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Q66GT5

- PTPM1_MOUSE

UniProt

Q66GT5 - PTPM1_MOUSE

Protein

Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1

Gene

Ptpmt1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (11 Oct 2004)
      Previous versions | rss
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    Functioni

    Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). PGP is an essential intermediate in the biosynthetic pathway of cardiolipin, a mitochondrial-specific phospholipid regulating the membrane integrity and activities of the organelle. Has also been shown to display phosphatase activity toward phosphoprotein substrates, specifically mediates dephosphorylation of mitochondrial proteins, thereby playing an essential role in ATP production. Has probably a preference for proteins phosphorylated on Ser and/or Thr residues compared to proteins phosphorylated on Tyr residues. Probably involved in regulation of insulin secretion in pancreatic beta cells By similarity.By similarity

    Catalytic activityi

    Phosphatidylglycerophosphate + H2O = phosphatidylglycerol + phosphate.
    Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation
    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei132 – 1321Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. phosphatidylglycerophosphatase activity Source: UniProtKB
    2. phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity Source: MGI
    3. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
    4. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cardiolipin biosynthetic process Source: UniProtKB
    2. inositol phosphate dephosphorylation Source: RefGenome
    3. phosphatidylinositol metabolic process Source: MGI
    4. protein dephosphorylation Source: RefGenome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Lipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism

    Enzyme and pathway databases

    ReactomeiREACT_199032. Synthesis of PG.
    UniPathwayiUPA00084; UER00504.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1 (EC:3.1.3.27)
    Alternative name(s):
    PTEN-like phosphatase
    Phosphoinositide lipid phosphatase
    Protein-tyrosine phosphatase mitochondrial 1 (EC:3.1.3.16, EC:3.1.3.48)
    Gene namesi
    Name:Ptpmt1
    Synonyms:Plip
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1913711. Ptpmt1.

    Subcellular locationi

    Mitochondrion inner membrane 1 Publication
    Note: Associated with the inner membrane.

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: MGI
    2. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice die prior to E8.5.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi73 – 731E → A: Fails to dephosphorylate PGP in vitro. 1 Publication
    Mutagenesisi76 – 761E → A: Fails to dephosphorylate PGP in vitro. 1 Publication
    Mutagenesisi101 – 1011D → A: Fails to dephosphorylate PGP in vitro. 1 Publication
    Mutagenesisi132 – 1321C → S: Does not affect level of Akt phosphorylation; Fails to dephosphorylate PGP in vitro. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3131MitochondrionSequence AnalysisAdd
    BLAST
    Chaini32 – 193162Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1PRO_0000025424Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei85 – 851N6-succinyllysine1 Publication

    Proteomic databases

    MaxQBiQ66GT5.
    PaxDbiQ66GT5.
    PRIDEiQ66GT5.

    PTM databases

    PhosphoSiteiQ66GT5.

    Expressioni

    Tissue specificityi

    Predominantly expressed in testis. Expressed at lower level in heart, brain, spleen, lung, liver, skeletal muscle, kidney, bone marrow, eye, lymph node, smooth muscle, prostate, thymus, stomach and uterus.1 Publication

    Gene expression databases

    CleanExiMM_PTPMT1.
    GenevestigatoriQ66GT5.

    Structurei

    Secondary structure

    1
    193
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi38 – 403
    Beta strandi42 – 498
    Helixi53 – 553
    Helixi56 – 627
    Beta strandi65 – 728
    Turni75 – 795
    Helixi84 – 896
    Beta strandi93 – 975
    Turni101 – 1033
    Helixi108 – 12417
    Beta strandi127 – 13711
    Helixi138 – 15114
    Helixi155 – 16511
    Helixi173 – 19018

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3RGOX-ray1.93A37-193[»]
    3RGQX-ray2.05A36-191[»]
    ProteinModelPortaliQ66GT5.
    SMRiQ66GT5. Positions 37-193.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ66GT5.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini109 – 17769Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiNOG146651.
    HOVERGENiHBG079822.
    InParanoidiQ66GT5.
    KOiK14165.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR000340. Dual-sp_phosphatase_cat-dom.
    IPR024950. DUSP.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view]
    PANTHERiPTHR10159. PTHR10159. 1 hit.
    PfamiPF00782. DSPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q66GT5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAASAWLEAG LARVLFYPTL LYTVFRGRVR GPAHRDWYHR IDHTVLLGAL    50
    PLKNMTRRLV LDENVRGVIT MNEEYETRFL CNTSKEWKKA GVEQLRLSTV 100
    DMTGVPTLAN LHKGVQFALK YQALGQCVYV HCKAGRSRSA TMVAAYLIQV 150
    HNWSPEEAIE AIAKIRSHIS IRPSQLEVLK EFHKEITARA AKN 193
    Length:193
    Mass (Da):21,943
    Last modified:October 11, 2004 - v1
    Checksum:i740D39798855D439
    GO

    Sequence cautioni

    The sequence BAB28400.1 differs from that shown. Reason: Frameshift at position 36.
    The sequence AAH26750.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAB29504.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK012674 mRNA. Translation: BAB28400.1. Frameshift.
    AK014691 mRNA. Translation: BAB29504.1. Different initiation.
    BC026750 mRNA. Translation: AAH26750.1. Different initiation.
    BK005540 mRNA. Translation: DAA05585.1.
    RefSeqiNP_079852.1. NM_025576.2.
    UniGeneiMm.23926.

    Genome annotation databases

    GeneIDi66461.
    KEGGimmu:66461.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK012674 mRNA. Translation: BAB28400.1 . Frameshift.
    AK014691 mRNA. Translation: BAB29504.1 . Different initiation.
    BC026750 mRNA. Translation: AAH26750.1 . Different initiation.
    BK005540 mRNA. Translation: DAA05585.1 .
    RefSeqi NP_079852.1. NM_025576.2.
    UniGenei Mm.23926.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3RGO X-ray 1.93 A 37-193 [» ]
    3RGQ X-ray 2.05 A 36-191 [» ]
    ProteinModelPortali Q66GT5.
    SMRi Q66GT5. Positions 37-193.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q66GT5.

    Proteomic databases

    MaxQBi Q66GT5.
    PaxDbi Q66GT5.
    PRIDEi Q66GT5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 66461.
    KEGGi mmu:66461.

    Organism-specific databases

    CTDi 114971.
    MGIi MGI:1913711. Ptpmt1.

    Phylogenomic databases

    eggNOGi NOG146651.
    HOVERGENi HBG079822.
    InParanoidi Q66GT5.
    KOi K14165.

    Enzyme and pathway databases

    UniPathwayi UPA00084 ; UER00504 .
    Reactomei REACT_199032. Synthesis of PG.

    Miscellaneous databases

    EvolutionaryTracei Q66GT5.
    NextBioi 321760.
    PROi Q66GT5.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_PTPMT1.
    Genevestigatori Q66GT5.

    Family and domain databases

    Gene3Di 3.90.190.10. 1 hit.
    InterProi IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR024950. DUSP.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    [Graphical view ]
    PANTHERi PTHR10159. PTHR10159. 1 hit.
    Pfami PF00782. DSPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Head.
    2. "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].
      Strain: FVB/N.
      Tissue: Liver.
    3. "A PTEN-like phosphatase with a novel substrate specificity."
      Pagliarini D.J., Worby C.A., Dixon J.E.
      J. Biol. Chem. 279:38590-38596(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-132.
    4. "Involvement of a mitochondrial phosphatase in the regulation of ATP production and insulin secretion in pancreatic beta cells."
      Pagliarini D.J., Wiley S.E., Kimple M.E., Dixon J.R., Kelly P., Worby C.A., Casey P.J., Dixon J.E.
      Mol. Cell 19:197-207(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS PROTEIN PHOSPHATASE, SUBCELLULAR LOCATION.
    5. Cited for: FUNCTION AS PHOSPHATIDYLGLYCEROPHOSPHATASE, DISRUPTION PHENOTYPE.
    6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    7. "Structural and functional analysis of PTPMT1, a phosphatase required for cardiolipin synthesis."
      Xiao J., Engel J.L., Zhang J., Chen M.J., Manning G., Dixon J.E.
      Proc. Natl. Acad. Sci. U.S.A. 108:11860-11865(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 37-193 IN COMPLEX WITH PHOSPHATIDYLINOSITOL 5-PHOSPHATE, MUTAGENESIS OF GLU-73; GLU-76; ASP-101 AND CYS-132.

    Entry informationi

    Entry nameiPTPM1_MOUSE
    AccessioniPrimary (citable) accession number: Q66GT5
    Secondary accession number(s): Q9CSJ8, Q9D622
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally (PubMed:15247229) thought to have phosphatidylinositol 5-phosphatase activity, however, it was later shown (PubMed:16039589) that it is probably not the case in vivo.2 Publications

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3