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P49597

- P2C56_ARATH

UniProt

P49597 - P2C56_ARATH

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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

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 kinase binding Source: UniProtKB
  3. 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
Complete GO annotation...

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-KW
  2. nucleus Source: TAIR
  3. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

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. 1 Publication
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. 1 Publication
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. 1 Publication
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. 1 Publication

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 – 1346Combined sources
Beta strandi138 – 1403Combined sources
Beta strandi143 – 1486Combined sources
Turni149 – 1524Combined sources
Helixi166 – 1694Combined sources
Beta strandi171 – 18212Combined sources
Helixi183 – 20321Combined sources
Helixi207 – 2104Combined sources
Helixi211 – 23121Combined sources
Helixi232 – 2343Combined sources
Beta strandi244 – 2496Combined sources
Beta strandi251 – 26111Combined sources
Beta strandi263 – 2686Combined sources
Beta strandi271 – 2755Combined sources
Helixi284 – 2929Combined sources
Beta strandi297 – 3059Combined sources
Turni306 – 3083Combined sources
Helixi318 – 3203Combined sources
Turni321 – 3233Combined sources
Beta strandi329 – 3346Combined sources
Beta strandi339 – 3457Combined sources
Helixi347 – 3504Combined sources
Helixi355 – 36915Combined sources
Helixi393 – 40816Combined sources
Beta strandi415 – 4217Combined sources

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

        10         20         30         40         50
MEEVSPAIAG PFRPFSETQM DFTGIRLGKG YCNNQYSNQD SENGDLMVSL
60 70 80 90 100
PETSSCSVSG SHGSESRKVL ISRINSPNLN MKESAAADIV VVDISAGDEI
110 120 130 140 150
NGSDITSEKK MISRTESRSL FEFKSVPLYG FTSICGRRPE MEDAVSTIPR
160 170 180 190 200
FLQSSSGSML DGRFDPQSAA HFFGVYDGHG GSQVANYCRE RMHLALAEEI
210 220 230 240 250
AKEKPMLCDG DTWLEKWKKA LFNSFLRVDS EIESVAPETV GSTSVVAVVF
260 270 280 290 300
PSHIFVANCG DSRAVLCRGK TALPLSVDHK PDREDEAARI EAAGGKVIQW
310 320 330 340 350
NGARVFGVLA MSRSIGDRYL KPSIIPDPEV TAVKRVKEDD CLILASDGVW
360 370 380 390 400
DVMTDEEACE MARKRILLWH KKNAVAGDAS LLADERRKEG KDPAAMSAAE
410 420 430
YLSKLAIQRG SKDNISVVVV DLKPRRKLKS KPLN
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

« Hide 'large scale' publications
  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 29, 2014
This is version 147 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