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Q9Z2C5

- MTM1_MOUSE

UniProt

Q9Z2C5 - MTM1_MOUSE

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Protein
Myotubularin
Gene
Mtm1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 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.2 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 intermediate By similarity

GO - Molecular functioni

  1. intermediate filament binding Source: UniProtKB
  2. phosphatidylinositol binding Source: UniProtKB
  3. phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity Source: UniProtKB
  4. phosphatidylinositol-3-phosphatase activity 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
Complete GO annotation...

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

GO - Cellular componenti

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

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 – 603603Myotubularin
PRO_0000094931Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei495 – 4951Phosphothreonine By similarity
Modified residuei588 – 5881Phosphoserine By 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.1 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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 9769GRAM
Add
BLAST
Domaini163 – 538376Myotubularin phosphatase
Add
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.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951K → Y in AAC77821. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 108 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

Similar proteinsi