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Q13613

- MTMR1_HUMAN

UniProt

Q13613 - MTMR1_HUMAN

Protein

Myotubularin-related protein 1

Gene

MTMR1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 4 (19 Jul 2003)
      Previous versions | rss
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    Functioni

    Lipid phosphatase that acts on phosphatidylinositol 3-phosphate and phosphatidylinositol (3,5)-bisphosphate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei438 – 4381Phosphocysteine intermediatePROSITE-ProRule annotation
    Binding sitei484 – 4841SubstrateBy similarity

    GO - Molecular functioni

    1. phosphatidylinositol-3-phosphatase activity Source: UniProtKB
    2. protein tyrosine phosphatase activity Source: InterPro

    GO - Biological processi

    1. phosphatidylinositol biosynthetic process Source: Reactome
    2. phospholipid metabolic process Source: Reactome
    3. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myotubularin-related protein 1 (EC:3.1.3.-)
    Gene namesi
    Name:MTMR1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:7449. MTMR1.

    Subcellular locationi

    Cell membrane 1 Publication; Peripheral membrane protein 1 Publication; Cytoplasmic side 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA31252.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 665665Myotubularin-related protein 1PRO_0000094932Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ13613.
    PaxDbiQ13613.
    PRIDEiQ13613.

    PTM databases

    PhosphoSiteiQ13613.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13613.
    BgeeiQ13613.
    CleanExiHS_MTMR1.
    GenevestigatoriQ13613.

    Organism-specific databases

    HPAiHPA018502.

    Interactioni

    Subunit structurei

    Interacts with MTMR12.1 Publication

    Protein-protein interaction databases

    BioGridi114306. 2 interactions.
    STRINGi9606.ENSP00000359417.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13613.
    SMRiQ13613. Positions 95-606.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini90 – 16172GRAMAdd
    BLAST
    Domaini226 – 601376Myotubularin phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni351 – 3544Substrate bindingBy similarity
    Regioni376 – 3772Substrate bindingBy similarity
    Regioni438 – 4447Substrate bindingBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi5 – 106Poly-Ala
    Compositional biasi14 – 174Poly-Gly
    Compositional biasi645 – 6484Poly-Ser

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG322789.
    HOGENOMiHOG000210598.
    HOVERGENiHBG000220.
    InParanoidiQ13613.
    KOiK18081.
    PhylomeDBiQ13613.
    TreeFamiTF315197.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13613-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDRPAAAAAA GCEGGGGPNP GPAGGRRPPR AAGGATAGSR QPSVETLDSP    50
    TGSHVEWCKQ LIAATISSQI SGSVTSENVS RDYKALRDGN KLAQMEEAPL 100
    FPGESIKAIV KDVMYICPFM GAVSGTLTVT DFKLYFKNVE RDPHFILDVP 150
    LGVISRVEKI GAQSHGDNSC GIEIVCKDMR NLRLAYKQEE QSKLGIFENL 200
    NKHAFPLSNG QALFAFSYKE KFPINGWKVY DPVSEYKRQG LPNESWKISK 250
    INSNYEFCDT YPAIIVVPTS VKDDDLSKVA AFRAKGRVPV LSWIHPESQA 300
    TITRCSQPLV GPNDKRCKED EKYLQTIMDA NAQSHKLIIF DARQNSVADT 350
    NKTKGGGYES ESAYPNAELV FLEIHNIHVM RESLRKLKEI VYPSIDEARW 400
    LSNVDGTHWL EYIRMLLAGA VRIADKIESG KTSVVVHCSD GWDRTAQLTS 450
    LAMLMLDSYY RTIKGFETLV EKEWISFGHR FALRVGHGND NHADADRSPI 500
    FLQFVDCVWQ MTRQFPSAFE FNELFLITIL DHLYSCLFGT FLCNCEQQRF 550
    KEDVYTKTIS LWSYINSQLD EFSNPFFVNY ENHVLYPVAS LSHLELWVNY 600
    YVRWNPRMRP QMPIHQNLKE LLAVRAELQK RVEGLQREVA TRAVSSSSER 650
    GSSPSHSATS VHTSV 665
    Length:665
    Mass (Da):74,678
    Last modified:July 19, 2003 - v4
    Checksum:i12E766859F0DCA75
    GO
    Isoform 1A (identifier: Q13613-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         553-568: DVYTKTISLWSYINSQ → AWGAGTQRARGSLRSR
         569-665: Missing.

    Show »
    Length:568
    Mass (Da):63,330
    Checksum:iEA1F7406012707B6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti541 – 5411F → L in CAA12271. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei553 – 56816DVYTK…YINSQ → AWGAGTQRARGSLRSR in isoform 1A. CuratedVSP_005169Add
    BLAST
    Alternative sequencei569 – 66597Missing in isoform 1A. CuratedVSP_005170Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF002223 Genomic DNA. No translation available.
    AJ224979 mRNA. Translation: CAA12271.1.
    AF057354 mRNA. Translation: AAD40368.1.
    U58032 mRNA. Translation: AAC79117.1.
    CCDSiCCDS14695.1. [Q13613-1]
    RefSeqiNP_003819.1. NM_003828.2. [Q13613-1]
    XP_006724918.1. XM_006724855.1. [Q13613-1]
    UniGeneiHs.347187.

    Genome annotation databases

    EnsembliENST00000370390; ENSP00000359417; ENSG00000063601. [Q13613-1]
    ENST00000485376; ENSP00000434105; ENSG00000063601. [Q13613-2]
    GeneIDi8776.
    KEGGihsa:8776.
    UCSCiuc004fei.3. human. [Q13613-1]

    Polymorphism databases

    DMDMi33112667.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF002223 Genomic DNA. No translation available.
    AJ224979 mRNA. Translation: CAA12271.1 .
    AF057354 mRNA. Translation: AAD40368.1 .
    U58032 mRNA. Translation: AAC79117.1 .
    CCDSi CCDS14695.1. [Q13613-1 ]
    RefSeqi NP_003819.1. NM_003828.2. [Q13613-1 ]
    XP_006724918.1. XM_006724855.1. [Q13613-1 ]
    UniGenei Hs.347187.

    3D structure databases

    ProteinModelPortali Q13613.
    SMRi Q13613. Positions 95-606.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114306. 2 interactions.
    STRINGi 9606.ENSP00000359417.

    PTM databases

    PhosphoSitei Q13613.

    Polymorphism databases

    DMDMi 33112667.

    Proteomic databases

    MaxQBi Q13613.
    PaxDbi Q13613.
    PRIDEi Q13613.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370390 ; ENSP00000359417 ; ENSG00000063601 . [Q13613-1 ]
    ENST00000485376 ; ENSP00000434105 ; ENSG00000063601 . [Q13613-2 ]
    GeneIDi 8776.
    KEGGi hsa:8776.
    UCSCi uc004fei.3. human. [Q13613-1 ]

    Organism-specific databases

    CTDi 8776.
    GeneCardsi GC0XP149861.
    H-InvDB HIX0017110.
    HGNCi HGNC:7449. MTMR1.
    HPAi HPA018502.
    MIMi 300171. gene.
    neXtProti NX_Q13613.
    PharmGKBi PA31252.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG322789.
    HOGENOMi HOG000210598.
    HOVERGENi HBG000220.
    InParanoidi Q13613.
    KOi K18081.
    PhylomeDBi Q13613.
    TreeFami TF315197.

    Enzyme and pathway databases

    Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.

    Miscellaneous databases

    GeneWikii MTMR1.
    GenomeRNAii 8776.
    NextBioi 32908.
    PROi Q13613.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13613.
    Bgeei Q13613.
    CleanExi HS_MTMR1.
    Genevestigatori Q13613.

    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. "Genomic organization of a 225-kb region in Xq28 containing the gene for X-linked myotubular myopathy (MTM1) and a related gene (MTMR1)."
      Kioschis P., Wiemann S., Heiss N.S., Francis F., Goetz C., Poustka A., Taudien S., Platzer M., Wiehe T., Beckmann G., Weber J., Nordsiek G., Rosenthal A.
      Genomics 54:256-266(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    2. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Ancient genomic duplication within the myotubular myopathy locus (MTM1) in human Xq28."
      Kioschis P., Wiemann S., Francis F., Goetz C., Poustka A., Taudien S., Platzer M., Wiehe T., Beckmann G., Weber J., Nordsiek G., Rosenthal A.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-665.
      Tissue: Brain.
    4. "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] OF 114-610.
    5. "A gene mutated in X-linked myotubular myopathy defines a new putative tyrosine phosphatase family conserved in yeast."
      Laporte J., Hu L.-J., Kretz C., Mandel J.-L., Kioschis P., Coy J., Klauck S.M., Poutska A., Dahl N.
      Nat. Genet. 13:175-182(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 404-535.
    6. "Identification of myotubularin as the lipid phosphatase catalytic subunit associated with the 3-phosphatase adapter protein, 3-PAP."
      Nandurkar H.H., Layton M., Laporte J., Selan C., Corcoran L., Caldwell K.K., Mochizuki Y., Majerus P.W., Mitchell C.A.
      Proc. Natl. Acad. Sci. U.S.A. 100:8660-8665(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MTMR12.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMTMR1_HUMAN
    AccessioniPrimary (citable) accession number: Q13613
    Secondary accession number(s): Q9UBX6, Q9UEM0, Q9UQD5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 19, 2003
    Last modified: October 1, 2014
    This is version 125 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3