Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Myotubularin

Gene

MTM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Regulates desmin intermediate filament assembly and architecture. Plays a role in mitochondrial morphology and positioning. Required for skeletal muscle maintenance but not for myogenesis.6 Publications

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O = 1-phosphatidyl-1D-myo-inositol + phosphate.4 Publications
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate.1 Publication

Enzyme regulationi

Allosterically activated by phosphatidylinositol 5-phosphate (PI5P).1 Publication

Kineticsi

  1. KM=39 µM for PI3P1 Publication
  2. KM=17 µM for PI(3,5)P21 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei375Phosphocysteine intermediatePROSITE-ProRule annotation1

    GO - Molecular functioni

    • intermediate filament binding Source: UniProtKB
    • phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity Source: UniProtKB
    • phosphatidylinositol-3-phosphatase activity Source: UniProtKB
    • phosphatidylinositol binding Source: UniProtKB
    • phosphoprotein phosphatase activity Source: UniProtKB
    • protein tyrosine phosphatase activity Source: InterPro

    GO - Biological processi

    • endosome to lysosome transport Source: UniProtKB
    • intermediate filament organization Source: UniProtKB
    • mitochondrion distribution Source: UniProtKB
    • mitochondrion morphogenesis Source: UniProtKB
    • muscle cell cellular homeostasis Source: Ensembl
    • negative regulation of autophagosome assembly Source: Ensembl
    • negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
    • negative regulation of protein kinase B signaling Source: Ensembl
    • negative regulation of TOR signaling Source: Ensembl
    • phosphatidylinositol biosynthetic process Source: Reactome
    • phosphatidylinositol dephosphorylation Source: UniProtKB
    • positive regulation of skeletal muscle tissue growth Source: Ensembl
    • protein dephosphorylation Source: UniProtKB
    • protein transport Source: UniProtKB-KW
    • regulation of vacuole organization Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Lipid metabolism, Protein transport, Transport

    Enzyme and pathway databases

    BioCyciZFISH:HS10241-MONOMER.
    BRENDAi3.1.3.64. 2681.
    3.1.3.95. 2681.
    ReactomeiR-HSA-1660499. Synthesis of PIPs at the plasma membrane.
    R-HSA-1660516. Synthesis of PIPs at the early endosome membrane.
    R-HSA-1660517. Synthesis of PIPs at the late endosome membrane.

    Chemistry databases

    SwissLipidsiSLP:000000846.
    SLP:000000847.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myotubularin
    Alternative name(s):
    Phosphatidylinositol-3,5-bisphosphate 3-phosphatase (EC:3.1.3.951 Publication)
    Phosphatidylinositol-3-phosphate phosphatase (EC:3.1.3.644 Publications)
    Gene namesi
    Name:MTM1
    Synonyms:CG2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome X

    Organism-specific databases

    HGNCiHGNC:7448. MTM1.

    Subcellular locationi

    • Cytoplasm 2 Publications
    • Cell membrane; Peripheral membrane protein 1 Publication
    • Cell projectionfilopodium 1 Publication
    • Cell projectionruffle 1 Publication
    • Late endosome 1 Publication

    • 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.2 Publications

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • filopodium Source: UniProtKB
    • I band Source: Ensembl
    • late endosome Source: UniProtKB
    • plasma membrane Source: UniProtKB
    • ruffle Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Myopathy, centronuclear, X-linked (CNMX)12 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA 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.
    See also OMIM:310400
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_00638647Missing in CNMX. 1 Publication1
    Natural variantiVAR_01822749V → 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. 2 PublicationsCorresponds to variant rs587783796dbSNPEnsembl.1
    Natural variantiVAR_01822868Y → D in CNMX. 1 Publication1
    Natural variantiVAR_00638769R → C in CNMX; mild; reduced response to PI5P and reduced binding to PI(3,5)P2. 5 PublicationsCorresponds to variant rs132630304dbSNPEnsembl.1
    Natural variantiVAR_01822969R → P in CNMX. 1 Publication1
    Natural variantiVAR_01823069R → S in CNMX; severe. 1 Publication1
    Natural variantiVAR_00638870L → F in CNMX; mild; reduced binding to PI(3,5)P2. 3 PublicationsCorresponds to variant rs587783809dbSNPEnsembl.1
    Natural variantiVAR_00638987L → P in CNMX; mild; reduced binding to PI(3,5)P2. 2 PublicationsCorresponds to variant rs587783816dbSNPEnsembl.1
    Natural variantiVAR_018231157E → K in CNMX. 1 PublicationCorresponds to variant rs132630307dbSNPEnsembl.1
    Natural variantiVAR_009217179P → S in CNMX; mild. 2 PublicationsCorresponds to variant rs587783832dbSNPEnsembl.1
    Natural variantiVAR_018232180N → K in CNMX; very mild. 1 Publication1
    Natural variantiVAR_006390184R → G in CNMX; severe; loss of activity; abolishes interaction with DES. 3 PublicationsCorresponds to variant rs587783835dbSNPEnsembl.1
    Natural variantiVAR_018233184R → L in CNMX. 1 Publication1
    Natural variantiVAR_018234186T → I in CNMX. 1 PublicationCorresponds to variant rs587783836dbSNPEnsembl.1
    Natural variantiVAR_006391189N → S in CNMX. 1 PublicationCorresponds to variant rs132630302dbSNPEnsembl.1
    Natural variantiVAR_018235197T → I in CNMX. 1 Publication1
    Natural variantiVAR_006392198Y → N in CNMX; severe. 1 Publication1
    Natural variantiVAR_018236199P → S in CNMX. 1 Publication1
    Natural variantiVAR_018237202L → S in CNMX; severe. 1 Publication1
    Natural variantiVAR_006393205P → L in CNMX; severe; dramatic decrease in phosphatase activity; abolishes interaction with DES. 6 PublicationsCorresponds to variant rs587783841dbSNPEnsembl.1
    Natural variantiVAR_009218225I → T in CNMX; mild. 2 Publications1
    Natural variantiVAR_018238226P → T in CNMX. 1 PublicationCorresponds to variant rs587783848dbSNPEnsembl.1
    Natural variantiVAR_018239227V → M in CNMX. 1 PublicationCorresponds to variant rs587783850dbSNPEnsembl.1
    Natural variantiVAR_018240228L → P in CNMX. 1 PublicationCorresponds to variant rs587783851dbSNPEnsembl.1
    Natural variantiVAR_006394229S → P in CNMX; mild. 1 Publication1
    Natural variantiVAR_018241230W → C in CNMX. 2 Publications1
    Natural variantiVAR_018242232H → R in CNMX. 1 Publication1
    Natural variantiVAR_006395241R → C in CNMX; mild to moderate; abolishes interaction with DES. 6 PublicationsCorresponds to variant rs132630305dbSNPEnsembl.1
    Natural variantiVAR_006396241R → L in CNMX; severe; loss of activity. 3 Publications1
    Natural variantiVAR_009219264I → S in CNMX; severe. 1 PublicationCorresponds to variant rs587783856dbSNPEnsembl.1
    Natural variantiVAR_018243279A → G in CNMX. 1 Publication1
    Natural variantiVAR_009220294Missing in CNMX; mild. 1 Publication1
    Natural variantiVAR_006397317M → R in CNMX; mild. 1 Publication1
    Natural variantiVAR_018244346W → C in CNMX; mild. 1 Publication1
    Natural variantiVAR_018245346W → S in CNMX. 1
    Natural variantiVAR_018246364V → G in CNMX. 1 Publication1
    Natural variantiVAR_018247374H → D in CNMX. Corresponds to variant rs587783754dbSNPEnsembl.1
    Natural variantiVAR_006398376S → N in CNMX; dramatic decrease in phosphatase activity. 2 Publications1
    Natural variantiVAR_018248378G → E in CNMX. 1 Publication1
    Natural variantiVAR_006399378G → R in CNMX; severe; dramatic decrease in phosphatase activity; does not affect EGFR degradation. 5 PublicationsCorresponds to variant rs587783755dbSNPEnsembl.1
    Natural variantiVAR_068846387S → Y in CNMX. 1 PublicationCorresponds to variant rs587783759dbSNPEnsembl.1
    Natural variantiVAR_018249389A → D in CNMX; severe. 1 Publication1
    Natural variantiVAR_018250391L → P in CNMX. 1 Publication1
    Natural variantiVAR_006400397Y → C in CNMX; severe; dramatic decrease in phosphatase activity. 5 PublicationsCorresponds to variant rs132630303dbSNPEnsembl.1
    Natural variantiVAR_006401402G → A in CNMX; mild. 1 PublicationCorresponds to variant rs587783762dbSNPEnsembl.1
    Natural variantiVAR_018251402G → R in CNMX. 3 Publications1
    Natural variantiVAR_018252402G → V in CNMX. 1 Publication1
    Natural variantiVAR_006402404E → K in CNMX; mild. 2 PublicationsCorresponds to variant rs781933660dbSNPEnsembl.1
    Natural variantiVAR_006403406L → P in CNMX; severe. 1 Publication1
    Natural variantiVAR_018253411W → C in CNMX. Corresponds to variant rs587783764dbSNPEnsembl.1
    Natural variantiVAR_009221420S → SFIQ in CNMX; severe. 1
    Natural variantiVAR_006404421R → Q in CNMX; severe; reduced activity and response to PI5P; does not affect interaction with DES. 6 PublicationsCorresponds to variant rs587783772dbSNPEnsembl.1
    Natural variantiVAR_006405421R → RFIQ in CNMX; severe. 1
    Natural variantiVAR_006406431D → N in CNMX. 1 Publication1
    Natural variantiVAR_006407433D → N in CNMX. 1 Publication1
    Natural variantiVAR_018254444C → Y in CNMX. 1 Publication1
    Natural variantiVAR_006408469H → P in CNMX. 2 Publications1
    Natural variantiVAR_018255470L → P in CNMX; severe. 1 Publication1
    Natural variantiVAR_018256481N → Y in CNMX; mild. 1 Publication1
    Natural variantiVAR_006409499W → R in CNMX; mild. 1 PublicationCorresponds to variant rs587783801dbSNPEnsembl.1
    Natural variantiVAR_009222510K → N in CNMX; severe. 1 Publication1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi114K → A: Reduced response to PI5P. 1 Publication1
    Mutagenesisi181H → A: Disrupts interaction with DES. Does not affect lipid phosphatase activity. 1 Publication1
    Mutagenesisi206Y → A: Disrupts interaction with DES. Does not affect lipid phosphatase activity. 1 Publication1
    Mutagenesisi209S → A: Disrupts interaction with DES. Does not affect lipid phosphatase activity. 1 Publication1
    Mutagenesisi220R → A: Loss of activity. 1 Publication1
    Mutagenesisi255K → A: Disrupts interaction with DES. 1 Publication1
    Mutagenesisi257D → A: No effect on subcellular location. 1 Publication1
    Mutagenesisi269K → A: Disrupts interaction with DES. Does not affect lipid phosphatase activity. 1 Publication1
    Mutagenesisi278D → A: Localizes to plasma membrane extensions. Does not affect interaction with DES. 3 Publications1
    Mutagenesisi375C → A: No effect on subcellular location. 5 Publications1
    Mutagenesisi375C → S: Lacks activity toward PI3P. Does not affect interaction with DES. 5 Publications1
    Mutagenesisi377D → A: No effect on subcellular location. 2 Publications1
    Mutagenesisi380D → A: Does not affect interaction with DES. 3 Publications1
    Mutagenesisi394D → A: Produces an unstable protein. 1 Publication1
    Mutagenesisi410E → A: Produces an unstable protein. 1 Publication1
    Mutagenesisi420S → D: Does not affect interaction with DES. 1 Publication1
    Mutagenesisi443D → A: Produces an unstable protein. 1 Publication1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNETi4534.
    MalaCardsiMTM1.
    MIMi310400. phenotype.
    OpenTargetsiENSG00000171100.
    Orphaneti596. X-linked centronuclear myopathy.
    PharmGKBiPA31251.

    Polymorphism and mutation databases

    BioMutaiMTM1.
    DMDMi2851537.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000949301 – 603MyotubularinAdd BLAST603

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei13PhosphoserineCombined sources1
    Modified residuei18PhosphoserineCombined sources1
    Modified residuei495PhosphothreonineCombined sources1
    Modified residuei588PhosphoserineCombined sources1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    EPDiQ13496.
    MaxQBiQ13496.
    PaxDbiQ13496.
    PeptideAtlasiQ13496.
    PRIDEiQ13496.

    PTM databases

    DEPODiQ13496.
    iPTMnetiQ13496.
    PhosphoSitePlusiQ13496.

    Expressioni

    Gene expression databases

    BgeeiENSG00000171100.
    CleanExiHS_MTM1.
    ExpressionAtlasiQ13496. baseline and differential.
    GenevisibleiQ13496. HS.

    Organism-specific databases

    HPAiHPA010008.
    HPA010665.

    Interactioni

    Subunit structurei

    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.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BIN1O004996EBI-2864109,EBI-719094
    DESP1766113EBI-2864109,EBI-1055572
    DesP310014EBI-2864109,EBI-298565From a different organism.
    MTMR12Q9C0I14EBI-2864109,EBI-2829520

    GO - Molecular functioni

    • intermediate filament binding Source: UniProtKB

    Protein-protein interaction databases

    BioGridi110630. 7 interactors.
    DIPiDIP-61934N.
    IntActiQ13496. 6 interactors.
    STRINGi9606.ENSP00000359423.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13496.
    SMRiQ13496.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini29 – 97GRAMAdd BLAST69
    Domaini163 – 538Myotubularin phosphatasePROSITE-ProRule annotationAdd BLAST376

    Domaini

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

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiKOG1089. Eukaryota.
    ENOG410XPTU. LUCA.
    GeneTreeiENSGT00760000118832.
    HOGENOMiHOG000210598.
    HOVERGENiHBG000220.
    InParanoidiQ13496.
    KOiK01108.
    OMAiPNHHWRI.
    OrthoDBiEOG091G04DS.
    PhylomeDBiQ13496.
    TreeFamiTF315197.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    3.90.190.10. 1 hit.
    InterProiIPR004182. GRAM.
    IPR010569. Myotubularin-like_Pase_dom.
    IPR030564. Myotubularin_fam.
    IPR011993. PH_dom-like.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR016130. Tyr_Pase_AS.
    IPR003595. Tyr_Pase_cat.
    IPR000387. TYR_PHOSPHATASE_dom.
    [Graphical view]
    PANTHERiPTHR10807. PTHR10807. 1 hit.
    PfamiPF02893. GRAM. 1 hit.
    PF06602. Myotub-related. 1 hit.
    [Graphical view]
    SMARTiSM00568. GRAM. 1 hit.
    SM00404. PTPc_motif. 1 hit.
    [Graphical view]
    SUPFAMiSSF50729. SSF50729. 1 hit.
    SSF52799. SSF52799. 1 hit.
    PROSITEiPS51339. PPASE_MYOTUBULARIN. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q13496-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MASASTSKYN SHSLENESIK RTSRDGVNRD LTEAVPRLPG ETLITDKEVI
    60 70 80 90 100
    YICPFNGPIK GRVYITNYRL YLRSLETDSS LILDVPLGVI SRIEKMGGAT
    110 120 130 140 150
    SRGENSYGLD ITCKDMRNLR FALKQEGHSR RDMFEILTRY AFPLAHSLPL
    160 170 180 190 200
    FAFLNEEKFN VDGWTVYNPV EEYRRQGLPN HHWRITFINK CYELCDTYPA
    210 220 230 240 250
    LLVVPYRASD DDLRRVATFR SRNRIPVLSW IHPENKTVIV RCSQPLVGMS
    260 270 280 290 300
    GKRNKDDEKY LDVIRETNKQ ISKLTIYDAR PSVNAVANKA TGGGYESDDA
    310 320 330 340 350
    YHNAELFFLD IHNIHVMRES LKKVKDIVYP NVEESHWLSS LESTHWLEHI
    360 370 380 390 400
    KLVLTGAIQV ADKVSSGKSS VLVHCSDGWD RTAQLTSLAM LMLDSFYRSI
    410 420 430 440 450
    EGFEILVQKE WISFGHKFAS RIGHGDKNHT DADRSPIFLQ FIDCVWQMSK
    460 470 480 490 500
    QFPTAFEFNE QFLIIILDHL YSCRFGTFLF NCESARERQK VTERTVSLWS
    510 520 530 540 550
    LINSNKEKFK NPFYTKEINR VLYPVASMRH LELWVNYYIR WNPRIKQQQP
    560 570 580 590 600
    NPVEQRYMEL LALRDEYIKR LEELQLANSA KLSDPPTSPS SPSQMMPHVQ

    THF
    Length:603
    Mass (Da):69,932
    Last modified:July 15, 1998 - v2
    Checksum:iBE9770F2471957C0
    GO
    Isoform 2 (identifier: Q13496-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         78-114: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:566
    Mass (Da):66,053
    Checksum:i237719B8DEB99D1B
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti410E → K in AAH30779 (PubMed:15489334).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_00638647Missing in CNMX. 1 Publication1
    Natural variantiVAR_01822749V → 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. 2 PublicationsCorresponds to variant rs587783796dbSNPEnsembl.1
    Natural variantiVAR_01822868Y → D in CNMX. 1 Publication1
    Natural variantiVAR_00638769R → C in CNMX; mild; reduced response to PI5P and reduced binding to PI(3,5)P2. 5 PublicationsCorresponds to variant rs132630304dbSNPEnsembl.1
    Natural variantiVAR_01822969R → P in CNMX. 1 Publication1
    Natural variantiVAR_01823069R → S in CNMX; severe. 1 Publication1
    Natural variantiVAR_00638870L → F in CNMX; mild; reduced binding to PI(3,5)P2. 3 PublicationsCorresponds to variant rs587783809dbSNPEnsembl.1
    Natural variantiVAR_00638987L → P in CNMX; mild; reduced binding to PI(3,5)P2. 2 PublicationsCorresponds to variant rs587783816dbSNPEnsembl.1
    Natural variantiVAR_018231157E → K in CNMX. 1 PublicationCorresponds to variant rs132630307dbSNPEnsembl.1
    Natural variantiVAR_009217179P → S in CNMX; mild. 2 PublicationsCorresponds to variant rs587783832dbSNPEnsembl.1
    Natural variantiVAR_018232180N → K in CNMX; very mild. 1 Publication1
    Natural variantiVAR_006390184R → G in CNMX; severe; loss of activity; abolishes interaction with DES. 3 PublicationsCorresponds to variant rs587783835dbSNPEnsembl.1
    Natural variantiVAR_018233184R → L in CNMX. 1 Publication1
    Natural variantiVAR_018234186T → I in CNMX. 1 PublicationCorresponds to variant rs587783836dbSNPEnsembl.1
    Natural variantiVAR_006391189N → S in CNMX. 1 PublicationCorresponds to variant rs132630302dbSNPEnsembl.1
    Natural variantiVAR_018235197T → I in CNMX. 1 Publication1
    Natural variantiVAR_006392198Y → N in CNMX; severe. 1 Publication1
    Natural variantiVAR_018236199P → S in CNMX. 1 Publication1
    Natural variantiVAR_018237202L → S in CNMX; severe. 1 Publication1
    Natural variantiVAR_006393205P → L in CNMX; severe; dramatic decrease in phosphatase activity; abolishes interaction with DES. 6 PublicationsCorresponds to variant rs587783841dbSNPEnsembl.1
    Natural variantiVAR_009218225I → T in CNMX; mild. 2 Publications1
    Natural variantiVAR_018238226P → T in CNMX. 1 PublicationCorresponds to variant rs587783848dbSNPEnsembl.1
    Natural variantiVAR_018239227V → M in CNMX. 1 PublicationCorresponds to variant rs587783850dbSNPEnsembl.1
    Natural variantiVAR_018240228L → P in CNMX. 1 PublicationCorresponds to variant rs587783851dbSNPEnsembl.1
    Natural variantiVAR_006394229S → P in CNMX; mild. 1 Publication1
    Natural variantiVAR_018241230W → C in CNMX. 2 Publications1
    Natural variantiVAR_018242232H → R in CNMX. 1 Publication1
    Natural variantiVAR_006395241R → C in CNMX; mild to moderate; abolishes interaction with DES. 6 PublicationsCorresponds to variant rs132630305dbSNPEnsembl.1
    Natural variantiVAR_006396241R → L in CNMX; severe; loss of activity. 3 Publications1
    Natural variantiVAR_009219264I → S in CNMX; severe. 1 PublicationCorresponds to variant rs587783856dbSNPEnsembl.1
    Natural variantiVAR_018243279A → G in CNMX. 1 Publication1
    Natural variantiVAR_009220294Missing in CNMX; mild. 1 Publication1
    Natural variantiVAR_006397317M → R in CNMX; mild. 1 Publication1
    Natural variantiVAR_018244346W → C in CNMX; mild. 1 Publication1
    Natural variantiVAR_018245346W → S in CNMX. 1
    Natural variantiVAR_018246364V → G in CNMX. 1 Publication1
    Natural variantiVAR_018247374H → D in CNMX. Corresponds to variant rs587783754dbSNPEnsembl.1
    Natural variantiVAR_006398376S → N in CNMX; dramatic decrease in phosphatase activity. 2 Publications1
    Natural variantiVAR_018248378G → E in CNMX. 1 Publication1
    Natural variantiVAR_006399378G → R in CNMX; severe; dramatic decrease in phosphatase activity; does not affect EGFR degradation. 5 PublicationsCorresponds to variant rs587783755dbSNPEnsembl.1
    Natural variantiVAR_068846387S → Y in CNMX. 1 PublicationCorresponds to variant rs587783759dbSNPEnsembl.1
    Natural variantiVAR_018249389A → D in CNMX; severe. 1 Publication1
    Natural variantiVAR_018250391L → P in CNMX. 1 Publication1
    Natural variantiVAR_006400397Y → C in CNMX; severe; dramatic decrease in phosphatase activity. 5 PublicationsCorresponds to variant rs132630303dbSNPEnsembl.1
    Natural variantiVAR_006401402G → A in CNMX; mild. 1 PublicationCorresponds to variant rs587783762dbSNPEnsembl.1
    Natural variantiVAR_018251402G → R in CNMX. 3 Publications1
    Natural variantiVAR_018252402G → V in CNMX. 1 Publication1
    Natural variantiVAR_006402404E → K in CNMX; mild. 2 PublicationsCorresponds to variant rs781933660dbSNPEnsembl.1
    Natural variantiVAR_006403406L → P in CNMX; severe. 1 Publication1
    Natural variantiVAR_018253411W → C in CNMX. Corresponds to variant rs587783764dbSNPEnsembl.1
    Natural variantiVAR_009221420S → SFIQ in CNMX; severe. 1
    Natural variantiVAR_006404421R → Q in CNMX; severe; reduced activity and response to PI5P; does not affect interaction with DES. 6 PublicationsCorresponds to variant rs587783772dbSNPEnsembl.1
    Natural variantiVAR_006405421R → RFIQ in CNMX; severe. 1
    Natural variantiVAR_006406431D → N in CNMX. 1 Publication1
    Natural variantiVAR_006407433D → N in CNMX. 1 Publication1
    Natural variantiVAR_018254444C → Y in CNMX. 1 Publication1
    Natural variantiVAR_006408469H → P in CNMX. 2 Publications1
    Natural variantiVAR_018255470L → P in CNMX; severe. 1 Publication1
    Natural variantiVAR_018256481N → Y in CNMX; mild. 1 Publication1
    Natural variantiVAR_006409499W → R in CNMX; mild. 1 PublicationCorresponds to variant rs587783801dbSNPEnsembl.1
    Natural variantiVAR_009222510K → N in CNMX; severe. 1 Publication1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_05620878 – 114Missing in isoform 2. 1 PublicationAdd BLAST37

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U46024 mRNA. Translation: AAC51682.1.
    AF020676
    , AF020664, AF020665, AF020666, AF020667, AF020668, AF020669, AF020670, AF020671, AF020672, AF020673, AF020674, AF020675 Genomic DNA. Translation: AAC12865.1.
    AK297021 mRNA. Translation: BAH12477.1.
    AC109994 Genomic DNA. No translation available.
    AF002223 Genomic DNA. No translation available.
    CH471169 Genomic DNA. Translation: EAW99377.1.
    BC030779 mRNA. Translation: AAH30779.1.
    CCDSiCCDS14694.1. [Q13496-1]
    RefSeqiNP_000243.1. NM_000252.2. [Q13496-1]
    XP_005274744.1. XM_005274687.2. [Q13496-1]
    XP_011529475.1. XM_011531173.2. [Q13496-1]
    XP_016885039.1. XM_017029550.1. [Q13496-2]
    UniGeneiHs.655056.

    Genome annotation databases

    EnsembliENST00000370396; ENSP00000359423; ENSG00000171100. [Q13496-1]
    GeneIDi4534.
    KEGGihsa:4534.
    UCSCiuc004fef.5. human. [Q13496-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Leiden Muscular Dystrophy pages, Myotubularin 1 (MTM1)

    Leiden Open Variation Database (LOVD)

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U46024 mRNA. Translation: AAC51682.1.
    AF020676
    , AF020664, AF020665, AF020666, AF020667, AF020668, AF020669, AF020670, AF020671, AF020672, AF020673, AF020674, AF020675 Genomic DNA. Translation: AAC12865.1.
    AK297021 mRNA. Translation: BAH12477.1.
    AC109994 Genomic DNA. No translation available.
    AF002223 Genomic DNA. No translation available.
    CH471169 Genomic DNA. Translation: EAW99377.1.
    BC030779 mRNA. Translation: AAH30779.1.
    CCDSiCCDS14694.1. [Q13496-1]
    RefSeqiNP_000243.1. NM_000252.2. [Q13496-1]
    XP_005274744.1. XM_005274687.2. [Q13496-1]
    XP_011529475.1. XM_011531173.2. [Q13496-1]
    XP_016885039.1. XM_017029550.1. [Q13496-2]
    UniGeneiHs.655056.

    3D structure databases

    ProteinModelPortaliQ13496.
    SMRiQ13496.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi110630. 7 interactors.
    DIPiDIP-61934N.
    IntActiQ13496. 6 interactors.
    STRINGi9606.ENSP00000359423.

    Chemistry databases

    SwissLipidsiSLP:000000846.
    SLP:000000847.

    PTM databases

    DEPODiQ13496.
    iPTMnetiQ13496.
    PhosphoSitePlusiQ13496.

    Polymorphism and mutation databases

    BioMutaiMTM1.
    DMDMi2851537.

    Proteomic databases

    EPDiQ13496.
    MaxQBiQ13496.
    PaxDbiQ13496.
    PeptideAtlasiQ13496.
    PRIDEiQ13496.

    Protocols and materials databases

    DNASUi4534.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000370396; ENSP00000359423; ENSG00000171100. [Q13496-1]
    GeneIDi4534.
    KEGGihsa:4534.
    UCSCiuc004fef.5. human. [Q13496-1]

    Organism-specific databases

    CTDi4534.
    DisGeNETi4534.
    GeneCardsiMTM1.
    GeneReviewsiMTM1.
    HGNCiHGNC:7448. MTM1.
    HPAiHPA010008.
    HPA010665.
    MalaCardsiMTM1.
    MIMi300415. gene.
    310400. phenotype.
    neXtProtiNX_Q13496.
    OpenTargetsiENSG00000171100.
    Orphaneti596. X-linked centronuclear myopathy.
    PharmGKBiPA31251.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1089. Eukaryota.
    ENOG410XPTU. LUCA.
    GeneTreeiENSGT00760000118832.
    HOGENOMiHOG000210598.
    HOVERGENiHBG000220.
    InParanoidiQ13496.
    KOiK01108.
    OMAiPNHHWRI.
    OrthoDBiEOG091G04DS.
    PhylomeDBiQ13496.
    TreeFamiTF315197.

    Enzyme and pathway databases

    BioCyciZFISH:HS10241-MONOMER.
    BRENDAi3.1.3.64. 2681.
    3.1.3.95. 2681.
    ReactomeiR-HSA-1660499. Synthesis of PIPs at the plasma membrane.
    R-HSA-1660516. Synthesis of PIPs at the early endosome membrane.
    R-HSA-1660517. Synthesis of PIPs at the late endosome membrane.

    Miscellaneous databases

    ChiTaRSiMTM1. human.
    GeneWikiiMyotubularin_1.
    GenomeRNAii4534.
    PROiQ13496.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000171100.
    CleanExiHS_MTM1.
    ExpressionAtlasiQ13496. baseline and differential.
    GenevisibleiQ13496. HS.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    3.90.190.10. 1 hit.
    InterProiIPR004182. GRAM.
    IPR010569. Myotubularin-like_Pase_dom.
    IPR030564. Myotubularin_fam.
    IPR011993. PH_dom-like.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR016130. Tyr_Pase_AS.
    IPR003595. Tyr_Pase_cat.
    IPR000387. TYR_PHOSPHATASE_dom.
    [Graphical view]
    PANTHERiPTHR10807. PTHR10807. 1 hit.
    PfamiPF02893. GRAM. 1 hit.
    PF06602. Myotub-related. 1 hit.
    [Graphical view]
    SMARTiSM00568. GRAM. 1 hit.
    SM00404. PTPc_motif. 1 hit.
    [Graphical view]
    SUPFAMiSSF50729. SSF50729. 1 hit.
    SSF52799. SSF52799. 1 hit.
    PROSITEiPS51339. PPASE_MYOTUBULARIN. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMTM1_HUMAN
    AccessioniPrimary (citable) accession number: Q13496
    Secondary accession number(s): A6NDB1
    , B7Z491, F2Z330, Q8NEL1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 15, 1998
    Last modified: November 30, 2016
    This is version 160 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.