Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P49597

- P2C56_ARATH

UniProt

P49597 - P2C56_ARATH

Protein

Protein phosphatase 2C 56

Gene

ABI1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (06 Jun 2002)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Key component and repressor of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, osmotic water permeability of the plasma membrane (Pos), drought-induced resistance and rhizogenesis, response to glucose, high light stress, seed germination and inhibition of vegetative growth. During the stomatal closure regulation, modulates the inward calcium-channel permeability as well as the actin reorganization in guard cells in response to ABA. Involved in the resistance to the bacterial pathogen Pseudomonas syringae pv. tomato. Controls negatively fibrillin expression that is involved in mediating ABA-induced photoprotection. May be involved in ABA content regulation. Plays a role in the Pro accumulation in response to reduced water availability (low water potential). Required for the ABA negative regulation of the ethylene-induced hyponastic growth. Involved in acquired thermotolerance of root growth and seedling survival. Activates/represses SRK2E/OST1 in response to ABA-dependent stimuli, especially in stomata closure regulation involving SLAC1.49 Publications

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.3 Publications

    Cofactori

    Binds 2 magnesium or manganese ions per subunit.2 Publications

    Enzyme regulationi

    Phosphatase activity repressed by oxidized GPX3 and phosphatidic acid (PA). PA is produced by PLD alpha 1 in response to ABA. Repressed by PYR/PYL/RCAR ABA receptors in an ABA-dependent manner.4 Publications

    pH dependencei

    Optimum pH is 8.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi177 – 1771Manganese 1By similarity
    Metal bindingi177 – 1771Manganese 2By similarity
    Metal bindingi178 – 1781Manganese 1; via carbonyl oxygenBy similarity
    Sitei300 – 3001Lock
    Metal bindingi347 – 3471Manganese 2By similarity
    Metal bindingi413 – 4131Manganese 2By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. abscisic acid-activated signaling pathway Source: UniProtKB-KW
    2. negative regulation of abscisic acid-activated signaling pathway Source: UniProtKB
    3. protein dephosphorylation Source: InterPro
    4. regulation of abscisic acid-activated signaling pathway Source: TAIR
    5. regulation of stomatal movement Source: TAIR
    6. response to abscisic acid Source: TAIR
    7. response to cold Source: TAIR
    8. response to heat Source: TAIR

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Abscisic acid signaling pathway

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT4G26080-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein phosphatase 2C 56 (EC:3.1.3.16)
    Short name:
    AtPP2C56
    Alternative name(s):
    Protein ABSCISIC ACID-INSENSITIVE 1
    Protein phosphatase 2C ABI1
    Short name:
    PP2C ABI1
    Gene namesi
    Name:ABI1
    Ordered Locus Names:At4g26080
    ORF Names:F20B18.190
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G26080.

    Subcellular locationi

    Nucleus. Cytoplasm. Cell membrane; Peripheral membrane protein
    Note: Associated to the plasma membrane when in complex with PA, subsequently to ABA signaling.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: TAIR
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 682RK → GA: Normal binding with PA, no reduction of phosphatase activity.
    Mutagenesisi73 – 731R → A: Loss of binding with PA, no reduction of phosphatase activity. 2 Publications
    Mutagenesisi93 – 931D → A: No phenotype. 1 Publication
    Mutagenesisi141 – 1433MED → IHG: Reduced inhibition of the ABA signaling pathway and loss of phosphatase activity.
    Mutagenesisi142 – 1421E → A: Reduced binding affinity for PYL1, and impaired phosphatase activity. 1 Publication
    Mutagenesisi174 – 1741G → D: No inhibition of the ABA signaling pathway and loss of phosphatase activity. 1 Publication
    Mutagenesisi177 – 1793DGH → KLN: No inhibition of the ABA signaling pathway and loss of phosphatase activity. 3 Publications
    Mutagenesisi177 – 1771D → A: Loss of phosphatase activity, impaired negative regulation of the ABA signaling pathway, reduced interaction with ATHB-6, and reduced negative control on fibrillin expression. 3 Publications
    Mutagenesisi180 – 1801G → D in abi1; wilty phenotype, reduced phosphatase activity, ABA-insensitive seed germination and growth, impaired ABA-mediated binding to PYR1, and reduced interaction with ATHB-6. Increased sensitivity to ABA and loss of phosphatase activity; when associated with T-185, or Y-259, or C-304, or D-307, or F-314, or L-328, or N-316. No inhibition of the ABA signaling pathway and loss of phosphatase activity; when associated with D-174. 8 Publications
    Mutagenesisi185 – 1851A → T: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication
    Mutagenesisi239 – 2391T → A: Normal affinity for PYL1. 1 Publication
    Mutagenesisi259 – 2591C → Y: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication
    Mutagenesisi298 – 2981I → A: Loss of affinity for PYL1. 1 Publication
    Mutagenesisi300 – 3001W → A: Loss of affinity for PYL1. 1 Publication
    Mutagenesisi304 – 3041R → A: Loss of affinity for PYL1. 2 Publications
    Mutagenesisi304 – 3041R → C: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 2 Publications
    Mutagenesisi306 – 3061F → A: Reduced affinity for PYL1. 1 Publication
    Mutagenesisi307 – 3071G → D: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication
    Mutagenesisi308 – 3081V → A: Reduced affinity for PYL1. 1 Publication
    Mutagenesisi314 – 3141S → F: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication
    Mutagenesisi319 – 3191Y → A: Reduced affinity for PYL1. 1 Publication
    Mutagenesisi328 – 3281P → L: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication
    Mutagenesisi416 – 4161S → N: Increased sensitivity to ABA and loss of phosphatase activity; when associated with D-180. 1 Publication
    Mutagenesisi425 – 4273RRK → QNN: Cytoplasmic subcellular localization, and loss of negative regulation of the ABA signaling pathway.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 434434Protein phosphatase 2C 56PRO_0000057766Add
    BLAST

    Proteomic databases

    PRIDEiP49597.

    Expressioni

    Tissue specificityi

    Expressed in seeds and seedlings. In roots, confined to lateral root caps and columella cells.2 Publications

    Inductioni

    Repressed by MYB44. Induced by low temperature, drought, high salt, ABA and ethylene.6 Publications

    Gene expression databases

    GenevestigatoriP49597.

    Interactioni

    Subunit structurei

    Interacts with ATHB-6, CIPK15/PKS3, GPX3, SRK2E/OST1, SRK2D, SRK2I, SCAR1, SCAR2, SCAR3 and SCARL. Binds to the PA released by the phospholipase D alpha 1 (PLDALPHA1) in response to ABA during the stomatal closure regulation. Interacts with ABA-bounded PYR1, PYL1, PYL2, PYL3, PYL4, PYL5, PYL6, PYL7, PYL8, PYL9, PYL10, and with free PYL2, PYL3 and PYL4. Binds to RPL12B, CPK21 and CPK23.16 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PYL4O809203EBI-782526,EBI-2349683
    PYL5Q9FLB13EBI-782526,EBI-2363181
    PYL9Q84MC74EBI-782526,EBI-2349513
    PYR1O496867EBI-782526,EBI-2349590
    SRK2DQ391924EBI-782526,EBI-2363308
    SRK2EQ940H64EBI-782526,EBI-782514
    SRK2IQ391933EBI-782526,EBI-2620383

    Protein-protein interaction databases

    BioGridi14001. 41 interactions.
    DIPiDIP-36706N.
    IntActiP49597. 22 interactions.
    MINTiMINT-8390807.

    Structurei

    Secondary structure

    1
    434
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi129 – 1346
    Beta strandi138 – 1403
    Beta strandi143 – 1486
    Turni149 – 1524
    Helixi166 – 1694
    Beta strandi171 – 18212
    Helixi183 – 20321
    Helixi207 – 2104
    Helixi211 – 23121
    Helixi232 – 2343
    Beta strandi244 – 2496
    Beta strandi251 – 26111
    Beta strandi263 – 2686
    Beta strandi271 – 2755
    Helixi284 – 2929
    Beta strandi297 – 3059
    Turni306 – 3083
    Helixi318 – 3203
    Turni321 – 3233
    Beta strandi329 – 3346
    Beta strandi339 – 3457
    Helixi347 – 3504
    Helixi355 – 36915
    Helixi393 – 40816
    Beta strandi415 – 4217

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3JRQX-ray2.10A125-429[»]
    3KDJX-ray1.88B119-434[»]
    3NMNX-ray2.15B/D117-434[»]
    ProteinModelPortaliP49597.
    SMRiP49597. Positions 125-424.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49597.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini127 – 415289PP2C-likeAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi423 – 4275Nuclear localization signal1 Publication

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi417 – 4204Poly-Val

    Domaini

    The 'lock' site stabilizes the complex made of PP2C, ABA and PYR/PYL/RCAR receptor by keeping receptor 'gate' and 'latch' loops in closed positions.

    Sequence similaritiesi

    Belongs to the PP2C family.Curated
    Contains 1 PP2C-like domain.Curated

    Phylogenomic databases

    eggNOGiCOG0631.
    HOGENOMiHOG000233896.
    InParanoidiP49597.
    KOiK14497.
    OMAiQRGSKDN.
    PhylomeDBiP49597.

    Family and domain databases

    Gene3Di3.60.40.10. 1 hit.
    InterProiIPR001932. PP2C-like_dom.
    IPR000222. PP2C_Mn2_Asp60_BS.
    IPR015655. Protein_Pase_2C.
    [Graphical view]
    PANTHERiPTHR13832. PTHR13832. 1 hit.
    PfamiPF00481. PP2C. 1 hit.
    [Graphical view]
    SMARTiSM00331. PP2C_SIG. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view]
    SUPFAMiSSF81606. SSF81606. 1 hit.
    PROSITEiPS01032. PP2C. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P49597-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEEVSPAIAG PFRPFSETQM DFTGIRLGKG YCNNQYSNQD SENGDLMVSL    50
    PETSSCSVSG SHGSESRKVL ISRINSPNLN MKESAAADIV VVDISAGDEI 100
    NGSDITSEKK MISRTESRSL FEFKSVPLYG FTSICGRRPE MEDAVSTIPR 150
    FLQSSSGSML DGRFDPQSAA HFFGVYDGHG GSQVANYCRE RMHLALAEEI 200
    AKEKPMLCDG DTWLEKWKKA LFNSFLRVDS EIESVAPETV GSTSVVAVVF 250
    PSHIFVANCG DSRAVLCRGK TALPLSVDHK PDREDEAARI EAAGGKVIQW 300
    NGARVFGVLA MSRSIGDRYL KPSIIPDPEV TAVKRVKEDD CLILASDGVW 350
    DVMTDEEACE MARKRILLWH KKNAVAGDAS LLADERRKEG KDPAAMSAAE 400
    YLSKLAIQRG SKDNISVVVV DLKPRRKLKS KPLN 434
    Length:434
    Mass (Da):47,506
    Last modified:June 6, 2002 - v2
    Checksum:i4A4C54F04195F572
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti24 – 241G → R in AAK59578. (PubMed:14593172)Curated
    Sequence conflicti105 – 1051I → V in CAA55484. (PubMed:8197457)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12856 mRNA. Translation: AAA50237.1.
    X77116 mRNA. Translation: CAA54383.1.
    X78886 Genomic DNA. Translation: CAA55484.1.
    AL049483 Genomic DNA. Translation: CAB39673.1.
    AL161564 Genomic DNA. Translation: CAB79463.1.
    CP002687 Genomic DNA. Translation: AEE85155.1.
    AY035073 mRNA. Translation: AAK59578.1.
    AY142623 mRNA. Translation: AAN13081.1.
    AK226529 mRNA. Translation: BAE98668.1.
    PIRiT04263.
    RefSeqiNP_194338.1. NM_118741.2.
    UniGeneiAt.21332.

    Genome annotation databases

    EnsemblPlantsiAT4G26080.1; AT4G26080.1; AT4G26080.
    GeneIDi828714.
    KEGGiath:AT4G26080.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U12856 mRNA. Translation: AAA50237.1 .
    X77116 mRNA. Translation: CAA54383.1 .
    X78886 Genomic DNA. Translation: CAA55484.1 .
    AL049483 Genomic DNA. Translation: CAB39673.1 .
    AL161564 Genomic DNA. Translation: CAB79463.1 .
    CP002687 Genomic DNA. Translation: AEE85155.1 .
    AY035073 mRNA. Translation: AAK59578.1 .
    AY142623 mRNA. Translation: AAN13081.1 .
    AK226529 mRNA. Translation: BAE98668.1 .
    PIRi T04263.
    RefSeqi NP_194338.1. NM_118741.2.
    UniGenei At.21332.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3JRQ X-ray 2.10 A 125-429 [» ]
    3KDJ X-ray 1.88 B 119-434 [» ]
    3NMN X-ray 2.15 B/D 117-434 [» ]
    ProteinModelPortali P49597.
    SMRi P49597. Positions 125-424.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 14001. 41 interactions.
    DIPi DIP-36706N.
    IntActi P49597. 22 interactions.
    MINTi MINT-8390807.

    Proteomic databases

    PRIDEi P49597.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G26080.1 ; AT4G26080.1 ; AT4G26080 .
    GeneIDi 828714.
    KEGGi ath:AT4G26080.

    Organism-specific databases

    TAIRi AT4G26080.

    Phylogenomic databases

    eggNOGi COG0631.
    HOGENOMi HOG000233896.
    InParanoidi P49597.
    KOi K14497.
    OMAi QRGSKDN.
    PhylomeDBi P49597.

    Enzyme and pathway databases

    BioCyci ARA:AT4G26080-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P49597.

    Gene expression databases

    Genevestigatori P49597.

    Family and domain databases

    Gene3Di 3.60.40.10. 1 hit.
    InterProi IPR001932. PP2C-like_dom.
    IPR000222. PP2C_Mn2_Asp60_BS.
    IPR015655. Protein_Pase_2C.
    [Graphical view ]
    PANTHERi PTHR13832. PTHR13832. 1 hit.
    Pfami PF00481. PP2C. 1 hit.
    [Graphical view ]
    SMARTi SM00331. PP2C_SIG. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81606. SSF81606. 1 hit.
    PROSITEi PS01032. PP2C. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The A. thaliana disease resistance gene RPS2 encodes a protein containing a nucleotide-binding site and leucine-rich repeats."
      Mindrinos M., Katagiri F., Yu G.-L., Ausubel F.M.
      Cell 78:1089-1099(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
      Tissue: Leaf.
    2. "Arabidopsis ABA response gene ABI1: features of a calcium-modulated protein phosphatase."
      Leung J., Bouvier-Durand M., Morris P.C., Guerrier D., Chefdor F., Giraudat J.
      Science 264:1448-1452(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Columbia.
      Tissue: Leaf.
    3. "A protein phosphatase 2C involved in ABA signal transduction in Arabidopsis thaliana."
      Meyer K., Leube M.P., Grill E.
      Science 264:1452-1455(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-180.
      Strain: cv. Landsberg erecta.
    4. "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.
    5. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    6. "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.
    7. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    8. "The isolation and characterization of abscisic-acid insensitive mutants of Arabidopsis thaliana."
      Kornneef M., Reuling G., Karssen C.M.
      Physiol. Plantarum 61:377-383(1984)
      Cited for: FUNCTION.
    9. "Cold acclimation and cold-regulated gene expression in ABA mutants of Arabidopsis thaliana."
      Gilmour S.J., Thomashow M.F.
      Plant Mol. Biol. 17:1233-1240(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Abscisic acid elicits the water-stress response in root hairs of Arabidopsis thaliana."
      Schnall J.A., Quatrano R.S.
      Plant Physiol. 100:216-218(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Abscisic acid-insensitive mutations provide evidence for stage-specific signal pathways regulating expression of an Arabidopsis late embryogenesis-abundant (lea) gene."
      Finkelstein R.R.
      Mol. Gen. Genet. 238:401-408(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Maternal effects govern variable dominance of two abscisic acid response mutations in Arabidopsis thaliana."
      Finkelstein R.R.
      Plant Physiol. 105:1203-1208(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Drought rhizogenesis in Arabidopsis thaliana (differential responses of hormonal mutants)."
      Vartanian N., Marcotte L., Giraudat J.
      Plant Physiol. 104:761-767(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Sensitivity to abscisic acid of guard-cell K+ channels is suppressed by abi1-1, a mutant Arabidopsis gene encoding a putative protein phosphatase."
      Armstrong F., Leung J., Grabov A., Brearley J., Giraudat J., Blatt M.R.
      Proc. Natl. Acad. Sci. U.S.A. 92:9520-9524(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Role of abscisic acid in drought-induced freezing tolerance, cold acclimation, and accumulation of lt178 and rab18 proteins in Arabidopsis thaliana."
      Maentylae E., Laang V., Palva E.T.
      Plant Physiol. 107:141-148(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Protein phosphatase activity of abscisic acid insensitive 1 (ABI1) protein from Arabidopsis thaliana."
      Bertauche N., Leung J., Giraudat J.
      Eur. J. Biochem. 241:193-200(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLY-180, CATALYTIC ACTIVITY, COFACTOR.
    17. "The Arabidopsis homeobox gene ATHB-7 is induced by water deficit and by abscisic acid."
      Soederman E., Mattsson J., Engstroem P.
      Plant J. 10:375-381(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    18. "Abscisic acid-independent and abscisic acid-dependent regulation of proline biosynthesis following cold and osmotic stresses in Arabidopsis thaliana."
      Savoure A., Hua X.-J., Bertauche N., Van Montagu M., Verbruggen N.
      Mol. Gen. Genet. 254:104-109(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. "Differential abscisic acid regulation of guard cell slow anion channels in Arabidopsis wild-type and abi1 and abi2 mutants."
      Pei Z.-M., Kuchitsu K., Ward J.M., Schwarz M., Schroeder J.I.
      Plant Cell 9:409-423(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "The Arabidopsis ABSCISIC ACID-INSENSITIVE2 (ABI2) and ABI1 genes encode homologous protein phosphatases 2C involved in abscisic acid signal transduction."
      Leung J., Merlot S., Giraudat J.
      Plant Cell 9:759-771(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "Interactions between the ABI1 and the ectopically expressed ABI3 genes in controlling abscisic acid responses in Arabidopsis vegetative tissues."
      Parcy F., Giraudat J.
      Plant J. 11:693-702(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    22. "Alteration of anion channel kinetics in wild-type and abi1-1 transgenic Nicotiana benthamiana guard cells by abscisic acid."
      Grabov A., Leung J., Giraudat J., Blatt M.R.
      Plant J. 12:203-213(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "Differential expression of two P5CS genes controlling proline accumulation during salt-stress requires ABA and is regulated by ABA1, ABI1 and AXR2 in Arabidopsis."
      Strizhov N., Abraham E., Oekresz L., Blickling S., Zilberstein A., Schell J., Koncz C., Szabados L.
      Plant J. 12:557-569(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    24. "Convergence of the abscisic acid, CO2, and extracellular calcium signal transduction pathways in stomatal guard cells."
      Webb A.A.R., Hetherington A.M.
      Plant Physiol. 114:1557-1560(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    25. "ABI1 of Arabidopsis is a protein serine/threonine phosphatase highly regulated by the proton and magnesium ion concentration."
      Leube M.P., Grill E., Amrhein N.
      FEBS Lett. 424:100-104(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF GLY-180, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
    26. "Mutational analysis of protein phosphatase 2C involved in abscisic acid signal transduction in higher plants."
      Sheen J.
      Proc. Natl. Acad. Sci. U.S.A. 95:975-980(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-93; 141-MET--ASP-143; GLY-174; 177-ASP--HIS-179 AND GLY-180.
    27. "The role of ABI1 in abscisic acid signal transduction: from gene to cell."
      Leung J., Merlot S., Gosti F., Bertauche N., Blatt M.R., Giraudat J.
      Symp. Soc. Exp. Biol. 51:65-71(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    28. "Arabidopsis abi1-1 and abi2-1 phosphatase mutations reduce abscisic acid-induced cytoplasmic calcium rises in guard cells."
      Allen G.J., Kuchitsu K., Chu S.P., Murata Y., Schroeder J.I.
      Plant Cell 11:1785-1798(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    29. "ABI1 protein phosphatase 2C is a negative regulator of abscisic acid signaling."
      Gosti F., Beaudoin N., Serizet C., Webb A.A.R., Vartanian N., Giraudat J.
      Plant Cell 11:1897-1909(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLY-180; ALA-185; CYS-259; ARG-304; GLY-307; SER-314; PRO-328 AND SER-416.
    30. "Analysis of Arabidopsis glucose insensitive mutants, gin5 and gin6, reveals a central role of the plant hormone ABA in the regulation of plant vegetative development by sugar."
      Arenas-Huertero F., Arroyo A., Zhou L., Sheen J., Leon P.
      Genes Dev. 14:2085-2096(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    31. "The genes ABI1 and ABI2 are involved in abscisic acid- and drought-inducible expression of the Daucus carota L. Dc3 promoter in guard cells of transgenic Arabidopsis thaliana (L.) Heynh."
      Chak R.K.F., Thomas T.L., Quatrano R.S., Rock C.D.
      Planta 210:875-883(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    32. "The role of ABA and the transpiration stream in the regulation of the osmotic water permeability of leaf cells."
      Morillon R., Chrispeels M.J.
      Proc. Natl. Acad. Sci. U.S.A. 98:14138-14143(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    33. "The ABI1 and ABI2 protein phosphatases 2C act in a negative feedback regulatory loop of the abscisic acid signalling pathway."
      Merlot S., Gosti F., Guerrier D., Vavasseur A., Giraudat J.
      Plant J. 25:295-303(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    34. "Dissection of abscisic acid signal transduction pathways in barley aleurone layers."
      Shen Q., Gomez-Cadenas A., Zhang P., Walker-Simmons M.K., Sheen J., Ho T.-H.D.
      Plant Mol. Biol. 47:437-448(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    35. "Cortical actin filaments in guard cells respond differently to abscisic acid in wild-type and abi1-1 mutant Arabidopsis."
      Eun S.-O., Bae S.-H., Lee Y.
      Planta 212:466-469(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    36. "Antisense inhibition of protein phosphatase 2C accelerates cold acclimation in Arabidopsis thaliana."
      Taehtiharju S., Palva T.
      Plant J. 26:461-470(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    37. "Abscisic acid activation of plasma membrane Ca(2+) channels in guard cells requires cytosolic NAD(P)H and is differentially disrupted upstream and downstream of reactive oxygen species production in abi1-1 and abi2-1 protein phosphatase 2C mutants."
      Murata Y., Pei Z.-M., Mori I.C., Schroeder J.
      Plant Cell 13:2513-2523(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    38. "A calcium sensor and its interacting protein kinase are global regulators of abscisic acid signaling in Arabidopsis."
      Guo Y., Xiong L., Song C.-P., Gong D., Halfter U., Zhu J.-K.
      Dev. Cell 3:233-244(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CIPK15/PKS3.
    39. "Homeodomain protein ATHB6 is a target of the protein phosphatase ABI1 and regulates hormone responses in Arabidopsis."
      Himmelbach A., Hoffmann T., Leube M., Hoehener B., Grill E.
      EMBO J. 21:3029-3038(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-177 AND GLY-180, INTERACTION WITH ATHB-6.
    40. "Genome-wide gene expression profiling in Arabidopsis thaliana reveals new targets of abscisic acid and largely impaired gene regulation in the abi1-1 mutant."
      Hoth S., Morgante M., Sanchez J.-P., Hanafey M.K., Tingey S.V., Chua N.-H.
      J. Cell Sci. 115:4891-4900(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    41. "Use of infrared thermal imaging to isolate Arabidopsis mutants defective in stomatal regulation."
      Merlot S., Mustilli A.-C., Genty B., North H., Lefebvre V., Sotta B., Vavasseur A., Giraudat J.
      Plant J. 30:601-609(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    42. "The abi1-1 mutation blocks ABA signaling downstream of cADPR action."
      Wu Y., Sanchez J.P., Lopez-Molina L., Himmelbach A., Grill E., Chua N.-H.
      Plant J. 34:307-315(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    43. "Synthesis of the Arabidopsis bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase enzyme of lysine catabolism is concertedly regulated by metabolic and stress-associated signals."
      Stepansky A., Galili G.
      Plant Physiol. 133:1407-1415(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    44. "Regulation of the ABA-sensitive Arabidopsis potassium channel gene GORK in response to water stress."
      Becker D., Hoth S., Ache P., Wenkel S., Roelfsema M.R.G., Meyerhoff O., Hartung W., Hedrich R.
      FEBS Lett. 554:119-126(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    45. "Control of Ascorbate Peroxidase 2 expression by hydrogen peroxide and leaf water status during excess light stress reveals a functional organisation of Arabidopsis leaves."
      Fryer M.J., Ball L., Oxborough K., Karpinski S., Mullineaux P.M., Baker N.R.
      Plant J. 33:691-705(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    46. "Gain-of-function and loss-of-function phenotypes of the protein phosphatase 2C HAB1 reveal its role as a negative regulator of abscisic acid signalling."
      Saez A., Apostolova N., Gonzalez-Guzman M., Gonzalez-Garcia M.P., Nicolas C., Lorenzo O., Rodriguez P.L.
      Plant J. 37:354-369(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY ABA.
    47. "Drought tolerance established by enhanced expression of the CC-NBS-LRR gene, ADR1, requires salicylic acid, EDS1 and ABI1."
      Chini A., Grant J.J., Seki M., Shinozaki K., Loake G.J.
      Plant J. 38:810-822(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    48. "Phospholipase D alpha 1-derived phosphatidic acid interacts with ABI1 phosphatase 2C and regulates abscisic acid signaling."
      Zhang W., Qin C., Zhao J., Wang X.
      Proc. Natl. Acad. Sci. U.S.A. 101:9508-9513(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF 67-ARG-LYS-68 AND ARG-73, SUBCELLULAR LOCATION, ENZYME REGULATION, INTERACTION WITH PA.
    49. "Plant PP2C phosphatases: emerging functions in stress signaling."
      Schweighofer A., Hirt H., Meskiene I.
      Trends Plant Sci. 9:236-243(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.
    50. "Generation of active pools of abscisic acid revealed by in vivo imaging of water-stressed Arabidopsis."
      Christmann A., Hoffmann T., Teplova I., Grill E., Mueller A.
      Plant Physiol. 137:209-219(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    51. "Heat stress phenotypes of Arabidopsis mutants implicate multiple signaling pathways in the acquisition of thermotolerance."
      Larkindale J., Hall J.D., Knight M.R., Vierling E.
      Plant Physiol. 138:882-897(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    52. "The regulatory domain of SRK2E/OST1/SnRK2.6 interacts with ABI1 and integrates abscisic acid (ABA) and osmotic stress signals controlling stomatal closure in Arabidopsis."
      Yoshida R., Umezawa T., Mizoguchi T., Takahashi S., Takahashi F., Shinozaki K.
      J. Biol. Chem. 281:5310-5318(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SRK2E.
    53. "Role of abscisic acid (ABA) and Arabidopsis thaliana ABA-insensitive loci in low water potential-induced ABA and proline accumulation."
      Verslues P.E., Bray E.A.
      J. Exp. Bot. 57:201-212(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    54. "An Arabidopsis glutathione peroxidase functions as both a redox transducer and a scavenger in abscisic acid and drought stress responses."
      Miao Y., Lv D., Wang P., Wang X.-C., Chen J., Miao C., Song C.-P.
      Plant Cell 18:2749-2766(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GPX3, REPRESSION BY OXIDIZED GPX3.
    55. "Fibrillin expression is regulated by abscisic acid response regulators and is involved in abscisic acid-mediated photoprotection."
      Yang Y., Sulpice R., Himmelbach A., Meinhard M., Christmann A., Grill E.
      Proc. Natl. Acad. Sci. U.S.A. 103:6061-6066(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-177.
    56. "ABA-hypersensitive germination3 encodes a protein phosphatase 2C (AtPP2CA) that strongly regulates abscisic acid signaling during germination among Arabidopsis protein phosphatase 2Cs."
      Yoshida T., Nishimura N., Kitahata N., Kuromori T., Ito T., Asami T., Shinozaki K., Hirayama T.
      Plant Physiol. 140:115-126(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY ABA, TISSUE SPECIFICITY.
    57. "Enhancement of abscisic acid sensitivity and reduction of water consumption in Arabidopsis by combined inactivation of the protein phosphatases type 2C ABI1 and HAB1."
      Saez A., Robert N., Maktabi M.H., Schroeder J.I., Serrano R., Rodriguez P.L.
      Plant Physiol. 141:1389-1399(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    58. "A bifurcating pathway directs abscisic acid effects on stomatal closure and opening in Arabidopsis."
      Mishra G., Zhang W., Deng F., Zhao J., Wang X.
      Science 312:264-266(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PA, ENZYME REGULATION, MUTAGENESIS OF ARG-73.
    59. "The role of Arabidopsis SCAR genes in ARP2-ARP3-dependent cell morphogenesis."
      Uhrig J.F., Mutondo M., Zimmermann I., Deeks M.J., Machesky L.M., Thomas P., Uhrig S., Rambke C., Hussey P.J., Huelskamp M.
      Development 134:967-977(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCAR1; SCAR2; SCAR3 AND SCARL.
    60. "Pseudomonas syringae pv. tomato hijacks the Arabidopsis abscisic acid signalling pathway to cause disease."
      de Torres-Zabala M., Truman W., Bennett M.H., Lafforgue G., Mansfield J.W., Rodriguez Egea P., Bogre L., Grant M.
      EMBO J. 26:1434-1443(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    61. "Abscisic acid antagonizes ethylene-induced hyponastic growth in Arabidopsis."
      Benschop J.J., Millenaar F.F., Smeets M.E., van Zanten M., Voesenek L.A.C.J., Peeters A.J.M.
      Plant Physiol. 143:1013-1023(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION BY ETHYLENE.
    62. "Genome-wide and expression analysis of protein phosphatase 2C in rice and Arabidopsis."
      Xue T., Wang D., Zhang S., Ehlting J., Ni F., Jacab S., Zheng C., Zhong Y.
      BMC Genomics 9:550-550(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE.
    63. "Nuclear localization of the mutant protein phosphatase abi1 is required for insensitivity towards ABA responses in Arabidopsis."
      Moes D., Himmelbach A., Korte A., Haberer G., Grill E.
      Plant J. 54:806-819(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF ASP-177; GLY-180 AND 425-ARG--LYS-427, NUCLEAR LOCALIZATION SIGNAL, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    64. "Overexpression of AtMYB44 enhances stomatal closure to confer abiotic stress tolerance in transgenic Arabidopsis."
      Jung C., Seo J.S., Han S.W., Koo Y.J., Kim C.H., Song S.I., Nahm B.H., Choi Y.D., Cheong J.-J.
      Plant Physiol. 146:623-635(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY MYB44 AND SALT.
    65. "PYR/PYL/RCAR family members are major in-vivo ABI1 protein phosphatase 2C-interacting proteins in Arabidopsis."
      Nishimura N., Sarkeshik A., Nito K., Park S.-Y., Wang A., Carvalho P.C., Lee S., Caddell D.F., Cutler S.R., Chory J., Yates J.R., Schroeder J.I.
      Plant J. 61:290-299(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RPL12B; PYR1; PYL1; PYL4; PYL5; PYL6; PYL7; PYL8; PYL9; PYL10; SRK2E/OST1; SRK2D/SNRK2-2 AND SRK2I/SNRK2-3.
    66. "Activity of guard cell anion channel SLAC1 is controlled by drought-stress signaling kinase-phosphatase pair."
      Geiger D., Scherzer S., Mumm P., Stange A., Marten I., Bauer H., Ache P., Matschi S., Liese A., Al-Rasheid K.A.S., Romeis T., Hedrich R.
      Proc. Natl. Acad. Sci. U.S.A. 106:21425-21430(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SRK2E/OST1.
    67. "Regulators of PP2C phosphatase activity function as abscisic acid sensors."
      Ma Y., Szostkiewicz I., Korte A., Moes D., Yang Y., Christmann A., Grill E.
      Science 324:1064-1068(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PYL9/RCAR1.
    68. Cited for: INTERACTION WITH PYR1; PYL1; PYL2; PYL3 AND PYL4, MUTAGENESIS OF GLY-180, ENZYME REGULATION.
    69. "Structural mechanism of abscisic acid binding and signaling by dimeric PYR1."
      Nishimura N., Hitomi K., Arvai A.S., Rambo R.P., Hitomi C., Cutler S.R., Schroeder J.I., Getzoff E.D.
      Science 326:1373-1379(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PYR1.
    70. "Closely related receptor complexes differ in their ABA selectivity and sensitivity."
      Szostkiewicz I., Richter K., Kepka M., Demmel S., Ma Y., Korte A., Assaad F.F., Christmann A., Grill E.
      Plant J. 61:25-35(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PYL8/RCAR3, ENZYME REGULATION BY PYR/PYL/RCAR.
    71. "Guard cell anion channel SLAC1 is regulated by CDPK protein kinases with distinct Ca2+ affinities."
      Geiger D., Scherzer S., Mumm P., Marten I., Ache P., Matschi S., Liese A., Wellmann C., Al-Rasheid K.A.S., Grill E., Romeis T., Hedrich R.
      Proc. Natl. Acad. Sci. U.S.A. 107:8023-8028(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CPK21 AND CPK23.
    72. "Structural insights into the mechanism of abscisic acid signaling by PYL proteins."
      Yin P., Fan H., Hao Q., Yuan X., Wu D., Pang Y., Yan C., Li W., Wang J., Yan N.
      Nat. Struct. Mol. Biol. 16:1230-1236(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 119-434 IN COMPLEX WITH ABA AND PYL1, INTERACTION WITH PYL2.
    73. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 125-429 IN COMPLEX WITH ABSCISIC ACID AND PYL1, MUTAGENESIS OF GLU-142; THR-239; ILE-298; TRP-300; ARG-304; PHE-306; VAL-308 AND TYR-319, INTERACTION WITH PYL1.

    Entry informationi

    Entry nameiP2C56_ARATH
    AccessioniPrimary (citable) accession number: P49597
    Secondary accession number(s): Q0WW30, Q43717, Q94C87
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: June 6, 2002
    Last modified: October 1, 2014
    This is version 146 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Enhanced ABA signaling repressor activity by the proteasomal inhibitor MG132 accompanied by a cytoplasmic localization.
    Plants insensitive to ABA (abi1-1) are more resistant to P.syringae.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3