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Q13614

- MTMR2_HUMAN

UniProt

Q13614 - MTMR2_HUMAN

Protein

Myotubularin-related protein 2

Gene

MTMR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 4 (04 Nov 2008)
      Previous versions | rss
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    Functioni

    Phosphatase that acts on lipids with a phosphoinositol headgroup. Has phosphatase activity towards phosphatidylinositol 3-phosphate and phosphatidylinositol 3,5-bisphosphate.2 Publications

    Enzyme regulationi

    interaction with SBF1 increases phosphatase activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei417 – 4171Phosphocysteine intermediate
    Binding sitei463 – 4631Substrate

    GO - Molecular functioni

    1. phosphatidylinositol phosphate phosphatase activity Source: Ensembl
    2. protein binding Source: UniProtKB
    3. protein tyrosine/serine/threonine phosphatase activity Source: UniProtKB
    4. protein tyrosine phosphatase activity Source: InterPro

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. dendritic spine maintenance Source: BHF-UCL
    3. inositol phosphate dephosphorylation Source: Ensembl
    4. myelin assembly Source: Ensembl
    5. negative regulation of endocytosis Source: BHF-UCL
    6. negative regulation of excitatory postsynaptic membrane potential Source: BHF-UCL
    7. negative regulation of myelination Source: Ensembl
    8. negative regulation of receptor catabolic process Source: BHF-UCL
    9. negative regulation of receptor internalization Source: BHF-UCL
    10. neuron development Source: Ensembl
    11. phosphatidylinositol biosynthetic process Source: Reactome
    12. phosphatidylinositol dephosphorylation Source: Ensembl
    13. phospholipid metabolic process Source: Reactome
    14. positive regulation of early endosome to late endosome transport Source: BHF-UCL
    15. protein dephosphorylation Source: UniProtKB
    16. protein tetramerization Source: Ensembl
    17. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BRENDAi3.1.3.64. 2681.
    ReactomeiREACT_120756. Synthesis of PIPs at the early endosome membrane.
    REACT_120918. Synthesis of PIPs at the late endosome membrane.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myotubularin-related protein 2 (EC:3.1.3.-)
    Gene namesi
    Name:MTMR2
    Synonyms:KIAA1073
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:7450. MTMR2.

    Subcellular locationi

    Cytoplasm. Early endosome membrane; Peripheral membrane protein
    Note: Partly associated with membranes.

    GO - Cellular componenti

    1. axon Source: BHF-UCL
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: BHF-UCL
    4. dendrite Source: BHF-UCL
    5. dendritic spine Source: BHF-UCL
    6. early endosome membrane Source: UniProtKB-SubCell
    7. neuronal postsynaptic density Source: BHF-UCL
    8. nucleus Source: UniProtKB
    9. synaptic membrane Source: BHF-UCL
    10. synaptic vesicle Source: BHF-UCL
    11. vacuolar membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Charcot-Marie-Tooth disease 4B1 (CMT4B1) [MIM:601382]: A recessive demyelinating form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Demyelinating neuropathies are characterized by severely reduced nerve conduction velocities (less than 38 m/sec), segmental demyelination and remyelination with onion bulb formations on nerve biopsy, slowly progressive distal muscle atrophy and weakness, absent deep tendon reflexes, and hollow feet. By convention autosomal recessive forms of demyelinating Charcot-Marie-Tooth disease are designated CMT4.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti283 – 2831R → W in CMT4B1. 1 Publication
    VAR_047947

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi417 – 4171C → S: Loss of activity. 2 Publications
    Mutagenesisi419 – 4191D → A: No effect. 1 Publication
    Mutagenesisi422 – 4221D → A: Loss of activity. 1 Publication
    Mutagenesisi607 – 6071L → Y: Reduces homodimerization and interaction with SBF1. 1 Publication

    Keywords - Diseasei

    Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

    Organism-specific databases

    MIMi601382. phenotype.
    Orphaneti99955. Charcot-Marie-Tooth disease type 4B1.
    PharmGKBiPA31253.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 643643Myotubularin-related protein 2PRO_0000094934Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei6 – 61PhosphoserineBy similarity
    Modified residuei58 – 581Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylation at Ser-58 decreases MTMR2 localization to endocytic vesicular structures.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13614.
    PaxDbiQ13614.
    PRIDEiQ13614.

    PTM databases

    PhosphoSiteiQ13614.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13614.
    BgeeiQ13614.
    CleanExiHS_MTMR2.
    GenevestigatoriQ13614.

    Organism-specific databases

    HPAiHPA049831.

    Interactioni

    Subunit structurei

    Homooligomer and heterooligomer. Interacts with SBF1 and SBF2.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NEFLP071962EBI-475631,EBI-475646

    Protein-protein interaction databases

    BioGridi114415. 13 interactions.
    IntActiQ13614. 5 interactions.
    MINTiMINT-6774021.
    STRINGi9606.ENSP00000345752.

    Structurei

    Secondary structure

    1
    643
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi84 – 9512
    Turni96 – 983
    Beta strandi99 – 12123
    Beta strandi123 – 1286
    Helixi129 – 1313
    Beta strandi132 – 1387
    Beta strandi145 – 1473
    Beta strandi149 – 1557
    Turni156 – 1583
    Beta strandi159 – 1646
    Helixi167 – 1693
    Helixi172 – 18211
    Turni185 – 1895
    Helixi193 – 1953
    Helixi205 – 2073
    Helixi211 – 2177
    Beta strandi223 – 2286
    Turni230 – 2334
    Beta strandi234 – 2363
    Beta strandi242 – 2476
    Helixi252 – 26110
    Helixi263 – 2653
    Beta strandi269 – 2735
    Turni275 – 2773
    Beta strandi280 – 2845
    Turni290 – 2934
    Helixi297 – 30913
    Beta strandi310 – 3123
    Beta strandi314 – 3207
    Helixi324 – 33310
    Turni340 – 3423
    Beta strandi346 – 3505
    Helixi356 – 37015
    Helixi376 – 3783
    Helixi379 – 3868
    Helixi388 – 40720
    Beta strandi413 – 4164
    Beta strandi418 – 4225
    Helixi423 – 43513
    Helixi437 – 4404
    Helixi442 – 45211
    Turni453 – 4575
    Helixi460 – 4645
    Turni465 – 4673
    Helixi479 – 49315
    Turni495 – 4973
    Helixi502 – 51413
    Beta strandi516 – 5183
    Beta strandi522 – 5243
    Helixi525 – 5306
    Helixi533 – 5364
    Helixi540 – 5456
    Helixi548 – 5514
    Turni554 – 5574
    Beta strandi560 – 5623
    Turni570 – 5723
    Helixi577 – 5804

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LW3X-ray2.30A1-643[»]
    1M7RX-ray2.60A/B1-643[»]
    1ZSQX-ray1.82A73-586[»]
    1ZVRX-ray1.98A73-586[»]
    ProteinModelPortaliQ13614.
    SMRiQ13614. Positions 73-585.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13614.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini68 – 13972GRAMAdd
    BLAST
    Domaini205 – 580376Myotubularin phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni330 – 3334Substrate binding
    Regioni355 – 3562Substrate binding
    Regioni417 – 4237Substrate binding

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili593 – 627351 PublicationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi4 – 5350Ser-richAdd
    BLAST

    Domaini

    The coiled-coil domain mediates interaction with SBF2.

    Sequence similaritiesi

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

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG322789.
    HOGENOMiHOG000210598.
    HOVERGENiHBG000220.
    InParanoidiQ13614.
    KOiK18081.
    OMAiPENGWKV.
    OrthoDBiEOG7XDBF9.
    PhylomeDBiQ13614.
    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: Q13614-1) [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

    MEKSSSCESL GSQPAAARPP SVDSLSSAST SHSENSVHTK SASVVSSDSI    50
    STSADNFSPD LRVLRESNKL AEMEEPPLLP GENIKDMAKD VTYICPFTGA 100
    VRGTLTVTNY RLYFKSMERD PPFVLDASLG VINRVEKIGG ASSRGENSYG 150
    LETVCKDIRN LRFAHKPEGR TRRSIFENLM KYAFPVSNNL PLFAFEYKEV 200
    FPENGWKLYD PLLEYRRQGI PNESWRITKI NERYELCDTY PALLVVPANI 250
    PDEELKRVAS FRSRGRIPVL SWIHPESQAT ITRCSQPMVG VSGKRSKEDE 300
    KYLQAIMDSN AQSHKIFIFD ARPSVNAVAN KAKGGGYESE DAYQNAELVF 350
    LDIHNIHVMR ESLRKLKEIV YPNIEETHWL SNLESTHWLE HIKLILAGAL 400
    RIADKVESGK TSVVVHCSDG WDRTAQLTSL AMLMLDGYYR TIRGFEVLVE 450
    KEWLSFGHRF QLRVGHGDKN HADADRSPVF LQFIDCVWQM TRQFPTAFEF 500
    NEYFLITILD HLYSCLFGTF LCNSEQQRGK ENLPKRTVSL WSYINSQLED 550
    FTNPLYGSYS NHVLYPVASM RHLELWVGYY IRWNPRMKPQ EPIHNRYKEL 600
    LAKRAELQKK VEELQREISN RSTSSSERAS SPAQCVTPVQ TVV 643
    Length:643
    Mass (Da):73,381
    Last modified:November 4, 2008 - v4
    Checksum:i10FD6508D0CDA719
    GO
    Isoform 2 (identifier: Q13614-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-72: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:571
    Mass (Da):65,959
    Checksum:iDBC304269CEFC843
    GO

    Sequence cautioni

    The sequence BAA83025.2 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti3 – 31K → T.2 Publications
    Corresponds to variant rs3824874 [ dbSNP | Ensembl ].
    VAR_047255
    Natural varianti283 – 2831R → W in CMT4B1. 1 Publication
    VAR_047947
    Natural varianti545 – 5451N → S.
    Corresponds to variant rs558018 [ dbSNP | Ensembl ].
    VAR_047256

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7272Missing in isoform 2. 1 PublicationVSP_044933Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB028996 mRNA. Translation: BAA83025.2. Different initiation.
    AK302940 mRNA. Translation: BAG64098.1.
    AP000870 Genomic DNA. No translation available.
    AP001877 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW66971.1.
    BC052990 mRNA. Translation: AAH52990.1.
    U58033 mRNA. Translation: AAC79118.1.
    CCDSiCCDS8305.1. [Q13614-1]
    CCDS8306.1. [Q13614-2]
    PIRiT09497.
    RefSeqiNP_001230500.1. NM_001243571.1. [Q13614-2]
    NP_057240.3. NM_016156.5. [Q13614-1]
    NP_958435.1. NM_201278.2. [Q13614-2]
    NP_958438.1. NM_201281.2. [Q13614-2]
    XP_005274431.1. XM_005274374.1. [Q13614-2]
    XP_005274432.1. XM_005274375.1. [Q13614-2]
    XP_006718997.1. XM_006718934.1. [Q13614-2]
    XP_006718998.1. XM_006718935.1. [Q13614-2]
    XP_006718999.1. XM_006718936.1. [Q13614-2]
    UniGeneiHs.181326.

    Genome annotation databases

    EnsembliENST00000346299; ENSP00000345752; ENSG00000087053. [Q13614-1]
    ENST00000352297; ENSP00000343737; ENSG00000087053. [Q13614-2]
    ENST00000393223; ENSP00000376915; ENSG00000087053. [Q13614-2]
    ENST00000409459; ENSP00000386882; ENSG00000087053. [Q13614-2]
    GeneIDi8898.
    KEGGihsa:8898.
    UCSCiuc001pfs.3. human. [Q13614-1]

    Polymorphism databases

    DMDMi212276520.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Inherited peripheral neuropathies mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB028996 mRNA. Translation: BAA83025.2 . Different initiation.
    AK302940 mRNA. Translation: BAG64098.1 .
    AP000870 Genomic DNA. No translation available.
    AP001877 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW66971.1 .
    BC052990 mRNA. Translation: AAH52990.1 .
    U58033 mRNA. Translation: AAC79118.1 .
    CCDSi CCDS8305.1. [Q13614-1 ]
    CCDS8306.1. [Q13614-2 ]
    PIRi T09497.
    RefSeqi NP_001230500.1. NM_001243571.1. [Q13614-2 ]
    NP_057240.3. NM_016156.5. [Q13614-1 ]
    NP_958435.1. NM_201278.2. [Q13614-2 ]
    NP_958438.1. NM_201281.2. [Q13614-2 ]
    XP_005274431.1. XM_005274374.1. [Q13614-2 ]
    XP_005274432.1. XM_005274375.1. [Q13614-2 ]
    XP_006718997.1. XM_006718934.1. [Q13614-2 ]
    XP_006718998.1. XM_006718935.1. [Q13614-2 ]
    XP_006718999.1. XM_006718936.1. [Q13614-2 ]
    UniGenei Hs.181326.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LW3 X-ray 2.30 A 1-643 [» ]
    1M7R X-ray 2.60 A/B 1-643 [» ]
    1ZSQ X-ray 1.82 A 73-586 [» ]
    1ZVR X-ray 1.98 A 73-586 [» ]
    ProteinModelPortali Q13614.
    SMRi Q13614. Positions 73-585.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114415. 13 interactions.
    IntActi Q13614. 5 interactions.
    MINTi MINT-6774021.
    STRINGi 9606.ENSP00000345752.

    PTM databases

    PhosphoSitei Q13614.

    Polymorphism databases

    DMDMi 212276520.

    Proteomic databases

    MaxQBi Q13614.
    PaxDbi Q13614.
    PRIDEi Q13614.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000346299 ; ENSP00000345752 ; ENSG00000087053 . [Q13614-1 ]
    ENST00000352297 ; ENSP00000343737 ; ENSG00000087053 . [Q13614-2 ]
    ENST00000393223 ; ENSP00000376915 ; ENSG00000087053 . [Q13614-2 ]
    ENST00000409459 ; ENSP00000386882 ; ENSG00000087053 . [Q13614-2 ]
    GeneIDi 8898.
    KEGGi hsa:8898.
    UCSCi uc001pfs.3. human. [Q13614-1 ]

    Organism-specific databases

    CTDi 8898.
    GeneCardsi GC11M095566.
    GeneReviewsi MTMR2.
    HGNCi HGNC:7450. MTMR2.
    HPAi HPA049831.
    MIMi 601382. phenotype.
    603557. gene.
    neXtProti NX_Q13614.
    Orphaneti 99955. Charcot-Marie-Tooth disease type 4B1.
    PharmGKBi PA31253.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG322789.
    HOGENOMi HOG000210598.
    HOVERGENi HBG000220.
    InParanoidi Q13614.
    KOi K18081.
    OMAi PENGWKV.
    OrthoDBi EOG7XDBF9.
    PhylomeDBi Q13614.
    TreeFami TF315197.

    Enzyme and pathway databases

    BRENDAi 3.1.3.64. 2681.
    Reactomei REACT_120756. Synthesis of PIPs at the early endosome membrane.
    REACT_120918. Synthesis of PIPs at the late endosome membrane.

    Miscellaneous databases

    ChiTaRSi MTMR2. human.
    EvolutionaryTracei Q13614.
    GeneWikii MTMR2.
    GenomeRNAii 8898.
    NextBioi 33423.
    PROi Q13614.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13614.
    Bgeei Q13614.
    CleanExi HS_MTMR2.
    Genevestigatori Q13614.

    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. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT THR-3.
      Tissue: Brain.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1), VARIANT THR-3.
      Tissue: Uterus.
    6. "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 384-643 (ISOFORM 1).
    7. "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 384-514 (ISOFORM 1).
    8. Cited for: INVOLVEMENT IN CMT4B1.
    9. "Regulation of myotubularin-related (MTMR)2 phosphatidylinositol phosphatase by MTMR5, a catalytically inactive phosphatase."
      Kim S.-A., Vacratsis P.O., Firestein R., Cleary M.L., Dixon J.E.
      Proc. Natl. Acad. Sci. U.S.A. 100:4492-4497(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-607, INTERACTION WITH SBF1.
    10. "The phosphoinositide-3-phosphatase MTMR2 associates with MTMR13, a membrane-associated pseudophosphatase also mutated in type 4B Charcot-Marie-Tooth disease."
      Robinson F.L., Dixon J.E.
      J. Biol. Chem. 280:31699-31707(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SBF2, SUBUNIT, SUBCELLULAR LOCATION.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Endosomal targeting of the phosphoinositide 3-phosphatase MTMR2 is regulated by an N-terminal phosphorylation site."
      Franklin N.E., Taylor G.S., Vacratsis P.O.
      J. Biol. Chem. 286:15841-15853(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-58.
    16. "Crystal structure of a phosphoinositide phosphatase, MTMR2: insights into myotubular myopathy and Charcot-Marie-Tooth syndrome."
      Begley M.J., Taylor G.S., Kim S.-A., Veine D.M., Dixon J.E., Stuckey J.A.
      Mol. Cell 12:1391-1402(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT SER-417 IN COMPLEX WITH PHOSPHOINOSITIDE, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF CYS-417; ASP-419 AND ASP-422.
    17. "Molecular basis for substrate recognition by MTMR2, a myotubularin family phosphoinositide phosphatase."
      Begley M.J., Taylor G.S., Brock M.A., Ghosh P., Woods V.L., Dixon J.E.
      Proc. Natl. Acad. Sci. U.S.A. 103:927-932(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 71-586 OF MUTANT SER-417 IN COMPLEX WITH PHOSPHOINOSITIDES, COILED-COIL DOMAIN, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF CYS-417.
    18. "A novel homozygous missense mutation in the myotubularin-related protein 2 gene associated with recessive Charcot-Marie-Tooth disease with irregularly folded myelin sheaths."
      Nelis E., Erdem S., Tan E., Loefgren A., Ceuterick C., De Jonghe P., Van Broeckhoven C., Timmerman V., Topaloglu H.
      Neuromuscul. Disord. 12:869-873(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMT4B1 TRP-283.

    Entry informationi

    Entry nameiMTMR2_HUMAN
    AccessioniPrimary (citable) accession number: Q13614
    Secondary accession number(s): A6NN98, Q9UPS9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 4, 2008
    Last modified: October 1, 2014
    This is version 151 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3