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Myotubularin-related protein 2 (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (EC 3.1.3.95) (Phosphatidylinositol-3-phosphate phosphatase) (EC 3.1.3.64)

 MTMR2_HUMAN             Reviewed;         643 AA.
Q13614; A6NN98; Q9UPS9;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
04-NOV-2008, sequence version 4.
22-NOV-2017, entry version 183.
RecName: Full=Myotubularin-related protein 2;
AltName: Full=Phosphatidylinositol-3,5-bisphosphate 3-phosphatase;
EC=3.1.3.95 {ECO:0000269|PubMed:12668758};
AltName: Full=Phosphatidylinositol-3-phosphate phosphatase;
EC=3.1.3.64 {ECO:0000269|PubMed:11733541, ECO:0000269|PubMed:12668758};
Name=MTMR2; Synonyms=KIAA1073;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-3.
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV.
The complete sequences of 100 new cDNA clones from brain which code
for large proteins in vitro.";
DNA Res. 6:197-205(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT THR-3.
TISSUE=Uterus;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 384-643 (ISOFORM 1).
PubMed=9736772; DOI=10.1093/hmg/7.11.1703;
Laporte J., Blondeau F., Buj-Bello A., Tentler D., Kretz C., Dahl N.,
Mandel J.-L.;
"Characterization of the myotubularin dual specificity phosphatase
gene family from yeast to human.";
Hum. Mol. Genet. 7:1703-1712(1998).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 384-514 (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).
[8]
INVOLVEMENT IN CMT4B1.
PubMed=10802647; DOI=10.1038/75542;
Bolino A., Muglia M., Conforti F.L., LeGuern E., Salih M.A.M.,
Georgiou D.-M., Christodoulou K., Hausmanowa-Petrusewicz I.,
Mandich P., Schenone A., Gambardella A., Bono F., Quattrone A.,
Devoto M., Monaco A.P.;
"Charcot-Marie-Tooth type 4B is caused by mutations in the gene
encoding myotubularin-related protein-2.";
Nat. Genet. 25:17-19(2000).
[9]
FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=11733541; DOI=10.1074/jbc.M111087200;
Kim S.A., Taylor G.S., Torgersen K.M., Dixon J.E.;
"Myotubularin and MTMR2, phosphatidylinositol 3-phosphatases mutated
in myotubular myopathy and type 4B Charcot-Marie-Tooth disease.";
J. Biol. Chem. 277:4526-4531(2002).
[10]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, IDENTIFICATION BY
MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF
LEU-607, AND INTERACTION WITH SBF1.
PubMed=12668758; DOI=10.1073/pnas.0431052100;
Kim S.-A., Vacratsis P.O., Firestein R., Cleary M.L., Dixon J.E.;
"Regulation of myotubularin-related (MTMR)2 phosphatidylinositol
phosphatase by MTMR5, a catalytically inactive phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 100:4492-4497(2003).
[11]
INTERACTION WITH SBF2, SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=15998640; DOI=10.1074/jbc.M505159200;
Robinson F.L., Dixon J.E.;
"The phosphoinositide-3-phosphatase MTMR2 associates with MTMR13, a
membrane-associated pseudophosphatase also mutated in type 4B Charcot-
Marie-Tooth disease.";
J. Biol. Chem. 280:31699-31707(2005).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, 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).
[13]
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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, 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).
[15]
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).
[16]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-58.
PubMed=21372139; DOI=10.1074/jbc.M110.209122;
Franklin N.E., Taylor G.S., Vacratsis P.O.;
"Endosomal targeting of the phosphoinositide 3-phosphatase MTMR2 is
regulated by an N-terminal phosphorylation site.";
J. Biol. Chem. 286:15841-15853(2011).
[17]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT SER-417 IN COMPLEX
WITH PHOSPHOINOSITIDE, IDENTIFICATION BY MASS SPECTROMETRY, AND
MUTAGENESIS OF CYS-417; ASP-419 AND ASP-422.
PubMed=14690594; DOI=10.1016/S1097-2765(03)00486-6;
Begley M.J., Taylor G.S., Kim S.-A., Veine D.M., Dixon J.E.,
Stuckey J.A.;
"Crystal structure of a phosphoinositide phosphatase, MTMR2: insights
into myotubular myopathy and Charcot-Marie-Tooth syndrome.";
Mol. Cell 12:1391-1402(2003).
[18]
X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 71-586 OF MUTANT SER-417 IN
COMPLEX WITH PHOSPHOINOSITIDES, COILED-COIL DOMAIN, IDENTIFICATION BY
MASS SPECTROMETRY, AND MUTAGENESIS OF CYS-417.
PubMed=16410353; DOI=10.1073/pnas.0510006103;
Begley M.J., Taylor G.S., Brock M.A., Ghosh P., Woods V.L.,
Dixon J.E.;
"Molecular basis for substrate recognition by MTMR2, a myotubularin
family phosphoinositide phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 103:927-932(2006).
[19]
VARIANT CMT4B1 TRP-283.
PubMed=12398840; DOI=10.1016/S0960-8966(02)00046-9;
Nelis E., Erdem S., Tan E., Loefgren A., Ceuterick C., De Jonghe P.,
Van Broeckhoven C., Timmerman V., Topaloglu H.;
"A novel homozygous missense mutation in the myotubularin-related
protein 2 gene associated with recessive Charcot-Marie-Tooth disease
with irregularly folded myelin sheaths.";
Neuromuscul. Disord. 12:869-873(2002).
-!- FUNCTION: Phosphatase that acts on lipids with a phosphoinositol
headgroup. Has phosphatase activity towards phosphatidylinositol
3-phosphate and phosphatidylinositol 3,5-bisphosphate.
{ECO:0000269|PubMed:11733541, ECO:0000269|PubMed:12668758,
ECO:0000269|PubMed:21372139}.
-!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 3-phosphate +
H(2)O = 1-phosphatidyl-1D-myo-inositol + phosphate.
{ECO:0000269|PubMed:11733541, ECO:0000269|PubMed:12668758}.
-!- CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 3,5-
bisphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 5-phosphate
+ phosphate. {ECO:0000269|PubMed:12668758}.
-!- ENZYME REGULATION: Interaction with SBF1 increases phosphatase
activity. {ECO:0000269|PubMed:12668758}.
-!- SUBUNIT: Homooligomer and heterooligomer. Interacts with SBF1 and
SBF2. {ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:14690594,
ECO:0000269|PubMed:15998640, ECO:0000269|PubMed:16410353}.
-!- INTERACTION:
P07196:NEFL; NbExp=2; IntAct=EBI-475631, EBI-475646;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11733541,
ECO:0000269|PubMed:12668758}. Early endosome membrane
{ECO:0000269|PubMed:21372139}; Peripheral membrane protein
{ECO:0000269|PubMed:21372139}. Note=Partly associated with
membranes. {ECO:0000269|PubMed:12668758,
ECO:0000269|PubMed:21372139, ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13614-1; Sequence=Displayed;
Name=2;
IsoId=Q13614-2; Sequence=VSP_044933;
Note=No experimental confirmation available.;
-!- DOMAIN: The coiled-coil domain mediates interaction with SBF2.
-!- PTM: Phosphorylation at Ser-58 decreases MTMR2 localization to
endocytic vesicular structures. {ECO:0000269|PubMed:21372139}.
-!- DISEASE: Charcot-Marie-Tooth disease 4B1 (CMT4B1) [MIM:601382]: A
recessive demyelinating form of Charcot-Marie-Tooth disease, a
disorder of the peripheral nervous system, characterized by
progressive weakness and atrophy, initially of the peroneal
muscles and later of the distal muscles of the arms. Charcot-
Marie-Tooth disease is classified in two main groups on the basis
of electrophysiologic properties and histopathology: primary
peripheral demyelinating neuropathies (designated CMT1 when they
are dominantly inherited) and primary peripheral axonal
neuropathies (CMT2). Demyelinating neuropathies are characterized
by severely reduced nerve conduction velocities (less than 38
m/sec), segmental demyelination and remyelination with onion bulb
formations on nerve biopsy, slowly progressive distal muscle
atrophy and weakness, absent deep tendon reflexes, and hollow
feet. By convention autosomal recessive forms of demyelinating
Charcot-Marie-Tooth disease are designated CMT4.
{ECO:0000269|PubMed:10802647, ECO:0000269|PubMed:12398840}.
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}.
-!- SEQUENCE CAUTION:
Sequence=BAA83025.2; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Inherited peripheral neuropathies mutation db;
URL="http://www.molgen.ua.ac.be/CMTMutations/";
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EMBL; AB028996; BAA83025.2; ALT_INIT; mRNA.
EMBL; AK302940; BAG64098.1; -; mRNA.
EMBL; AP000870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP001877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471065; EAW66971.1; -; Genomic_DNA.
EMBL; BC052990; AAH52990.1; -; mRNA.
EMBL; U58033; AAC79118.1; -; mRNA.
CCDS; CCDS8305.1; -. [Q13614-1]
CCDS; CCDS8306.1; -. [Q13614-2]
PIR; T09497; T09497.
RefSeq; NP_001230500.1; NM_001243571.1. [Q13614-2]
RefSeq; NP_057240.3; NM_016156.5. [Q13614-1]
RefSeq; NP_958435.1; NM_201278.2. [Q13614-2]
RefSeq; NP_958438.1; NM_201281.2. [Q13614-2]
RefSeq; XP_005274431.1; XM_005274374.2. [Q13614-2]
RefSeq; XP_005274432.1; XM_005274375.2. [Q13614-2]
RefSeq; XP_006718997.1; XM_006718934.2. [Q13614-2]
RefSeq; XP_006718998.1; XM_006718935.2. [Q13614-2]
RefSeq; XP_006718999.1; XM_006718936.3. [Q13614-2]
RefSeq; XP_016874006.1; XM_017018517.1. [Q13614-2]
RefSeq; XP_016874007.1; XM_017018518.1. [Q13614-2]
UniGene; Hs.181326; -.
PDB; 1LW3; X-ray; 2.30 A; A=1-643.
PDB; 1M7R; X-ray; 2.60 A; A/B=1-643.
PDB; 1ZSQ; X-ray; 1.82 A; A=73-586.
PDB; 1ZVR; X-ray; 1.98 A; A=73-586.
PDB; 5GNH; X-ray; 2.60 A; A/B=73-643.
PDBsum; 1LW3; -.
PDBsum; 1M7R; -.
PDBsum; 1ZSQ; -.
PDBsum; 1ZVR; -.
PDBsum; 5GNH; -.
ProteinModelPortal; Q13614; -.
SMR; Q13614; -.
BioGrid; 114415; 34.
IntAct; Q13614; 5.
MINT; MINT-6774021; -.
STRING; 9606.ENSP00000345752; -.
SwissLipids; SLP:000001135; -.
DEPOD; Q13614; -.
iPTMnet; Q13614; -.
PhosphoSitePlus; Q13614; -.
SwissPalm; Q13614; -.
BioMuta; MTMR2; -.
DMDM; 212276520; -.
EPD; Q13614; -.
MaxQB; Q13614; -.
PaxDb; Q13614; -.
PeptideAtlas; Q13614; -.
PRIDE; Q13614; -.
Ensembl; ENST00000346299; ENSP00000345752; ENSG00000087053. [Q13614-1]
Ensembl; ENST00000352297; ENSP00000343737; ENSG00000087053. [Q13614-2]
Ensembl; ENST00000393223; ENSP00000376915; ENSG00000087053. [Q13614-2]
Ensembl; ENST00000409459; ENSP00000386882; ENSG00000087053. [Q13614-2]
GeneID; 8898; -.
KEGG; hsa:8898; -.
UCSC; uc001pft.4; human. [Q13614-1]
CTD; 8898; -.
DisGeNET; 8898; -.
EuPathDB; HostDB:ENSG00000087053.18; -.
GeneCards; MTMR2; -.
GeneReviews; MTMR2; -.
HGNC; HGNC:7450; MTMR2.
HPA; HPA049831; -.
MalaCards; MTMR2; -.
MIM; 601382; phenotype.
MIM; 603557; gene.
neXtProt; NX_Q13614; -.
OpenTargets; ENSG00000087053; -.
Orphanet; 99955; Charcot-Marie-Tooth disease type 4B1.
PharmGKB; PA31253; -.
eggNOG; KOG1089; Eukaryota.
eggNOG; ENOG410XPTU; LUCA.
GeneTree; ENSGT00760000118832; -.
HOGENOM; HOG000210598; -.
HOVERGEN; HBG000220; -.
InParanoid; Q13614; -.
KO; K18081; -.
OMA; IMEANAQ; -.
OrthoDB; EOG091G04DS; -.
PhylomeDB; Q13614; -.
TreeFam; TF315197; -.
BRENDA; 3.1.3.64; 2681.
BRENDA; 3.1.3.95; 2681.
Reactome; R-HSA-1483248; Synthesis of PIPs at the ER membrane.
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.
ChiTaRS; MTMR2; human.
EvolutionaryTrace; Q13614; -.
GeneWiki; MTMR2; -.
GenomeRNAi; 8898; -.
PRO; PR:Q13614; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000087053; -.
CleanEx; HS_MTMR2; -.
ExpressionAtlas; Q13614; baseline and differential.
Genevisible; Q13614; HS.
GO; GO:0030424; C:axon; ISS:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:BHF-UCL.
GO; GO:0043197; C:dendritic spine; ISS:BHF-UCL.
GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; ISS:BHF-UCL.
GO; GO:0097060; C:synaptic membrane; ISS:BHF-UCL.
GO; GO:0008021; C:synaptic vesicle; ISS:BHF-UCL.
GO; GO:0005774; C:vacuolar membrane; IEA:Ensembl.
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:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:InterPro.
GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; NAS:UniProtKB.
GO; GO:0097062; P:dendritic spine maintenance; ISS:BHF-UCL.
GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:Ensembl.
GO; GO:0032288; P:myelin assembly; IEA:Ensembl.
GO; GO:0045806; P:negative regulation of endocytosis; ISS:BHF-UCL.
GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; ISS:BHF-UCL.
GO; GO:0031642; P:negative regulation of myelination; IEA:Ensembl.
GO; GO:2000645; P:negative regulation of receptor catabolic process; ISS:BHF-UCL.
GO; GO:0002091; P:negative regulation of receptor internalization; ISS:BHF-UCL.
GO; GO:0048666; P:neuron development; IEA:Ensembl.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IDA:UniProtKB.
GO; GO:2000643; P:positive regulation of early endosome to late endosome transport; ISS:BHF-UCL.
GO; GO:0006470; P:protein dephosphorylation; NAS:UniProtKB.
GO; GO:0051262; P:protein tetramerization; IEA:Ensembl.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR004182; GRAM.
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.
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;
3D-structure; Alternative splicing; Charcot-Marie-Tooth disease;
Coiled coil; Complete proteome; Cytoplasm; Disease mutation; Endosome;
Hydrolase; Lipid metabolism; Membrane; Neurodegeneration; Neuropathy;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 643 Myotubularin-related protein 2.
/FTId=PRO_0000094934.
DOMAIN 68 139 GRAM.
DOMAIN 205 580 Myotubularin phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU00669}.
REGION 330 333 Substrate binding.
{ECO:0000269|PubMed:14690594}.
REGION 355 356 Substrate binding.
{ECO:0000269|PubMed:14690594}.
REGION 417 423 Substrate binding.
{ECO:0000269|PubMed:14690594}.
COILED 593 627 {ECO:0000269|PubMed:16410353}.
COMPBIAS 4 53 Ser-rich.
ACT_SITE 417 417 Phosphocysteine intermediate.
BINDING 463 463 Substrate.
MOD_RES 6 6 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z2D1}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000250|UniProtKB:Q9Z2D1}.
MOD_RES 58 58 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:21372139}.
VAR_SEQ 1 72 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044933.
VARIANT 3 3 K -> T (in dbSNP:rs3824874).
{ECO:0000269|PubMed:10470851,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_047255.
VARIANT 283 283 R -> W (in CMT4B1).
{ECO:0000269|PubMed:12398840}.
/FTId=VAR_047947.
VARIANT 545 545 N -> S (in dbSNP:rs558018).
/FTId=VAR_047256.
MUTAGEN 417 417 C->S: Loss of activity.
{ECO:0000269|PubMed:14690594,
ECO:0000269|PubMed:16410353}.
MUTAGEN 419 419 D->A: No effect.
{ECO:0000269|PubMed:14690594}.
MUTAGEN 422 422 D->A: Loss of activity.
{ECO:0000269|PubMed:14690594}.
MUTAGEN 607 607 L->Y: Reduces homodimerization and
interaction with SBF1.
{ECO:0000269|PubMed:12668758}.
STRAND 84 95 {ECO:0000244|PDB:1ZSQ}.
TURN 96 98 {ECO:0000244|PDB:1ZSQ}.
STRAND 99 121 {ECO:0000244|PDB:1ZSQ}.
STRAND 123 128 {ECO:0000244|PDB:1ZSQ}.
HELIX 129 131 {ECO:0000244|PDB:1ZSQ}.
STRAND 132 138 {ECO:0000244|PDB:1ZSQ}.
STRAND 145 147 {ECO:0000244|PDB:1ZVR}.
STRAND 149 155 {ECO:0000244|PDB:1ZSQ}.
TURN 156 158 {ECO:0000244|PDB:1ZSQ}.
STRAND 159 164 {ECO:0000244|PDB:1ZSQ}.
HELIX 167 169 {ECO:0000244|PDB:1ZSQ}.
HELIX 172 182 {ECO:0000244|PDB:1ZSQ}.
TURN 185 189 {ECO:0000244|PDB:1ZSQ}.
HELIX 193 195 {ECO:0000244|PDB:1ZSQ}.
HELIX 205 207 {ECO:0000244|PDB:1ZSQ}.
HELIX 211 217 {ECO:0000244|PDB:1ZSQ}.
STRAND 223 228 {ECO:0000244|PDB:1ZSQ}.
TURN 230 233 {ECO:0000244|PDB:1ZSQ}.
STRAND 234 236 {ECO:0000244|PDB:1ZSQ}.
STRAND 242 247 {ECO:0000244|PDB:1ZSQ}.
HELIX 252 261 {ECO:0000244|PDB:1ZSQ}.
HELIX 263 265 {ECO:0000244|PDB:1ZSQ}.
STRAND 269 273 {ECO:0000244|PDB:1ZSQ}.
TURN 275 277 {ECO:0000244|PDB:1ZSQ}.
STRAND 280 284 {ECO:0000244|PDB:1ZSQ}.
TURN 290 293 {ECO:0000244|PDB:1ZSQ}.
HELIX 297 309 {ECO:0000244|PDB:1ZSQ}.
STRAND 310 312 {ECO:0000244|PDB:1ZSQ}.
STRAND 314 320 {ECO:0000244|PDB:1ZSQ}.
HELIX 324 333 {ECO:0000244|PDB:1ZSQ}.
TURN 340 342 {ECO:0000244|PDB:1ZSQ}.
STRAND 346 350 {ECO:0000244|PDB:1ZSQ}.
HELIX 356 370 {ECO:0000244|PDB:1ZSQ}.
HELIX 376 378 {ECO:0000244|PDB:1ZSQ}.
HELIX 379 386 {ECO:0000244|PDB:1ZSQ}.
HELIX 388 407 {ECO:0000244|PDB:1ZSQ}.
STRAND 413 416 {ECO:0000244|PDB:1ZSQ}.
STRAND 418 422 {ECO:0000244|PDB:1ZSQ}.
HELIX 423 435 {ECO:0000244|PDB:1ZSQ}.
HELIX 437 440 {ECO:0000244|PDB:1ZSQ}.
HELIX 442 452 {ECO:0000244|PDB:1ZSQ}.
TURN 453 457 {ECO:0000244|PDB:1ZSQ}.
HELIX 460 464 {ECO:0000244|PDB:1ZSQ}.
TURN 465 467 {ECO:0000244|PDB:1ZSQ}.
HELIX 479 493 {ECO:0000244|PDB:1ZSQ}.
TURN 495 497 {ECO:0000244|PDB:1ZSQ}.
HELIX 502 514 {ECO:0000244|PDB:1ZSQ}.
STRAND 516 518 {ECO:0000244|PDB:1ZSQ}.
STRAND 522 524 {ECO:0000244|PDB:1ZSQ}.
HELIX 525 530 {ECO:0000244|PDB:1ZSQ}.
HELIX 533 536 {ECO:0000244|PDB:1ZSQ}.
HELIX 540 545 {ECO:0000244|PDB:1ZSQ}.
HELIX 548 551 {ECO:0000244|PDB:1ZSQ}.
TURN 554 557 {ECO:0000244|PDB:1ZSQ}.
STRAND 560 562 {ECO:0000244|PDB:1ZSQ}.
TURN 570 572 {ECO:0000244|PDB:1ZSQ}.
HELIX 577 580 {ECO:0000244|PDB:1ZSQ}.
SEQUENCE 643 AA; 73381 MW; 10FD6508D0CDA719 CRC64;
MEKSSSCESL GSQPAAARPP SVDSLSSAST SHSENSVHTK SASVVSSDSI STSADNFSPD
LRVLRESNKL AEMEEPPLLP GENIKDMAKD VTYICPFTGA VRGTLTVTNY RLYFKSMERD
PPFVLDASLG VINRVEKIGG ASSRGENSYG LETVCKDIRN LRFAHKPEGR TRRSIFENLM
KYAFPVSNNL PLFAFEYKEV FPENGWKLYD PLLEYRRQGI PNESWRITKI NERYELCDTY
PALLVVPANI PDEELKRVAS FRSRGRIPVL SWIHPESQAT ITRCSQPMVG VSGKRSKEDE
KYLQAIMDSN AQSHKIFIFD ARPSVNAVAN KAKGGGYESE DAYQNAELVF LDIHNIHVMR
ESLRKLKEIV YPNIEETHWL SNLESTHWLE HIKLILAGAL RIADKVESGK TSVVVHCSDG
WDRTAQLTSL AMLMLDGYYR TIRGFEVLVE KEWLSFGHRF QLRVGHGDKN HADADRSPVF
LQFIDCVWQM TRQFPTAFEF NEYFLITILD HLYSCLFGTF LCNSEQQRGK ENLPKRTVSL
WSYINSQLED FTNPLYGSYS NHVLYPVASM RHLELWVGYY IRWNPRMKPQ EPIHNRYKEL
LAKRAELQKK VEELQREISN RSTSSSERAS SPAQCVTPVQ TVV


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