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Q66GT5

- PTPM1_MOUSE

UniProt

Q66GT5 - PTPM1_MOUSE

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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

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
Complete GO annotation...

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
Complete GO annotation...

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

        10         20         30         40         50
MAASAWLEAG LARVLFYPTL LYTVFRGRVR GPAHRDWYHR IDHTVLLGAL
60 70 80 90 100
PLKNMTRRLV LDENVRGVIT MNEEYETRFL CNTSKEWKKA GVEQLRLSTV
110 120 130 140 150
DMTGVPTLAN LHKGVQFALK YQALGQCVYV HCKAGRSRSA TMVAAYLIQV
160 170 180 190
HNWSPEEAIE AIAKIRSHIS IRPSQLEVLK EFHKEITARA AKN
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

« Hide 'large scale' publications
  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