Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9Z2C5

- MTM1_MOUSE

UniProt

Q9Z2C5 - MTM1_MOUSE

Protein

Myotubularin

Gene

Mtm1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (28 Jun 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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 By similarity. Regulates desmin intermediate filament assembly and architecture. Plays a role in mitochondrial morphology and positioning. Required for skeletal muscle maintenance but not for myogenesis.By similarity2 Publications

    Catalytic activityi

    1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O = 1-phosphatidyl-1D-myo-inositol + phosphate.

    Enzyme regulationi

    Allosterically activated by phosphatidylinositol 5-phosphate (PI5P).By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei375 – 3751Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. intermediate filament binding Source: UniProtKB
    2. phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity Source: UniProtKB
    3. phosphatidylinositol-3-phosphatase activity Source: UniProtKB
    4. phosphatidylinositol binding Source: UniProtKB
    5. phosphoprotein phosphatase activity Source: UniProtKB
    6. protein binding Source: IntAct
    7. protein tyrosine phosphatase activity Source: InterPro

    GO - Biological processi

    1. endosome to lysosome transport Source: UniProtKB
    2. intermediate filament organization Source: UniProtKB
    3. mitochondrion distribution Source: UniProtKB
    4. mitochondrion morphogenesis Source: UniProtKB
    5. muscle cell cellular homeostasis Source: MGI
    6. phosphatidylinositol dephosphorylation Source: UniProtKB
    7. protein dephosphorylation Source: UniProtKB
    8. protein transport Source: UniProtKB-KW
    9. regulation of vacuole organization Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_198972. Synthesis of PIPs at the late endosome membrane.
    REACT_198973. Synthesis of PIPs at the plasma membrane.
    REACT_198975. Synthesis of PIPs at the early endosome membrane.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myotubularin (EC:3.1.3.64)
    Gene namesi
    Name:Mtm1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1099452. Mtm1.

    Subcellular locationi

    Cytoplasm 1 Publication. Cell membrane By similarity; Peripheral membrane protein By similarity. Cell projectionfilopodium 1 Publication. Cell projectionruffle 1 Publication. Late endosome By similarity
    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.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. filopodium Source: UniProtKB
    3. I band Source: MGI
    4. late endosome Source: UniProtKB
    5. plasma membrane Source: UniProtKB
    6. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice are viable although lifespan is severely reduced. An under-representation of mutant males suggests some prenatal lethality. Generalized and progressive myopathy starts at around 4 weeks of age with amyotrophy and accumulation of central nuclei in skeletal muscle fibers, leading to death at 6-14 weeks. Mutants also show mitochondrial disorganization and increased levels of desmin with abnormal desmin intermediate filament formation and architecture.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 603603MyotubularinPRO_0000094931Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei495 – 4951PhosphothreonineBy similarity
    Modified residuei588 – 5881PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Z2C5.
    PaxDbiQ9Z2C5.
    PRIDEiQ9Z2C5.

    PTM databases

    PhosphoSiteiQ9Z2C5.

    Expressioni

    Tissue specificityi

    Widely expressed with highest levels detected in heart and muscle and low levels in brain (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ9Z2C5.
    BgeeiQ9Z2C5.
    CleanExiMM_MTM1.
    GenevestigatoriQ9Z2C5.

    Interactioni

    Subunit structurei

    Interacts with MTMR12; the interaction modulates MTM1 intracellular localization. Interacts with KMT2A/MLL1 (via SET domain) By similarity. Interacts with DES in skeletal muscle but not in cardiac muscle.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Bin1O085393EBI-6861578,EBI-775152
    DesP310014EBI-6861578,EBI-298565

    Protein-protein interaction databases

    IntActiQ9Z2C5. 5 interactions.
    MINTiMINT-4102552.
    STRINGi10090.ENSMUSP00000099041.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z2C5.
    SMRiQ9Z2C5. Positions 33-543.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini29 – 9769GRAMAdd
    BLAST
    Domaini163 – 538376Myotubularin phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The GRAM domain mediates binding to PI(3,5)P2 and, with lower affinity, to other phosphoinositides.By similarity

    Sequence similaritiesi

    Contains 1 GRAM domain.Curated
    Contains 1 myotubularin phosphatase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG322789.
    GeneTreeiENSGT00670000097670.
    HOGENOMiHOG000210598.
    HOVERGENiHBG000220.
    InParanoidiQ5BKQ5.
    KOiK01108.
    OMAiQGLPNHH.
    OrthoDBiEOG7XDBF9.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR004182. GRAM.
    IPR010569. Myotubularin-like_Pase_dom.
    IPR011993. PH_like_dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    PfamiPF02893. GRAM. 1 hit.
    PF06602. Myotub-related. 1 hit.
    [Graphical view]
    SMARTiSM00568. GRAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    PROSITEiPS51339. PPASE_MYOTUBULARIN. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Z2C5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASASASKYN SHSLENESIK KVSQDGVSQD VSETVPRLPG ELLITEKEVI    50
    YICPFNGPIK GRVYITNYRL YLRSLETDSA LILDVPLGVI SRIEKMGGAT 100
    SRGENSYGLD ITCKDLRNLR FALKQEGHSR RDMFEILVKH AFPLAHNLPL 150
    FAFVNEEKFN VDGWTVYNPV EEYRRQGLPN HHWRISFINK CYELCETYPA 200
    LLVVPYRTSD DDLRRIATFR SRNRLPVLSW IHPENKMVIM RCSQPLVGMS 250
    GKRNKDDEKY LDVIRETNKQ TSKLMIYDAR PSVNAVANKA TGGGYESDDA 300
    YQNSELSFLD IHNIHVMRES LKKVKDIVYP NIEESHWLSS LESTHWLEHI 350
    KLVLTGAIQV ADQVSSGKSS VLVHCSDGWD RTAQLTSLAM LMLDSFYRTI 400
    EGFEILVQKE WISFGHKFAS RIGHGDKNHA DADRSPIFLQ FIDCVWQMSK 450
    QFPTAFEFNE GFLITVLDHL YSCRFGTFLF NCDSARERQK LTERTVSLWS 500
    LINSNKDKFK NPFYTKEINR VLYPVASMRH LELWVNYYIR WNPRVKQQQP 550
    NPVEQRYMEL LALRDDYIKR LEELQLANSA KLADAPASTS SSSQMVPHVQ 600
    THF 603
    Length:603
    Mass (Da):69,559
    Last modified:June 28, 2011 - v2
    Checksum:i65929312F07FFCC7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti95 – 951K → Y in AAC77821. (PubMed:9736772)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF073996 mRNA. Translation: AAC77821.1.
    AL731843, AL772294 Genomic DNA. Translation: CAM20185.1.
    BC090984 mRNA. Translation: AAH90984.1.
    CCDSiCCDS30177.1.
    RefSeqiNP_001157662.1. NM_001164190.1.
    NP_001157663.1. NM_001164191.1.
    NP_001157664.1. NM_001164192.1.
    NP_064310.2. NM_019926.3.
    UniGeneiMm.274981.
    Mm.423278.

    Genome annotation databases

    EnsembliENSMUST00000033700; ENSMUSP00000033700; ENSMUSG00000031337.
    ENSMUST00000061970; ENSMUSP00000057182; ENSMUSG00000031337.
    ENSMUST00000114617; ENSMUSP00000110264; ENSMUSG00000031337.
    ENSMUST00000171933; ENSMUSP00000125798; ENSMUSG00000031337.
    GeneIDi17772.
    KEGGimmu:17772.
    UCSCiuc009tjq.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF073996 mRNA. Translation: AAC77821.1 .
    AL731843 , AL772294 Genomic DNA. Translation: CAM20185.1 .
    BC090984 mRNA. Translation: AAH90984.1 .
    CCDSi CCDS30177.1.
    RefSeqi NP_001157662.1. NM_001164190.1.
    NP_001157663.1. NM_001164191.1.
    NP_001157664.1. NM_001164192.1.
    NP_064310.2. NM_019926.3.
    UniGenei Mm.274981.
    Mm.423278.

    3D structure databases

    ProteinModelPortali Q9Z2C5.
    SMRi Q9Z2C5. Positions 33-543.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9Z2C5. 5 interactions.
    MINTi MINT-4102552.
    STRINGi 10090.ENSMUSP00000099041.

    PTM databases

    PhosphoSitei Q9Z2C5.

    Proteomic databases

    MaxQBi Q9Z2C5.
    PaxDbi Q9Z2C5.
    PRIDEi Q9Z2C5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033700 ; ENSMUSP00000033700 ; ENSMUSG00000031337 .
    ENSMUST00000061970 ; ENSMUSP00000057182 ; ENSMUSG00000031337 .
    ENSMUST00000114617 ; ENSMUSP00000110264 ; ENSMUSG00000031337 .
    ENSMUST00000171933 ; ENSMUSP00000125798 ; ENSMUSG00000031337 .
    GeneIDi 17772.
    KEGGi mmu:17772.
    UCSCi uc009tjq.2. mouse.

    Organism-specific databases

    CTDi 4534.
    MGIi MGI:1099452. Mtm1.

    Phylogenomic databases

    eggNOGi NOG322789.
    GeneTreei ENSGT00670000097670.
    HOGENOMi HOG000210598.
    HOVERGENi HBG000220.
    InParanoidi Q5BKQ5.
    KOi K01108.
    OMAi QGLPNHH.
    OrthoDBi EOG7XDBF9.

    Enzyme and pathway databases

    Reactomei REACT_198972. Synthesis of PIPs at the late endosome membrane.
    REACT_198973. Synthesis of PIPs at the plasma membrane.
    REACT_198975. Synthesis of PIPs at the early endosome membrane.

    Miscellaneous databases

    NextBioi 292491.
    PROi Q9Z2C5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z2C5.
    Bgeei Q9Z2C5.
    CleanExi MM_MTM1.
    Genevestigatori Q9Z2C5.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR004182. GRAM.
    IPR010569. Myotubularin-like_Pase_dom.
    IPR011993. PH_like_dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view ]
    Pfami PF02893. GRAM. 1 hit.
    PF06602. Myotub-related. 1 hit.
    [Graphical view ]
    SMARTi SM00568. GRAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    PROSITEi PS51339. PPASE_MYOTUBULARIN. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the myotubularin dual specificity phosphatase gene family from yeast to human."
      Laporte J., Blondeau F., Buj-Bello A., Tentler D., Kretz C., Dahl N., Mandel J.-L.
      Hum. Mol. Genet. 7:1703-1712(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: CD-1.
      Tissue: Pituitary.
    4. "The PtdIns3P phosphatase myotubularin is a cytoplasmic protein that also localizes to Rac1-inducible plasma membrane ruffles."
      Laporte J., Blondeau F., Gansmuller A., Lutz Y., Vonesch J.L., Mandel J.L.
      J. Cell Sci. 115:3105-3117(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    5. "The lipid phosphatase myotubularin is essential for skeletal muscle maintenance but not for myogenesis in mice."
      Buj-Bello A., Laugel V., Messaddeq N., Zahreddine H., Laporte J., Pellissier J.F., Mandel J.L.
      Proc. Natl. Acad. Sci. U.S.A. 99:15060-15065(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    6. "Myotubularin controls desmin intermediate filament architecture and mitochondrial dynamics in human and mouse skeletal muscle."
      Hnia K., Tronchere H., Tomczak K.K., Amoasii L., Schultz P., Beggs A.H., Payrastre B., Mandel J.L., Laporte J.
      J. Clin. Invest. 121:70-85(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DES, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiMTM1_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z2C5
    Secondary accession number(s): Q5BKQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: June 28, 2011
    Last modified: October 1, 2014
    This is version 109 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3