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P48529

- PPX1_ARATH

UniProt

P48529 - PPX1_ARATH

Protein

Serine/threonine-protein phosphatase PP-X isozyme 1

Gene

PPX1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi51 – 511Manganese 1By similarity
    Metal bindingi53 – 531Manganese 1By similarity
    Metal bindingi79 – 791Manganese 1By similarity
    Metal bindingi79 – 791Manganese 2By similarity
    Metal bindingi111 – 1111Manganese 2By similarity
    Active sitei112 – 1121Proton donorBy similarity
    Metal bindingi161 – 1611Manganese 2By similarity
    Metal bindingi236 – 2361Manganese 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein serine/threonine phosphatase activity Source: TAIR

    GO - Biological processi

    1. dephosphorylation Source: GOC

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT4G26720-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase PP-X isozyme 1 (EC:3.1.3.16)
    Gene namesi
    Name:PPX1
    Synonyms:EP124, EP129
    Ordered Locus Names:At4g26720
    ORF Names:F10M23.60
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G26720.

    Subcellular locationi

    Plastid stroma 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: TAIR
    2. nucleus Source: TAIR
    3. plastid stroma Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Plastid

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 305305Serine/threonine-protein phosphatase PP-X isozyme 1PRO_0000058886Add
    BLAST

    Proteomic databases

    PaxDbiP48529.
    PRIDEiP48529.

    Expressioni

    Tissue specificityi

    Ubiquitous, mostly expressed in root mersitems, flowers, and vascular tissues.1 Publication

    Gene expression databases

    GenevestigatoriP48529.

    Interactioni

    Protein-protein interaction databases

    BioGridi14066. 1 interaction.
    STRINGi3702.AT4G26720.1-P.

    Structurei

    3D structure databases

    ProteinModelPortaliP48529.
    SMRiP48529. Positions 3-287.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172696.
    InParanoidiP48529.
    KOiK15423.
    OMAiYIARAHQ.
    PhylomeDBiP48529.

    Family and domain databases

    Gene3Di3.60.21.10. 1 hit.
    InterProiIPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view]
    PfamiPF00149. Metallophos. 1 hit.
    [Graphical view]
    PRINTSiPR00114. STPHPHTASE.
    SMARTiSM00156. PP2Ac. 1 hit.
    [Graphical view]
    SUPFAMiSSF56300. SSF56300. 1 hit.
    PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P48529-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDLDRQIGQ LKRCEPLSES EVKALCLKAM EILVEESNVQ RVDAPVTLCG    50
    DIHGQFYDMM ELFKVGGDCP KTNYLFMGDF VDRGYYSVET FLLLLALKVR 100
    YPDRITLIRG NHESRQITQV YGFYDECLRK YGSSNVWRYC TDIFDYMSLS 150
    AVVENKIFCV HGGLSPAIMT LDQIRTIDRK QEVPHDGAMC DLLWSDPEDI 200
    VDGWGLSPRG AGFLFGGSVV TSFNHSNNID YIARAHQLVM EGYKWMFDSQ 250
    IVTVWSAPNY CYRCGNVASI LELDENLNKE FRVFDAAQQD SRGPPAKKPA 300
    PDYFL 305
    Length:305
    Mass (Da):34,738
    Last modified:February 1, 1996 - v1
    Checksum:i3FBBEADB2DA5B650
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z22587 mRNA. Translation: CAA80302.1.
    AF030289 Genomic DNA. Translation: AAB86418.1.
    AL035440 Genomic DNA. Translation: CAB36518.1.
    AL161565 Genomic DNA. Translation: CAB79527.1.
    CP002687 Genomic DNA. Translation: AEE85245.1.
    PIRiS42558.
    RefSeqiNP_194402.1. NM_118806.5.
    UniGeneiAt.106.

    Genome annotation databases

    EnsemblPlantsiAT4G26720.1; AT4G26720.1; AT4G26720.
    GeneIDi828779.
    KEGGiath:AT4G26720.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z22587 mRNA. Translation: CAA80302.1 .
    AF030289 Genomic DNA. Translation: AAB86418.1 .
    AL035440 Genomic DNA. Translation: CAB36518.1 .
    AL161565 Genomic DNA. Translation: CAB79527.1 .
    CP002687 Genomic DNA. Translation: AEE85245.1 .
    PIRi S42558.
    RefSeqi NP_194402.1. NM_118806.5.
    UniGenei At.106.

    3D structure databases

    ProteinModelPortali P48529.
    SMRi P48529. Positions 3-287.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 14066. 1 interaction.
    STRINGi 3702.AT4G26720.1-P.

    Proteomic databases

    PaxDbi P48529.
    PRIDEi P48529.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G26720.1 ; AT4G26720.1 ; AT4G26720 .
    GeneIDi 828779.
    KEGGi ath:AT4G26720.

    Organism-specific databases

    TAIRi AT4G26720.

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172696.
    InParanoidi P48529.
    KOi K15423.
    OMAi YIARAHQ.
    PhylomeDBi P48529.

    Enzyme and pathway databases

    BioCyci ARA:AT4G26720-MONOMER.

    Gene expression databases

    Genevestigatori P48529.

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR029052. Metallo-depent_PP-like.
    IPR006186. Ser/Thr-sp_prot-phosphatase.
    [Graphical view ]
    Pfami PF00149. Metallophos. 1 hit.
    [Graphical view ]
    PRINTSi PR00114. STPHPHTASE.
    SMARTi SM00156. PP2Ac. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56300. SSF56300. 1 hit.
    PROSITEi PS00125. SER_THR_PHOSPHATASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and molecular cloning of two homologues of protein phosphatase X from Arabidopsis thaliana."
      Perez-Callejon E., Casamayor A., Pujol G., Clua E., Ferrer A., Arino J.
      Plant Mol. Biol. 23:1177-1185(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Leaf.
    2. "The Arabidopsis thaliana PPX/PP4 phosphatases: molecular cloning and structural organization of the genes and immunolocalization of the proteins to plastids."
      Pujol G., Baskin T.I., Casamayor A., Cortadellas N., Ferrer A., Arino J.
      Plant Mol. Biol. 44:499-511(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Strain: cv. Columbia.
    3. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    5. "Arabidopsis PPP family of serine/threonine phosphatases."
      Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C.
      Trends Plant Sci. 12:169-176(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.

    Entry informationi

    Entry nameiPPX1_ARATH
    AccessioniPrimary (citable) accession number: P48529
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3