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Collapse Statistics
226 human active and 11 inactive phosphatases in total;
194 phosphatases have substrate data;
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305 protein substrates;
89 non-protein substrates;
1114 dephosphorylation interactions;
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213 KEGG pathways;
206 NCI Nature PID pathways
560 Reactome pathways;
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last update: 18 Feb, 2016

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MTM1

Gene Name MTM1 (QuickGO)SynonymsMTM1 CG2
Protein NameMyotubularin
Alternative name(s)
Myotubularin (EC 3.1.3.48)
Ensembl Gene IDENSG00000171100EntrezGene ID4534
UniProt AC (Human)Q13496 (protein sequence)Enzyme ClassEC 3.1.3.64 (BRENDA )
Molecular Weight69932Protein Length603
Phosphatase activityactive
Protein DomainInterPro | Pfam3D Structure * PDB | PDBe | DrugPort
* ModBase | SwissModel
Structure-based FamilyFamily 1 (CATH: 3.90.190.10)Historical ClassPTPs >> Class I Cys-based PTPs >> VH1-like or dual-specificity phosphatases (DSPs) >> Myotubularins
Localization cytoplasm (PubMed: 10900271 | Europe PMC)
Catalytic SiteCatalytic Site Atlas Target by Small MoleculesN/A
Gene ExpressionGene Expression Atlas

The Human Protein Atlas

Function and DiseaseOMIM
Protein-protein Interaction Database STRING | IntAct | MINT
Kinase Database Phospho.ELM | PhosphoSite | NetworKIN
Function (UniProt annotation)
FUNCTION: 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.
Catalytic Activity (UniProt annotation)
CATALYTIC ACTIVITY: 1-phosphatidyl-1D-myo-inositol 3-phosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol + phosphate.
Protein Sequence
MASASTSKYN SHSLENESIK RTSRDGVNRD LTEAVPRLPG ETLITDKEVI YICPFNGPIK GRVYITNYRL YLRSLETDSS LILDVPLGVI SRIEKMGGAT SRGENSYGLD ITCKDMRNLR FALKQEGHSR RDMFEILTRY AFPLAHSLPL FAFLNEEKFN VDGWTVYNPV EEYRRQGLPN HHWRITFINK CYELCDTYPA LLVVPYRASD DDLRRVATFR SRNRIPVLSW IHPENKTVIV RCSQPLVGMS GKRNKDDEKY LDVIRETNKQ ISKLTIYDAR PSVNAVANKA TGGGYESDDA YHNAELFFLD IHNIHVMRES LKKVKDIVYP NVEESHWLSS LESTHWLEHI KLVLTGAIQV ADKVSSGKSS VLVHCSDGWD RTAQLTSLAM LMLDSFYRSI EGFEILVQKE WISFGHKFAS RIGHGDKNHT DADRSPIFLQ FIDCVWQMSK QFPTAFEFNE QFLIIILDHL YSCRFGTFLF NCESARERQK VTERTVSLWS LINSNKEKFK NPFYTKEINR VLYPVASMRH LELWVNYYIR WNPRIKQQQP NPVEQRYMEL LALRDEYIKR LEELQLANSA KLSDPPTSPS SPSQMMPHVQ THF
ELM motif
N/A
Gene Ontology
GO:0008333endosome to lysosome transport
GO:0030175filopodium
GO:0019215intermediate filament binding
GO:0045109intermediate filament organization
GO:0005770late endosome
GO:0048311mitochondrion distribution
GO:0070584mitochondrion morphogenesis
GO:0035091phosphatidylinositol binding
GO:0046856phosphatidylinositol dephosphorylation
GO:0052629phosphatidylinositol-3,5-bisphosphate 3-phosphatase activity
GO:0004438phosphatidylinositol-3-phosphatase activity
GO:0005886plasma membrane
GO:0015031protein transport
GO:0004725protein tyrosine phosphatase activity
GO:0044088regulation of vacuole organization
GO:0001726ruffle

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