Myotubularin 1

Protein-coding gene in the species Homo sapiens
MTM1
Identifiers
AliasesMTM1, CNM, MTMX, XLMTM, Myotubularin 1, myotubularin, CNMX
External IDsOMIM: 300415 MGI: 1099452 HomoloGene: 37279 GeneCards: MTM1
Gene location (Human)
X chromosome (human)
Chr.X chromosome (human)[1]
X chromosome (human)
Genomic location for MTM1
Genomic location for MTM1
BandXq28Start150,568,417 bp[1]
End150,673,143 bp[1]
Gene location (Mouse)
X chromosome (mouse)
Chr.X chromosome (mouse)[2]
X chromosome (mouse)
Genomic location for MTM1
Genomic location for MTM1
BandX A7.2- A7.3|X 36.55 cMStart70,254,373 bp[2]
End70,359,297 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • secondary oocyte

  • rectum

  • germinal epithelium

  • monocyte

  • jejunal mucosa

  • Achilles tendon

  • bone marrow cells

  • right adrenal gland

  • left adrenal gland

  • hair follicle
Top expressed in
  • left colon

  • jejunum

  • ileum

  • soleus muscle

  • cerebellar vermis

  • brown adipose tissue

  • myocardium of ventricle

  • digastric muscle

  • thoracic diaphragm

  • intercostal muscle
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • phosphoprotein phosphatase activity
  • intermediate filament binding
  • phosphatase activity
  • protein binding
  • phosphatidylinositol binding
  • protein tyrosine phosphatase activity
  • hydrolase activity
  • phosphatidylinositol-3-phosphatase activity
  • phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity
Cellular component
  • cytoplasm
  • endosome
  • late endosome
  • cell projection
  • membrane
  • I band
  • filopodium
  • ruffle
  • plasma membrane
  • cytosol
  • sarcomere
Biological process
  • negative regulation of autophagosome assembly
  • negative regulation of protein kinase B signaling
  • muscle cell cellular homeostasis
  • lipid metabolism
  • protein dephosphorylation
  • negative regulation of TOR signaling
  • mitochondrion distribution
  • negative regulation of proteasomal ubiquitin-dependent protein catabolic process
  • protein transport
  • phosphatidylinositol biosynthetic process
  • peptidyl-tyrosine dephosphorylation
  • mitochondrion morphogenesis
  • positive regulation of skeletal muscle tissue growth
  • dephosphorylation
  • endosome to lysosome transport
  • regulation of vacuole organization
  • intermediate filament organization
  • phosphatidylinositol dephosphorylation
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

4534

17772

Ensembl

ENSG00000171100

ENSMUSG00000031337

UniProt

Q13496

Q9Z2C5

RefSeq (mRNA)

NM_000252
NM_001376906
NM_001376907
NM_001376908

NM_001164190
NM_001164191
NM_001164192
NM_001164193
NM_019926

NM_001358113

RefSeq (protein)

NP_000243
NP_001363835
NP_001363836
NP_001363837

NP_001157662
NP_001157663
NP_001157664
NP_001157665
NP_064310

NP_001345042

Location (UCSC)Chr X: 150.57 – 150.67 MbChr X: 70.25 – 70.36 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Myotubularin is a protein that in humans is encoded by the MTM1 gene.[5]

This gene is a member of a gene family that encodes lipid phosphatases. Myotubularin is required for muscle cell differentiation and mutations in this gene have been identified as being responsible for X-linked myotubular myopathy.[5]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000171100 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031337 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: MTM1 myotubularin 1".

Further reading

  • Laporte J, Biancalana V, Tanner SM, et al. (2000). "MTM1 mutations in X-linked myotubular myopathy". Hum. Mutat. 15 (5): 393–409. doi:10.1002/(SICI)1098-1004(200005)15:5<393::AID-HUMU1>3.0.CO;2-R. PMID 10790201. S2CID 27091541.
  • Wishart MJ, Dixon JE (2003). "PTEN and myotubularin phosphatases: from 3-phosphoinositide dephosphorylation to disease". Trends Cell Biol. 12 (12): 579–85. doi:10.1016/S0962-8924(02)02412-1. PMID 12495846.
  • Laporte J, Bedez F, Bolino A, Mandel JL (2004). "Myotubularins, a large disease-associated family of cooperating catalytically active and inactive phosphoinositides phosphatases". Hum. Mol. Genet. 12. Spec No 2 (90002): R285–92. doi:10.1093/hmg/ddg273. PMID 12925573.
  • Kovács SK, Korcsik J, Szabó H, et al. (2007). "[Myotubular myopathy. Case report and review of the literature]". Orvosi Hetilap. 148 (37): 1757–62. doi:10.1556/OH.2007.28054. PMID 17827085.
  • Magnussen E (1975). "[In memoriam: Elisabeth Larsen]". Sygeplejersken. 75 (9): 16–7. PMID 1090027.
  • Liechti-Gallati S, Müller B, Grimm T, et al. (1992). "X-linked centronuclear myopathy: mapping the gene to Xq28". Neuromuscul. Disord. 1 (4): 239–45. doi:10.1016/0960-8966(91)90096-B. PMID 1822801. S2CID 34044731.
  • Laporte J, Hu LJ, Kretz C, et al. (1996). "A gene mutated in X-linked myotubular myopathy defines a new putative tyrosine phosphatase family conserved in yeast". Nat. Genet. 13 (2): 175–82. doi:10.1038/ng0696-175. PMID 8640223. S2CID 30028223.
  • de Gouyon BM, Zhao W, Laporte J, et al. (1998). "Characterization of mutations in the myotubularin gene in twenty six patients with X-linked myotubular myopathy". Hum. Mol. Genet. 6 (9): 1499–504. doi:10.1093/hmg/6.9.1499. PMID 9285787.
  • Laporte J, Guiraud-Chaumeil C, Vincent MC, et al. (1998). "Mutations in the MTM1 gene implicated in X-linked myotubular myopathy. ENMC International Consortium on Myotubular Myopathy. European Neuro-Muscular Center". Hum. Mol. Genet. 6 (9): 1505–11. doi:10.1093/hmg/6.9.1505. PMID 9305655.
  • Tanner SM, Laporte J, Guiraud-Chaumeil C, Liechti-Gallati S (1998). "Confirmation of prenatal diagnosis results of X-linked recessive myotubular myopathy by mutational screening, and description of three new mutations in the MTM1 gene". Hum. Mutat. 11 (1): 62–8. doi:10.1002/(SICI)1098-1004(1998)11:1<62::AID-HUMU10>3.0.CO;2-X. PMID 9450905. S2CID 39568857.
  • Cui X, De Vivo I, Slany R, et al. (1998). "Association of SET domain and myotubularin-related proteins modulates growth control". Nat. Genet. 18 (4): 331–7. doi:10.1038/ng0498-331. PMID 9537414. S2CID 25209204.
  • Laporte J, Blondeau F, Buj-Bello A, et al. (1998). "Characterization of the myotubularin dual specificity phosphatase gene family from yeast to human". Hum. Mol. Genet. 7 (11): 1703–12. doi:10.1093/hmg/7.11.1703. PMID 9736772.
  • Laporte J, Guiraud-Chaumeil C, Tanner SM, et al. (1998). "Genomic organization of the MTM1 gene implicated in X-linked myotubular myopathy". Eur. J. Hum. Genet. 6 (4): 325–30. doi:10.1038/sj.ejhg.5200189. PMID 9781038.
  • Kioschis P, Wiemann S, Heiss NS, et al. (1999). "Genomic organization of a 225-kb region in Xq28 containing the gene for X-linked myotubular myopathy (MTM1) and a related gene (MTMR1)". Genomics. 54 (2): 256–66. doi:10.1006/geno.1998.5560. PMID 9828128.
  • Nishino I, Minami N, Kobayashi O, et al. (1999). "MTM1 gene mutations in Japanese patients with the severe infantile form of myotubular myopathy". Neuromuscul. Disord. 8 (7): 453–8. doi:10.1016/S0960-8966(98)00075-3. PMID 9829274. S2CID 7841418.
  • Tanner SM, Schneider V, Thomas NS, et al. (1999). "Characterization of 34 novel and six known MTM1 gene mutations in 47 unrelated X-linked myotubular myopathy patients". Neuromuscul. Disord. 9 (1): 41–9. doi:10.1016/S0960-8966(98)00090-X. PMID 10063835. S2CID 10574620.
  • Häne BG, Rogers RC, Schwartz CE (1999). "Germline mosaicism in X-linked myotubular myopathy". Clin. Genet. 56 (1): 77–81. doi:10.1034/j.1399-0004.1999.560111.x. PMID 10466421. S2CID 826588.
  • Buj-Bello A, Biancalana V, Moutou C, et al. (1999). "Identification of novel mutations in the MTM1 gene causing severe and mild forms of X-linked myotubular myopathy". Hum. Mutat. 14 (4): 320–5. doi:10.1002/(SICI)1098-1004(199910)14:4<320::AID-HUMU7>3.0.CO;2-O. PMID 10502779. S2CID 6417585.
  • Taylor GS, Maehama T, Dixon JE (2000). "Inaugural article: myotubularin, a protein tyrosine phosphatase mutated in myotubular myopathy, dephosphorylates the lipid second messenger, phosphatidylinositol 3-phosphate". Proc. Natl. Acad. Sci. U.S.A. 97 (16): 8910–5. Bibcode:2000PNAS...97.8910T. doi:10.1073/pnas.160255697. PMC 16795. PMID 10900271.

External links

  • GeneReviews/NCBI/NIH/UW entry on X-Linked Myotubular Myopathy or Centronuclear Myopathy
  • v
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Class I
Classical PTPs
Receptor type PTPs
Non receptor type PTPs
VH1-like or
dual specific
phosphatases
(DSPs)
MAPK phosphatases (MKPs)
Slingshots
PRLs
CDC14s
Atypical DSPs
Phosphatase and tensin
homologs (PTENs)
Myotubularins
Class IIClass IIIClass IV
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