the X-linked
lymphoproliferative disease gene product SAP.";
Blood 97:3867-3874(2001).
[21]
INTERACTION WITH CD84.
PubMed=11414741; DOI=10.1006/clim.2001.5035;
Lewis J., Eiben L.J., Nelson D.L., Cohen J.I., Nichols K.E.,
Ochs H.D., Notarangelo L.D., Duckett C.S.;
"Distinct interactions of the X-linked lymphoproliferative syndrome
gene product SAP with cytoplasmic domains of members of the CD2
receptor family.";
Clin. Immunol. 100:15-23(2001).
[22]
INTERACTION WITH SIT1.
PubMed=11433379;
DOI=10.1002/1521-4141(200106)31:6<1825::AID-IMMU1825>3.0.CO;2-V;
Pfrepper K.-I., Marie-Cardine A., Simeoni L., Kuramitsu Y., Leo A.,
Spicka J., Hilgert I., Scherer J., Schraven B.;
"Structural and functional dissection of the cytoplasmic domain of the
transmembrane adaptor protein SIT (SHP2-interacting transmembrane
adaptor protein).";
Eur. J. Immunol. 31:1825-1836(2001).
[23]
INTERACTION WITH FER AND PECAM1.
PubMed=12972546; DOI=10.1091/mbc.E03-02-0080;
Kogata N., Masuda M., Kamioka Y., Yamagishi A., Endo A., Okada M.,
Mochizuki N.;
"Identification of Fer tyrosine kinase localized on microtubules as a
platelet endothelial cell adhesion molecule-1 phosphorylating kinase
in vascular endothelial cells.";
Mol. Biol. Cell 14:3553-3564(2003).
[24]
INTERACTION WITH FCRL4.
PubMed=14597715; DOI=10.1073/pnas.1935944100;
Ehrhardt G.R.A., Davis R.S., Hsu J.T., Leu C.-M., Ehrhardt A.,
Cooper M.D.;
"The inhibitory potential of Fc receptor homolog 4 on memory B
cells.";
Proc. Natl. Acad. Sci. U.S.A. 100:13489-13494(2003).
[25]
REVIEW ON ROLE IN KIT SIGNALING.
PubMed=15526160; DOI=10.1007/s00018-004-4189-6;
Ronnstrand L.;
"Signal transduction via the stem cell factor receptor/c-Kit.";
Cell. Mol. Life Sci. 61:2535-2548(2004).
[26]
INTERACTION WITH FLT4.
PubMed=15102829; DOI=10.1074/jbc.M314015200;
Wang J.F., Zhang X., Groopman J.E.;
"Activation of vascular endothelial growth factor receptor-3 and its
downstream signaling promote cell survival under oxidative stress.";
J. Biol. Chem. 279:27088-27097(2004).
[27]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[28]
INTERACTION WITH ANKHD1.
PubMed=16956752; DOI=10.1016/j.bbadis.2006.07.010;
Traina F., Favaro P.M.B., Medina Sde S., Duarte Ada S.,
Winnischofer S.M., Costa F.F., Saad S.T.O.;
"ANKHD1, ankyrin repeat and KH domain containing 1, is overexpressed
in acute leukemias and is associated with SHP2 in K562 cells.";
Biochim. Biophys. Acta 1762:828-834(2006).
[29]
INTERACTION WITH ROS1.
PubMed=16885344; DOI=10.1158/0008-5472.CAN-06-1193;
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.;
"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.";
Cancer Res. 66:7473-7481(2006).
[30]
INTERACTION WITH FCRL6.
PubMed=17213291; DOI=10.1182/blood-2006-06-030023;
Wilson T.J., Presti R.M., Tassi I., Overton E.T., Cella M.,
Colonna M.;
"FcRL6, a new ITIM-bearing receptor on cytolytic cells, is broadly
expressed by lymphocytes following HIV-1 infection.";
Blood 109:3786-3793(2007).
[31]
INTERACTION WITH TERT, AND FUNCTION.
PubMed=18829466; DOI=10.1074/jbc.M805138200;
Jakob S., Schroeder P., Lukosz M., Buchner N., Spyridopoulos I.,
Altschmied J., Haendeler J.;
"Nuclear protein tyrosine phosphatase Shp-2 is one important negative
regulator of nuclear export of telomerase reverse transcriptase.";
J. Biol. Chem. 283:33155-33161(2008).
[32]
FUNCTION.
PubMed=18559669; DOI=10.1083/jcb.200710187;
Lee H.H., Chang Z.F.;
"Regulation of RhoA-dependent ROCKII activation by Shp2.";
J. Cell Biol. 181:999-1012(2008).
[33]
INTERACTION WITH KIR2DL1.
PubMed=18604210; DOI=10.1038/ni.1635;
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.;
"An essential function for beta-arrestin 2 in the inhibitory signaling
of natural killer cells.";
Nat. Immunol. 9:898-907(2008).
[34]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[35]
INTERACTION WITH GAREM1.
PubMed=19509291; DOI=10.1074/jbc.M109.021139;
Tashiro K., Tsunematsu T., Okubo H., Ohta T., Sano E., Yamauchi E.,
Taniguchi H., Konishi H.;
"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.";
J. Biol. Chem. 284:20206-20214(2009).
[36]
INTERACTION WITH PECAM1.
PubMed=19342684; DOI=10.4049/jimmunol.0803192;
Dasgupta B., Dufour E., Mamdouh Z., Muller W.A.;
"A novel and critical role for tyrosine 663 in platelet endothelial
cell adhesion molecule-1 trafficking and transendothelial migration.";
J. Immunol. 182:5041-5051(2009).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-62 AND TYR-584, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[38]
PHOSPHORYLATION, AND INTERACTION WITH PDGFRB.
PubMed=20494825; DOI=10.1016/j.cellsig.2010.05.004;
Wardega P., Heldin C.H., Lennartsson J.;
"Mutation of tyrosine residue 857 in the PDGF beta-receptor affects
cell proliferation but not migration.";
Cell. Signal. 22:1363-1368(2010).
[39]
INVOLVEMENT IN MC.
PubMed=20577567; DOI=10.1371/journal.pgen.1000991;
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.;
"Whole-genome sequencing of a single proband together with linkage
analysis identifies a Mendelian disease gene.";
PLoS Genet. 6:E1000991-E1000991(2010).
[40]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[41]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[42]
INTERACTION WITH MPIG6B.
PubMed=23112346; DOI=10.1126/scisignal.2002936;
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.;
"Mice lacking the ITIM-containing receptor G6b-B exhibit
macrothrombocytopenia and aberrant platelet function.";
Sci. Signal. 5:RA78-RA78(2012).
[43]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-584, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[44]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[45]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 3-530 (ISOFORM 2).
PubMed=9491886; DOI=10.1016/S0092-8674(00)80938-1;
Hof P., Pluskey S., Dhe-Paganon S., Eck M.J., Shoelson S.E.;
"Crystal structure of the tyrosine phosphatase SHP-2.";
Cell 92:441-450(1998).
[46]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 237-533.
PubMed=19167335; DOI=10.1016/j.cell.2008.11.038;
Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P.,
Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.;
"Large-scale structural analysis of the classical human protein
tyrosine phosphatome.";
Cell 136:352-363(2009).
[47]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 262-532 IN COMPLEX WITH
INHIBITOR, AND CATALYTIC ACTIVITY.
PubMed=20170098; DOI=10.1021/jm901645u;
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.;
"Salicylic acid based small molecule inhibitor for the oncogenic Src
homology-2 domain containing protein tyrosine phosphatase-2 (SHP2).";
J. Med. Chem. 53:2482-2493(2010).
[48]
VARIANTS NS1 GLY-61; CYS-63; GLY-72; SER-72; ASP-76; ARG-79; VAL-282;
ASP-308 AND VAL-508.
PubMed=11704759; DOI=10.1038/ng772;
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.;
"Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2,
cause Noonan syndrome.";
Nat. Genet. 29:465-468(2001).
[49]
ERRATUM.
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. 29:491-491(2001).
[50]
ERRATUM.
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. 30:123-123(2001).
[51]
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.
PubMed=11992261; DOI=10.1086/340847;
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.;
"PTPN11 mutations in Noonan syndrome: molecular spectrum, genotype-
phenotype correlation, and phenotypic heterogeneity.";
Am. J. Hum. Genet. 70:1555-1563(2002).
[52]
VARIANTS LPRD1 CYS-279 AND MET-472.
PubMed=12058348; DOI=10.1086/341528;
Digilio M.C., Conti E., Sarkozy A., Mingarelli R., Dottorini T.,
Marino B., Pizzuti A., Dallapiccola B.;
"Grouping of multiple-lentigines/LEOPARD and Noonan syndromes on the
PTPN11 gene.";
Am. J. Hum. Genet. 71:389-394(2002).
[53]
VARIANTS NS1 ASP-62; CYS-63 AND THR-506.
PubMed=12325025; DOI=10.1002/humu.10129;
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.;
"PTPN11 mutations in Noonan syndrome type I: detection of recurrent
mutations in exons 3 and 13.";
Hum. Mutat. 20:298-304(2002).
[54]
VARIANTS NS1 GLY-61; CYS-63; SER-72; ILE-73; SER-285 AND ASP-308.
PubMed=12161469; DOI=10.1210/jcem.87.8.8694;
Kosaki K., Suzuki T., Muroya K., Hasegawa T., Sato S., Matsuo N.,
Kosaki R., Nagai T., Hasegawa Y., Ogata T.;
"PTPN11 (protein-tyrosine phosphatase, nonreceptor-type 11) mutations
in seven Japanese patients with Noonan syndrome.";
J. Clin. Endocrinol. Metab. 87:3529-3533(2002).
[55]
VARIANT NS1 ARG-79.
PubMed=12529711; DOI=10.1038/sj.ejhg.5200915;
Schollen E., Matthijs G., Gewillig M., Fryns J.-P., Legius E.;
"PTPN11 mutation in a large family with Noonan syndrome and dizygous
twinning.";
Eur. J. Hum. Genet. 11:85-88(2003).
[56]
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.
PubMed=12634870; DOI=10.1038/sj.ejhg.5200935;
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.;
"Spectrum of mutations in PTPN11 and genotype-phenotype correlation in
96 patients with Noonan syndrome and five patients with cardio-facio-
cutaneous syndrome.";
Eur. J. Hum. Genet. 11:201-206(2003).
[57]
ERRATUM.
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. 11:551-551(2003).
[58]
VARIANT NS1 THR-506.
PubMed=12739139; DOI=10.1007/s00431-003-1227-6;
Kondoh T., Ishii E., Aoki Y., Shimizu T., Zaitsu M., Matsubara Y.,
Moriuchi H.;
"Noonan syndrome with leukaemoid reaction and overproduction of
catecholamines: a case report.";
Eur. J. Pediatr. 162:548-549(2003).
[59]
VARIANT LPRD1 PRO-510.
PubMed=14961557; DOI=10.1002/humu.9149;
Conti E., Dottorini T., Sarkozy A., Tiller G.E., Esposito G.,
Pizzuti A., Dallapiccola B.;
"A novel PTPN11 mutation in LEOPARD syndrome.";
Hum. Mutat. 21:654-654(2003).
[60]
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.
PubMed=12960218; DOI=10.1136/jmg.40.9.704;
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.;
"Correlation between PTPN11 gene mutations and congenital heart
defects in Noonan and LEOPARD syndromes.";
J. Med. Genet. 40:704-708(2003).
[61]
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, AND VARIANT ACUTE MYELOID LEUKEMIA LYS-71.
PubMed=12717436; DOI=10.1038/ng1156;
Tartaglia M., Niemeyer C.M., Fragale A., Song X., Buechner J.,
Jung A., Haehlen K., Hasle H., Licht J.D., Gelb B.D.;
"Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia,
myelodysplastic syndromes and acute myeloid leukemia.";
Nat. Genet. 34:148-150(2003).
[62]
VARIANT NS1 MET-415.
PubMed=15384080; DOI=10.1002/ajmg.a.30270;
Bertola D.R., Pereira A.C., de Oliveira P.S.L., Kim C.A.,
Krieger J.E.;
"Clinical variability in a Noonan syndrome family with a new PTPN11
gene mutation.";
Am. J. Med. Genet. A 130:378-383(2004).
[63]
VARIANTS LPRD1 THR-465 AND ALA-468.
PubMed=15389709; DOI=10.1002/ajmg.a.30281;
Yoshida R., Nagai T., Hasegawa T., Kinoshita E., Tanaka T., Ogata T.;
"Two novel and one recurrent PTPN11 mutations in LEOPARD syndrome.";
Am. J. Med. Genet. A 130:432-434(2004).
[64]
VARIANTS LPRD1 CYS-279; SER-279; MET-472 AND PRO-514.
PubMed=15520399; DOI=10.1136/jmg.2004.021451;
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.;
"PTPN11 mutations in patients with LEOPARD syndrome: a French
multicentric experience.";
J. Med. Genet. 41:E117-E117(2004).
[65]
VARIANTS LPRD1 CYS-279; SER-279; ALA-468; MET-472; TRP-502; LEU-502
AND PRO-510.
PubMed=15121796; DOI=10.1136/jmg.2003.013466;
Sarkozy A., Conti E., Digilio M.C., Marino B., Morini E., Pacileo G.,
Wilson M., Calabro R., Pizzuti A., Dallapiccola B.;
"Clinical and molecular analysis of 30 patients with multiple
lentigines LEOPARD syndrome.";
J. Med. Genet. 41:E68-E68(2004).
[66]
VARIANT NS1 ARG-510.
PubMed=15948193; DOI=10.1002/ajmg.a.30813;
Bertola D.R., Pereira A.C., Passetti F., de Oliveira P.S.L.,
Messiaen L., Gelb B.D., Kim C.A., Krieger J.E.;
"Neurofibromatosis-Noonan syndrome: molecular evidence of the
concurrence of both disorders in a patient.";
Am. J. Med. Genet. A 136:242-245(2005).
[67]
VARIANT NS1 GLU-514.
PubMed=15889278; DOI=10.1007/s00431-005-1679-y;
Takahashi K., Kogaki S., Kurotobi S., Nasuno S., Ohta M., Okabe H.,
Wada K., Sakai N., Taniike M., Ozono K.;
"A novel mutation in the PTPN11 gene in a patient with Noonan syndrome
and rapidly progressive hypertrophic cardiomyopathy.";
Eur. J. Pediatr. 164:497-500(2005).
[68]
VARIANT LPRD1 PRO-510.
PubMed=15690106; DOI=10.1007/s10038-004-0212-x;
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.;
"Genetic heterogeneity in LEOPARD syndrome: two families with no
mutations in PTPN11.";
J. Hum. Genet. 50:21-25(2005).
[69]
VARIANT LPRD1 GLU-514.
PubMed=16733669; DOI=10.1007/s00431-006-0163-7;
Digilio M.C., Sarkozy A., Pacileo G., Limongelli G., Marino B.,
Dallapiccola B.;
"PTPN11 gene mutations: linking the Gln510Glu mutation to the 'LEOPARD
syndrome phenotype'.";
Eur. J. Pediatr. 165:803-805(2006).
[70]
VARIANT LPRD1 CYS-279.
PubMed=16679933; DOI=10.1097/01.mph.0000199590.21797.0b;
Ucar C., Calyskan U., Martini S., Heinritz W.;
"Acute myelomonocytic leukemia in a boy with LEOPARD syndrome (PTPN11
gene mutation positive).";
J. Pediatr. Hematol. Oncol. 28:123-125(2006).
[71]
VARIANT NS1 ALA-59.
PubMed=19020799; DOI=10.1007/s10038-008-0343-6;
Ko J.M., Kim J.M., Kim G.H., Yoo H.W.;
"PTPN11, SOS1, KRAS, and RAF1 gene analysis, and genotype-phenotype
correlation in Korean patients with Noonan syndrome.";
J. Hum. Genet. 53:999-1006(2008).
[72]
VARIANT NS1 SER-495, VARIANT LPRD1 TRP-502, CHARACTERIZATION OF
VARIANTS NS1 SER-495, AND CHARACTERIZATION OF VARIANT LPRD1 TRP-502.
PubMed=24891296; DOI=10.1002/ajmg.a.36620;
Edwards J.J., Martinelli S., Pannone L., Lo I.F., Shi L., Edelmann L.,
Tartaglia M., Luk H.M., Gelb B.D.;
"A PTPN11 allele encoding a catalytically impaired SHP2 protein in a
patient with a Noonan syndrome phenotype.";
Am. J. Med. Genet. A 164:2351-2355(2014).
[73]
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, AND SUBCELLULAR LOCATION.
PubMed=26742426; DOI=10.1016/j.bbrc.2015.12.117;
Noda S., Takahashi A., Hayashi T., Tanuma S., Hatakeyama M.;
"Determination of the catalytic activity of LEOPARD syndrome-
associated SHP2 mutants toward parafibromin, a bona fide SHP2
substrate involved in Wnt signaling.";
Biochem. Biophys. Res. Commun. 469:1133-1139(2016).
[74]
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, AND CATALYTIC ACTIVITY.
PubMed=28074573; DOI=10.1002/humu.23175;
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.;
"Structural, Functional, and Clinical Characterization of a Novel
PTPN11 Mutation Cluster Underlying Noonan Syndrome.";
Hum. Mutat. 38:451-459(2017).
-!- FUNCTION: Acts downstream of various receptor and cytoplasmic
protein tyrosine kinases to participate in the signal transduction
from the cell surface to the nucleus. Positively regulates MAPK
signal transduction pathway (PubMed:28074573). Dephosphorylates
GAB1, ARHGAP35 and EGFR (PubMed:28074573). Dephosphorylates ROCK2
at 'Tyr-722' resulting in stimulatation of its RhoA binding
activity. Dephosphorylates CDC73 (PubMed:26742426).
{ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:18559669,
ECO:0000269|PubMed:18829466, ECO:0000269|PubMed:26742426,
ECO:0000269|PubMed:28074573}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044,
ECO:0000269|PubMed:20170098, ECO:0000269|PubMed:26742426,
ECO:0000269|PubMed:28074573}.
-!- SUBUNIT: Interacts with phosphorylated LIME1 and BCAR3. Interacts
with SHB and INPP5D/SHIP1 (By similarity). Interacts with MILR1
(tyrosine-phosphorylated). Interacts with FLT1 (tyrosine-
phosphorylated), FLT3 (tyrosine-phosphorylated), FLT4 (tyrosine-
phosphorylated), KIT and GRB2. Interacts with PDGFRA (tyrosine
phosphorylated). Interacts (via SH2 domain) with TEK/TIE2
(tyrosine phosphorylated) (By similarity). Interacts with PTPNS1
and CD84. Interacts with phosphorylated SIT1 and MPZL1. Interacts
with FCRL3, FCRL4, FCRL6 and ANKHD1. Interacts with KIR2DL1; the
interaction is enhanced by ARRB2. Interacts with GAB2. Interacts
with TERT; the interaction retains TERT in the nucleus. Interacts
with PECAM1 and FER. Interacts with EPHA2 (activated);
participates in PTK2/FAK1 dephosphorylation in EPHA2 downstream
signaling. Interacts with ROS1; mediates PTPN11 phosphorylation.
Interacts with PDGFRB (tyrosine phosphorylated); this interaction
increases the PTPN11 phosphatase activity. Interacts with GAREM1
isoform 1 (tyrosine phosphorylated); the interaction increases
MAPK/ERK activity and does not affect the GRB2/SOS complex
formation. Interacts with CDC73 (PubMed:26742426). Interacts with
CEACAM1 (via cytoplasmic domain); this interaction depends on the
monomer/dimer equilibrium and is phosphorylation-dependent (By
similarity). Interacts with MPIG6B (via ITIM motif)
(PubMed:23112346). Interacts with SIGLEC10 (By similarity).
{ECO:0000250, ECO:0000250|UniProtKB:P35235,
ECO:0000269|PubMed:10068651, ECO:0000269|PubMed:10209036,
ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:10681522,
ECO:0000269|PubMed:11162587, ECO:0000269|PubMed:11389028,
ECO:0000269|PubMed:11414741, ECO:0000269|PubMed:11433379,
ECO:0000269|PubMed:12972546, ECO:0000269|PubMed:14597715,
ECO:0000269|PubMed:15102829, ECO:0000269|PubMed:16885344,
ECO:0000269|PubMed:16956752, ECO:0000269|PubMed:17213291,
ECO:0000269|PubMed:18604210, ECO:0000269|PubMed:18829466,
ECO:0000269|PubMed:19342684, ECO:0000269|PubMed:19509291,
ECO:0000269|PubMed:20170098, ECO:0000269|PubMed:20494825,
ECO:0000269|PubMed:23112346, ECO:0000269|PubMed:26742426,
ECO:0000269|PubMed:7691811, ECO:0000269|PubMed:8810330,
ECO:0000269|PubMed:9062191, ECO:0000269|PubMed:9600074}.
-!- INTERACTION:
P10275:AR; NbExp=12; IntAct=EBI-297779, EBI-608057;
P32239:CCKBR; NbExp=5; IntAct=EBI-297779, EBI-1753137;
Q9BZW8:CD244; NbExp=5; IntAct=EBI-297779, EBI-1580565;
P20138:CD33; NbExp=5; IntAct=EBI-297779, EBI-3906571;
Q08345:DDR1; NbExp=4; IntAct=EBI-297779, EBI-711879;
P68105:EEF1A1 (xeno); NbExp=2; IntAct=EBI-297779, EBI-7645934;
Q71V39:EEF1A2 (xeno); NbExp=2; IntAct=EBI-297779, EBI-7645815;
P04626:ERBB2; NbExp=2; IntAct=EBI-297779, EBI-641062;
P17948:FLT1; NbExp=2; IntAct=EBI-297779, EBI-1026718;
Q13480:GAB1; NbExp=39; IntAct=EBI-297779, EBI-517684;
Q9UQC2:GAB2; NbExp=4; IntAct=EBI-297779, EBI-975200;
O75496:GMNN; NbExp=4; IntAct=EBI-297779, EBI-371669;
P62993:GRB2; NbExp=6; IntAct=EBI-297779, EBI-401755;
P08069:IGF1R; NbExp=3; IntAct=EBI-297779, EBI-475981;
P06213:INSR; NbExp=2; IntAct=EBI-297779, EBI-475899;
P35568:IRS1; NbExp=3; IntAct=EBI-297779, EBI-517592;
P35570:Irs1 (xeno); NbExp=3; IntAct=EBI-297779, EBI-520230;
P43628:KIR2DL3; NbExp=4; IntAct=EBI-297779, EBI-8632435;
P10721:KIT; NbExp=29; IntAct=EBI-297779, EBI-1379503;
P08581:MET; NbExp=13; IntAct=EBI-297779, EBI-1039152;
O95297:MPZL1; NbExp=4; IntAct=EBI-297779, EBI-963338;
P09619:PDGFRB; NbExp=8; IntAct=EBI-297779, EBI-641237;
P16284:PECAM1; NbExp=7; IntAct=EBI-297779, EBI-716404;
P49023:PXN; NbExp=3; IntAct=EBI-297779, EBI-702209;
P49247:RPIA; NbExp=4; IntAct=EBI-297779, EBI-744831;
P97710:Sirpa (xeno); NbExp=3; IntAct=EBI-297779, EBI-7945080;
Q13049:TRIM32; NbExp=3; IntAct=EBI-297779, EBI-742790;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26742426}.
Nucleus {ECO:0000269|PubMed:26742426}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=PTP2Ci;
IsoId=Q06124-1; Sequence=Displayed;
Name=2; Synonyms=PTP2C;
IsoId=Q06124-2; Sequence=VSP_016672;
Name=3;
IsoId=Q06124-3; Sequence=VSP_016672, VSP_016673, VSP_016674;
-!- TISSUE SPECIFICITY: Widely expressed, with highest levels in
heart, brain, and skeletal muscle. {ECO:0000269|PubMed:1280823,
ECO:0000269|PubMed:7681589, ECO:0000269|PubMed:8216283}.
-!- DOMAIN: The SH2 domains repress phosphatase activity. Binding of
these domains to phosphotyrosine-containing proteins relieves this
auto-inhibition, possibly by inducing a conformational change in
the enzyme.
-!- PTM: Phosphorylated on Tyr-546 and Tyr-584 upon receptor protein
tyrosine kinase activation; which creates a binding site for GRB2
and other SH2-containing proteins. Phosphorylated upon activation
of the receptor-type kinase FLT3. Phosphorylated upon activation
of the receptor-type kinase PDGFRA (By similarity). Phosphorylated
by activated PDGFRB. {ECO:0000250, ECO:0000269|PubMed:20494825,
ECO:0000269|PubMed:7681217, ECO:0000269|PubMed:7691811,
ECO:0000269|PubMed:8041791}.
-!- DISEASE: LEOPARD syndrome 1 (LPRD1) [MIM:151100]: A disorder
characterized by lentigines, electrocardiographic conduction
abnormalities, ocular hypertelorism, pulmonic stenosis,
abnormalities of genitalia, retardation of growth, and
sensorineural deafness. {ECO:0000269|PubMed:12058348,
ECO:0000269|PubMed:14961557, ECO:0000269|PubMed:15121796,
ECO:0000269|PubMed:15389709, ECO:0000269|PubMed:15520399,
ECO:0000269|PubMed:15690106, ECO:0000269|PubMed:16679933,
ECO:0000269|PubMed:16733669, ECO:0000269|PubMed:24891296,
ECO:0000269|PubMed:26742426}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Noonan syndrome 1 (NS1) [MIM:163950]: A form of Noonan
syndrome, a disease characterized by short stature, facial
dysmorphic features such as hypertelorism, a downward eyeslant and
low-set posteriorly rotated ears, and a high incidence of
congenital heart defects and hypertrophic cardiomyopathy. Other
features can include a short neck with webbing or redundancy of
skin, deafness, motor delay, variable intellectual deficits,
multiple skeletal defects, cryptorchidism, and bleeding diathesis.
Individuals with Noonan syndrome are at risk of juvenile
myelomonocytic leukemia, a myeloproliferative disorder
characterized by excessive production of myelomonocytic cells.
Some patients with NS1 develop multiple giant cell lesions of the
jaw or other bony or soft tissues, which are classified as
pigmented villonodular synovitis (PVNS) when occurring in the jaw
or joints. {ECO:0000269|PubMed:11704759,
ECO:0000269|PubMed:11992261, ECO:0000269|PubMed:12161469,
ECO:0000269|PubMed:12325025, ECO:0000269|PubMed:12529711,
ECO:0000269|PubMed:12634870, ECO:0000269|PubMed:12717436,
ECO:0000269|PubMed:12739139, ECO:0000269|PubMed:12960218,
ECO:0000269|PubMed:15384080, ECO:0000269|PubMed:15889278,
ECO:0000269|PubMed:15948193, ECO:0000269|PubMed:19020799,
ECO:0000269|PubMed:24891296, ECO:0000269|PubMed:28074573}.
Note=The disease is caused by mutations affecting the gene
represented in this entry. Mutations in PTPN11 account for more
than 50% of the cases.
-!- DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An
aggressive pediatric myelodysplastic syndrome/myeloproliferative
disorder characterized by malignant transformation in the
hematopoietic stem cell compartment with proliferation of
differentiated progeny. Patients have splenomegaly, enlarged lymph
nodes, rashes, and hemorrhages. {ECO:0000269|PubMed:12717436,
ECO:0000269|PubMed:26742426}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Metachondromatosis (MC) [MIM:156250]: A skeletal disorder
with radiologic features of both multiple exostoses and Ollier
disease, characterized by the presence of exostoses, commonly of
the bones of the hands and feet, and enchondromas of the
metaphyses of long bones and iliac crest.
{ECO:0000269|PubMed:20577567}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class 2 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PTPN11ID41910ch12q24.html";
-----------------------------------------------------------------------
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EMBL; D13540; BAA02740.2; -; mRNA.
EMBL; L03535; AAA36611.1; -; mRNA.
EMBL; L07527; AAA17022.1; -; mRNA.
EMBL; L08807; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; X70766; CAA50045.1; -; mRNA.
EMBL; BT007106; AAP35770.1; -; mRNA.
EMBL; AK289854; BAF82543.1; -; mRNA.
EMBL; CH471054; EAW98012.1; -; Genomic_DNA.
EMBL; BC008692; AAH08692.1; -; mRNA.
CCDS; CCDS58280.1; -. [Q06124-3]
CCDS; CCDS81741.1; -. [Q06124-1]
CCDS; CCDS9163.1; -. [Q06124-2]
PIR; JN0805; JN0805.
RefSeq; NP_001317366.1; NM_001330437.1. [Q06124-1]
RefSeq; NP_002825.3; NM_002834.4. [Q06124-2]
RefSeq; NP_542168.1; NM_080601.2. [Q06124-3]
UniGene; Hs.506852; -.
PDB; 2SHP; X-ray; 2.00 A; A/B=1-529.
PDB; 3B7O; X-ray; 1.60 A; A=237-533.
PDB; 3MOW; X-ray; 2.30 A; A=262-532.
PDB; 3O5X; X-ray; 2.00 A; A=262-532.
PDB; 3TKZ; X-ray; 1.80 A; A=1-106.
PDB; 3TL0; X-ray; 2.05 A; A=1-106.
PDB; 3ZM0; X-ray; 1.50 A; A=248-531.
PDB; 3ZM1; X-ray; 1.40 A; A=248-531.
PDB; 3ZM2; X-ray; 1.50 A; A=248-531.
PDB; 3ZM3; X-ray; 1.50 A; A=248-531.
PDB; 4DGP; X-ray; 2.30 A; A=1-532.
PDB; 4DGX; X-ray; 2.30 A; A=1-532.
PDB; 4GWF; X-ray; 2.10 A; A/B=1-543.
PDB; 4H1O; X-ray; 2.20 A; A=1-543.
PDB; 4H34; X-ray; 2.70 A; A=1-543.
PDB; 4JE4; X-ray; 2.31 A; A=1-103.
PDB; 4JEG; X-ray; 2.30 A; A=97-217.
PDB; 4JMG; X-ray; 1.40 A; B=579-591.
PDB; 4NWF; X-ray; 2.10 A; A/B=1-543.
PDB; 4NWG; X-ray; 2.45 A; A/B=1-543.
PDB; 4OHD; X-ray; 2.70 A; A=1-532.
PDB; 4OHE; X-ray; 2.51 A; A=1-467, A=469-532.
PDB; 4OHH; X-ray; 2.70 A; A=1-532.
PDB; 4OHI; X-ray; 2.20 A; A=1-532.
PDB; 4OHL; X-ray; 2.40 A; A/B=1-532.
PDB; 4PVG; X-ray; 2.40 A; A=240-532.
PDB; 4QSY; X-ray; 2.10 A; A=1-106.
PDB; 4RDD; X-ray; 1.60 A; A=262-532.
PDB; 5DF6; X-ray; 1.78 A; A=1-222.
PDB; 5EHP; X-ray; 1.85 A; A/B=1-529.
PDB; 5EHR; X-ray; 1.70 A; A/B=1-529.
PDB; 5I6V; X-ray; 1.87 A; A/B=1-529.
PDB; 5IBM; X-ray; 2.18 A; A/B=1-529.
PDB; 5IBS; X-ray; 2.32 A; A/B=1-529.
PDBsum; 2SHP; -.
PDBsum; 3B7O; -.
PDBsum; 3MOW; -.
PDBsum; 3O5X; -.
PDBsum; 3TKZ; -.
PDBsum; 3TL0; -.
PDBsum; 3ZM0; -.
PDBsum; 3ZM1; -.
PDBsum; 3ZM2; -.
PDBsum; 3ZM3; -.
PDBsum; 4DGP; -.
PDBsum; 4DGX; -.
PDBsum; 4GWF; -.
PDBsum; 4H1O; -.
PDBsum; 4H34; -.
PDBsum; 4JE4; -.
PDBsum; 4JEG; -.
PDBsum; 4JMG; -.
PDBsum; 4NWF; -.
PDBsum; 4NWG; -.
PDBsum; 4OHD; -.
PDBsum; 4OHE; -.
PDBsum; 4OHH; -.
PDBsum; 4OHI; -.
PDBsum; 4OHL; -.
PDBsum; 4PVG; -.
PDBsum; 4QSY; -.
PDBsum; 4RDD; -.
PDBsum; 5DF6; -.
PDBsum; 5EHP; -.
PDBsum; 5EHR; -.
PDBsum; 5I6V; -.
PDBsum; 5IBM; -.
PDBsum; 5IBS; -.
ProteinModelPortal; Q06124; -.
SMR; Q06124; -.
BioGrid; 111745; 132.
DIP; DIP-516N; -.
ELM; Q06124; -.
IntAct; Q06124; 72.
MINT; MINT-199832; -.
STRING; 9606.ENSP00000340944; -.
BindingDB; Q06124; -.
ChEMBL; CHEMBL3864; -.
DrugBank; DB02779; Dodecane-Trimethylamine.
DEPOD; Q06124; -.
iPTMnet; Q06124; -.
PhosphoSitePlus; Q06124; -.
BioMuta; PTPN11; -.
DMDM; 84028248; -.
EPD; Q06124; -.
MaxQB; Q06124; -.
PaxDb; Q06124; -.
PeptideAtlas; Q06124; -.
PRIDE; Q06124; -.
TopDownProteomics; Q06124-2; -. [Q06124-2]
DNASU; 5781; -.
Ensembl; ENST00000351677; ENSP00000340944; ENSG00000179295. [Q06124-2]
Ensembl; ENST00000392597; ENSP00000376376; ENSG00000179295. [Q06124-3]
Ensembl; ENST00000635625; ENSP00000489597; ENSG00000179295. [Q06124-1]
GeneID; 5781; -.
KEGG; hsa:5781; -.
UCSC; uc001ttw.2; human. [Q06124-1]
CTD; 5781; -.
DisGeNET; 5781; -.
GeneCards; PTPN11; -.
GeneReviews; PTPN11; -.
HGNC; HGNC:9644; PTPN11.
HPA; CAB005377; -.
MalaCards; PTPN11; -.
MIM; 151100; phenotype.
MIM; 156250; phenotype.
MIM; 163950; phenotype.
MIM; 176876; gene.
MIM; 607785; phenotype.
neXtProt; NX_Q06124; -.
OpenTargets; ENSG00000179295; -.
Orphanet; 86834; Juvenile myelomonocytic leukemia.
Orphanet; 500; LEOPARD syndrome.
Orphanet; 2499; Metachondromatosis.
Orphanet; 648; Noonan syndrome.
PharmGKB; PA33986; -.
eggNOG; KOG0790; Eukaryota.
eggNOG; COG5599; LUCA.
GeneTree; ENSGT00880000137849; -.
HOGENOM; HOG000273907; -.
HOVERGEN; HBG000223; -.
InParanoid; Q06124; -.
KO; K07293; -.
OMA; KEYGAMR; -.
OrthoDB; EOG091G0VZ3; -.
PhylomeDB; Q06124; -.
TreeFam; TF351632; -.
BRENDA; 3.1.3.48; 2681.
Reactome; R-HSA-109704; PI3K Cascade.
Reactome; R-HSA-110056; MAPK3 (ERK1) activation.
Reactome; R-HSA-112411; MAPK1 (ERK2) activation.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-1170546; Prolactin receptor signaling.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1295596; Spry regulation of FGF signaling.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-180292; GAB1 signalosome.
Reactome; R-HSA-186763; Downstream signal transduction.
Reactome; R-HSA-210990; PECAM1 interactions.
Reactome; R-HSA-210993; Tie2 Signaling.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-2586552; Signaling by Leptin.
Reactome; R-HSA-388841; Costimulation by the CD28 family.
Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
Reactome; R-HSA-389948; PD-1 signaling.
Reactome; R-HSA-391160; Signal regulatory protein (SIRP) family interactions.
Reactome; R-HSA-418886; Netrin mediated repulsion signals.
Reactome; R-HSA-432142; Platelet sensitization by LDL.
Reactome; R-HSA-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-HSA-5654689; PI-3K cascade:FGFR1.
Reactome; R-HSA-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-HSA-5654695; PI-3K cascade:FGFR2.
Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-HSA-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-HSA-5654710; PI-3K cascade:FGFR3.
Reactome; R-HSA-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-HSA-5654720; PI-3K cascade:FGFR4.
Reactome; R-HSA-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-HSA-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-HSA-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-HSA-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-HSA-6783589; Interleukin-6 family signaling.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-877312; Regulation of IFNG signaling.
Reactome; R-HSA-8853659; RET signaling.
Reactome; R-HSA-8865999; MET activates PTPN11.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
Reactome; R-HSA-912694; Regulation of IFNA signaling.
Reactome; R-HSA-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
SignaLink; Q06124; -.
SIGNOR; Q06124; -.
ChiTaRS; PTPN11; human.
EvolutionaryTrace; Q06124; -.
GeneWiki; PTPN11; -.
GenomeRNAi; 5781; -.
PRO; PR:Q06124; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000179295; -.
CleanEx; HS_PTPN11; -.
ExpressionAtlas; Q06124; baseline and differential.
Genevisible; Q06124; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; TAS:Reactome.
GO; GO:0050839; F:cell adhesion molecule binding; IEA:Ensembl.
GO; GO:0031748; F:D1 dopamine receptor binding; IEA:Ensembl.
GO; GO:0005158; F:insulin receptor binding; IPI:BHF-UCL.
GO; GO:0043560; F:insulin receptor substrate binding; IEA:Ensembl.
GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IMP:UniProtKB.
GO; GO:0051428; F:peptide hormone receptor binding; IEA:Ensembl.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0043274; F:phospholipase binding; IEA:Ensembl.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
GO; GO:0030971; F:receptor tyrosine kinase binding; IEA:Ensembl.
GO; GO:0005070; F:SH3/SH2 adaptor activity; IPI:BHF-UCL.
GO; GO:0033277; P:abortive mitotic cell cycle; IEA:Ensembl.
GO; GO:0000187; P:activation of MAPK activity; IEA:Ensembl.
GO; GO:0036302; P:atrioventricular canal development; IMP:BHF-UCL.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0060020; P:Bergmann glial cell differentiation; IEA:Ensembl.
GO; GO:0007420; P:brain development; IMP:BHF-UCL.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IMP:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0021697; P:cerebellar cortex formation; IEA:Ensembl.
GO; GO:0000077; P:DNA damage checkpoint; IEA:Ensembl.
GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0038127; P:ERBB signaling pathway; IDA:UniProtKB.
GO; GO:0060325; P:face morphogenesis; IMP:BHF-UCL.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0048806; P:genitalia development; IMP:BHF-UCL.
GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
GO; GO:0007507; P:heart development; IMP:BHF-UCL.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
GO; GO:0042445; P:hormone metabolic process; IEA:Ensembl.
GO; GO:0009755; P:hormone-mediated signaling pathway; IEA:Ensembl.
GO; GO:0048839; P:inner ear development; IMP:BHF-UCL.
GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:Ensembl.
GO; GO:0061582; P:intestinal epithelial cell migration; IEA:Ensembl.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
GO; GO:0032528; P:microvillus organization; IEA:Ensembl.
GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
GO; GO:0048609; P:multicellular organismal reproductive process; IEA:Ensembl.
GO; GO:0033629; P:negative regulation of cell adhesion mediated by integrin; IEA:Ensembl.
GO; GO:0051463; P:negative regulation of cortisol secretion; IEA:Ensembl.
GO; GO:0060125; P:negative regulation of growth hormone secretion; IEA:Ensembl.
GO; GO:0046676; P:negative regulation of insulin secretion; IEA:Ensembl.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IEA:Ensembl.
GO; GO:0035265; P:organ growth; IEA:Ensembl.
GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IDA:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0030220; P:platelet formation; IEA:Ensembl.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:2001275; P:positive regulation of glucose import in response to insulin stimulus; IDA:BHF-UCL.
GO; GO:0046887; P:positive regulation of hormone secretion; IEA:Ensembl.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IEA:Ensembl.
GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IMP:UniProtKB.
GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0043254; P:regulation of protein complex assembly; IDA:BHF-UCL.
GO; GO:0046825; P:regulation of protein export from nucleus; IEA:Ensembl.
GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; TAS:Reactome.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0006641; P:triglyceride metabolic process; IEA:Ensembl.
Gene3D; 3.30.505.10; -; 2.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR000980; SH2.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR012152; Tyr_Pase_non-rcpt_typ-6/11.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF00017; SH2; 2.
Pfam; PF00102; Y_phosphatase; 1.
PIRSF; PIRSF000929; Tyr-Ptase_nr_6; 1.
PRINTS; PR00700; PRTYPHPHTASE.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00194; PTPc; 1.
SMART; SM00404; PTPc_motif; 1.
SMART; SM00252; SH2; 2.
SUPFAM; SSF52799; SSF52799; 1.
SUPFAM; SSF55550; SSF55550; 2.
PROSITE; PS50001; SH2; 2.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Deafness; Disease mutation; Hydrolase; Nucleus;
Phosphoprotein; Protein phosphatase; Reference proteome; Repeat;
SH2 domain.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 597 Tyrosine-protein phosphatase non-receptor
type 11.
/FTId=PRO_0000094767.
DOMAIN 6 102 SH2 1. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 112 216 SH2 2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 247 521 Tyrosine-protein phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 463 469 Substrate binding. {ECO:0000250}.
ACT_SITE 463 463 Phosphocysteine intermediate.
BINDING 429 429 Substrate. {ECO:0000250}.
BINDING 510 510 Substrate. {ECO:0000250}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 62 62 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 66 66 Phosphotyrosine.
{ECO:0000250|UniProtKB:P35235}.
MOD_RES 546 546 Phosphotyrosine; by PDGFR.
{ECO:0000250|UniProtKB:P35235}.
MOD_RES 584 584 Phosphotyrosine; by PDGFR.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 408 411 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:1280823,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7681217,
ECO:0000303|PubMed:7681589,
ECO:0000303|PubMed:8216283,
ECO:0000303|Ref.6}.
/FTId=VSP_016672.
VAR_SEQ 464 464 S -> R (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.6}.
/FTId=VSP_016673.
VAR_SEQ 465 597 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.6}.
/FTId=VSP_016674.
VARIANT 2 2 T -> I (in NS1; dbSNP:rs267606990).
{ECO:0000269|PubMed:12960218}.
/FTId=VAR_027183.
VARIANT 42 42 T -> A (in NS1; dbSNP:rs397507501).
{ECO:0000269|PubMed:11992261,
ECO:0000269|PubMed:12960218}.
/FTId=VAR_015601.
VARIANT 58 58 N -> K (in NS1; dbSNP:rs397507506).
{ECO:0000269|PubMed:12634870}.
/FTId=VAR_027184.
VARIANT 59 59 T -> A (in NS1).
{ECO:0000269|PubMed:19020799}.
/FTId=VAR_066060.
VARIANT 60 60 G -> A (in NS1; dbSNP:rs397507509).
{ECO:0000269|PubMed:11992261}.
/FTId=VAR_015602.
VARIANT 60 60 G -> V (in myelodysplastic syndrome;
dbSNP:rs397507509).
{ECO:0000269|PubMed:12717436}.
/FTId=VAR_015990.
VARIANT 61 61 D -> G (in NS1; dbSNP:rs121918461).
{ECO:0000269|PubMed:11704759,
ECO:0000269|PubMed:11992261,
ECO:0000269|PubMed:12161469,
ECO:0000269|PubMed:12634870}.
/FTId=VAR_015603.
VARIANT 61 61 D -> N (in NS1; dbSNP:rs397507510).
{ECO:0000269|PubMed:11992261,
ECO:0000269|PubMed:12634870}.
/FTId=VAR_015604.
VARIANT 61 61 D -> V (in JMML; also in myelodysplastic
syndrome; dbSNP:rs121918461).
{ECO:0000269|PubMed:12717436}.
/FTId=VAR_015991.
VARIANT 61 61 D -> Y (in JMML).
{ECO:0000269|PubMed:12717436}.
/FTId=VAR_015992.
VARIANT 62 62 Y -> D (in NS1; also in Noonan patients
manifesting juvenile myelomonocytic
leukemia; dbSNP:rs121918460).
{ECO:0000269|PubMed:11992261,
ECO:0000269|PubMed:12325025,
ECO:0000269|PubMed:12717436,
ECO:0000269|PubMed:12960218}.
/FTId=VAR_015605.
VARIANT 63 63 Y -> C (in NS1; dbSNP:rs121918459).
{ECO:0000269|PubMed:11704759,
ECO:0000269|PubMed:11992261,
ECO:0000269|PubMed:12161469,
ECO:0000269|PubMed:12325025,
ECO:0000269|PubMed:12634870,
ECO:0000269|PubMed:12960218}.
/FTId=VAR_015606.
VARIANT 69 69 E -> K (in JMML; also in myelodysplastic
syndrome). {ECO:0000269|PubMed:12717436}.
/FTId=VAR_015993.
VARIANT 69 69 E -> Q (in NS1; dbSNP:rs397507511).
{ECO:0000269|PubMed:12634870}.
/FTId=VAR_027185.
VARIANT 71 71 F -> K (in acute myeloid leukemia;
requires 2 nucleotide substitutions).
{ECO:0000269|PubMed:12717436}.
/FTId=VAR_015994.
VARIANT 71 71 F -> L (in myelodysplastic syndrome;
dbSNP:rs397507512).
{ECO:0000269|PubMed:12634870,
ECO:0000269|PubMed:12717436}.
/FTId=VAR_015995.
VARIANT 72 72 A -> G (in NS1; dbSNP:rs121918454).
{ECO:0000269|PubMed:11704759,
ECO:0000269|PubMed:11992261,
ECO:0000269|PubMed:12960218}.
/FTId=VAR_015607.
VARIANT 72 72 A -> S (in NS1; dbSNP:rs121918453).
{ECO:0000269|PubMed:11704759,
ECO:0000269|PubMed:12161469,
ECO:0000269|PubMed:12634870}.
/FTId=VAR_015608.
VARIANT 72 72 A -> T (in JMML; dbSNP:rs121918453).
{ECO:0000269|PubMed:12717436}.
/FTId=VAR_015996.
VARIANT 72 72 A -> V (in JMML; dbSNP:rs121918454).
{ECO:0000269|PubMed:12717436}.
/FTId=VAR_015997.
VARIANT 73 73 T -> I (in NS1; also in Noonan patients
manifesting juvenile myelomonocytic
leukemia; dbSNP:rs121918462).
{ECO:0000269|PubMed:11992261,
ECO:0000269|PubMed:12161469,
ECO:0000269|PubMed:12634870,
ECO:0000269|PubMed:12717436}.
/FTId=VAR_015609.
VARIANT 76 76 E -> A (in JMML; also in myelodysplastic
syndrome; dbSNP:rs121918465).
{ECO:0000269|PubMed:12717436}.
/FTId=VAR_015998.
VARIANT 76 76 E -> D (in NS1; dbSNP:rs397507514).
{ECO:0000269|PubMed:11704759,
ECO:0000269|PubMed:11992261,
ECO:0000269|PubMed:12634870}.
/FTId=VAR_015610.
VARIANT 76 76 E -> G (in JMML; dbSNP:rs121918465).
{ECO:0000269|PubMed:12717436}.
/FTId=VAR_015999.
VARIANT 76 76 E -> K (in JMML; increases protein
tyrosine phosphatase activity against
CDC73; dbSNP:rs121918464).
{ECO:0000269|PubMed:12717436,
ECO:0000269|PubMed:26742426}.
/FTId=VAR_016000.
VARIANT 76 76 E -> V (in JMML; dbSNP:rs121918465).
{ECO:0000269|PubMed:12717436}.
/FTId=VAR_016001.
VARIANT 79 79 Q -> P (in NS1).
{ECO:0000269|PubMed:12960218}.
/FTId=VAR_027186.
VARIANT 79 79 Q -> R (in NS1; dbSNP:rs121918466).
{ECO:0000269|PubMed:11704759,
ECO:0000269|PubMed:11992261,
ECO:0000269|PubMed:12529711,
ECO:0000269|PubMed:12634870}.
/FTId=VAR_015611.
VARIANT 106 106 D -> A (in NS1; dbSNP:rs397507517).
{ECO:0000269|PubMed:11992261,
ECO:0000269|PubMed:12960218}.
/FTId=VAR_015612.
VARIANT 139 139 E -> D (in NS1; dbSNP:rs397507520).
{ECO:0000269|PubMed:11992261,
ECO:0000269|PubMed:12634870}.
/FTId=VAR_015613.
VARIANT 256 256 Q -> R (in NS1; dbSNP:rs397507523).
{ECO:0000269|PubMed:12634870}.
/FTId=VAR_027187.
VARIANT 261 261 L -> F (in NS1; increases MAPK signaling;
increases protein tyrosine phosphatase
activity; changed substrate selectivity
for GAB1; dbSNP:rs397507525).
{ECO:0000269|PubMed:28074573}.
/FTId=VAR_078101.
VARIANT 261 261 L -> H (in NS1; increases MAPK signaling;
increased protein tyrosine phosphatase
activity; dbSNP:rs765642157).
{ECO:0000269|PubMed:28074573}.
/FTId=VAR_078102.
VARIANT 262 262 L -> F (in NS1; increases MAPK signaling;
increased protein tyrosine phosphatase
activity). {ECO:0000269|PubMed:28074573}.
/FTId=VAR_078103.
VARIANT 262 262 L -> R (in NS1; increases MAPK signaling;
increased protein tyrosine phosphatase
activity; dbSNP:rs397507526).
{ECO:0000269|PubMed:28074573}.
/FTId=VAR_078104.
VARIANT 265 265 R -> Q (in NS1; increases MAPK signaling;
increased protein tyrosine phosphatase
activity; dbSNP:rs376607329).
{ECO:0000269|PubMed:28074573}.
/FTId=VAR_078105.
VARIANT 279 279 Y -> C (in NS1 and LPRD1; does not affect
subcellular location; decreases protein
tyrosine phosphatase activity against
CDC73; dbSNP:rs121918456).
{ECO:0000269|PubMed:11992261,
ECO:0000269|PubMed:12058348,
ECO:0000269|PubMed:12960218,
ECO:0000269|PubMed:15121796,
ECO:0000269|PubMed:15520399,
ECO:0000269|PubMed:16679933,
ECO:0000269|PubMed:26742426}.
/FTId=VAR_015614.
VARIANT 279 279 Y -> S (in LPRD1; dbSNP:rs121918456).
{ECO:0000269|PubMed:15121796,
ECO:0000269|PubMed:15520399}.
/FTId=VAR_027188.
VARIANT 282 282 I -> V (in NS1; dbSNP:rs397507529).
{ECO:0000269|PubMed:11704759,
ECO:0000269|PubMed:11992261,
ECO:0000269|PubMed:12634870}.
/FTId=VAR_015615.
VARIANT 285 285 F -> L (in NS1; dbSNP:rs397507531).
{ECO:0000269|PubMed:11992261}.
/FTId=VAR_015617.
VARIANT 285 285 F -> S (in NS1; dbSNP:rs121918463).
{ECO:0000269|PubMed:11992261,
ECO:0000269|PubMed:12161469}.
/FTId=VAR_015616.
VARIANT 308 308 N -> D (in NS1; common mutation;
dbSNP:rs28933386).
{ECO:0000269|PubMed:11704759,
ECO:0000269|PubMed:11992261,
ECO:0000269|PubMed:12161469,
ECO:0000269|PubMed:12634870,
ECO:0000269|PubMed:12960218}.
/FTId=VAR_015619.
VARIANT 308 308 N -> S (in NS1; some patients also
manifest giant cell lesions of bone and
soft tissue; dbSNP:rs121918455).
{ECO:0000269|PubMed:11992261,
ECO:0000269|PubMed:12960218}.
/FTId=VAR_015618.
VARIANT 309 309 I -> V (in NS1; unknown pathological
significance; dbSNP:rs201787206).
{ECO:0000269|PubMed:11992261}.
/FTId=VAR_015620.
VARIANT 415 415 T -> M (in NS1; dbSNP:rs121918467).
{ECO:0000269|PubMed:15384080}.
/FTId=VAR_027189.
VARIANT 465 465 A -> T (in LPRD1; dbSNP:rs121918468).
{ECO:0000269|PubMed:15389709}.
/FTId=VAR_027190.
VARIANT 468 468 G -> A (in LPRD1; dbSNP:rs121918469).
{ECO:0000269|PubMed:15121796,
ECO:0000269|PubMed:15389709}.
/FTId=VAR_027191.
VARIANT 472 472 T -> M (in LPRD1; does not affect
subcellular location; decreases protein
tyrosine phosphatase activity against
CDC73; dbSNP:rs121918457).
{ECO:0000269|PubMed:12058348,
ECO:0000269|PubMed:12960218,
ECO:0000269|PubMed:15121796,
ECO:0000269|PubMed:15520399,
ECO:0000269|PubMed:26742426}.
/FTId=VAR_015621.
VARIANT 495 495 P -> S (in NS1; increased phosphatase
activity; dbSNP:rs397507539).
{ECO:0000269|PubMed:24891296}.
/FTId=VAR_071706.
VARIANT 502 502 R -> L (in LPRD1; dbSNP:rs397507542).
{ECO:0000269|PubMed:15121796}.
/FTId=VAR_027192.
VARIANT 502 502 R -> W (in LPRD1; reduced phosphatase
activity; dbSNP:rs397507541).
{ECO:0000269|PubMed:15121796,
ECO:0000269|PubMed:24891296}.
/FTId=VAR_027193.
VARIANT 505 505 R -> K (in NS1; dbSNP:rs397507543).
{ECO:0000269|PubMed:11992261}.
/FTId=VAR_015622.
VARIANT 506 506 S -> T (in NS1; dbSNP:rs121918458).
{ECO:0000269|PubMed:12325025,
ECO:0000269|PubMed:12739139}.
/FTId=VAR_015623.
VARIANT 507 507 G -> A (in JMML; dbSNP:rs397507546).
{ECO:0000269|PubMed:12717436}.
/FTId=VAR_016002.
VARIANT 507 507 G -> R (in NS1 and JMML; JMML patient
also shows growth retardation and
pulmonic stenosis; dbSNP:rs397507545).
{ECO:0000269|PubMed:12717436,
ECO:0000269|PubMed:12960218}.
/FTId=VAR_016003.
VARIANT 508 508 M -> V (in NS1; dbSNP:rs397507547).
{ECO:0000269|PubMed:11704759,
ECO:0000269|PubMed:11992261,
ECO:0000269|PubMed:12960218}.
/FTId=VAR_015624.
VARIANT 510 510 Q -> P (in LPRD1; does not affect
subcellular location; decreases protein
tyrosine phosphatase activity against
CDC73; dbSNP:rs397509345).
{ECO:0000269|PubMed:14961557,
ECO:0000269|PubMed:15121796,
ECO:0000269|PubMed:15690106,
ECO:0000269|PubMed:26742426}.
/FTId=VAR_027194.
VARIANT 510 510 Q -> R (in NS1).
{ECO:0000269|PubMed:15948193}.
/FTId=VAR_027195.
VARIANT 514 514 Q -> E (in NS1 and LPRD1; does not affect
subcellular location; decreases protein
tyrosine phosphatase activity against
CDC73; dbSNP:rs397507549).
{ECO:0000269|PubMed:15889278,
ECO:0000269|PubMed:16733669,
ECO:0000269|PubMed:26742426}.
/FTId=VAR_076499.
VARIANT 514 514 Q -> P (in LPRD1; dbSNP:rs121918470).
{ECO:0000269|PubMed:15520399}.
/FTId=VAR_027196.
VARIANT 564 564 L -> F (in NS1; dbSNP:rs397516797).
{ECO:0000269|PubMed:12960218}.
/FTId=VAR_027197.
MUTAGEN 463 463 C->S: Abolishes phosphatase activity.
{ECO:0000269|PubMed:8216283}.
CONFLICT 539 539 S -> R (in Ref. 3; BAA02740).
{ECO:0000305}.
CONFLICT 552 552 S -> P (in Ref. 3; BAA02740).
{ECO:0000305}.
TURN 3 6 {ECO:0000244|PDB:4OHD}.
HELIX 13 23 {ECO:0000244|PDB:5EHR}.
STRAND 28 33 {ECO:0000244|PDB:5EHR}.
STRAND 35 37 {ECO:0000244|PDB:5EHR}.
STRAND 41 47 {ECO:0000244|PDB:5EHR}.
STRAND 50 57 {ECO:0000244|PDB:5EHR}.
STRAND 59 61 {ECO:0000244|PDB:5EHR}.
STRAND 63 65 {ECO:0000244|PDB:5EHR}.
STRAND 70 73 {ECO:0000244|PDB:5EHR}.
HELIX 74 82 {ECO:0000244|PDB:5EHR}.
STRAND 83 85 {ECO:0000244|PDB:4OHD}.
STRAND 87 90 {ECO:0000244|PDB:3TKZ}.
STRAND 91 93 {ECO:0000244|PDB:4NWG}.
HELIX 107 109 {ECO:0000244|PDB:4DGX}.
STRAND 113 116 {ECO:0000244|PDB:5EHP}.
HELIX 119 129 {ECO:0000244|PDB:5EHR}.
STRAND 134 139 {ECO:0000244|PDB:5EHR}.
STRAND 141 143 {ECO:0000244|PDB:5DF6}.
STRAND 147 153 {ECO:0000244|PDB:5EHR}.
STRAND 154 156 {ECO:0000244|PDB:5DF6}.
STRAND 166 175 {ECO:0000244|PDB:5EHR}.
STRAND 178 184 {ECO:0000244|PDB:5EHR}.
STRAND 187 189 {ECO:0000244|PDB:5EHR}.
HELIX 190 199 {ECO:0000244|PDB:5EHR}.
STRAND 202 204 {ECO:0000244|PDB:5DF6}.
STRAND 208 210 {ECO:0000244|PDB:4JEG}.
STRAND 218 222 {ECO:0000244|PDB:4OHD}.
HELIX 223 225 {ECO:0000244|PDB:5EHR}.
HELIX 226 234 {ECO:0000244|PDB:5EHR}.
HELIX 251 253 {ECO:0000244|PDB:3ZM1}.
HELIX 256 258 {ECO:0000244|PDB:4PVG}.
HELIX 259 262 {ECO:0000244|PDB:3B7O}.
HELIX 266 269 {ECO:0000244|PDB:3ZM1}.
HELIX 271 276 {ECO:0000244|PDB:3ZM1}.
STRAND 277 279 {ECO:0000244|PDB:2SHP}.
HELIX 286 288 {ECO:0000244|PDB:3ZM1}.
STRAND 289 291 {ECO:0000244|PDB:3ZM1}.
STRAND 304 310 {ECO:0000244|PDB:3ZM1}.
STRAND 319 321 {ECO:0000244|PDB:4RDD}.
HELIX 323 325 {ECO:0000244|PDB:5EHP}.
STRAND 327 331 {ECO:0000244|PDB:3ZM1}.
HELIX 335 337 {ECO:0000244|PDB:3ZM1}.
HELIX 338 347 {ECO:0000244|PDB:3ZM1}.
STRAND 352 355 {ECO:0000244|PDB:3ZM1}.
STRAND 359 361 {ECO:0000244|PDB:3ZM1}.
STRAND 364 366 {ECO:0000244|PDB:3ZM0}.
STRAND 376 380 {ECO:0000244|PDB:3ZM1}.
STRAND 383 392 {ECO:0000244|PDB:3ZM1}.
STRAND 394 405 {ECO:0000244|PDB:3ZM1}.
HELIX 413 415 {ECO:0000244|PDB:5I6V}.
STRAND 417 424 {ECO:0000244|PDB:3ZM1}.
STRAND 429 431 {ECO:0000244|PDB:3ZM1}.
STRAND 434 436 {ECO:0000244|PDB:3ZM1}.
HELIX 437 451 {ECO:0000244|PDB:3ZM1}.
STRAND 459 467 {ECO:0000244|PDB:3ZM1}.
HELIX 468 486 {ECO:0000244|PDB:3ZM1}.
STRAND 488 492 {ECO:0000244|PDB:5EHR}.
HELIX 494 502 {ECO:0000244|PDB:3ZM1}.
HELIX 512 528 {ECO:0000244|PDB:3ZM1}.
STRAND 585 589 {ECO:0000244|PDB:4JMG}.
SEQUENCE 597 AA; 68436 MW; 37E8BFC7ECA2D03F CRC64;
MTSRRWFHPN ITGVEAENLL LTRGVDGSFL ARPSKSNPGD FTLSVRRNGA VTHIKIQNTG
DYYDLYGGEK FATLAELVQY YMEHHGQLKE KNGDVIELKY PLNCADPTSE RWFHGHLSGK
EAEKLLTEKG KHGSFLVRES QSHPGDFVLS VRTGDDKGES NDGKSKVTHV MIRCQELKYD
VGGGERFDSL TDLVEHYKKN PMVETLGTVL QLKQPLNTTR INAAEIESRV RELSKLAETT
DKVKQGFWEE FETLQQQECK LLYSRKEGQR QENKNKNRYK NILPFDHTRV VLHDGDPNEP
VSDYINANII MPEFETKCNN SKPKKSYIAT QGCLQNTVND FWRMVFQENS RVIVMTTKEV
ERGKSKCVKY WPDEYALKEY GVMRVRNVKE SAAHDYTLRE LKLSKVGQAL LQGNTERTVW
QYHFRTWPDH GVPSDPGGVL DFLEEVHHKQ ESIMDAGPVV VHCSAGIGRT GTFIVIDILI
DIIREKGVDC DIDVPKTIQM VRSQRSGMVQ TEAQYRFIYM AVQHYIETLQ RRIEEEQKSK
RKGHEYTNIK YSLADQTSGD QSPLPPCTPT PPCAEMREDS ARVYENVGLM QQQKSFR


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