Mtm1
entrez
17772
canonical
uniprot
Q9Z2C5
canonical
ensembl
ENSMUSG00000031337
resolver
ensp
ENSMUSP00000025391
resolver
ensp
ENSMUSP00000033700
resolver
ensp
ENSMUSP00000057182
resolver
ensp
ENSMUSP00000099040
resolver
ensp
ENSMUSP00000110264
resolver
ensp
ENSMUSP00000110268
resolver
ensp
ENSMUSP00000125798
resolver
ensp
ENSMUSP00000195245
resolver
ensp
ENSMUSP00000195247
resolver
ensp
ENSMUSP00000195251
resolver
ensp
ENSMUSP00000195260
resolver
enst
ENSMUST00000025391
resolver
enst
ENSMUST00000033700
resolver
enst
ENSMUST00000061970
resolver
enst
ENSMUST00000101501
resolver
enst
ENSMUST00000114617
resolver
enst
ENSMUST00000114621
resolver
enst
ENSMUST00000171933
resolver
genesymbol
Mtm1
resolver
uniprot
B1AW21
resolver
uniprot
F6SZ33
resolver
uniprot
Q3UDN6
resolver
uniprot
Q5BKQ5
resolver
uniprot
Q9D4L1
resolver
uniprot_entry
B1AW21_MOUSE
resolver
uniprot_entry
F6SZ33_MOUSE
resolver
uniprot_entry
MTM1_MOUSE
resolver
uniprot_entry
Q3UDN6_MOUSE
resolver
uniprot_entry
Q9D4L1_MOUSE
resolver
uniprot_sec
Q5BKQ5
resolver
activity_regulation
ACTIVITY REGULATION: Allosterically activated by phosphatidylinositol 5-phosphate (PI5P). {ECO:0000250|UniProtKB:Q13496}.
uniprot
proteins
amino_acid_sequence
MASASASKYNSHSLENESIKKVSQDGVSQDVSETVPRLPGELLITEKEVIYICPFNGPIKGRVYITNYRLYLRSLETDSALILDVPLGVISRIEKMGGATSRGENSYGLDITCKDLRNLRFALKQEGHSRRDMFEILVKHAFPLAHNLPLFAFVNEEKFNVDGWTVYNPVEEYRRQGLPNHHWRISFINKCYELCETYPALLVVPYRTSDDDLRRIATFRSRNRLPVLSWIHPENKMVIMRCSQPLVGMSGKRNKDDEKYLDVIRETNKQTSKLMIYDARPSVNAVANKATGGGYESDDAYQNSELSFLDIHNIHVMRESLKKVKDIVYPNIEESHWLSSLESTHWLEHIKLVLTGAIQVADQVSSGKSSVLVHCSDGWDRTAQLTSLAMLMLDSFYRTIEGFEILVQKEWISFGHKFASRIGHGDKNHADADRSPIFLQFIDCVWQMSKQFPTAFEFNEGFLITVLDHLYSCRFGTFLFNCDSARERQKLTERTVSLWSLINSNKDKFKNPFYTKEINRVLYPVASMRHLELWVNYYIRWNPRVKQQQPNPVEQRYMELLALRDDYIKRLEELQLANSAKLADAPASTSSSSQMVPHVQTHF
uniprot
proteins
ec_number
3.1.3.95
uniprot
proteins
function
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 (By similarity). Regulates desmin intermediate filament assembly and architecture. Plays a role in mitochondrial morphology and positioning (PubMed:21135508). Required for skeletal muscle maintenance but not for myogenesis (PubMed:12391329). In skeletal muscles, stabilizes MTMR12 protein levels (PubMed:23818870). {ECO:0000250|UniProtKB:Q13496, ECO:0000269|PubMed:12391329, ECO:0000269|PubMed:21135508, ECO:0000269|PubMed:23818870}.
uniprot
proteins
mass_dalton
69559
uniprot
proteins
protein_family
Non-receptor class myotubularin subfamily
uniprot
proteins
protein_family
Protein-tyrosine phosphatase family
uniprot
proteins
pubmed
12118066
uniprot
proteins
pubmed
12391329
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21135508
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23818870
uniprot
proteins
pubmed
9736772
uniprot
proteins
sequence_length
603
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12118066}. Cell membrane {ECO:0000250|UniProtKB:Q13496}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13496}. Cell projection, filopodium {ECO:0000269|PubMed:12118066}. Cell projection, ruffle {ECO:0000269|PubMed:12118066}. Late endosome {ECO:0000250|UniProtKB:Q13496}. Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:23818870}. 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). In skeletal muscles, co-localizes with MTMR12 in the sarcomere (PubMed:23818870). {ECO:0000250|UniProtKB:Q13496, ECO:0000269|PubMed:23818870}.
uniprot
proteins