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Q5R9S3

- MTM1_PONAB

UniProt

Q5R9S3 - MTM1_PONAB

Protein

Myotubularin

Gene

MTM1

Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (21 Dec 2004)
      Previous versions | rss
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    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. 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 similarity.By similarity

    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 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. phosphatidylinositol dephosphorylation Source: UniProtKB
    6. protein dephosphorylation Source: UniProtKB
    7. protein transport Source: UniProtKB-KW
    8. regulation of vacuole organization Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myotubularin (EC:3.1.3.64)
    Gene namesi
    Name:MTM1
    OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
    Taxonomic identifieri9601 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
    ProteomesiUP000001595: Unplaced

    Subcellular locationi

    Cytoplasm By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity. Cell projectionfilopodium By similarity. Cell projectionruffle By similarity. 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.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. filopodium Source: UniProtKB
    3. late endosome Source: UniProtKB
    4. plasma membrane Source: UniProtKB
    5. ruffle Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Endosome, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 603603MyotubularinPRO_0000328656Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ5R9S3.

    Interactioni

    Subunit structurei

    Interacts with MTMR12; the interaction modulates MTM1 intracellular localization. Interacts with KMT2A/MLL1 (via SET domain). Interacts with DES in skeletal muscle but not in cardiac muscle By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ5R9S3.
    SMRiQ5R9S3. Positions 33-544.
    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

    HOGENOMiHOG000210598.
    HOVERGENiHBG000220.
    KOiK01108.

    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.

    Q5R9S3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASASTSKYN SHSLENESIK RTSRDGVNRD LTEAVPRLPG ETLITDKEVI    50
    YICPFNGPIK GRVYITNYRL YLRSLETDSA LILDVPLGVI SRIEKMGGAT 100
    SRGENSYGLD ITCKDMRNLR FALKQEGHSR RDMFEILTRY AFPLAHSLPL 150
    FAFLNEEKFN VDGWTVYNPV EEYRRQGLPN HHWRITFINK CYELCDTYPA 200
    PLVVPYRASD DDLRRVATFR SRNRIPVLSW IHPENKTVIV RCSQPLVGMS 250
    GKRNKDDEKY LDVIRETNKQ ISKLTIYDAR PSVNAVANKA TGGGYESDDA 300
    YHNAELFFLD IHNIHVMRES LKKVKDIVYP NVEESHWLSS LESTHWLEHI 350
    KLVLTGAIQV ADKVSSGKSS VLVHCSDGWD RTAQLTSLAM LMLDSFYRSI 400
    EGFEILVQKE WISFGHKFAS RIGHGDKNHT DADRSPIFLQ FIDCVWQMSK 450
    QFPTAFEFNE QFLIIILDHL YSCRFGTFLF NCESARERQK VTERTVSLWS 500
    LINSNKEKFK NPFYTKEINR VLYPVASMRH LELWVNYYIR WNPRIKQQQP 550
    NPVEQRYMEL LALRDEYIKR LEELQLANSA KLSDPPTSPS SPSQMMPHVQ 600
    THF 603
    Length:603
    Mass (Da):69,900
    Last modified:December 21, 2004 - v1
    Checksum:iC4A50B462190D484
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR859309 mRNA. Translation: CAH91487.1.
    RefSeqiNP_001127425.1. NM_001133953.1.
    UniGeneiPab.9382.

    Genome annotation databases

    GeneIDi100174495.
    KEGGipon:100174495.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CR859309 mRNA. Translation: CAH91487.1 .
    RefSeqi NP_001127425.1. NM_001133953.1.
    UniGenei Pab.9382.

    3D structure databases

    ProteinModelPortali Q5R9S3.
    SMRi Q5R9S3. Positions 33-544.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q5R9S3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 100174495.
    KEGGi pon:100174495.

    Organism-specific databases

    CTDi 4534.

    Phylogenomic databases

    HOGENOMi HOG000210598.
    HOVERGENi HBG000220.
    KOi K01108.

    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

    1. The German cDNA consortium
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.

    Entry informationi

    Entry nameiMTM1_PONAB
    AccessioniPrimary (citable) accession number: Q5R9S3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 8, 2008
    Last sequence update: December 21, 2004
    Last modified: October 1, 2014
    This is version 55 of the entry and version 1 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3