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P48486

- PP16_ARATH

UniProt

P48486 - PP16_ARATH

Protein

Serine/threonine-protein phosphatase PP1 isozyme 6

Gene

TOPP6

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 2 (29 May 2007)
      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 bindingi61 – 611Manganese 1By similarity
    Metal bindingi63 – 631Manganese 1By similarity
    Metal bindingi89 – 891Manganese 1By similarity
    Metal bindingi89 – 891Manganese 2By similarity
    Metal bindingi121 – 1211Manganese 2By similarity
    Active sitei122 – 1221Proton donorBy similarity
    Metal bindingi170 – 1701Manganese 2By similarity
    Metal bindingi245 – 2451Manganese 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:AT4G11240-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase PP1 isozyme 6 (EC:3.1.3.16)
    Gene namesi
    Name:TOPP6
    Synonyms:PP1BG
    Ordered Locus Names:At4g11240
    ORF Names:F8L21.30
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G11240.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 322322Serine/threonine-protein phosphatase PP1 isozyme 6PRO_0000058802Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP48486.
    PRIDEiP48486.

    Expressioni

    Tissue specificityi

    Strongly up-regulated within developing flowers, especially in the tapetum, the developing and mature pollen and in the ovaries.

    Gene expression databases

    GenevestigatoriP48486.

    Interactioni

    Protein-protein interaction databases

    BioGridi12025. 2 interactions.
    IntActiP48486. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP48486.
    SMRiP48486. Positions 6-294.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PPP phosphatase family. PP-1 subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172697.
    InParanoidiP48486.
    KOiK06269.
    OMAiKFNFFLL.
    PhylomeDBiP48486.

    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.

    P48486-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDETLLDDII RRLLATNNGR TVKQAQITET EIRQLCLASK EVFLSQPNLL    50
    ELEAPIKICG DVHGQFPDLL RLFEYGGYPP AANYLFLGDY VDRGKQSIET 100
    ICLLLAYKVK YKFNFFLLRG NHECASINRV YGFYDECKRR YNVRLWKTFT 150
    ECFNCLPVSA LIDDKILCMH GGLSPDIKSL DDIRRIPRPI DVPDQGILCD 200
    LLWADPDREI QGWGENDRGV SYTFGADKVA EFLQTHDLDL ICRAHQVVED 250
    GYEFFAKRQL VTIFSAPNYC GEFDNAGALM SVDDSLTCSF QILKASEKKG 300
    RFGFNNNVPR PGTPPHKGGK GR 322
    Length:322
    Mass (Da):36,567
    Last modified:May 29, 2007 - v2
    Checksum:iB2320EB8E472AEDF
    GO

    Sequence cautioni

    The sequence CAB51408.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAB81225.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti248 – 2481V → D(PubMed:7773310)Curated
    Sequence conflicti248 – 2481V → D(PubMed:9617814)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46253 mRNA. Translation: CAA86339.1.
    U80921 Genomic DNA. Translation: AAC39460.1.
    AL096882 Genomic DNA. Translation: CAB51408.1. Sequence problems.
    AL161531 Genomic DNA. Translation: CAB81225.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE82988.1.
    AY090365 mRNA. Translation: AAL91268.1.
    AY122904 mRNA. Translation: AAM67437.1.
    AY086060 mRNA. Translation: AAM63269.1.
    PIRiT13015.
    RefSeqiNP_567375.1. NM_117195.4.
    UniGeneiAt.3651.

    Genome annotation databases

    EnsemblPlantsiAT4G11240.1; AT4G11240.1; AT4G11240.
    GeneIDi826726.
    KEGGiath:AT4G11240.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z46253 mRNA. Translation: CAA86339.1 .
    U80921 Genomic DNA. Translation: AAC39460.1 .
    AL096882 Genomic DNA. Translation: CAB51408.1 . Sequence problems.
    AL161531 Genomic DNA. Translation: CAB81225.1 . Sequence problems.
    CP002687 Genomic DNA. Translation: AEE82988.1 .
    AY090365 mRNA. Translation: AAL91268.1 .
    AY122904 mRNA. Translation: AAM67437.1 .
    AY086060 mRNA. Translation: AAM63269.1 .
    PIRi T13015.
    RefSeqi NP_567375.1. NM_117195.4.
    UniGenei At.3651.

    3D structure databases

    ProteinModelPortali P48486.
    SMRi P48486. Positions 6-294.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 12025. 2 interactions.
    IntActi P48486. 2 interactions.

    Proteomic databases

    PaxDbi P48486.
    PRIDEi P48486.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G11240.1 ; AT4G11240.1 ; AT4G11240 .
    GeneIDi 826726.
    KEGGi ath:AT4G11240.

    Organism-specific databases

    TAIRi AT4G11240.

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172697.
    InParanoidi P48486.
    KOi K06269.
    OMAi KFNFFLL.
    PhylomeDBi P48486.

    Enzyme and pathway databases

    BioCyci ARA:AT4G11240-MONOMER.

    Gene expression databases

    Genevestigatori P48486.

    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. "A novel Arabidopsis type 1 protein phosphatase is highly expressed in male and female tissues and functionally complements a conditional cell cycle mutant of Aspergillus."
      Arundhati A., Feiler H., Traas J., Zhang H., Lunness P.A., Doonan J.H.
      Plant J. 7:823-834(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular cloning and chromosomal mapping of type one serine/threonine protein phosphatases in Arabidopsis thaliana."
      Lin Q., Li J., Smith R.D., Walker J.C.
      Plant Mol. Biol. 37:471-481(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    6. "Full-length cDNA from Arabidopsis thaliana."
      Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
      Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    7. "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.
    8. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPP16_ARATH
    AccessioniPrimary (citable) accession number: P48486
    Secondary accession number(s): Q8RX64, Q9SUT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: May 29, 2007
    Last modified: October 1, 2014
    This is version 110 of the entry and version 2 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