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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.By similarity2 Publications

Catalytic activityi

1-phosphatidyl-1D-myo-inositol 3-phosphate + H2O = 1-phosphatidyl-1D-myo-inositol + phosphate.By similarity
1-phosphatidyl-1D-myo-inositol 3,5-bisphosphate + H2O = 1-phosphatidyl-1D-myo-inositol 5-phosphate + phosphate.By similarity

Enzyme regulationi

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

Sites

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

GO - Molecular functioni

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

Lipid metabolism, 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
Alternative name(s):
Phosphatidylinositol-3,5-bisphosphate 3-phosphatase (EC:3.1.3.95By similarity)
Phosphatidylinositol-3-phosphate phosphatase (EC:3.1.3.64By similarity)
Gene namesi
Name:Mtm1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:1099452. Mtm1.

Subcellular locationi

Cytoplasm 1 Publication. Cell membrane By similarity; Peripheral membrane protein By similarity. Cell projectionfilopodium 1 Publication. Cell projectionruffle 1 Publication. Late endosome By similarity
Note: Localizes as a dense cytoplasmic network. Also localizes to the plasma membrane, including plasma membrane extensions such as filopodia and ruffles. Predominantly located in the cytoplasm following interaction with MTMR12. Recruited to the late endosome following EGF stimulation.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. filopodium Source: UniProtKB
  3. I band Source: MGI
  4. late endosome Source: UniProtKB
  5. plasma membrane Source: UniProtKB
  6. ruffle Source: UniProtKB
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 – 603603MyotubularinPRO_0000094931Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9Z2C5.
PaxDbiQ9Z2C5.
PRIDEiQ9Z2C5.

PTM databases

PhosphoSiteiQ9Z2C5.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9Z2C5.
CleanExiMM_MTM1.
ExpressionAtlasiQ9Z2C5. baseline and differential.
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. Interacts with SPEG (By similarity).By similarity1 Publication

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

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

Domaini

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG322789.
HOGENOMiHOG000210598.
HOVERGENiHBG000220.
InParanoidiQ9Z2C5.
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

        10         20         30         40         50
MASASASKYN SHSLENESIK KVSQDGVSQD VSETVPRLPG ELLITEKEVI
60 70 80 90 100
YICPFNGPIK GRVYITNYRL YLRSLETDSA LILDVPLGVI SRIEKMGGAT
110 120 130 140 150
SRGENSYGLD ITCKDLRNLR FALKQEGHSR RDMFEILVKH AFPLAHNLPL
160 170 180 190 200
FAFVNEEKFN VDGWTVYNPV EEYRRQGLPN HHWRISFINK CYELCETYPA
210 220 230 240 250
LLVVPYRTSD DDLRRIATFR SRNRLPVLSW IHPENKMVIM RCSQPLVGMS
260 270 280 290 300
GKRNKDDEKY LDVIRETNKQ TSKLMIYDAR PSVNAVANKA TGGGYESDDA
310 320 330 340 350
YQNSELSFLD IHNIHVMRES LKKVKDIVYP NIEESHWLSS LESTHWLEHI
360 370 380 390 400
KLVLTGAIQV ADQVSSGKSS VLVHCSDGWD RTAQLTSLAM LMLDSFYRTI
410 420 430 440 450
EGFEILVQKE WISFGHKFAS RIGHGDKNHA DADRSPIFLQ FIDCVWQMSK
460 470 480 490 500
QFPTAFEFNE GFLITVLDHL YSCRFGTFLF NCDSARERQK LTERTVSLWS
510 520 530 540 550
LINSNKDKFK NPFYTKEINR VLYPVASMRH LELWVNYYIR WNPRVKQQQP
560 570 580 590 600
NPVEQRYMEL LALRDDYIKR LEELQLANSA KLADAPASTS SSSQMVPHVQ

THF
Length:603
Mass (Da):69,559
Last modified:June 28, 2011 - v2
Checksum:i65929312F07FFCC7
GO

Experimental Info

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
HOGENOMi HOG000210598.
HOVERGENi HBG000220.
InParanoidi Q9Z2C5.
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

Bgeei Q9Z2C5.
CleanExi MM_MTM1.
ExpressionAtlasi Q9Z2C5. baseline and differential.
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: October 29, 2014
This is version 110 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