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Q9CAJ0

- P2C16_ARATH

UniProt

Q9CAJ0 - P2C16_ARATH

Protein

Protein phosphatase 2C 16

Gene

HAB1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Key component and repressor of the abscisic acid (ABA) signaling pathway that regulates numerous ABA responses, such as stomatal closure, seed germination and inhibition of vegetative growth. Confers enhanced sensitivity to drought.4 Publications

    Catalytic activityi

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

    Cofactori

    Binds 2 magnesium or manganese ions per subunit.By similarity

    Enzyme regulationi

    Repressed by PYR/PYL/RCAR ABA receptors in an ABA-dependent manner.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi243 – 2431Manganese 1By similarity
    Metal bindingi243 – 2431Manganese 2By similarity
    Metal bindingi244 – 2441Manganese 1; via carbonyl oxygenBy similarity
    Sitei385 – 3851Lock
    Metal bindingi432 – 4321Manganese 2By similarity
    Metal bindingi492 – 4921Manganese 2By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. abscisic acid-activated signaling pathway Source: UniProtKB-KW
    2. protein dephosphorylation Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Abscisic acid signaling pathway

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding

    Enzyme and pathway databases

    BioCyciARA:AT1G72770-MONOMER.
    ARA:GQT-2826-MONOMER.
    ARA:GQT-408-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein phosphatase 2C 16 (EC:3.1.3.16)
    Short name:
    AtPP2C16
    Alternative name(s):
    AtP2C-HA
    Protein HYPERSENSITIVE TO ABA 1
    Protein phosphatase 2C HAB1
    Short name:
    PP2C HAB1
    Gene namesi
    Name:HAB1
    Synonyms:P2C-HA
    Ordered Locus Names:At1g72770
    ORF Names:F28P22.4
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 1

    Organism-specific databases

    TAIRiAT1G72770.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Mainly cytoplasmic.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi246 – 2461G → D: Reduced phosphatase activity, impaired affinity for PYR/PYL/RCAR receptors, and insensitivity to ABA. 3 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 511489Protein phosphatase 2C 16PRO_0000344524Add
    BLAST

    Proteomic databases

    PRIDEiQ9CAJ0.

    Expressioni

    Tissue specificityi

    Expressed in seeds, roots, stems, leaves and flowers, especially in meristematic tissues, guard cells, embryo and siliques.3 Publications

    Inductioni

    Repressed by MYB44. Induced by ABA.4 Publications

    Gene expression databases

    GenevestigatoriQ9CAJ0.

    Interactioni

    Subunit structurei

    Interacts with SWI3B (via N-terminus). Interacts with ABA-bounded PYR1, PYL1, PYL2, PYL3, PYL4, PYL5, PYL6, PYL8 and PYL9, and with free PYL2, PYL3 and PYL4.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PYL1Q8VZS82EBI-2309302,EBI-2363104
    PYL5Q9FLB16EBI-2309302,EBI-2363181
    PYL6Q8S8E34EBI-2309302,EBI-2363192
    PYL8Q9FGM13EBI-2309302,EBI-2429535
    PYR1O496868EBI-2309302,EBI-2349590
    SWI3BQ84JG24EBI-2309302,EBI-1102271

    Protein-protein interaction databases

    BioGridi28828. 17 interactions.
    DIPiDIP-48988N.
    IntActiQ9CAJ0. 16 interactions.
    MINTiMINT-8299472.

    Structurei

    Secondary structure

    1
    511
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi181 – 1833
    Beta strandi190 – 1956
    Beta strandi199 – 2013
    Beta strandi204 – 21613
    Helixi217 – 2193
    Beta strandi233 – 24816
    Helixi249 – 26820
    Turni269 – 2713
    Helixi284 – 30219
    Beta strandi319 – 3213
    Beta strandi329 – 3346
    Beta strandi336 – 34611
    Beta strandi348 – 3536
    Beta strandi356 – 3605
    Helixi369 – 3779
    Beta strandi382 – 3909
    Turni391 – 3933
    Helixi403 – 4053
    Turni406 – 4083
    Beta strandi414 – 4196
    Beta strandi424 – 4307
    Helixi432 – 4354
    Helixi440 – 45819
    Turni463 – 4686
    Helixi472 – 48716
    Beta strandi494 – 5007

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KB3X-ray1.95B186-506[»]
    3NMTX-ray2.56B172-511[»]
    3QN1X-ray1.80B178-511[»]
    3RT0X-ray2.11A/B172-511[»]
    3UJGX-ray2.60B172-511[»]
    3ZVUX-ray2.10B178-511[»]
    4DS8X-ray2.21B169-511[»]
    4LA7X-ray1.98B178-505[»]
    4LG5X-ray2.88B172-511[»]
    4LGAX-ray2.70B172-511[»]
    4LGBX-ray3.15B172-511[»]
    ProteinModelPortaliQ9CAJ0.
    SMRiQ9CAJ0. Positions 180-510.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9CAJ0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini135 – 433299PP2C-likeAdd
    BLAST

    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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG0631.
    HOGENOMiHOG000233896.
    InParanoidiQ9CAJ0.
    KOiK14497.
    OMAiYARIENA.
    PhylomeDBiQ9CAJ0.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9CAJ0-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MEEMTPAVAM TLSLAANTMC ESSPVEITQL KNVTDAADLL SDSENQSFCN    50
    GGTECTMEDV SELEEVGEQD LLKTLSDTRS GSSNVFDEDD VLSVVEDNSA 100
    VISEGLLVVD AGSELSLSNT AMEIDNGRVL ATAIIVGESS IEQVPTAEVL 150
    IAGVNQDTNT SEVVIRLPDE NSNHLVKGRS VYELDCIPLW GTVSIQGNRS 200
    EMEDAFAVSP HFLKLPIKML MGDHEGMSPS LTHLTGHFFG VYDGHGGHKV 250
    ADYCRDRLHF ALAEEIERIK DELCKRNTGE GRQVQWDKVF TSCFLTVDGE 300
    IEGKIGRAVV GSSDKVLEAV ASETVGSTAV VALVCSSHIV VSNCGDSRAV 350
    LFRGKEAMPL SVDHKPDRED EYARIENAGG KVIQWQGARV FGVLAMSRSI 400
    GDRYLKPYVI PEPEVTFMPR SREDECLILA SDGLWDVMNN QEVCEIARRR 450
    ILMWHKKNGA PPLAERGKGI DPACQAAADY LSMLALQKGS KDNISIIVID 500
    LKAQRKFKTR T 511
    Length:511
    Mass (Da):55,744
    Last modified:June 1, 2001 - v1
    Checksum:iB001BAF0DD8333E1
    GO
    Isoform 2 (identifier: Q9CAJ0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         402-406: DRYLK → KHCFF
         407-511: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:406
    Mass (Da):43,866
    Checksum:i489298C9592A9F43
    GO

    Sequence cautioni

    The sequence BAH56780.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461Q → P in CAA05875. (PubMed:9862504)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei402 – 4065DRYLK → KHCFF in isoform 2. 1 PublicationVSP_034844
    Alternative sequencei407 – 511105Missing in isoform 2. 1 PublicationVSP_034845Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ003119 Genomic DNA. Translation: CAA05875.1.
    AC010926 Genomic DNA. Translation: AAG51849.1.
    CP002684 Genomic DNA. Translation: AEE35370.1.
    CP002684 Genomic DNA. Translation: AEE35371.1.
    CP002684 Genomic DNA. Translation: AEE35372.1.
    BT015409 mRNA. Translation: AAU05532.1.
    AK230171 mRNA. Translation: BAF01980.1.
    AK318665 mRNA. Translation: BAH56780.1. Different initiation.
    PIRiF96752.
    RefSeqiNP_001077815.1. NM_001084346.2. [Q9CAJ0-2]
    NP_001185385.1. NM_001198456.1. [Q9CAJ0-1]
    NP_177421.1. NM_105936.3. [Q9CAJ0-1]
    UniGeneiAt.46635.
    At.67356.

    Genome annotation databases

    EnsemblPlantsiAT1G72770.1; AT1G72770.1; AT1G72770. [Q9CAJ0-1]
    AT1G72770.3; AT1G72770.3; AT1G72770. [Q9CAJ0-1]
    GeneIDi843609.
    KEGGiath:AT1G72770.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ003119 Genomic DNA. Translation: CAA05875.1 .
    AC010926 Genomic DNA. Translation: AAG51849.1 .
    CP002684 Genomic DNA. Translation: AEE35370.1 .
    CP002684 Genomic DNA. Translation: AEE35371.1 .
    CP002684 Genomic DNA. Translation: AEE35372.1 .
    BT015409 mRNA. Translation: AAU05532.1 .
    AK230171 mRNA. Translation: BAF01980.1 .
    AK318665 mRNA. Translation: BAH56780.1 . Different initiation.
    PIRi F96752.
    RefSeqi NP_001077815.1. NM_001084346.2. [Q9CAJ0-2 ]
    NP_001185385.1. NM_001198456.1. [Q9CAJ0-1 ]
    NP_177421.1. NM_105936.3. [Q9CAJ0-1 ]
    UniGenei At.46635.
    At.67356.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3KB3 X-ray 1.95 B 186-506 [» ]
    3NMT X-ray 2.56 B 172-511 [» ]
    3QN1 X-ray 1.80 B 178-511 [» ]
    3RT0 X-ray 2.11 A/B 172-511 [» ]
    3UJG X-ray 2.60 B 172-511 [» ]
    3ZVU X-ray 2.10 B 178-511 [» ]
    4DS8 X-ray 2.21 B 169-511 [» ]
    4LA7 X-ray 1.98 B 178-505 [» ]
    4LG5 X-ray 2.88 B 172-511 [» ]
    4LGA X-ray 2.70 B 172-511 [» ]
    4LGB X-ray 3.15 B 172-511 [» ]
    ProteinModelPortali Q9CAJ0.
    SMRi Q9CAJ0. Positions 180-510.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 28828. 17 interactions.
    DIPi DIP-48988N.
    IntActi Q9CAJ0. 16 interactions.
    MINTi MINT-8299472.

    Proteomic databases

    PRIDEi Q9CAJ0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT1G72770.1 ; AT1G72770.1 ; AT1G72770 . [Q9CAJ0-1 ]
    AT1G72770.3 ; AT1G72770.3 ; AT1G72770 . [Q9CAJ0-1 ]
    GeneIDi 843609.
    KEGGi ath:AT1G72770.

    Organism-specific databases

    TAIRi AT1G72770.

    Phylogenomic databases

    eggNOGi COG0631.
    HOGENOMi HOG000233896.
    InParanoidi Q9CAJ0.
    KOi K14497.
    OMAi YARIENA.
    PhylomeDBi Q9CAJ0.

    Enzyme and pathway databases

    BioCyci ARA:AT1G72770-MONOMER.
    ARA:GQT-2826-MONOMER.
    ARA:GQT-408-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q9CAJ0.

    Gene expression databases

    Genevestigatori Q9CAJ0.

    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. "Molecular cloning in Arabidopsis thaliana of a new protein phosphatase 2C (PP2C) with homology to ABI1 and ABI2."
      Rodriguez P.L., Leube M.P., Grill E.
      Plant Mol. Biol. 38:879-883(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY, INDUCTION BY ABA.
      Strain: cv. Landsberg erecta.
    2. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
      Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
      , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
      Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Arabidopsis ORF clones."
      Cheuk R.F., Chen H., Kim C.J., Shinn P., Ecker J.R.
      Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: cv. Columbia.
    5. "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] (ISOFORM 2).
      Strain: cv. Columbia.
    6. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
      Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
      DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 148-511 (ISOFORM 1).
      Tissue: Rosette leaf.
    7. "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: FUNCTION, TISSUE SPECIFICITY, INDUCTION BY ABA.
    8. "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.
    9. "A hypermorphic mutation in the protein phosphatase 2C HAB1 strongly affects ABA signaling in Arabidopsis."
      Robert N., Merlot S., N'guyen V., Boisson-Dernier A., Schroeder J.I.
      FEBS Lett. 580:4691-4696(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF GLY-246.
    10. "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.
    11. "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.
    12. "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.
    13. "HAB1-SWI3B interaction reveals a link between abscisic acid signaling and putative SWI/SNF chromatin-remodeling complexes in Arabidopsis."
      Saez A., Rodrigues A., Santiago J., Rubio S., Rodriguez P.L.
      Plant Cell 20:2972-2988(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SWI3B, MUTAGENESIS OF GLY-246.
    14. "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.
    15. "Modulation of drought resistance by the abscisic acid receptor PYL5 through inhibition of clade A PP2Cs."
      Santiago J., Rodrigues A., Saez A., Rubio S., Antoni R., Dupeux F., Park S.-Y., Marquez J.A., Cutler S.R., Rodriguez P.L.
      Plant J. 60:575-588(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PYL5; PYL6 AND PYL8, MUTAGENESIS OF GLY-246.
    16. "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.
    17. Cited for: INTERACTION WITH PYR1; PYL1; PYL2; PYL3 AND PYL4, ENZYME REGULATION.
    18. Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 186-506 IN COMPLEX WITH ABSCISIC ACID AND PYL2, INTERACTION WITH PYR1; PYL1; PYL2; PYL3; PYL4; PYL5 AND PYL6, LOCK SITE.

    Entry informationi

    Entry nameiP2C16_ARATH
    AccessioniPrimary (citable) accession number: Q9CAJ0
    Secondary accession number(s): C0Z251, O81709, Q0WLM7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 22, 2008
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 102 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

    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