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Q13615

- MTMR3_HUMAN

UniProt

Q13615 - MTMR3_HUMAN

Protein

Myotubularin-related protein 3

Gene

MTMR3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (19 Jul 2003)
      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. May also dephosphorylate proteins phosphorylated on Ser, Thr, and Tyr residues.1 Publication

    Catalytic activityi

    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei413 – 4131Phosphocysteine intermediatePROSITE-ProRule annotation
    Binding sitei459 – 4591SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1119 – 117961FYVE-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphatidylinositol-3-phosphatase activity Source: UniProtKB
    3. protein serine/threonine phosphatase activity Source: UniProtKB
    4. protein tyrosine phosphatase activity Source: UniProtKB

    GO - Biological processi

    1. peptidyl-tyrosine dephosphorylation Source: GOC
    2. phosphatidylinositol biosynthetic process Source: Reactome
    3. phosphatidylinositol dephosphorylation Source: UniProtKB
    4. phospholipid metabolic process Source: Reactome
    5. protein dephosphorylation Source: UniProtKB
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02045-MONOMER.
    ReactomeiREACT_121025. Synthesis of PIPs at the plasma membrane.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myotubularin-related protein 3 (EC:3.1.3.48)
    Alternative name(s):
    FYVE domain-containing dual specificity protein phosphatase 1
    Short name:
    FYVE-DSP1
    Zinc finger FYVE domain-containing protein 10
    Gene namesi
    Name:MTMR3
    Synonyms:KIAA0371, ZFYVE10
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:7451. MTMR3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. membrane Source: UniProtKB
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi413 – 4131C → S: Loss of activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA31254.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11981198Myotubularin-related protein 3PRO_0000094936Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei633 – 6331Phosphoserine1 Publication
    Modified residuei647 – 6471Phosphoserine2 Publications
    Modified residuei731 – 7311Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13615.
    PaxDbiQ13615.
    PRIDEiQ13615.

    PTM databases

    PhosphoSiteiQ13615.

    Expressioni

    Gene expression databases

    ArrayExpressiQ13615.
    BgeeiQ13615.
    CleanExiHS_MTMR3.
    GenevestigatoriQ13615.

    Organism-specific databases

    HPAiHPA034515.
    HPA034516.

    Interactioni

    Protein-protein interaction databases

    BioGridi114414. 3 interactions.
    IntActiQ13615. 6 interactions.
    STRINGi9606.ENSP00000384651.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13615.
    SMRiQ13615. Positions 53-577, 1125-1175.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini155 – 576422Myotubularin phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni326 – 3294Substrate bindingBy similarity
    Regioni351 – 3522Substrate bindingBy similarity
    Regioni413 – 4197Substrate bindingBy similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1029 – 106234Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 1 FYVE-type zinc finger.PROSITE-ProRule annotation
    Contains 1 myotubularin phosphatase domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1119 – 117961FYVE-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG322789.
    HOVERGENiHBG052526.
    InParanoidiQ13615.
    KOiK18082.
    OMAiTDTIQQR.
    OrthoDBiEOG7PVWNJ.
    PhylomeDBiQ13615.
    TreeFamiTF315197.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProiIPR010569. Myotubularin-like_Pase_dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR016130. Tyr_Pase_AS.
    IPR000306. Znf_FYVE.
    IPR017455. Znf_FYVE-rel.
    IPR011011. Znf_FYVE_PHD.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF01363. FYVE. 1 hit.
    PF06602. Myotub-related. 1 hit.
    [Graphical view]
    SMARTiSM00064. FYVE. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 2 hits.
    SSF57903. SSF57903. 1 hit.
    PROSITEiPS51339. PPASE_MYOTUBULARIN. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50178. ZF_FYVE. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform B (identifier: Q13615-1) [UniParc]FASTAAdd to Basket

    Also known as: FYVE-DSP1b

    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

    MDEETRHSLE CIQANQIFPR KQLIREDENL QVPFLELHGE STEFVGRAED     50
    AIIALSNYRL HIKFKESLVN VPLQLIESVE CRDIFQLHLT CKDCKVIRCQ 100
    FSTFEQCQEW LKRLNNAIRP PAKIEDLFSF AYHAWCMEVY ASEKEQHGDL 150
    CRPGEHVTSR FKNEVERMGF DMNNAWRISN INEKYKLCGS YPQELIVPAW 200
    ITDKELESVS SFRSWKRIPA VIYRHQSNGA VIARCGQPEV SWWGWRNADD 250
    EHLVQSVAKA CASDSRSSGS KLSTRNTSRD FPNGGDLSDV EFDSSLSNAS 300
    GAESLAIQPQ KLLILDARSY AAAVANRAKG GGCECPEYYP NCEVVFMGMA 350
    NIHSIRRSFQ SLRLLCTQMP DPGNWLSALE STKWLHHLSV LLKSALLVVH 400
    AVDQDQRPVL VHCSDGWDRT PQIVALAKLL LDPYYRTIEG FQVLVEMEWL 450
    DFGHKFADRC GHGENSDDLN ERCPVFLQWL DCVHQLQRQF PCSFEFNEAF 500
    LVKLVQHTYS CLFGTFLCNN AKERGEKHTQ ERTCSVWSLL RAGNKAFKNL 550
    LYSSQSEAVL YPVCHVRNLM LWSAVYLPCP SPTTPVDDSC APYPAPGTSP 600
    DDPPLSRLPK TRSYDNLTTA CDNTVPLASR RCSDPSLNEK WQEHRRSLEL 650
    SSLAGPGEDP LSADSLGKPT RVPGGAELSV AAGVAEGQME NILQEATKEE 700
    SGVEEPAHRA GIEIQEGKED PLLEKESRRK TPEASAIGLH QDPELGDAAL 750
    RSHLDMSWPL FSQGISEQQS GLSVLLSSLQ VPPRGEDSLE VPVEQFRIEE 800
    IAEGREEAVL PIPVDAKVGY GTSQSCSLLP SQVPFETRGP NVDSSTDMLV 850
    EDKVKSVSGP QGHHRSCLVN SGKDRLPQTM EPSPSETSLV ERPQVGSVVH 900
    RTSLGSTLSL TRSPCALPLA ECKEGLVCNG APETENRASE QPPGLSTLQM 950
    YPTPNGHCAN GEAGRSKDSL SRQLSAMSCS SAHLHSRNLH HKWLHSHSGR 1000
    PSATSSPDQP SRSHLDDDGM SVYTDTIQQR LRQIESGHQQ EVETLKKQVQ 1050
    ELKSRLESQY LTSSLHFNGD FGDEVTSIPD SESNLDQNCL SRCSTEIFSE 1100
    ASWEQVDKQD TEMTRWLPDH LAAHCYACDS AFWLASRKHH CRNCGNVFCS 1150
    SCCNQKVPVP SQQLFEPSRV CKSCYSSLHP TSSSIDLELD KPIAATSN 1198
    Length:1,198
    Mass (Da):133,619
    Last modified:July 19, 2003 - v3
    Checksum:iFE6F4B165074D5F8
    GO
    Isoform A (identifier: Q13615-2) [UniParc]FASTAAdd to Basket

    Also known as: FYVE-DSP1a

    The sequence of this isoform differs from the canonical sequence as follows:
         1076-1112: Missing.
         1142-1142: R → RDTDRVDQTW

    Show »
    Length:1,170
    Mass (Da):130,561
    Checksum:iB51B10E3E7245433
    GO
    Isoform C (identifier: Q13615-3) [UniParc]FASTAAdd to Basket

    Also known as: FYVE-DSP1c

    The sequence of this isoform differs from the canonical sequence as follows:
         1076-1112: Missing.

    Show »
    Length:1,161
    Mass (Da):129,444
    Checksum:i18C795D42EFB1177
    GO

    Sequence cautioni

    The sequence BAA20826.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti560 – 57819LYPVC…AVYLP → CILQPFHCGQQKEFGVGYI(PubMed:9736772)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti221 – 2211V → L in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035656

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1076 – 111237Missing in isoform A and isoform C. 1 PublicationVSP_007781Add
    BLAST
    Alternative sequencei1142 – 11421R → RDTDRVDQTW in isoform A. CuratedVSP_007782

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF233436 mRNA. Translation: AAF40203.2.
    AF233437 mRNA. Translation: AAF40204.1.
    AF233438 mRNA. Translation: AAF40205.1.
    AB002369 mRNA. Translation: BAA20826.2. Different initiation.
    CR456525 mRNA. Translation: CAG30411.1.
    CH471095 Genomic DNA. Translation: EAW59852.1.
    CH471095 Genomic DNA. Translation: EAW59855.1.
    BC142713 mRNA. Translation: AAI42714.1.
    BC148216 mRNA. Translation: AAI48217.1.
    BC152455 mRNA. Translation: AAI52456.1.
    AC003071 Genomic DNA. Translation: AAB83949.1.
    U58034 Genomic DNA. Translation: AAC79119.1.
    CCDSiCCDS13870.1. [Q13615-1]
    CCDS13871.1. [Q13615-2]
    CCDS46682.1. [Q13615-3]
    RefSeqiNP_066576.1. NM_021090.3. [Q13615-1]
    NP_694690.1. NM_153050.2. [Q13615-2]
    NP_694691.1. NM_153051.2. [Q13615-3]
    UniGeneiHs.474536.

    Genome annotation databases

    EnsembliENST00000333027; ENSP00000331649; ENSG00000100330. [Q13615-2]
    ENST00000351488; ENSP00000307271; ENSG00000100330. [Q13615-3]
    ENST00000401950; ENSP00000384651; ENSG00000100330. [Q13615-1]
    ENST00000406629; ENSP00000384077; ENSG00000100330. [Q13615-2]
    GeneIDi8897.
    KEGGihsa:8897.
    UCSCiuc003agu.4. human. [Q13615-2]
    uc003agv.4. human. [Q13615-1]
    uc003agw.4. human. [Q13615-3]

    Polymorphism databases

    DMDMi33112668.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF233436 mRNA. Translation: AAF40203.2 .
    AF233437 mRNA. Translation: AAF40204.1 .
    AF233438 mRNA. Translation: AAF40205.1 .
    AB002369 mRNA. Translation: BAA20826.2 . Different initiation.
    CR456525 mRNA. Translation: CAG30411.1 .
    CH471095 Genomic DNA. Translation: EAW59852.1 .
    CH471095 Genomic DNA. Translation: EAW59855.1 .
    BC142713 mRNA. Translation: AAI42714.1 .
    BC148216 mRNA. Translation: AAI48217.1 .
    BC152455 mRNA. Translation: AAI52456.1 .
    AC003071 Genomic DNA. Translation: AAB83949.1 .
    U58034 Genomic DNA. Translation: AAC79119.1 .
    CCDSi CCDS13870.1. [Q13615-1 ]
    CCDS13871.1. [Q13615-2 ]
    CCDS46682.1. [Q13615-3 ]
    RefSeqi NP_066576.1. NM_021090.3. [Q13615-1 ]
    NP_694690.1. NM_153050.2. [Q13615-2 ]
    NP_694691.1. NM_153051.2. [Q13615-3 ]
    UniGenei Hs.474536.

    3D structure databases

    ProteinModelPortali Q13615.
    SMRi Q13615. Positions 53-577, 1125-1175.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114414. 3 interactions.
    IntActi Q13615. 6 interactions.
    STRINGi 9606.ENSP00000384651.

    PTM databases

    PhosphoSitei Q13615.

    Polymorphism databases

    DMDMi 33112668.

    Proteomic databases

    MaxQBi Q13615.
    PaxDbi Q13615.
    PRIDEi Q13615.

    Protocols and materials databases

    DNASUi 8897.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000333027 ; ENSP00000331649 ; ENSG00000100330 . [Q13615-2 ]
    ENST00000351488 ; ENSP00000307271 ; ENSG00000100330 . [Q13615-3 ]
    ENST00000401950 ; ENSP00000384651 ; ENSG00000100330 . [Q13615-1 ]
    ENST00000406629 ; ENSP00000384077 ; ENSG00000100330 . [Q13615-2 ]
    GeneIDi 8897.
    KEGGi hsa:8897.
    UCSCi uc003agu.4. human. [Q13615-2 ]
    uc003agv.4. human. [Q13615-1 ]
    uc003agw.4. human. [Q13615-3 ]

    Organism-specific databases

    CTDi 8897.
    GeneCardsi GC22P030279.
    HGNCi HGNC:7451. MTMR3.
    HPAi HPA034515.
    HPA034516.
    MIMi 603558. gene.
    neXtProti NX_Q13615.
    PharmGKBi PA31254.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG322789.
    HOVERGENi HBG052526.
    InParanoidi Q13615.
    KOi K18082.
    OMAi TDTIQQR.
    OrthoDBi EOG7PVWNJ.
    PhylomeDBi Q13615.
    TreeFami TF315197.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS02045-MONOMER.
    Reactomei REACT_121025. Synthesis of PIPs at the plasma membrane.

    Miscellaneous databases

    ChiTaRSi MTMR3. human.
    GeneWikii MTMR3.
    GenomeRNAii 8897.
    NextBioi 33415.
    PROi Q13615.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13615.
    Bgeei Q13615.
    CleanExi HS_MTMR3.
    Genevestigatori Q13615.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    3.90.190.10. 1 hit.
    InterProi IPR010569. Myotubularin-like_Pase_dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR016130. Tyr_Pase_AS.
    IPR000306. Znf_FYVE.
    IPR017455. Znf_FYVE-rel.
    IPR011011. Znf_FYVE_PHD.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF01363. FYVE. 1 hit.
    PF06602. Myotub-related. 1 hit.
    [Graphical view ]
    SMARTi SM00064. FYVE. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 2 hits.
    SSF57903. SSF57903. 1 hit.
    PROSITEi PS51339. PPASE_MYOTUBULARIN. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50178. ZF_FYVE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "FYVE-DSP1, a dual-specificity protein phosphatase containing an FYVE domain."
      Zhao R., Qi Y., Zhao Z.J.
      Biochem. Biophys. Res. Commun. 270:222-229(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS A; B AND C), CHARACTERIZATION.
    2. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
    4. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS B AND C).
    7. "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 OF 374-578.
    8. "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 [GENOMIC DNA] OF 381-463.
    9. "Characterization of MTMR3. an inositol lipid 3-phosphatase with novel substrate specificity."
      Walker D.M., Urbe S., Dove S.K., Tenza D., Raposo G., Clague M.J.
      Curr. Biol. 11:1600-1605(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-413.
    10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-647, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-633; SER-647 AND THR-731, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-221.

    Entry informationi

    Entry nameiMTMR3_HUMAN
    AccessioniPrimary (citable) accession number: Q13615
    Secondary accession number(s): A5PL26
    , A7MD32, Q9NYN5, Q9NYN6, Q9UDX6, Q9UEG3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 19, 2003
    Last modified: October 1, 2014
    This is version 138 of the entry and version 3 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 22
      Human chromosome 22: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3