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Protein

Protein phosphatase methylesterase 1

Gene

Ppme1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Demethylates proteins that have been reversibly carboxymethylated. Demethylates PPP2CB (in vitro) and PPP2CA. Binding to PPP2CA displaces the manganese ion and inactivates the enzyme (By similarity).By similarity

Catalytic activityi

[Phosphatase 2A protein]-leucine methyl ester + H2O = [phosphatase 2A protein]-leucine + methanol.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei156 – 1561By similarity
Active sitei181 – 1811By similarity
Active sitei349 – 3491By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Protein family/group databases

ESTHERimouse-PPME1. PPase_methylesterase_euk.
MEROPSiS33.984.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase methylesterase 1 (EC:3.1.1.89)
Short name:
PME-1
Gene namesi
Name:Ppme1
Synonyms:Pme1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1919840. Ppme1.

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2189138.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 386385Protein phosphatase methylesterase 1PRO_0000090391Add
BLAST

Post-translational modificationi

Phosphorylated by SIK1 following increases in intracellular sodium, leading to dissociation from the protein phosphatase 2A (PP2A) complex and subsequent dephosphorylation of sodium/potassium-transporting ATPase ATP1A1.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BVQ5.
MaxQBiQ8BVQ5.
PaxDbiQ8BVQ5.
PRIDEiQ8BVQ5.

PTM databases

iPTMnetiQ8BVQ5.
PhosphoSiteiQ8BVQ5.

Expressioni

Tissue specificityi

Ubiquitous. Highly expressed in testis and brain.1 Publication

Gene expression databases

BgeeiQ8BVQ5.
CleanExiMM_PPME1.
GenevisibleiQ8BVQ5. MM.

Interactioni

Subunit structurei

Binds PPP2CA and PPP2CB.By similarity

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-46211N.
IntActiQ8BVQ5. 3 interactions.
MINTiMINT-4108015.
STRINGi10090.ENSMUSP00000032963.

Chemistry

BindingDBiQ8BVQ5.

Structurei

3D structure databases

ProteinModelPortaliQ8BVQ5.
SMRiQ8BVQ5. Positions 39-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi256 – 2638Poly-Glu

Sequence similaritiesi

Belongs to the AB hydrolase superfamily.Curated

Phylogenomic databases

eggNOGiKOG2564. Eukaryota.
COG0596. LUCA.
GeneTreeiENSGT00390000004396.
HOVERGENiHBG053622.
InParanoidiQ8BVQ5.
KOiK13617.
OMAiLYTWRIE.
OrthoDBiEOG741Z2K.
PhylomeDBiQ8BVQ5.
TreeFamiTF314697.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR016812. PPase_methylesterase_euk.
[Graphical view]
PANTHERiPTHR14189. PTHR14189. 1 hit.
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PIRSFiPIRSF022950. PPase_methylesterase_euk. 1 hit.
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 2 hits.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8BVQ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSALEKSMHL GRLPSRPPLP GSGGSQSGAK MRMGPGRKRD FTPVPWSQYF
60 70 80 90 100
ESMEDVEVEN ETGKDTFRVY KSGSEGPVLL LLHGGGHSAL SWAVFTAAII
110 120 130 140 150
SRVQCRIVAL DLRGHGETKV KNSEDLSAET MAKDVGNVVE AMYGDLPPPV
160 170 180 190 200
MLIGHSMGGA IAVHTAAANL VPSLLGLCMI DVVEGTAMDA LNSMQNFLRG
210 220 230 240 250
RPKTFKSLEN AIEWSVKSGQ IRNLESARVS MVGQVKQCEG ITSPEGSKSI
260 270 280 290 300
VEGIIEEEEE DEEGSESVNK RKKEDDMETK KDHPYTWRIE LAKTEKYWDG
310 320 330 340 350
WFRGLSNLFL SCPIPKLLLL AGVDRLDKDL TIGQMQGKFQ MQVLPQCGHA
360 370 380
VHEDAPDKVA EAVATFLIRH RFAEPIGGFQ CVFPGC
Length:386
Mass (Da):42,256
Last modified:January 23, 2007 - v5
Checksum:i2BD07B588299DB6D
GO

Sequence cautioni

The sequence BAE32896.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171P → T in BAE27027 (PubMed:16141072).Curated
Sequence conflicti86 – 861G → D in AAH29064 (PubMed:15489334).Curated
Sequence conflicti370 – 3701H → R in BAE27027 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012256 mRNA. Translation: BAB28122.1.
AK146051 mRNA. Translation: BAE26861.1.
AK146268 mRNA. Translation: BAE27027.1.
AK154876 mRNA. Translation: BAE32896.1. Different initiation.
BC014867 mRNA. Translation: AAH14867.1.
BC029064 mRNA. Translation: AAH29064.1.
CCDSiCCDS40036.1.
RefSeqiNP_082568.1. NM_028292.2.
UniGeneiMm.177502.
Mm.490280.

Genome annotation databases

EnsembliENSMUST00000032963; ENSMUSP00000032963; ENSMUSG00000030718.
GeneIDi72590.
KEGGimmu:72590.
UCSCiuc009imu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012256 mRNA. Translation: BAB28122.1.
AK146051 mRNA. Translation: BAE26861.1.
AK146268 mRNA. Translation: BAE27027.1.
AK154876 mRNA. Translation: BAE32896.1. Different initiation.
BC014867 mRNA. Translation: AAH14867.1.
BC029064 mRNA. Translation: AAH29064.1.
CCDSiCCDS40036.1.
RefSeqiNP_082568.1. NM_028292.2.
UniGeneiMm.177502.
Mm.490280.

3D structure databases

ProteinModelPortaliQ8BVQ5.
SMRiQ8BVQ5. Positions 39-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-46211N.
IntActiQ8BVQ5. 3 interactions.
MINTiMINT-4108015.
STRINGi10090.ENSMUSP00000032963.

Chemistry

BindingDBiQ8BVQ5.
ChEMBLiCHEMBL2189138.

Protein family/group databases

ESTHERimouse-PPME1. PPase_methylesterase_euk.
MEROPSiS33.984.

PTM databases

iPTMnetiQ8BVQ5.
PhosphoSiteiQ8BVQ5.

Proteomic databases

EPDiQ8BVQ5.
MaxQBiQ8BVQ5.
PaxDbiQ8BVQ5.
PRIDEiQ8BVQ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032963; ENSMUSP00000032963; ENSMUSG00000030718.
GeneIDi72590.
KEGGimmu:72590.
UCSCiuc009imu.1. mouse.

Organism-specific databases

CTDi51400.
MGIiMGI:1919840. Ppme1.

Phylogenomic databases

eggNOGiKOG2564. Eukaryota.
COG0596. LUCA.
GeneTreeiENSGT00390000004396.
HOVERGENiHBG053622.
InParanoidiQ8BVQ5.
KOiK13617.
OMAiLYTWRIE.
OrthoDBiEOG741Z2K.
PhylomeDBiQ8BVQ5.
TreeFamiTF314697.

Miscellaneous databases

ChiTaRSiPpme1. mouse.
PROiQ8BVQ5.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BVQ5.
CleanExiMM_PPME1.
GenevisibleiQ8BVQ5. MM.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR016812. PPase_methylesterase_euk.
[Graphical view]
PANTHERiPTHR14189. PTHR14189. 1 hit.
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PIRSFiPIRSF022950. PPase_methylesterase_euk. 1 hit.
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 2 hits.
PROSITEiPS00120. LIPASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 and NOD.
    Tissue: Dendritic cell, Embryo and Placenta.
  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: Mammary gland.
  3. "A protein phosphatase methylesterase (PME-1) is one of several novel proteins stably associating with two inactive mutants of protein phosphatase 2A."
    Ogris E., Du X., Nelson K.C., Mak E.K., Yu X.X., Lane W.S., Pallas D.C.
    J. Biol. Chem. 274:14382-14391(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, TISSUE SPECIFICITY.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiPPME1_MOUSE
AccessioniPrimary (citable) accession number: Q8BVQ5
Secondary accession number(s): Q3U392
, Q3UJX8, Q3UKE0, Q8K311, Q91YR8, Q9CSP7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 113 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.