MTMR9_HUMAN
ID MTMR9_HUMAN Reviewed; 549 AA.
AC Q96QG7; B7Z291; Q52LU3; Q8WW11; Q96QG6; Q9NX50;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Myotubularin-related protein 9;
DE AltName: Full=Inactive phosphatidylinositol 3-phosphatase 9 {ECO:0000305};
GN Name=MTMR9; Synonyms=C8orf9, MTMR8;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), AND TISSUE
RP SPECIFICITY.
RX PubMed=11472061; DOI=10.1006/geno.2001.6591;
RA Appel S., Reichwald K., Zimmermann W., Reis A., Rosenthal A., Hennies H.C.;
RT "Identification and localization of a new human myotubularin-related
RT protein gene, MTMR8, on 8p22-p23.";
RL Genomics 75:6-8(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH MTMR6.
RX PubMed=12890864; DOI=10.1073/pnas.1333958100;
RA Mochizuki Y., Majerus P.W.;
RT "Characterization of myotubularin-related protein 7 and its binding
RT partner, myotubularin-related protein 9.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9768-9773(2003).
RN [6]
RP INTERACTION WITH MTMR6 AND MTMR8, AND SUBCELLULAR LOCATION.
RX PubMed=16787938; DOI=10.1242/jcs.03040;
RA Lorenzo O., Urbe S., Clague M.J.;
RT "Systematic analysis of myotubularins: heteromeric interactions,
RT subcellular localisation and endosome related functions.";
RL J. Cell Sci. 119:2953-2959(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP FUNCTION, INTERACTION WITH MTMR6, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=19038970; DOI=10.1074/jbc.m804292200;
RA Zou J., Chang S.C., Marjanovic J., Majerus P.W.;
RT "MTMR9 increases MTMR6 enzyme activity, stability, and role in apoptosis.";
RL J. Biol. Chem. 284:2064-2071(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP FUNCTION, AND INTERACTION WITH MTMR8.
RX PubMed=22647598; DOI=10.1073/pnas.1207021109;
RA Zou J., Zhang C., Marjanovic J., Kisseleva M.V., Majerus P.W., Wilson M.P.;
RT "Myotubularin-related protein (MTMR) 9 determines the enzymatic activity,
RT substrate specificity, and role in autophagy of MTMR8.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:9539-9544(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP INTERACTION WITH MTMR6, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23188820; DOI=10.1074/jbc.m112.395087;
RA Mochizuki Y., Ohashi R., Kawamura T., Iwanari H., Kodama T., Naito M.,
RA Hamakubo T.;
RT "Phosphatidylinositol 3-phosphatase myotubularin-related protein 6 (MTMR6)
RT is regulated by small GTPase Rab1B in the early secretory and autophagic
RT pathways.";
RL J. Biol. Chem. 288:1009-1021(2013).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP FUNCTION.
RX PubMed=24591580; DOI=10.1073/pnas.1311029111;
RA Maekawa M., Terasaka S., Mochizuki Y., Kawai K., Ikeda Y., Araki N.,
RA Skolnik E.Y., Taguchi T., Arai H.;
RT "Sequential breakdown of 3-phosphorylated phosphoinositides is essential
RT for the completion of macropinocytosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:E978-E987(2014).
RN [20]
RP VARIANT ILE-472.
RX PubMed=30237576; DOI=10.1038/s41436-018-0138-x;
RA Maddirevula S., Alzahrani F., Al-Owain M., Al Muhaizea M.A., Kayyali H.R.,
RA AlHashem A., Rahbeeni Z., Al-Otaibi M., Alzaidan H.I., Balobaid A.,
RA El Khashab H.Y., Bubshait D.K., Faden M., Yamani S.A., Dabbagh O.,
RA Al-Mureikhi M., Jasser A.A., Alsaif H.S., Alluhaydan I., Seidahmed M.Z.,
RA Alabbasi B.H., Almogarri I., Kurdi W., Akleh H., Qari A., Al Tala S.M.,
RA Alhomaidi S., Kentab A.Y., Salih M.A., Chedrawi A., Alameer S., Tabarki B.,
RA Shamseldin H.E., Patel N., Ibrahim N., Abdulwahab F., Samira M., Goljan E.,
RA Abouelhoda M., Meyer B.F., Hashem M., Shaheen R., AlShahwan S.,
RA Alfadhel M., Ben-Omran T., Al-Qattan M.M., Monies D., Alkuraya F.S.;
RT "Autozygome and high throughput confirmation of disease genes candidacy.";
RL Genet. Med. 21:736-742(2019).
CC -!- FUNCTION: Acts as an adapter for myotubularin-related phosphatases
CC (PubMed:19038970, PubMed:22647598). Increases lipid phosphatase MTMR6
CC catalytic activity, specifically towards phosphatidylinositol 3,5-
CC bisphosphate and MTMR6 binding affinity for phosphorylated
CC phosphatidylinositols (PubMed:19038970, PubMed:22647598). Positively
CC regulates lipid phosphatase MTMR7 catalytic activity (By similarity).
CC Increases MTMR8 catalytic activity towards phosphatidylinositol 3-
CC phosphate (PubMed:22647598). The formation of the MTMR6-MTMR9 complex,
CC stabilizes both MTMR6 and MTMR9 protein levels (PubMed:19038970).
CC Stabilizes MTMR8 protein levels (PubMed:22647598). Plays a role in the
CC late stages of macropinocytosis possibly by regulating MTMR6-mediated
CC dephosphorylation of phosphatidylinositol 3-phosphate in membrane
CC ruffles (PubMed:24591580). Negatively regulates autophagy, in part via
CC its association with MTMR8 (PubMed:22647598). Negatively regulates DNA
CC damage-induced apoptosis, in part via its association with MTMR6
CC (PubMed:19038970, PubMed:22647598). Does not bind mono-, di- and tri-
CC phosphorylated phosphatidylinositols, phosphatidic acid and
CC phosphatidylserine (PubMed:19038970). {ECO:0000250|UniProtKB:Q9Z2D0,
CC ECO:0000269|PubMed:19038970, ECO:0000269|PubMed:22647598,
CC ECO:0000269|PubMed:24591580}.
CC -!- SUBUNIT: Homodimer (PubMed:19038970). Heterodimer (via C-terminus) with
CC lipid phosphatase MTMR6 (via C-terminus) (PubMed:16787938,
CC PubMed:12890864, PubMed:19038970, PubMed:23188820). Heterodimer (via
CC coiled coil domain) with lipid phosphatase MTMR7 (via C-terminus) (By
CC similarity). Heterodimer with lipid phosphatase MTMR8 (PubMed:22647598,
CC PubMed:16787938). {ECO:0000250|UniProtKB:Q9Z2D0,
CC ECO:0000269|PubMed:12890864, ECO:0000269|PubMed:16787938,
CC ECO:0000269|PubMed:19038970, ECO:0000269|PubMed:22647598,
CC ECO:0000269|PubMed:23188820}.
CC -!- INTERACTION:
CC Q96QG7; O75140-2: DEPDC5; NbExp=3; IntAct=EBI-744593, EBI-12366971;
CC Q96QG7; Q9Y6C2: EMILIN1; NbExp=10; IntAct=EBI-744593, EBI-744586;
CC Q96QG7; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-744593, EBI-11748557;
CC Q96QG7; Q9Y6X4: FAM169A; NbExp=3; IntAct=EBI-744593, EBI-1220497;
CC Q96QG7; Q6IC98: GRAMD4; NbExp=3; IntAct=EBI-744593, EBI-10962409;
CC Q96QG7; Q0VD86: INCA1; NbExp=3; IntAct=EBI-744593, EBI-6509505;
CC Q96QG7; Q86T90: KIAA1328; NbExp=3; IntAct=EBI-744593, EBI-3437878;
CC Q96QG7; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-744593, EBI-3044087;
CC Q96QG7; Q8TBB1: LNX1; NbExp=5; IntAct=EBI-744593, EBI-739832;
CC Q96QG7; A8MW99: MEI4; NbExp=3; IntAct=EBI-744593, EBI-19944212;
CC Q96QG7; P00540: MOS; NbExp=6; IntAct=EBI-744593, EBI-1757866;
CC Q96QG7; Q9Y217: MTMR6; NbExp=12; IntAct=EBI-744593, EBI-766064;
CC Q96QG7; Q9Y216: MTMR7; NbExp=14; IntAct=EBI-744593, EBI-10293003;
CC Q96QG7; Q96EF0: MTMR8; NbExp=6; IntAct=EBI-744593, EBI-750578;
CC Q96QG7; Q96EF0-1: MTMR8; NbExp=3; IntAct=EBI-744593, EBI-15985865;
CC Q96QG7; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-744593, EBI-10172876;
CC Q96QG7; Q13287: NMI; NbExp=9; IntAct=EBI-744593, EBI-372942;
CC Q96QG7; P26045: PTPN3; NbExp=3; IntAct=EBI-744593, EBI-1047946;
CC Q96QG7; Q08AM6: VAC14; NbExp=3; IntAct=EBI-744593, EBI-2107455;
CC Q96QG7; Q8N720: ZNF655; NbExp=3; IntAct=EBI-744593, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16787938,
CC ECO:0000269|PubMed:19038970}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:Q9Z2D0}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, perinuclear
CC region {ECO:0000269|PubMed:16787938, ECO:0000269|PubMed:19038970}.
CC Endoplasmic reticulum {ECO:0000269|PubMed:19038970}. Note=Localizes to
CC ruffles during EGF-induced macropinocytosis (By similarity).
CC Colocalizes with MTMR6 to the perinuclear region (PubMed:19038970).
CC Partially localizes to the endoplasmic reticulum (PubMed:19038970).
CC {ECO:0000250|UniProtKB:Q9Z2D0, ECO:0000269|PubMed:19038970}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96QG7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96QG7-2; Sequence=VSP_056209;
CC -!- TISSUE SPECIFICITY: Expressed in many tissues.
CC {ECO:0000269|PubMed:11472061}.
CC -!- DOMAIN: The GRAM domain is required for cell membrane localization.
CC {ECO:0000250|UniProtKB:Q9Z2D0}.
CC -!- DOMAIN: The coiled coil domain mediates interaction with MTMR9.
CC {ECO:0000250|UniProtKB:Q9Z2D0}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class myotubularin subfamily. {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the non-receptor class myotubularin
CC subfamily, lacks the conserved active site cysteine residue at position
CC 333 in the dsPTPase catalytic loop, suggesting that it has no
CC phosphatase activity. {ECO:0000305}.
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DR EMBL; AJ297823; CAC51114.1; -; mRNA.
DR EMBL; AJ297824; CAC51115.1; -; Genomic_DNA.
DR EMBL; AK000444; BAA91170.1; -; mRNA.
DR EMBL; AK294463; BAH11777.1; -; mRNA.
DR EMBL; AF131216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022003; AAH22003.1; -; mRNA.
DR EMBL; BC034990; AAH34990.1; -; mRNA.
DR EMBL; BC093788; AAH93788.1; -; mRNA.
DR EMBL; BC101623; AAI01624.1; -; mRNA.
DR CCDS; CCDS5979.1; -. [Q96QG7-1]
DR RefSeq; NP_056273.2; NM_015458.3. [Q96QG7-1]
DR AlphaFoldDB; Q96QG7; -.
DR SMR; Q96QG7; -.
DR BioGRID; 122455; 61.
DR DIP; DIP-54283N; -.
DR IntAct; Q96QG7; 39.
DR MINT; Q96QG7; -.
DR STRING; 9606.ENSP00000221086; -.
DR DEPOD; MTMR9; -.
DR iPTMnet; Q96QG7; -.
DR PhosphoSitePlus; Q96QG7; -.
DR BioMuta; MTMR9; -.
DR DMDM; 33112393; -.
DR EPD; Q96QG7; -.
DR jPOST; Q96QG7; -.
DR MassIVE; Q96QG7; -.
DR MaxQB; Q96QG7; -.
DR PaxDb; Q96QG7; -.
DR PeptideAtlas; Q96QG7; -.
DR PRIDE; Q96QG7; -.
DR ProteomicsDB; 6422; -.
DR ProteomicsDB; 77877; -. [Q96QG7-1]
DR Antibodypedia; 22096; 124 antibodies from 29 providers.
DR DNASU; 66036; -.
DR Ensembl; ENST00000221086.8; ENSP00000221086.3; ENSG00000104643.10. [Q96QG7-1]
DR Ensembl; ENST00000526292.1; ENSP00000433239.1; ENSG00000104643.10. [Q96QG7-2]
DR Ensembl; ENST00000644306.2; ENSP00000495551.2; ENSG00000285032.2. [Q96QG7-1]
DR Ensembl; ENST00000646141.2; ENSP00000496677.2; ENSG00000285032.2. [Q96QG7-1]
DR GeneID; 66036; -.
DR KEGG; hsa:66036; -.
DR MANE-Select; ENST00000221086.8; ENSP00000221086.3; NM_015458.4; NP_056273.2.
DR UCSC; uc003wtm.4; human. [Q96QG7-1]
DR CTD; 66036; -.
DR DisGeNET; 66036; -.
DR GeneCards; MTMR9; -.
DR HGNC; HGNC:14596; MTMR9.
DR HPA; ENSG00000104643; Low tissue specificity.
DR MIM; 606260; gene.
DR neXtProt; NX_Q96QG7; -.
DR OpenTargets; ENSG00000104643; -.
DR PharmGKB; PA37904; -.
DR VEuPathDB; HostDB:ENSG00000104643; -.
DR eggNOG; KOG1089; Eukaryota.
DR GeneTree; ENSGT00940000157818; -.
DR HOGENOM; CLU_001839_3_1_1; -.
DR InParanoid; Q96QG7; -.
DR OMA; RHENGAT; -.
DR OrthoDB; 824298at2759; -.
DR PhylomeDB; Q96QG7; -.
DR TreeFam; TF315197; -.
DR PathwayCommons; Q96QG7; -.
DR Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
DR Reactome; R-HSA-1660517; Synthesis of PIPs at the late endosome membrane.
DR Reactome; R-HSA-1855183; Synthesis of IP2, IP, and Ins in the cytosol.
DR SignaLink; Q96QG7; -.
DR BioGRID-ORCS; 66036; 36 hits in 1097 CRISPR screens.
DR ChiTaRS; MTMR9; human.
DR GeneWiki; MTMR9; -.
DR GenomeRNAi; 66036; -.
DR Pharos; Q96QG7; Tbio.
DR PRO; PR:Q96QG7; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q96QG7; protein.
DR Bgee; ENSG00000104643; Expressed in endothelial cell and 207 other tissues.
DR ExpressionAtlas; Q96QG7; baseline and differential.
DR Genevisible; Q96QG7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030234; F:enzyme regulator activity; IEA:Ensembl.
DR GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IBA:GO_Central.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0010507; P:negative regulation of autophagy; IPI:UniProtKB.
DR GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR GO; GO:0010922; P:positive regulation of phosphatase activity; IDA:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR GO; GO:0060304; P:regulation of phosphatidylinositol dephosphorylation; IDA:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR PANTHER; PTHR10807; PTHR10807; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Cell projection;
KW Coiled coil; Cytoplasm; Disease variant; Endocytosis;
KW Endoplasmic reticulum; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..549
FT /note="Myotubularin-related protein 9"
FT /id="PRO_0000094943"
FT DOMAIN 4..99
FT /note="GRAM"
FT /evidence="ECO:0000255"
FT DOMAIN 123..498
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT COILED 508..542
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..85
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056209"
FT VARIANT 472
FT /note="N -> I (found in a patient with global developmental
FT delay, spasticity and epilepsy; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30237576"
FT /id="VAR_082147"
FT CONFLICT 194
FT /note="K -> R (in Ref. 2; BAA91170)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="Q -> L (in Ref. 4; AAH22003)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 549 AA; 63462 MW; 910F7D2907F9707E CRC64;
MEFAELIKTP RVDNVVLHRP FYPAVEGTLC LTGHHLILSS RQDNTEELWL LHSNIDAIDK
RFVGSLGTII IKCKDFRIIQ LDIPGMEECL NIASSIEALS TLDSITLMYP FFYRPMFEVI
EDGWHSFLPE QEFELYSSAT SEWRLSYVNK EFAVCPSYPP IVTVPKSIDD EALRKVATFR
HGGRFPVLSY YHKKNGMVIM RSGQPLTGTN GRRCKEDEKL INATLRAGKR GYIIDTRSLN
VAQQTRAKGG GFEQEAHYPQ WRRIHKSIER YHILQESLIK LVEACNDQTH NMDRWLSKLE
ASNWLTHIKE ILTTACLAAQ CIDREGASIL IHGTEGTDST LQVTSLAQII LEPRSRTIRG
FEALIEREWL QAGHPFQQRC AQSAYCNTKQ KWEAPVFLLF LDCVWQILRQ FPCSFEFNEN
FLIMLFEHAY ASQFGTFLGN NESERCKLKL QQKTMSLWSW VNQPSELSKF TNPLFEANNL
VIWPSVAPQS LPLWEGIFLR WNRSSKYLDE AYEEMVNIIE YNKELQAKVN ILRRQLAELE
TEDGMQESP
