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Myotubularin (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (EC 3.1.3.95) (Phosphatidylinositol-3-phosphate phosphatase) (EC 3.1.3.64)

 MTM1_HUMAN              Reviewed;         603 AA.
Q13496; A6NDB1; B7Z491; F2Z330; Q8NEL1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
22-NOV-2017, entry version 167.
RecName: Full=Myotubularin;
AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
EC=3.1.3.95 {ECO:0000269|PubMed:12646134};
AltName: Full=Phosphatidylinositol-3-phosphate phosphatase;
EC=3.1.3.64 {ECO:0000269|PubMed:10900271, ECO:0000269|PubMed:11001925, ECO:0000269|PubMed:12646134, ECO:0000269|PubMed:12847286};
Name=MTM1; Synonyms=CG2;
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).
PubMed=8640223; DOI=10.1038/ng0696-175;
Laporte J., Hu L.-J., Kretz C., Mandel J.-L., Kioschis P., Coy J.,
Klauck S.M., Poutska A., Dahl N.;
"A gene mutated in X-linked myotubular myopathy defines a new putative
tyrosine phosphatase family conserved in yeast.";
Nat. Genet. 13:175-182(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9781038; DOI=10.1038/sj.ejhg.5200189;
Laporte J., Guiraud-Chaumeil C., Tanner S.M., Blondeau F., Hu L.J.,
Vicaire S., Liechti-Gallati S., Mandel J.-L.;
"Genomic organization of the MTM1 gene implicated in X-linked
myotubular myopathy.";
Eur. J. Hum. Genet. 6:325-330(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Umbilical cord blood;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
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).
[7]
FUNCTION, AND INTERACTION WITH KMT2A/MLL1.
PubMed=9537414; DOI=10.1038/ng0498-331;
Cui X., De Vivo I., Slany R., Miyamoto A., Firestein R., Cleary M.L.;
"Association of SET domain and myotubularin-related proteins modulates
growth control.";
Nat. Genet. 18:331-337(1998).
[8]
REVIEW ON VARIANTS CNMX.
PubMed=10790201;
DOI=10.1002/(SICI)1098-1004(200005)15:5<393::AID-HUMU1>3.0.CO;2-R;
Laporte J., Biancalana V., Tanner S.M., Kress W., Schneider V.,
Wallgren-Pettersson C., Herger F., Buj-Bello A., Blondeau F.,
Liechti-Gallati S., Mandel J.-L.;
"MTM1 mutations in X-linked myotubular myopathy.";
Hum. Mutat. 15:393-409(2000).
[9]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
ASP-278; CYS-375; ASP-377; ASP-380; ASP-394; GLU-410 AND ASP-443.
PubMed=11001925; DOI=10.1093/oxfordjournals.hmg.a018913;
Blondeau F., Laporte J., Bodin S., Superti-Furga G., Payrastre B.,
Mandel J.L.;
"Myotubularin, a phosphatase deficient in myotubular myopathy, acts on
phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate
pathway.";
Hum. Mol. Genet. 9:2223-2229(2000).
[10]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, CHARACTERIZATION
OF VARIANTS LEU-205; LEU-241; ASN-376; ARG-378 AND CYS-397, AND
MUTAGENESIS OF CYS-375.
PubMed=10900271; DOI=10.1073/pnas.160255697;
Taylor G.S., Maehama T., Dixon J.E.;
"Myotubularin, a protein tyrosine phosphatase mutated in myotubular
myopathy, dephosphorylates the lipid second messenger,
phosphatidylinositol 3-phosphate.";
Proc. Natl. Acad. Sci. U.S.A. 97:8910-8915(2000).
[11]
SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-257; ASP-278; CYS-375;
ASP-377 AND ASP-380.
PubMed=12118066;
Laporte J., Blondeau F., Gansmuller A., Lutz Y., Vonesch J.L.,
Mandel J.L.;
"The PtdIns3P phosphatase myotubularin is a cytoplasmic protein that
also localizes to Rac1-inducible plasma membrane ruffles.";
J. Cell Sci. 115:3105-3117(2002).
[12]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, CHARACTERIZATION OF
VARIANTS CYS-69; GLY-184; LEU-241 AND GLN-421, AND MUTAGENESIS OF
LYS-114; ARG-220 AND CYS-375.
PubMed=12646134; DOI=10.1016/S0960-9822(03)00132-5;
Schaletzky J., Dove S.K., Short B., Lorenzo O., Clague M.J.,
Barr F.A.;
"Phosphatidylinositol-5-phosphate activation and conserved substrate
specificity of the myotubularin phosphatidylinositol 3-phosphatases.";
Curr. Biol. 13:504-509(2003).
[13]
CATALYTIC ACTIVITY, INTERACTION WITH MTMR12, SUBCELLULAR LOCATION, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12847286; DOI=10.1073/pnas.1033097100;
Nandurkar H.H., Layton M., Laporte J., Selan C., Corcoran L.,
Caldwell K.K., Mochizuki Y., Majerus P.W., Mitchell C.A.;
"Identification of myotubularin as the lipid phosphatase catalytic
subunit associated with the 3-phosphatase adapter protein, 3-PAP.";
Proc. Natl. Acad. Sci. U.S.A. 100:8660-8665(2003).
[14]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, ROLE OF
GRAM DOMAIN, AND CHARACTERIZATION OF VARIANTS PHE-49; CYS-69; PHE-70
AND PRO-87.
PubMed=14722070; DOI=10.1074/jbc.M312294200;
Tsujita K., Itoh T., Ijuin T., Yamamoto A., Shisheva A., Laporte J.,
Takenawa T.;
"Myotubularin regulates the function of the late endosome through the
gram domain-phosphatidylinositol 3,5-bisphosphate interaction.";
J. Biol. Chem. 279:13817-13824(2004).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-495, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, AND 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).
[18]
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).
[19]
FUNCTION, INTERACTION WITH DES, CHARACTERIZATION OF VARIANTS GLY-184;
LEU-205; CYS-241 AND GLN-421, AND MUTAGENESIS OF HIS-181; TYR-206;
SER-209; LYS-255; LYS-269; ASP-278; CYS-375; ASP-380 AND SER-420.
PubMed=21135508; DOI=10.1172/JCI44021;
Hnia K., Tronchere H., Tomczak K.K., Amoasii L., Schultz P.,
Beggs A.H., Payrastre B., Mandel J.L., Laporte J.;
"Myotubularin controls desmin intermediate filament architecture and
mitochondrial dynamics in human and mouse skeletal muscle.";
J. Clin. Invest. 121:70-85(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-18, 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).
[21]
INTERACTION WITH SPEG.
PubMed=25087613; DOI=10.1016/j.ajhg.2014.07.004;
Agrawal P.B., Pierson C.R., Joshi M., Liu X., Ravenscroft G.,
Moghadaszadeh B., Talabere T., Viola M., Swanson L.C., Haliloglu G.,
Talim B., Yau K.S., Allcock R.J., Laing N.G., Perrella M.A.,
Beggs A.H.;
"SPEG interacts with myotubularin, and its deficiency causes
centronuclear myopathy with dilated cardiomyopathy.";
Am. J. Hum. Genet. 95:218-226(2014).
[22]
VARIANTS CNMX CYS-69; GLY-184; ASN-198; LEU-241; ARG-317; CYS-397;
LYS-404; PRO-406; GLN-421 AND ARG-499.
PubMed=9285787; DOI=10.1093/hmg/6.9.1499;
de Gouyon B.M., Zhao W., Laporte J., Mandel J.-L., Metzenberg A.,
Herman G.E.;
"Characterization of mutations in the myotubularin gene in twenty six
patients with X-linked myotubular myopathy.";
Hum. Mol. Genet. 6:1499-1504(1997).
[23]
VARIANTS CNMX CYS-69; PHE-70; PRO-87; SER-189; LEU-205; PRO-229;
CYS-241; ASN-376; ARG-378; CYS-397; ALA-402; GLN-421; ASN-431; ASN-433
AND PRO-469.
PubMed=9305655; DOI=10.1093/hmg/6.9.1505;
Laporte J., Guiraud-Chaumeil C., Vincent M.-C., Mandel J.-L.,
Tanner S.M., Liechti-Gallati S., Wallgren-Pettersson C., Dahl N.,
Kress W., Bolhuis P.A., Fardeau M., Samson F., Bertini E.;
"Mutations in the MTM1 gene implicated in X-linked myotubular
myopathy.";
Hum. Mol. Genet. 6:1505-1511(1997).
[24]
VARIANT CNMX VAL-402.
PubMed=9829274; DOI=10.1016/S0960-8966(98)00075-3;
Nishino I., Minami N., Kobayashi O., Ikezawa M., Goto Y., Arahata K.,
Nonaka I.;
"MTM1 gene mutations in Japanese patients with the severe infantile
form of myotubular myopathy.";
Neuromuscul. Disord. 8:453-458(1998).
[25]
VARIANT CNMX GLU-378.
PubMed=10466421; DOI=10.1034/j.1399-0004.1999.560111.x;
Haene B.G., Rogers R.C., Schwartz C.E.;
"Germline mosaicism in X-linked myotubular myopathy.";
Clin. Genet. 56:77-81(1999).
[26]
VARIANTS CNMX SER-179; THR-225; CYS-241; SER-264; GLY-294 DEL; ARG-378
AND ASN-510.
PubMed=10502779;
DOI=10.1002/(SICI)1098-1004(199910)14:4<320::AID-HUMU7>3.0.CO;2-O;
Buj-Bello A., Biancalana V., Moutou C., Laporte J., Mandel J.-L.;
"Identification of novel mutations in the MTM1 gene causing severe and
mild forms of X-linked myotubular myopathy.";
Hum. Mutat. 14:320-325(1999).
[27]
VARIANTS CNMX LEU-205; THR-225; CYS-230; ARG-232; CYS-241; ARG-402 AND
TYR-444.
PubMed=10063835; DOI=10.1016/S0960-8966(98)00090-X;
Tanner S.M., Schneider V., Thomas N.S.T., Clarke A., Lazarou L.,
Liechti-Gallati S.;
"Characterization of 34 novel and six known MTM1 gene mutations in 47
unrelated X-linked myotubular myopathy patients.";
Neuromuscul. Disord. 9:41-49(1999).
[28]
VARIANTS CNMX PHE-49; CYS-69; SER-179; ILE-186; LEU-205; MET-227;
PRO-228; CYS-241; GLY-279; ARG-378; PRO-391; CYS-397; ARG-402 AND
GLN-421.
PubMed=11793470; DOI=10.1002/humu.10033;
Herman G.E., Kopacz K., Zhao W., Mills P.L., Metzenberg A., Das S.;
"Characterization of mutations in fifty North American patients with
X-linked myotubular myopathy.";
Hum. Mutat. 19:114-121(2002).
[29]
VARIANTS CNMX ILE-197; SER-199; ARG-378 AND ARG-402.
PubMed=12031625; DOI=10.1016/S0960-8966(01)00328-5;
Flex E., De Luca A., D'Apice M.R., Buccino A., Dallapiccola B.,
Novelli G.;
"Rapid scanning of myotubularin (MTM1) gene by denaturing high-
performance liquid chromatography (DHPLC).";
Neuromuscul. Disord. 12:501-505(2002).
[30]
VARIANT CNMX LYS-157.
PubMed=12859411; DOI=10.1034/j.1399-0004.2003.00118.x;
Yu S., Manson J., White S., Bourne A., Waddy H., Davis M., Haan E.;
"X-linked myotubular myopathy in a family with three adult
survivors.";
Clin. Genet. 64:148-152(2003).
[31]
VARIANTS CNMX LYS-47 DEL; ASP-68; PRO-69; SER-69; PHE-70; LYS-180;
LEU-184; SER-202; LEU-205; THR-226; CYS-230; CYS-241; CYS-346;
GLY-364; ASP-389; CYS-397; GLN-421; PRO-469; PRO-470 AND TYR-481.
PubMed=12522554; DOI=10.1007/s00439-002-0869-1;
Biancalana V., Caron O., Gallati S., Baas F., Kress W., Novelli G.,
D'Apice M.R., Lagier-Tourenne C., Buj-Bello A., Romero N.B.,
Mandel J.-L.;
"Characterisation of mutations in 77 patients with X-linked myotubular
myopathy, including a family with a very mild phenotype.";
Hum. Genet. 112:135-142(2003).
[32]
VARIANT CNMX LYS-404.
PubMed=17005396; DOI=10.1016/j.nmd.2006.07.020;
Hoffjan S., Thiels C., Vorgerd M., Neuen-Jacob E., Epplen J.T.,
Kress W.;
"Extreme phenotypic variability in a German family with X-linked
myotubular myopathy associated with E404K mutation in MTM1.";
Neuromuscul. Disord. 16:749-753(2006).
[33]
VARIANT CNMX TYR-387.
PubMed=19129059; DOI=10.1016/S0929-6646(09)60022-X;
Chang C.Y., Lin S.P., Lin H.Y., Chuang C.K., Ho C.S., Su Y.N.;
"X-linked myotubular myopathy with a novel MTM1 mutation in a
Taiwanese child.";
J. Formos. Med. Assoc. 107:965-970(2008).
-!- FUNCTION: Lipid phosphatase which dephosphorylates
phosphatidylinositol 3-monophosphate (PI3P) and
phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2). Has also been
shown to dephosphorylate phosphotyrosine- and phosphoserine-
containing peptides. Negatively regulates EGFR degradation through
regulation of EGFR trafficking from the late endosome to the
lysosome. Plays a role in vacuolar formation and morphology.
Regulates desmin intermediate filament assembly and architecture.
Plays a role in mitochondrial morphology and positioning. Required
for skeletal muscle maintenance but not for myogenesis.
{ECO:0000269|PubMed:10900271, ECO:0000269|PubMed:11001925,
ECO:0000269|PubMed:12646134, ECO:0000269|PubMed:14722070,
ECO:0000269|PubMed:21135508, ECO:0000269|PubMed:9537414}.
-!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 3-phosphate +
H(2)O = 1-phosphatidyl-1D-myo-inositol + phosphate.
{ECO:0000269|PubMed:10900271, ECO:0000269|PubMed:11001925,
ECO:0000269|PubMed:12646134, ECO:0000269|PubMed:12847286}.
-!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 3,5-
bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 5-phosphate
+ phosphate. {ECO:0000269|PubMed:12646134}.
-!- ENZYME REGULATION: Allosterically activated by
phosphatidylinositol 5-phosphate (PI5P).
{ECO:0000269|PubMed:12646134}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=39 uM for PI3P {ECO:0000269|PubMed:14722070};
KM=17 uM for PI(3,5)P2 {ECO:0000269|PubMed:14722070};
-!- SUBUNIT: Interacts with MTMR12; the interaction modulates MTM1
intracellular localization. Interacts with KMT2A/MLL1 (via SET
domain). Interacts with DES in skeletal muscle but not in cardiac
muscle. Interacts with SPEG. {ECO:0000269|PubMed:12847286,
ECO:0000269|PubMed:21135508, ECO:0000269|PubMed:25087613,
ECO:0000269|PubMed:9537414}.
-!- INTERACTION:
O00499:BIN1; NbExp=6; IntAct=EBI-2864109, EBI-719094;
P17661:DES; NbExp=13; IntAct=EBI-2864109, EBI-1055572;
P31001:Des (xeno); NbExp=4; IntAct=EBI-2864109, EBI-298565;
Q96A65:EXOC4; NbExp=2; IntAct=EBI-2864109, EBI-355383;
Q9C0I1:MTMR12; NbExp=4; IntAct=EBI-2864109, EBI-2829520;
O70172:Pip4k2a (xeno); NbExp=2; IntAct=EBI-2864109, EBI-644828;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10900271,
ECO:0000269|PubMed:11001925}. Cell membrane; Peripheral membrane
protein {ECO:0000269|PubMed:11001925}. Cell projection, filopodium
{ECO:0000269|PubMed:12118066}. Cell projection, ruffle
{ECO:0000269|PubMed:12118066}. Late endosome
{ECO:0000269|PubMed:14722070}. Note=Localizes as a dense
cytoplasmic network. Also localizes to the plasma membrane,
including plasma membrane extensions such as filopodia and
ruffles. Predominantly located in the cytoplasm following
interaction with MTMR12. Recruited to the late endosome following
EGF stimulation. {ECO:0000269|PubMed:11001925,
ECO:0000269|PubMed:12118066}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13496-1; Sequence=Displayed;
Name=2;
IsoId=Q13496-2; Sequence=VSP_056208;
Note=No experimental confirmation available.;
-!- DOMAIN: The GRAM domain mediates binding to PI(3,5)P2 and, with
lower affinity, to other phosphoinositides.
-!- DISEASE: Myopathy, centronuclear, X-linked (CNMX) [MIM:310400]: A
congenital muscle disorder characterized by progressive muscular
weakness and wasting involving mainly limb girdle, trunk, and neck
muscles. It may also affect distal muscles. Weakness may be
present during childhood or adolescence or may not become evident
until the third decade of life. Ptosis is a frequent clinical
feature. The most prominent histopathologic features include high
frequency of centrally located nuclei in muscle fibers not
secondary to regeneration, radial arrangement of sarcoplasmic
strands around the central nuclei, and predominance and hypotrophy
of type 1 fibers. {ECO:0000269|PubMed:10063835,
ECO:0000269|PubMed:10466421, ECO:0000269|PubMed:10502779,
ECO:0000269|PubMed:10790201, ECO:0000269|PubMed:11793470,
ECO:0000269|PubMed:12031625, ECO:0000269|PubMed:12522554,
ECO:0000269|PubMed:12859411, ECO:0000269|PubMed:17005396,
ECO:0000269|PubMed:19129059, ECO:0000269|PubMed:9285787,
ECO:0000269|PubMed:9305655, ECO:0000269|PubMed:9829274}. 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 myotubularin subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Leiden Muscular Dystrophy pages, Myotubularin 1
(MTM1); Note=Leiden Open Variation Database (LOVD);
URL="http://www.lovd.nl/MTM1";
-----------------------------------------------------------------------
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EMBL; U46024; AAC51682.1; -; mRNA.
EMBL; AF020676; AAC12865.1; -; Genomic_DNA.
EMBL; AF020664; AAC12865.1; JOINED; Genomic_DNA.
EMBL; AF020665; AAC12865.1; JOINED; Genomic_DNA.
EMBL; AF020666; AAC12865.1; JOINED; Genomic_DNA.
EMBL; AF020667; AAC12865.1; JOINED; Genomic_DNA.
EMBL; AF020668; AAC12865.1; JOINED; Genomic_DNA.
EMBL; AF020669; AAC12865.1; JOINED; Genomic_DNA.
EMBL; AF020670; AAC12865.1; JOINED; Genomic_DNA.
EMBL; AF020671; AAC12865.1; JOINED; Genomic_DNA.
EMBL; AF020672; AAC12865.1; JOINED; Genomic_DNA.
EMBL; AF020673; AAC12865.1; JOINED; Genomic_DNA.
EMBL; AF020674; AAC12865.1; JOINED; Genomic_DNA.
EMBL; AF020675; AAC12865.1; JOINED; Genomic_DNA.
EMBL; AK297021; BAH12477.1; -; mRNA.
EMBL; AC109994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF002223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471169; EAW99377.1; -; Genomic_DNA.
EMBL; BC030779; AAH30779.1; -; mRNA.
CCDS; CCDS14694.1; -. [Q13496-1]
RefSeq; NP_000243.1; NM_000252.2. [Q13496-1]
RefSeq; XP_005274744.1; XM_005274687.2. [Q13496-1]
RefSeq; XP_011529475.1; XM_011531173.2. [Q13496-1]
RefSeq; XP_016885039.1; XM_017029550.1. [Q13496-2]
UniGene; Hs.655056; -.
ProteinModelPortal; Q13496; -.
SMR; Q13496; -.
BioGrid; 110630; 33.
DIP; DIP-61934N; -.
IntAct; Q13496; 8.
STRING; 9606.ENSP00000359423; -.
SwissLipids; SLP:000000846; -.
SwissLipids; SLP:000000847; -.
DEPOD; Q13496; -.
iPTMnet; Q13496; -.
PhosphoSitePlus; Q13496; -.
BioMuta; MTM1; -.
DMDM; 2851537; -.
EPD; Q13496; -.
MaxQB; Q13496; -.
PaxDb; Q13496; -.
PeptideAtlas; Q13496; -.
PRIDE; Q13496; -.
DNASU; 4534; -.
Ensembl; ENST00000370396; ENSP00000359423; ENSG00000171100. [Q13496-1]
GeneID; 4534; -.
KEGG; hsa:4534; -.
UCSC; uc004fef.5; human. [Q13496-1]
CTD; 4534; -.
DisGeNET; 4534; -.
EuPathDB; HostDB:ENSG00000171100.14; -.
GeneCards; MTM1; -.
GeneReviews; MTM1; -.
HGNC; HGNC:7448; MTM1.
HPA; HPA010008; -.
HPA; HPA010665; -.
MalaCards; MTM1; -.
MIM; 300415; gene.
MIM; 310400; phenotype.
neXtProt; NX_Q13496; -.
OpenTargets; ENSG00000171100; -.
Orphanet; 596; X-linked centronuclear myopathy.
PharmGKB; PA31251; -.
eggNOG; KOG1089; Eukaryota.
eggNOG; ENOG410XPTU; LUCA.
GeneTree; ENSGT00760000118832; -.
HOGENOM; HOG000210598; -.
HOVERGEN; HBG000220; -.
InParanoid; Q13496; -.
KO; K01108; -.
OMA; PNHHWRI; -.
OrthoDB; EOG091G04DS; -.
PhylomeDB; Q13496; -.
TreeFam; TF315197; -.
BRENDA; 3.1.3.64; 2681.
BRENDA; 3.1.3.95; 2681.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-HSA-1660516; Synthesis of PIPs at the early endosome membrane.
Reactome; R-HSA-1660517; Synthesis of PIPs at the late endosome membrane.
SABIO-RK; Q13496; -.
ChiTaRS; MTM1; human.
GeneWiki; Myotubularin_1; -.
GenomeRNAi; 4534; -.
PRO; PR:Q13496; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000171100; -.
CleanEx; HS_MTM1; -.
ExpressionAtlas; Q13496; baseline and differential.
Genevisible; Q13496; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0030175; C:filopodium; IDA:UniProtKB.
GO; GO:0031674; C:I band; IEA:Ensembl.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IDA:UniProtKB.
GO; GO:0019215; F:intermediate filament binding; IDA:UniProtKB.
GO; GO:0035091; F:phosphatidylinositol binding; IDA:UniProtKB.
GO; GO:0052629; F:phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity; IDA:UniProtKB.
GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IDA:UniProtKB.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:UniProtKB.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
GO; GO:0008333; P:endosome to lysosome transport; IDA:UniProtKB.
GO; GO:0045109; P:intermediate filament organization; IMP:UniProtKB.
GO; GO:0048311; P:mitochondrion distribution; IMP:UniProtKB.
GO; GO:0070584; P:mitochondrion morphogenesis; IDA:UniProtKB.
GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
GO; GO:1902902; P:negative regulation of autophagosome assembly; IEA:Ensembl.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:0032007; P:negative regulation of TOR signaling; IEA:Ensembl.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
GO; GO:0048633; P:positive regulation of skeletal muscle tissue growth; IEA:Ensembl.
GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0044088; P:regulation of vacuole organization; IDA:UniProtKB.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR004182; GRAM.
InterPro; IPR030561; Myotubularin.
InterPro; IPR010569; Myotubularin-like_Pase_dom.
InterPro; IPR030564; Myotubularin_fam.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
PANTHER; PTHR10807; PTHR10807; 1.
PANTHER; PTHR10807:SF69; PTHR10807:SF69; 1.
Pfam; PF02893; GRAM; 1.
Pfam; PF06602; Myotub-related; 1.
SMART; SM00568; GRAM; 1.
SMART; SM00404; PTPc_motif; 1.
SUPFAM; SSF50729; SSF50729; 1.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Disease mutation; Endosome; Hydrolase;
Lipid metabolism; Membrane; Phosphoprotein; Protein phosphatase;
Protein transport; Reference proteome; Transport.
CHAIN 1 603 Myotubularin.
/FTId=PRO_0000094930.
DOMAIN 29 97 GRAM.
DOMAIN 163 538 Myotubularin phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU00669}.
ACT_SITE 375 375 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU10044}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 495 495 Phosphothreonine.
{ECO:0000244|PubMed:16964243}.
MOD_RES 588 588 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
VAR_SEQ 78 114 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056208.
VARIANT 47 47 Missing (in CNMX).
{ECO:0000269|PubMed:12522554}.
/FTId=VAR_006386.
VARIANT 49 49 V -> F (in CNMX; greatly reduced binding
to PI(3,5)P2; does not translocate to the
late endosome following EGF stimulation;
shows normal EGFR degradation;
dbSNP:rs587783796).
{ECO:0000269|PubMed:11793470,
ECO:0000269|PubMed:14722070}.
/FTId=VAR_018227.
VARIANT 68 68 Y -> D (in CNMX).
{ECO:0000269|PubMed:12522554}.
/FTId=VAR_018228.
VARIANT 69 69 R -> C (in CNMX; mild; reduced response
to PI5P and reduced binding to PI(3,5)P2;
dbSNP:rs132630304).
{ECO:0000269|PubMed:11793470,
ECO:0000269|PubMed:12646134,
ECO:0000269|PubMed:14722070,
ECO:0000269|PubMed:9285787,
ECO:0000269|PubMed:9305655}.
/FTId=VAR_006387.
VARIANT 69 69 R -> P (in CNMX).
{ECO:0000269|PubMed:12522554}.
/FTId=VAR_018229.
VARIANT 69 69 R -> S (in CNMX; severe).
{ECO:0000269|PubMed:12522554}.
/FTId=VAR_018230.
VARIANT 70 70 L -> F (in CNMX; mild; reduced binding to
PI(3,5)P2; dbSNP:rs587783809).
{ECO:0000269|PubMed:12522554,
ECO:0000269|PubMed:14722070,
ECO:0000269|PubMed:9305655}.
/FTId=VAR_006388.
VARIANT 87 87 L -> P (in CNMX; mild; reduced binding to
PI(3,5)P2; dbSNP:rs587783816).
{ECO:0000269|PubMed:14722070,
ECO:0000269|PubMed:9305655}.
/FTId=VAR_006389.
VARIANT 157 157 E -> K (in CNMX; dbSNP:rs132630307).
{ECO:0000269|PubMed:12859411}.
/FTId=VAR_018231.
VARIANT 179 179 P -> S (in CNMX; mild;
dbSNP:rs587783832).
{ECO:0000269|PubMed:10502779,
ECO:0000269|PubMed:11793470}.
/FTId=VAR_009217.
VARIANT 180 180 N -> K (in CNMX; very mild).
{ECO:0000269|PubMed:12522554}.
/FTId=VAR_018232.
VARIANT 184 184 R -> G (in CNMX; severe; loss of
activity; abolishes interaction with DES;
dbSNP:rs587783835).
{ECO:0000269|PubMed:12646134,
ECO:0000269|PubMed:21135508,
ECO:0000269|PubMed:9285787}.
/FTId=VAR_006390.
VARIANT 184 184 R -> L (in CNMX).
{ECO:0000269|PubMed:12522554}.
/FTId=VAR_018233.
VARIANT 186 186 T -> I (in CNMX; dbSNP:rs587783836).
{ECO:0000269|PubMed:11793470}.
/FTId=VAR_018234.
VARIANT 189 189 N -> S (in CNMX; dbSNP:rs132630302).
{ECO:0000269|PubMed:9305655}.
/FTId=VAR_006391.
VARIANT 197 197 T -> I (in CNMX).
{ECO:0000269|PubMed:12031625}.
/FTId=VAR_018235.
VARIANT 198 198 Y -> N (in CNMX; severe).
{ECO:0000269|PubMed:9285787}.
/FTId=VAR_006392.
VARIANT 199 199 P -> S (in CNMX).
{ECO:0000269|PubMed:12031625}.
/FTId=VAR_018236.
VARIANT 202 202 L -> S (in CNMX; severe).
{ECO:0000269|PubMed:12522554}.
/FTId=VAR_018237.
VARIANT 205 205 P -> L (in CNMX; severe; dramatic
decrease in phosphatase activity;
abolishes interaction with DES;
dbSNP:rs587783841).
{ECO:0000269|PubMed:10063835,
ECO:0000269|PubMed:10900271,
ECO:0000269|PubMed:11793470,
ECO:0000269|PubMed:12522554,
ECO:0000269|PubMed:21135508,
ECO:0000269|PubMed:9305655}.
/FTId=VAR_006393.
VARIANT 225 225 I -> T (in CNMX; mild).
{ECO:0000269|PubMed:10063835,
ECO:0000269|PubMed:10502779}.
/FTId=VAR_009218.
VARIANT 226 226 P -> T (in CNMX; dbSNP:rs587783848).
{ECO:0000269|PubMed:12522554}.
/FTId=VAR_018238.
VARIANT 227 227 V -> M (in CNMX; dbSNP:rs587783850).
{ECO:0000269|PubMed:11793470}.
/FTId=VAR_018239.
VARIANT 228 228 L -> P (in CNMX; dbSNP:rs587783851).
{ECO:0000269|PubMed:11793470}.
/FTId=VAR_018240.
VARIANT 229 229 S -> P (in CNMX; mild).
{ECO:0000269|PubMed:9305655}.
/FTId=VAR_006394.
VARIANT 230 230 W -> C (in CNMX).
{ECO:0000269|PubMed:10063835,
ECO:0000269|PubMed:12522554}.
/FTId=VAR_018241.
VARIANT 232 232 H -> R (in CNMX).
{ECO:0000269|PubMed:10063835}.
/FTId=VAR_018242.
VARIANT 241 241 R -> C (in CNMX; mild to moderate;
abolishes interaction with DES;
dbSNP:rs132630305).
{ECO:0000269|PubMed:10063835,
ECO:0000269|PubMed:10502779,
ECO:0000269|PubMed:11793470,
ECO:0000269|PubMed:12522554,
ECO:0000269|PubMed:21135508,
ECO:0000269|PubMed:9305655}.
/FTId=VAR_006395.
VARIANT 241 241 R -> L (in CNMX; severe; loss of
activity). {ECO:0000269|PubMed:10900271,
ECO:0000269|PubMed:12646134,
ECO:0000269|PubMed:9285787}.
/FTId=VAR_006396.
VARIANT 264 264 I -> S (in CNMX; severe;
dbSNP:rs587783856).
{ECO:0000269|PubMed:10502779}.
/FTId=VAR_009219.
VARIANT 279 279 A -> G (in CNMX).
{ECO:0000269|PubMed:11793470}.
/FTId=VAR_018243.
VARIANT 294 294 Missing (in CNMX; mild).
{ECO:0000269|PubMed:10502779}.
/FTId=VAR_009220.
VARIANT 317 317 M -> R (in CNMX; mild).
{ECO:0000269|PubMed:9285787}.
/FTId=VAR_006397.
VARIANT 346 346 W -> C (in CNMX; mild).
{ECO:0000269|PubMed:12522554}.
/FTId=VAR_018244.
VARIANT 346 346 W -> S (in CNMX).
/FTId=VAR_018245.
VARIANT 364 364 V -> G (in CNMX).
{ECO:0000269|PubMed:12522554}.
/FTId=VAR_018246.
VARIANT 374 374 H -> D (in CNMX; dbSNP:rs587783754).
/FTId=VAR_018247.
VARIANT 376 376 S -> N (in CNMX; dramatic decrease in
phosphatase activity).
{ECO:0000269|PubMed:10900271,
ECO:0000269|PubMed:9305655}.
/FTId=VAR_006398.
VARIANT 378 378 G -> E (in CNMX).
{ECO:0000269|PubMed:10466421}.
/FTId=VAR_018248.
VARIANT 378 378 G -> R (in CNMX; severe; dramatic
decrease in phosphatase activity; does
not affect EGFR degradation;
dbSNP:rs587783755).
{ECO:0000269|PubMed:10502779,
ECO:0000269|PubMed:10900271,
ECO:0000269|PubMed:11793470,
ECO:0000269|PubMed:12031625,
ECO:0000269|PubMed:9305655}.
/FTId=VAR_006399.
VARIANT 387 387 S -> Y (in CNMX; dbSNP:rs587783759).
{ECO:0000269|PubMed:19129059}.
/FTId=VAR_068846.
VARIANT 389 389 A -> D (in CNMX; severe).
{ECO:0000269|PubMed:12522554}.
/FTId=VAR_018249.
VARIANT 391 391 L -> P (in CNMX).
{ECO:0000269|PubMed:11793470}.
/FTId=VAR_018250.
VARIANT 397 397 Y -> C (in CNMX; severe; dramatic
decrease in phosphatase activity;
dbSNP:rs132630303).
{ECO:0000269|PubMed:10900271,
ECO:0000269|PubMed:11793470,
ECO:0000269|PubMed:12522554,
ECO:0000269|PubMed:9285787,
ECO:0000269|PubMed:9305655}.
/FTId=VAR_006400.
VARIANT 402 402 G -> A (in CNMX; mild;
dbSNP:rs587783762).
{ECO:0000269|PubMed:9305655}.
/FTId=VAR_006401.
VARIANT 402 402 G -> R (in CNMX).
{ECO:0000269|PubMed:10063835,
ECO:0000269|PubMed:11793470,
ECO:0000269|PubMed:12031625}.
/FTId=VAR_018251.
VARIANT 402 402 G -> V (in CNMX).
{ECO:0000269|PubMed:9829274}.
/FTId=VAR_018252.
VARIANT 404 404 E -> K (in CNMX; mild;
dbSNP:rs781933660).
{ECO:0000269|PubMed:17005396,
ECO:0000269|PubMed:9285787}.
/FTId=VAR_006402.
VARIANT 406 406 L -> P (in CNMX; severe).
{ECO:0000269|PubMed:9285787}.
/FTId=VAR_006403.
VARIANT 411 411 W -> C (in CNMX; dbSNP:rs587783764).
/FTId=VAR_018253.
VARIANT 420 420 S -> SFIQ (in CNMX; severe).
/FTId=VAR_009221.
VARIANT 421 421 R -> Q (in CNMX; severe; reduced activity
and response to PI5P; does not affect
interaction with DES; dbSNP:rs587783772).
{ECO:0000269|PubMed:11793470,
ECO:0000269|PubMed:12522554,
ECO:0000269|PubMed:12646134,
ECO:0000269|PubMed:21135508,
ECO:0000269|PubMed:9285787,
ECO:0000269|PubMed:9305655}.
/FTId=VAR_006404.
VARIANT 421 421 R -> RFIQ (in CNMX; severe).
/FTId=VAR_006405.
VARIANT 431 431 D -> N (in CNMX).
{ECO:0000269|PubMed:9305655}.
/FTId=VAR_006406.
VARIANT 433 433 D -> N (in CNMX).
{ECO:0000269|PubMed:9305655}.
/FTId=VAR_006407.
VARIANT 444 444 C -> Y (in CNMX).
{ECO:0000269|PubMed:10063835}.
/FTId=VAR_018254.
VARIANT 469 469 H -> P (in CNMX).
{ECO:0000269|PubMed:12522554,
ECO:0000269|PubMed:9305655}.
/FTId=VAR_006408.
VARIANT 470 470 L -> P (in CNMX; severe).
{ECO:0000269|PubMed:12522554}.
/FTId=VAR_018255.
VARIANT 481 481 N -> Y (in CNMX; mild).
{ECO:0000269|PubMed:12522554}.
/FTId=VAR_018256.
VARIANT 499 499 W -> R (in CNMX; mild;
dbSNP:rs587783801).
{ECO:0000269|PubMed:9285787}.
/FTId=VAR_006409.
VARIANT 510 510 K -> N (in CNMX; severe).
{ECO:0000269|PubMed:10502779}.
/FTId=VAR_009222.
MUTAGEN 114 114 K->A: Reduced response to PI5P.
{ECO:0000269|PubMed:12646134}.
MUTAGEN 181 181 H->A: Disrupts interaction with DES. Does
not affect lipid phosphatase activity.
{ECO:0000269|PubMed:21135508}.
MUTAGEN 206 206 Y->A: Disrupts interaction with DES. Does
not affect lipid phosphatase activity.
{ECO:0000269|PubMed:21135508}.
MUTAGEN 209 209 S->A: Disrupts interaction with DES. Does
not affect lipid phosphatase activity.
{ECO:0000269|PubMed:21135508}.
MUTAGEN 220 220 R->A: Loss of activity.
{ECO:0000269|PubMed:12646134}.
MUTAGEN 255 255 K->A: Disrupts interaction with DES.
{ECO:0000269|PubMed:21135508}.
MUTAGEN 257 257 D->A: No effect on subcellular location.
{ECO:0000269|PubMed:12118066}.
MUTAGEN 269 269 K->A: Disrupts interaction with DES. Does
not affect lipid phosphatase activity.
{ECO:0000269|PubMed:21135508}.
MUTAGEN 278 278 D->A: Localizes to plasma membrane
extensions. Does not affect interaction
with DES. {ECO:0000269|PubMed:11001925,
ECO:0000269|PubMed:12118066,
ECO:0000269|PubMed:21135508}.
MUTAGEN 375 375 C->A: No effect on subcellular location.
{ECO:0000269|PubMed:10900271,
ECO:0000269|PubMed:11001925,
ECO:0000269|PubMed:12118066,
ECO:0000269|PubMed:12646134,
ECO:0000269|PubMed:21135508}.
MUTAGEN 375 375 C->S: Lacks activity toward PI3P. Does
not affect interaction with DES.
{ECO:0000269|PubMed:10900271,
ECO:0000269|PubMed:11001925,
ECO:0000269|PubMed:12118066,
ECO:0000269|PubMed:12646134,
ECO:0000269|PubMed:21135508}.
MUTAGEN 377 377 D->A: No effect on subcellular location.
{ECO:0000269|PubMed:11001925,
ECO:0000269|PubMed:12118066}.
MUTAGEN 380 380 D->A: Does not affect interaction with
DES. {ECO:0000269|PubMed:11001925,
ECO:0000269|PubMed:12118066,
ECO:0000269|PubMed:21135508}.
MUTAGEN 394 394 D->A: Produces an unstable protein.
{ECO:0000269|PubMed:11001925}.
MUTAGEN 410 410 E->A: Produces an unstable protein.
{ECO:0000269|PubMed:11001925}.
MUTAGEN 420 420 S->D: Does not affect interaction with
DES. {ECO:0000269|PubMed:21135508}.
MUTAGEN 443 443 D->A: Produces an unstable protein.
{ECO:0000269|PubMed:11001925}.
CONFLICT 410 410 E -> K (in Ref. 6; AAH30779).
{ECO:0000305}.
SEQUENCE 603 AA; 69932 MW; BE9770F2471957C0 CRC64;
MASASTSKYN SHSLENESIK RTSRDGVNRD LTEAVPRLPG ETLITDKEVI YICPFNGPIK
GRVYITNYRL YLRSLETDSS LILDVPLGVI SRIEKMGGAT SRGENSYGLD ITCKDMRNLR
FALKQEGHSR RDMFEILTRY AFPLAHSLPL FAFLNEEKFN VDGWTVYNPV EEYRRQGLPN
HHWRITFINK CYELCDTYPA LLVVPYRASD DDLRRVATFR SRNRIPVLSW IHPENKTVIV
RCSQPLVGMS GKRNKDDEKY LDVIRETNKQ ISKLTIYDAR PSVNAVANKA TGGGYESDDA
YHNAELFFLD IHNIHVMRES LKKVKDIVYP NVEESHWLSS LESTHWLEHI KLVLTGAIQV
ADKVSSGKSS VLVHCSDGWD RTAQLTSLAM LMLDSFYRSI EGFEILVQKE WISFGHKFAS
RIGHGDKNHT DADRSPIFLQ FIDCVWQMSK QFPTAFEFNE QFLIIILDHL YSCRFGTFLF
NCESARERQK VTERTVSLWS LINSNKEKFK NPFYTKEINR VLYPVASMRH LELWVNYYIR
WNPRIKQQQP NPVEQRYMEL LALRDEYIKR LEELQLANSA KLSDPPTSPS SPSQMMPHVQ
THF


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