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Q13496

- MTM1_HUMAN

UniProt

Q13496 - MTM1_HUMAN

Protein

Myotubularin

Gene

MTM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (15 Jul 1998)
      Previous versions | rss
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    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.

    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)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: Ensembl
    6. phosphatidylinositol biosynthetic process Source: Reactome
    7. phosphatidylinositol dephosphorylation Source: UniProtKB
    8. phospholipid metabolic process Source: Reactome
    9. protein dephosphorylation Source: UniProtKB
    10. protein transport Source: UniProtKB-KW
    11. regulation of vacuole organization Source: UniProtKB
    12. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Protein transport, Transport

    Enzyme and pathway databases

    BRENDAi3.1.3.64. 2681.
    ReactomeiREACT_120756. Synthesis of PIPs at the early endosome membrane.
    REACT_120918. Synthesis of PIPs at the late endosome membrane.
    REACT_121025. Synthesis of PIPs at the plasma membrane.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myotubularin (EC:3.1.3.64)
    Gene namesi
    Name:MTM1
    Synonyms:CG2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:7448. MTM1.

    Subcellular locationi

    Cytoplasm. Cell membrane; Peripheral membrane protein. Cell projectionfilopodium. Cell projectionruffle. Late endosome
    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. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. filopodium Source: UniProtKB
    5. I band Source: Ensembl
    6. late endosome Source: UniProtKB
    7. plasma membrane Source: UniProtKB
    8. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Myopathy, centronuclear, X-linked (CNMX) [MIM:310400]: A congenital muscle disorder characterized by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles. It may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life. Ptosis is a frequent clinical feature. The most prominent histopathologic features include high frequency of centrally located nuclei in muscle fibers not secondary to regeneration, radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers.12 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti47 – 471Missing in CNMX. 1 Publication
    VAR_006386
    Natural varianti49 – 491V → 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. 1 Publication
    VAR_018227
    Natural varianti68 – 681Y → D in CNMX. 1 Publication
    VAR_018228
    Natural varianti69 – 691R → C in CNMX; mild; reduced response to PI5P and reduced binding to PI(3,5)P2. 3 Publications
    VAR_006387
    Natural varianti69 – 691R → P in CNMX. 1 Publication
    VAR_018229
    Natural varianti69 – 691R → S in CNMX; severe. 1 Publication
    VAR_018230
    Natural varianti70 – 701L → F in CNMX; mild; reduced binding to PI(3,5)P2. 2 Publications
    VAR_006388
    Natural varianti87 – 871L → P in CNMX; mild; reduced binding to PI(3,5)P2. 1 Publication
    VAR_006389
    Natural varianti157 – 1571E → K in CNMX. 1 Publication
    VAR_018231
    Natural varianti179 – 1791P → S in CNMX; mild. 2 Publications
    VAR_009217
    Natural varianti180 – 1801N → K in CNMX; very mild. 1 Publication
    VAR_018232
    Natural varianti184 – 1841R → G in CNMX; severe; loss of activity; abolishes interaction with DES. 1 Publication
    VAR_006390
    Natural varianti184 – 1841R → L in CNMX; reduced activity and response to PI5P. 1 Publication
    VAR_018233
    Natural varianti186 – 1861T → I in CNMX. 1 Publication
    VAR_018234
    Natural varianti189 – 1891N → S in CNMX. 1 Publication
    VAR_006391
    Natural varianti197 – 1971T → I in CNMX. 1 Publication
    VAR_018235
    Natural varianti198 – 1981Y → N in CNMX; severe. 1 Publication
    VAR_006392
    Natural varianti199 – 1991P → S in CNMX. 1 Publication
    VAR_018236
    Natural varianti202 – 2021L → S in CNMX; severe. 1 Publication
    VAR_018237
    Natural varianti205 – 2051P → L in CNMX; severe; dramatic decrease in phosphatase activity; abolishes interaction with DES. 4 Publications
    VAR_006393
    Natural varianti225 – 2251I → T in CNMX; mild. 2 Publications
    VAR_009218
    Natural varianti226 – 2261P → T in CNMX. 1 Publication
    VAR_018238
    Natural varianti227 – 2271V → M in CNMX. 1 Publication
    VAR_018239
    Natural varianti228 – 2281L → P in CNMX. 1 Publication
    VAR_018240
    Natural varianti229 – 2291S → P in CNMX; mild. 1 Publication
    VAR_006394
    Natural varianti230 – 2301W → C in CNMX. 2 Publications
    VAR_018241
    Natural varianti232 – 2321H → R in CNMX. 1 Publication
    VAR_018242
    Natural varianti241 – 2411R → C in CNMX; mild to moderate; abolishes interaction with DES. 5 Publications
    VAR_006395
    Natural varianti241 – 2411R → L in CNMX; severe; loss of activity. 1 Publication
    VAR_006396
    Natural varianti264 – 2641I → S in CNMX; severe. 1 Publication
    VAR_009219
    Natural varianti279 – 2791A → G in CNMX. 1 Publication
    VAR_018243
    Natural varianti294 – 2941Missing in CNMX; mild. 1 Publication
    VAR_009220
    Natural varianti317 – 3171M → R in CNMX; mild. 1 Publication
    VAR_006397
    Natural varianti346 – 3461W → C in CNMX; mild. 1 Publication
    VAR_018244
    Natural varianti346 – 3461W → S in CNMX.
    VAR_018245
    Natural varianti364 – 3641V → G in CNMX. 1 Publication
    VAR_018246
    Natural varianti374 – 3741H → D in CNMX.
    VAR_018247
    Natural varianti376 – 3761S → N in CNMX; dramatic decrease in phosphatase activity. 1 Publication
    VAR_006398
    Natural varianti378 – 3781G → E in CNMX. 1 Publication
    VAR_018248
    Natural varianti378 – 3781G → R in CNMX; severe; dramatic decrease in phosphatase activity; does not affect EGFR degradation. 4 Publications
    VAR_006399
    Natural varianti387 – 3871S → Y in CNMX. 1 Publication
    VAR_068846
    Natural varianti389 – 3891A → D in CNMX; severe. 1 Publication
    VAR_018249
    Natural varianti391 – 3911L → P in CNMX. 1 Publication
    VAR_018250
    Natural varianti397 – 3971Y → C in CNMX; severe; dramatic decrease in phosphatase activity. 4 Publications
    VAR_006400
    Natural varianti402 – 4021G → A in CNMX; mild. 1 Publication
    VAR_006401
    Natural varianti402 – 4021G → R in CNMX. 3 Publications
    VAR_018251
    Natural varianti402 – 4021G → V in CNMX. 1 Publication
    VAR_018252
    Natural varianti404 – 4041E → K in CNMX; mild. 2 Publications
    VAR_006402
    Natural varianti406 – 4061L → P in CNMX; severe. 1 Publication
    VAR_006403
    Natural varianti411 – 4111W → C in CNMX.
    VAR_018253
    Natural varianti420 – 4201S → SFIQ in CNMX; severe.
    VAR_009221
    Natural varianti421 – 4211R → Q in CNMX; severe; reduced activity and response to PI5P; does not affect interaction with DES. 4 Publications
    VAR_006404
    Natural varianti421 – 4211R → RFIQ in CNMX; severe.
    VAR_006405
    Natural varianti431 – 4311D → N in CNMX. 1 Publication
    VAR_006406
    Natural varianti433 – 4331D → N in CNMX. 1 Publication
    VAR_006407
    Natural varianti444 – 4441C → Y in CNMX. 1 Publication
    VAR_018254
    Natural varianti469 – 4691H → P in CNMX; loss of activity. 2 Publications
    VAR_006408
    Natural varianti470 – 4701L → P in CNMX; severe. 1 Publication
    VAR_018255
    Natural varianti481 – 4811N → Y in CNMX; mild. 1 Publication
    VAR_018256
    Natural varianti499 – 4991W → R in CNMX; mild. 1 Publication
    VAR_006409
    Natural varianti510 – 5101K → N in CNMX; severe. 1 Publication
    VAR_009222

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi114 – 1141K → A: Reduced response to PI5P. 1 Publication
    Mutagenesisi181 – 1811H → A: Disrupts interaction with DES. Does not affect lipid phosphatase activity. 1 Publication
    Mutagenesisi206 – 2061Y → A: Disrupts interaction with DES. Does not affect lipid phosphatase activity. 1 Publication
    Mutagenesisi209 – 2091S → A: Disrupts interaction with DES. Does not affect lipid phosphatase activity. 1 Publication
    Mutagenesisi220 – 2201R → A: Loss of activity. 1 Publication
    Mutagenesisi255 – 2551K → A: Disrupts interaction with DES. 1 Publication
    Mutagenesisi257 – 2571D → A: No effect on subcellular location. 1 Publication
    Mutagenesisi269 – 2691K → A: Disrupts interaction with DES. Does not affect lipid phosphatase activity. 1 Publication
    Mutagenesisi278 – 2781D → A: Localizes to plasma membrane extensions. Does not affect interaction with DES. 3 Publications
    Mutagenesisi375 – 3751C → A: No effect on subcellular location. 5 Publications
    Mutagenesisi375 – 3751C → S: Lacks activity toward PI3P. Does not affect interaction with DES. 5 Publications
    Mutagenesisi377 – 3771D → A: No effect on subcellular location. 2 Publications
    Mutagenesisi380 – 3801D → A: Does not affect interaction with DES. 3 Publications
    Mutagenesisi394 – 3941D → A: Produces an unstable protein. 1 Publication
    Mutagenesisi410 – 4101E → A: Produces an unstable protein. 1 Publication
    Mutagenesisi420 – 4201S → D: Does not affect interaction with DES. 1 Publication
    Mutagenesisi443 – 4431D → A: Produces an unstable protein. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi310400. phenotype.
    Orphaneti596. X-linked centronuclear myopathy.
    PharmGKBiPA31251.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 603603MyotubularinPRO_0000094930Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei495 – 4951Phosphothreonine1 Publication
    Modified residuei588 – 5881Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13496.
    PaxDbiQ13496.
    PRIDEiQ13496.

    PTM databases

    PhosphoSiteiQ13496.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13496.
    BgeeiQ13496.
    CleanExiHS_MTM1.
    GenevestigatoriQ13496.

    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.3 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

    Protein-protein interaction databases

    BioGridi110630. 3 interactions.
    IntActiQ13496. 6 interactions.
    STRINGi9606.ENSP00000359423.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13496.
    SMRiQ13496. 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.

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG322789.
    HOGENOMiHOG000210598.
    HOVERGENiHBG000220.
    InParanoidiQ13496.
    KOiK01108.
    OMAiQGLPNHH.
    PhylomeDBiQ13496.
    TreeFamiTF315197.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    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

    MASASTSKYN SHSLENESIK RTSRDGVNRD LTEAVPRLPG ETLITDKEVI    50
    YICPFNGPIK GRVYITNYRL YLRSLETDSS LILDVPLGVI SRIEKMGGAT 100
    SRGENSYGLD ITCKDMRNLR FALKQEGHSR RDMFEILTRY AFPLAHSLPL 150
    FAFLNEEKFN VDGWTVYNPV EEYRRQGLPN HHWRITFINK CYELCDTYPA 200
    LLVVPYRASD DDLRRVATFR SRNRIPVLSW IHPENKTVIV RCSQPLVGMS 250
    GKRNKDDEKY LDVIRETNKQ ISKLTIYDAR PSVNAVANKA TGGGYESDDA 300
    YHNAELFFLD IHNIHVMRES LKKVKDIVYP NVEESHWLSS LESTHWLEHI 350
    KLVLTGAIQV ADKVSSGKSS VLVHCSDGWD RTAQLTSLAM LMLDSFYRSI 400
    EGFEILVQKE WISFGHKFAS RIGHGDKNHT DADRSPIFLQ FIDCVWQMSK 450
    QFPTAFEFNE QFLIIILDHL YSCRFGTFLF NCESARERQK VTERTVSLWS 500
    LINSNKEKFK NPFYTKEINR VLYPVASMRH LELWVNYYIR WNPRIKQQQP 550
    NPVEQRYMEL LALRDEYIKR LEELQLANSA KLSDPPTSPS SPSQMMPHVQ 600
    THF 603
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti410 – 4101E → K in AAH30779. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti47 – 471Missing in CNMX. 1 Publication
    VAR_006386
    Natural varianti49 – 491V → 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. 1 Publication
    VAR_018227
    Natural varianti68 – 681Y → D in CNMX. 1 Publication
    VAR_018228
    Natural varianti69 – 691R → C in CNMX; mild; reduced response to PI5P and reduced binding to PI(3,5)P2. 3 Publications
    VAR_006387
    Natural varianti69 – 691R → P in CNMX. 1 Publication
    VAR_018229
    Natural varianti69 – 691R → S in CNMX; severe. 1 Publication
    VAR_018230
    Natural varianti70 – 701L → F in CNMX; mild; reduced binding to PI(3,5)P2. 2 Publications
    VAR_006388
    Natural varianti87 – 871L → P in CNMX; mild; reduced binding to PI(3,5)P2. 1 Publication
    VAR_006389
    Natural varianti157 – 1571E → K in CNMX. 1 Publication
    VAR_018231
    Natural varianti179 – 1791P → S in CNMX; mild. 2 Publications
    VAR_009217
    Natural varianti180 – 1801N → K in CNMX; very mild. 1 Publication
    VAR_018232
    Natural varianti184 – 1841R → G in CNMX; severe; loss of activity; abolishes interaction with DES. 1 Publication
    VAR_006390
    Natural varianti184 – 1841R → L in CNMX; reduced activity and response to PI5P. 1 Publication
    VAR_018233
    Natural varianti186 – 1861T → I in CNMX. 1 Publication
    VAR_018234
    Natural varianti189 – 1891N → S in CNMX. 1 Publication
    VAR_006391
    Natural varianti197 – 1971T → I in CNMX. 1 Publication
    VAR_018235
    Natural varianti198 – 1981Y → N in CNMX; severe. 1 Publication
    VAR_006392
    Natural varianti199 – 1991P → S in CNMX. 1 Publication
    VAR_018236
    Natural varianti202 – 2021L → S in CNMX; severe. 1 Publication
    VAR_018237
    Natural varianti205 – 2051P → L in CNMX; severe; dramatic decrease in phosphatase activity; abolishes interaction with DES. 4 Publications
    VAR_006393
    Natural varianti225 – 2251I → T in CNMX; mild. 2 Publications
    VAR_009218
    Natural varianti226 – 2261P → T in CNMX. 1 Publication
    VAR_018238
    Natural varianti227 – 2271V → M in CNMX. 1 Publication
    VAR_018239
    Natural varianti228 – 2281L → P in CNMX. 1 Publication
    VAR_018240
    Natural varianti229 – 2291S → P in CNMX; mild. 1 Publication
    VAR_006394
    Natural varianti230 – 2301W → C in CNMX. 2 Publications
    VAR_018241
    Natural varianti232 – 2321H → R in CNMX. 1 Publication
    VAR_018242
    Natural varianti241 – 2411R → C in CNMX; mild to moderate; abolishes interaction with DES. 5 Publications
    VAR_006395
    Natural varianti241 – 2411R → L in CNMX; severe; loss of activity. 1 Publication
    VAR_006396
    Natural varianti264 – 2641I → S in CNMX; severe. 1 Publication
    VAR_009219
    Natural varianti279 – 2791A → G in CNMX. 1 Publication
    VAR_018243
    Natural varianti294 – 2941Missing in CNMX; mild. 1 Publication
    VAR_009220
    Natural varianti317 – 3171M → R in CNMX; mild. 1 Publication
    VAR_006397
    Natural varianti346 – 3461W → C in CNMX; mild. 1 Publication
    VAR_018244
    Natural varianti346 – 3461W → S in CNMX.
    VAR_018245
    Natural varianti364 – 3641V → G in CNMX. 1 Publication
    VAR_018246
    Natural varianti374 – 3741H → D in CNMX.
    VAR_018247
    Natural varianti376 – 3761S → N in CNMX; dramatic decrease in phosphatase activity. 1 Publication
    VAR_006398
    Natural varianti378 – 3781G → E in CNMX. 1 Publication
    VAR_018248
    Natural varianti378 – 3781G → R in CNMX; severe; dramatic decrease in phosphatase activity; does not affect EGFR degradation. 4 Publications
    VAR_006399
    Natural varianti387 – 3871S → Y in CNMX. 1 Publication
    VAR_068846
    Natural varianti389 – 3891A → D in CNMX; severe. 1 Publication
    VAR_018249
    Natural varianti391 – 3911L → P in CNMX. 1 Publication
    VAR_018250
    Natural varianti397 – 3971Y → C in CNMX; severe; dramatic decrease in phosphatase activity. 4 Publications
    VAR_006400
    Natural varianti402 – 4021G → A in CNMX; mild. 1 Publication
    VAR_006401
    Natural varianti402 – 4021G → R in CNMX. 3 Publications
    VAR_018251
    Natural varianti402 – 4021G → V in CNMX. 1 Publication
    VAR_018252
    Natural varianti404 – 4041E → K in CNMX; mild. 2 Publications
    VAR_006402
    Natural varianti406 – 4061L → P in CNMX; severe. 1 Publication
    VAR_006403
    Natural varianti411 – 4111W → C in CNMX.
    VAR_018253
    Natural varianti420 – 4201S → SFIQ in CNMX; severe.
    VAR_009221
    Natural varianti421 – 4211R → Q in CNMX; severe; reduced activity and response to PI5P; does not affect interaction with DES. 4 Publications
    VAR_006404
    Natural varianti421 – 4211R → RFIQ in CNMX; severe.
    VAR_006405
    Natural varianti431 – 4311D → N in CNMX. 1 Publication
    VAR_006406
    Natural varianti433 – 4331D → N in CNMX. 1 Publication
    VAR_006407
    Natural varianti444 – 4441C → Y in CNMX. 1 Publication
    VAR_018254
    Natural varianti469 – 4691H → P in CNMX; loss of activity. 2 Publications
    VAR_006408
    Natural varianti470 – 4701L → P in CNMX; severe. 1 Publication
    VAR_018255
    Natural varianti481 – 4811N → Y in CNMX; mild. 1 Publication
    VAR_018256
    Natural varianti499 – 4991W → R in CNMX; mild. 1 Publication
    VAR_006409
    Natural varianti510 – 5101K → N in CNMX; severe. 1 Publication
    VAR_009222

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei78 – 11437Missing in isoform 2. 1 PublicationVSP_056208Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    RefSeqiNP_000243.1. NM_000252.2.
    XP_005274744.1. XM_005274687.1.
    UniGeneiHs.655056.

    Genome annotation databases

    EnsembliENST00000370396; ENSP00000359423; ENSG00000171100.
    ENST00000413012; ENSP00000389157; ENSG00000171100.
    GeneIDi4534.
    KEGGihsa:4534.
    UCSCiuc004fef.4. human.

    Polymorphism databases

    DMDMi2851537.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS14694.1.
    RefSeqi NP_000243.1. NM_000252.2.
    XP_005274744.1. XM_005274687.1.
    UniGenei Hs.655056.

    3D structure databases

    ProteinModelPortali Q13496.
    SMRi Q13496. Positions 33-543.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110630. 3 interactions.
    IntActi Q13496. 6 interactions.
    STRINGi 9606.ENSP00000359423.

    PTM databases

    PhosphoSitei Q13496.

    Polymorphism databases

    DMDMi 2851537.

    Proteomic databases

    MaxQBi Q13496.
    PaxDbi Q13496.
    PRIDEi Q13496.

    Protocols and materials databases

    DNASUi 4534.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370396 ; ENSP00000359423 ; ENSG00000171100 .
    ENST00000413012 ; ENSP00000389157 ; ENSG00000171100 .
    GeneIDi 4534.
    KEGGi hsa:4534.
    UCSCi uc004fef.4. human.

    Organism-specific databases

    CTDi 4534.
    GeneCardsi GC0XP149738.
    GeneReviewsi MTM1.
    HGNCi HGNC:7448. MTM1.
    HPAi HPA010008.
    HPA010665.
    MIMi 300415. gene.
    310400. phenotype.
    neXtProti NX_Q13496.
    Orphaneti 596. X-linked centronuclear myopathy.
    PharmGKBi PA31251.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG322789.
    HOGENOMi HOG000210598.
    HOVERGENi HBG000220.
    InParanoidi Q13496.
    KOi K01108.
    OMAi QGLPNHH.
    PhylomeDBi Q13496.
    TreeFami TF315197.

    Enzyme and pathway databases

    BRENDAi 3.1.3.64. 2681.
    Reactomei REACT_120756. Synthesis of PIPs at the early endosome membrane.
    REACT_120918. Synthesis of PIPs at the late endosome membrane.
    REACT_121025. Synthesis of PIPs at the plasma membrane.

    Miscellaneous databases

    ChiTaRSi MTM1. human.
    GeneWikii Myotubularin_1.
    GenomeRNAii 4534.
    NextBioi 17492.
    PROi Q13496.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13496.
    Bgeei Q13496.
    CleanExi HS_MTM1.
    Genevestigatori Q13496.

    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. "A gene mutated in X-linked myotubular myopathy defines a new putative tyrosine phosphatase family conserved in yeast."
      Laporte J., Hu L.-J., Kretz C., Mandel J.-L., Kioschis P., Coy J., Klauck S.M., Poutska A., Dahl N.
      Nat. Genet. 13:175-182(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Genomic organization of the MTM1 gene implicated in X-linked myotubular myopathy."
      Laporte J., Guiraud-Chaumeil C., Tanner S.M., Blondeau F., Hu L.J., Vicaire S., Liechti-Gallati S., Mandel J.-L.
      Eur. J. Hum. Genet. 6:325-330(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Umbilical cord blood.
    4. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Testis.
    7. "Association of SET domain and myotubularin-related proteins modulates growth control."
      Cui X., De Vivo I., Slany R., Miyamoto A., Firestein R., Cleary M.L.
      Nat. Genet. 18:331-337(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KMT2A/MLL1.
    8. Cited for: REVIEW ON VARIANTS CNMX.
    9. "Myotubularin, a phosphatase deficient in myotubular myopathy, acts on phosphatidylinositol 3-kinase and phosphatidylinositol 3-phosphate pathway."
      Blondeau F., Laporte J., Bodin S., Superti-Furga G., Payrastre B., Mandel J.L.
      Hum. Mol. Genet. 9:2223-2229(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-278; CYS-375; ASP-377; ASP-380; ASP-394; GLU-410 AND ASP-443.
    10. "Myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate."
      Taylor G.S., Maehama T., Dixon J.E.
      Proc. Natl. Acad. Sci. U.S.A. 97:8910-8915(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS LEU-205; LEU-241; ASN-376; ARG-378 AND CYS-397, MUTAGENESIS OF CYS-375.
    11. "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, MUTAGENESIS OF ASP-257; ASP-278; CYS-375; ASP-377 AND ASP-380.
    12. "Phosphatidylinositol-5-phosphate activation and conserved substrate specificity of the myotubularin phosphatidylinositol 3-phosphatases."
      Schaletzky J., Dove S.K., Short B., Lorenzo O., Clague M.J., Barr F.A.
      Curr. Biol. 13:504-509(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, CHARACTERIZATION OF VARIANTS CYS-69; GLY-184; LEU-241; GLN-421 AND PRO-469, MUTAGENESIS OF LYS-114; ARG-220 AND CYS-375.
    13. "Identification of myotubularin as the lipid phosphatase catalytic subunit associated with the 3-phosphatase adapter protein, 3-PAP."
      Nandurkar H.H., Layton M., Laporte J., Selan C., Corcoran L., Caldwell K.K., Mochizuki Y., Majerus P.W., Mitchell C.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:8660-8665(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MTMR12, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    14. "Myotubularin regulates the function of the late endosome through the gram domain-phosphatidylinositol 3,5-bisphosphate interaction."
      Tsujita K., Itoh T., Ijuin T., Yamamoto A., Shisheva A., Laporte J., Takenawa T.
      J. Biol. Chem. 279:13817-13824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, ROLE OF GRAM DOMAIN, CHARACTERIZATION OF VARIANTS PHE-49; CYS-69; PHE-70 AND PRO-87.
    15. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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, CHARACTERIZATION OF VARIANTS GLY-184; LEU-205; CYS-241 AND GLN-421, MUTAGENESIS OF HIS-181; TYR-206; SER-209; LYS-255; LYS-269; ASP-278; CYS-375; ASP-380 AND SER-420.
    20. "Characterization of mutations in the myotubularin gene in twenty six patients with X-linked myotubular myopathy."
      de Gouyon B.M., Zhao W., Laporte J., Mandel J.-L., Metzenberg A., Herman G.E.
      Hum. Mol. Genet. 6:1499-1504(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CNMX CYS-69; GLY-184; ASN-198; LEU-241; ARG-317; CYS-397; LYS-404; PRO-406; GLN-421 AND ARG-499.
    21. Cited for: VARIANTS CNMX CYS-69; PHE-70; PRO-87; SER-189; LEU-205; PRO-229; CYS-241; ASN-376; ARG-378; CYS-397; ALA-402; GLN-421; ASN-431; ASN-433 AND PRO-469.
    22. "MTM1 gene mutations in Japanese patients with the severe infantile form of myotubular myopathy."
      Nishino I., Minami N., Kobayashi O., Ikezawa M., Goto Y., Arahata K., Nonaka I.
      Neuromuscul. Disord. 8:453-458(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CNMX VAL-402.
    23. "Germline mosaicism in X-linked myotubular myopathy."
      Haene B.G., Rogers R.C., Schwartz C.E.
      Clin. Genet. 56:77-81(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CNMX GLU-378.
    24. "Identification of novel mutations in the MTM1 gene causing severe and mild forms of X-linked myotubular myopathy."
      Buj-Bello A., Biancalana V., Moutou C., Laporte J., Mandel J.-L.
      Hum. Mutat. 14:320-325(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CNMX SER-179; THR-225; CYS-241; SER-264; GLY-294 DEL; ARG-378 AND ASN-510.
    25. "Characterization of 34 novel and six known MTM1 gene mutations in 47 unrelated X-linked myotubular myopathy patients."
      Tanner S.M., Schneider V., Thomas N.S.T., Clarke A., Lazarou L., Liechti-Gallati S.
      Neuromuscul. Disord. 9:41-49(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CNMX LEU-205; THR-225; CYS-230; ARG-232; CYS-241; ARG-402 AND TYR-444.
    26. "Characterization of mutations in fifty North American patients with X-linked myotubular myopathy."
      Herman G.E., Kopacz K., Zhao W., Mills P.L., Metzenberg A., Das S.
      Hum. Mutat. 19:114-121(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CNMX PHE-49; CYS-69; SER-179; ILE-186; LEU-205; MET-227; PRO-228; CYS-241; GLY-279; ARG-378; PRO-391; CYS-397; ARG-402 AND GLN-421.
    27. "Rapid scanning of myotubularin (MTM1) gene by denaturing high-performance liquid chromatography (DHPLC)."
      Flex E., De Luca A., D'Apice M.R., Buccino A., Dallapiccola B., Novelli G.
      Neuromuscul. Disord. 12:501-505(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CNMX ILE-197; SER-199; ARG-378 AND ARG-402.
    28. "X-linked myotubular myopathy in a family with three adult survivors."
      Yu S., Manson J., White S., Bourne A., Waddy H., Davis M., Haan E.
      Clin. Genet. 64:148-152(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CNMX LYS-157.
    29. "Characterisation of mutations in 77 patients with X-linked myotubular myopathy, including a family with a very mild phenotype."
      Biancalana V., Caron O., Gallati S., Baas F., Kress W., Novelli G., D'Apice M.R., Lagier-Tourenne C., Buj-Bello A., Romero N.B., Mandel J.-L.
      Hum. Genet. 112:135-142(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CNMX LYS-47 DEL; ASP-68; PRO-69; SER-69; PHE-70; LYS-180; LEU-184; SER-202; LEU-205; THR-226; CYS-230; CYS-241; CYS-346; GLY-364; ASP-389; CYS-397; GLN-421; PRO-469; PRO-470 AND TYR-481.
    30. "Extreme phenotypic variability in a German family with X-linked myotubular myopathy associated with E404K mutation in MTM1."
      Hoffjan S., Thiels C., Vorgerd M., Neuen-Jacob E., Epplen J.T., Kress W.
      Neuromuscul. Disord. 16:749-753(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CNMX LYS-404.
    31. "X-linked myotubular myopathy with a novel MTM1 mutation in a Taiwanese child."
      Chang C.Y., Lin S.P., Lin H.Y., Chuang C.K., Ho C.S., Su Y.N.
      J. Formos. Med. Assoc. 107:965-970(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CNMX TYR-387.

    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: October 1, 2014
    This is version 137 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

    External Data

    Dasty 3