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P48482

- PP12_ARATH

UniProt

P48482 - PP12_ARATH

Protein

Serine/threonine-protein phosphatase PP1 isozyme 2

Gene

TOPP2

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 111 (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 bindingi70 – 701Manganese 1By similarity
    Metal bindingi72 – 721Manganese 1By similarity
    Metal bindingi98 – 981Manganese 1By similarity
    Metal bindingi98 – 981Manganese 2By similarity
    Metal bindingi130 – 1301Manganese 2By similarity
    Active sitei131 – 1311Proton donorBy similarity
    Metal bindingi179 – 1791Manganese 2By similarity
    Metal bindingi254 – 2541Manganese 2By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. protein dephosphorylation Source: TAIR

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT5G59160-MONOMER.
    ARA:GQT-2764-MONOMER.
    ARA:GQT-2765-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase PP1 isozyme 2 (EC:3.1.3.16)
    Gene namesi
    Name:TOPP2
    Ordered Locus Names:At5g59160
    ORF Names:MNC17.7
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G59160.

    Subcellular locationi

    GO - Cellular componenti

    1. protein phosphatase type 1 complex Source: TAIR

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 312311Serine/threonine-protein phosphatase PP1 isozyme 2PRO_0000058798Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiP48482.
    PRIDEiP48482.

    Expressioni

    Gene expression databases

    GenevestigatoriP48482.

    Structurei

    3D structure databases

    ProteinModelPortaliP48482.
    SMRiP48482. Positions 14-305.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0639.
    HOGENOMiHOG000172697.
    InParanoidiP48482.
    KOiK06269.
    OMAiYLSSACY.
    PhylomeDBiP48482.

    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.

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

    P48482-1 [UniParc]FASTAAdd to Basket

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    MAQQGQGSMD PAALDDIIRR LLDYRNPKPG TKQAMLNESE IRQLCIVSRE    50
    IFLQQPNLLE LEAPIKICGD IHGQYSDLLR LFEYGGFPPT ANYLFLGDYV 100
    DRGKQSLETI CLLLAYKIKY PENFFLLRGN HECASINRIY GFYDECKRRF 150
    SVRLWKVFTD SFNCLPVAAV IDDKILCMHG GLSPDLTNVE QIKNIKRPTD 200
    VPDSGLLCDL LWSDPSKDVK GWGMNDRGVS YTFGPDKVAE FLIKNDMDLI 250
    CRAHQVVEDG YEFFADRQLV TIFSAPNYCG EFDNAGAMMS VDESLMCSFQ 300
    ILKPADRKPR FL 312
    Length:312
    Mass (Da):35,532
    Last modified:February 1, 1996 - v1
    Checksum:iDF71C23B5CB53CC2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti181 – 1822GL → AI in CAA78153. (PubMed:8220477)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93409 mRNA. Translation: AAA32837.1.
    Z12163 mRNA. Translation: CAA78153.1.
    AB016890 Genomic DNA. Translation: BAB09762.1.
    CP002688 Genomic DNA. Translation: AED97150.1.
    CP002688 Genomic DNA. Translation: AED97151.1.
    CP002688 Genomic DNA. Translation: AED97152.1.
    AY042840 mRNA. Translation: AAK68780.1.
    BT002401 mRNA. Translation: AAO00761.1.
    BT024861 mRNA. Translation: ABD65592.1.
    PIRiS24264.
    S31086.
    RefSeqiNP_001032103.1. NM_001037026.1.
    NP_200724.1. NM_125306.2.
    NP_851218.1. NM_180887.4.
    UniGeneiAt.20932.
    At.311.

    Genome annotation databases

    EnsemblPlantsiAT5G59160.1; AT5G59160.1; AT5G59160.
    AT5G59160.2; AT5G59160.2; AT5G59160.
    AT5G59160.3; AT5G59160.3; AT5G59160.
    GeneIDi836034.
    KEGGiath:AT5G59160.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93409 mRNA. Translation: AAA32837.1 .
    Z12163 mRNA. Translation: CAA78153.1 .
    AB016890 Genomic DNA. Translation: BAB09762.1 .
    CP002688 Genomic DNA. Translation: AED97150.1 .
    CP002688 Genomic DNA. Translation: AED97151.1 .
    CP002688 Genomic DNA. Translation: AED97152.1 .
    AY042840 mRNA. Translation: AAK68780.1 .
    BT002401 mRNA. Translation: AAO00761.1 .
    BT024861 mRNA. Translation: ABD65592.1 .
    PIRi S24264.
    S31086.
    RefSeqi NP_001032103.1. NM_001037026.1.
    NP_200724.1. NM_125306.2.
    NP_851218.1. NM_180887.4.
    UniGenei At.20932.
    At.311.

    3D structure databases

    ProteinModelPortali P48482.
    SMRi P48482. Positions 14-305.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PaxDbi P48482.
    PRIDEi P48482.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G59160.1 ; AT5G59160.1 ; AT5G59160 .
    AT5G59160.2 ; AT5G59160.2 ; AT5G59160 .
    AT5G59160.3 ; AT5G59160.3 ; AT5G59160 .
    GeneIDi 836034.
    KEGGi ath:AT5G59160.

    Organism-specific databases

    TAIRi AT5G59160.

    Phylogenomic databases

    eggNOGi COG0639.
    HOGENOMi HOG000172697.
    InParanoidi P48482.
    KOi K06269.
    OMAi YLSSACY.
    PhylomeDBi P48482.

    Enzyme and pathway databases

    BioCyci ARA:AT5G59160-MONOMER.
    ARA:GQT-2764-MONOMER.
    ARA:GQT-2765-MONOMER.

    Gene expression databases

    Genevestigatori P48482.

    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. "Expression of multiple type 1 phosphoprotein phosphatases in Arabidopsis thaliana."
      Smith R.D., Walker J.C.
      Plant Mol. Biol. 21:307-316(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "A protein phosphatase 1 from Arabidopsis thaliana restores temperature sensitivity of a Schizosaccharomyces pombe cdc25ts/wee1-double mutant."
      Ferreira P.C.G., Hemerly A.S., van Montagu M., Inze D.
      Plant J. 4:81-87(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence features of the regions of 1,081,958 bp covered by seventeen physically assigned P1 and TAC clones."
      Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N., Tabata S.
      DNA Res. 5:379-391(1998) [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. "Arabidopsis ORF clones."
      Kim C.J., Chen H., Shinn P., Ecker J.R.
      Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPP12_ARATH
    AccessioniPrimary (citable) accession number: P48482
    Secondary accession number(s): Q24JM8, Q94B57
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 111 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