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Q8WUK0 (PTPM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PTPMT1
Synonyms:MOSP, PLIP
ORF Names:PNAS-129
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

Phosphatidylglycerophosphate + H2O = phosphatidylglycerol + phosphate.

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Pathway

Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2.

Subcellular location

Mitochondrion inner membrane By similarity. Note: Associated with the inner membrane By similarity.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Caution

Was originally erroneously termed DUSP23.

Sequence caution

The sequence AAH14048.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAK07545.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processLipid biosynthesis
Lipid metabolism
Phospholipid biosynthesis
Phospholipid metabolism
   Cellular componentMembrane
Mitochondrion
Mitochondrion inner membrane
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   Molecular functionHydrolase
Protein phosphatase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiolipin biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

glycerophospholipid biosynthetic process

Traceable author statement. Source: Reactome

inositol phosphate dephosphorylation

Inferred from Biological aspect of Ancestor. Source: RefGenome

phosphatidylglycerol biosynthetic process

Traceable author statement. Source: Reactome

phospholipid metabolic process

Traceable author statement. Source: Reactome

protein dephosphorylation

Inferred from Biological aspect of Ancestor. Source: RefGenome

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionphosphatidylglycerophosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphatidylinositol-4,5-bisphosphate 5-phosphatase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein tyrosine/serine/threonine phosphatase activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8WUK0-1)

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.
Isoform 2 (identifier: Q8WUK0-2)

The sequence of this isoform differs from the canonical sequence as follows:
     85-148: Missing.
Isoform 3 (identifier: Q8WUK0-3)

The sequence of this isoform differs from the canonical sequence as follows:
     59-151: LVQDENVRGV...MVAAYLIQVH → VSRAGEPGPL...PHQAWPAGCS
     152-201: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2727Mitochondrion Potential
Chain28 – 201174Phosphatidylglycerophosphatase and protein-tyrosine phosphatase 1
PRO_0000025423

Regions

Domain109 – 18375Tyrosine-protein phosphatase

Sites

Active site1321Phosphocysteine intermediate By similarity

Natural variations

Alternative sequence59 – 15193LVQDE…LIQVH → VSRAGEPGPLPRPRRSVPVG PLGSPPSLLSHLFASAAGTG RERARGDHHERGVRDEVPVQ LFTGAQMESRGGCKSHRQDP VIHPHQAWPAGCS in isoform 3.
VSP_045030
Alternative sequence85 – 14864Missing in isoform 2.
VSP_015009
Alternative sequence152 – 20150Missing in isoform 3.
VSP_045031

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 88A4CC76EEFD0835

FASTA20122,844
        10         20         30         40         50         60 
MAATALLEAG LARVLFYPTL LYTLFRGKVP GRAHRDWYHR IDPTVLLGAL PLRSLTRQLV 

        70         80         90        100        110        120 
QDENVRGVIT MNEEYETRFL CNSSQEWKRL GVEQLRLSTV DMTGIPTLDN LQKGVQFALK 

       130        140        150        160        170        180 
YQSLGQCVYV HCKAGRSRSA TMVAAYLIQV HKWSPEEAVR AIAKIRSYIH IRPGQLDVLK 

       190        200 
EFHKQITARA TKDGTFVISK T 

« Hide

Isoform 2 [UniParc].

Checksum: E1B3966F55F1065D
Show »

FASTA13715,689
Isoform 3 [UniParc].

Checksum: 59DFA3B7642E84F0
Show »

FASTA15116,459

References

[1]Lin L., Ke R., Li H., Zhou G., Shen C., Yu R., Zhong G., Xiao W., Li M., Yang S.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[2]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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 2 AND 3).
Tissue: Cervix, Kidney and Kidney adenocarcinoma.
[4]"Human acute promyelocytic leukemia cell line NB4's apoptosis/differentiation related genes."
Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W., Yang H., Zhao Z.-L.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 68-201 (ISOFORM 2).
Tissue: Promyelocytic leukemia.
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY333987 mRNA. Translation: AAP94732.1.
AC090559 Genomic DNA. No translation available.
AC104942 Genomic DNA. No translation available.
BC014048 mRNA. Translation: AAH14048.1. Different initiation.
BC020242 mRNA. Translation: AAH20242.1.
BC073798 mRNA. No translation available.
AF277187 mRNA. Translation: AAK07545.1. Different initiation.
RefSeqNP_001137456.1. NM_001143984.1.
NP_783859.1. NM_175732.2.
UniGeneHs.656205.
Hs.742231.

3D structure databases

ProteinModelPortalQ8WUK0.
SMRQ8WUK0. Positions 37-193.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125402. 5 interactions.
IntActQ8WUK0. 3 interactions.
MINTMINT-8247525.
STRING9606.ENSP00000325958.

Chemistry

ChEMBLCHEMBL2052033.

PTM databases

PhosphoSiteQ8WUK0.

Polymorphism databases

DMDM73621420.

Proteomic databases

PaxDbQ8WUK0.
PRIDEQ8WUK0.

Protocols and materials databases

DNASU114971.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326656; ENSP00000325882; ENSG00000110536. [Q8WUK0-2]
ENST00000326674; ENSP00000325958; ENSG00000110536. [Q8WUK0-1]
ENST00000426530; ENSP00000410272; ENSG00000110536. [Q8WUK0-3]
GeneID114971.
KEGGhsa:114971.
UCSCuc001nfs.4. human. [Q8WUK0-1]
uc009ylt.3. human. [Q8WUK0-2]

Organism-specific databases

CTD114971.
GeneCardsGC11P047586.
HGNCHGNC:26965. PTPMT1.
HPAHPA043932.
MIM609538. gene.
neXtProtNX_Q8WUK0.
PharmGKBPA142671115.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG146651.
HOGENOMHOG000220855.
HOVERGENHBG079822.
InParanoidQ8WUK0.
KOK14165.
OMANSSQEWK.
OrthoDBEOG7KDFCN.
PhylomeDBQ8WUK0.
TreeFamTF319745.

Enzyme and pathway databases

BioCycMetaCyc:HS03319-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00084; UER00504.

Gene expression databases

ArrayExpressQ8WUK0.
BgeeQ8WUK0.
CleanExHS_PTPMT1.
GenevestigatorQ8WUK0.

Family and domain databases

InterProIPR000340. Dual-sp_phosphatase_cat-dom.
IPR024950. DUSP.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPMT1. human.
GenomeRNAi114971.
NextBio79464.
PROQ8WUK0.
SOURCESearch...

Entry information

Entry namePTPM1_HUMAN
AccessionPrimary (citable) accession number: Q8WUK0
Secondary accession number(s): E9PAT8 expand/collapse secondary AC list , Q7Z557, Q96CR2, Q9BXV8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: March 1, 2002
Last modified: April 16, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM