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Q9LDI3

- CIPKO_ARATH

UniProt

Q9LDI3 - CIPKO_ARATH

Protein

CBL-interacting serine/threonine-protein kinase 24

Gene

CIPK24

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 110 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Involved in the regulatory pathway for the control of intracellular Na+ and K+ homeostasis and salt tolerance. Activates the vacuolar H+/Ca2+ antiporter CAX1 and operates in synergy with CBL4/SOS3 to activate the plasma membrane Na+/H+ antiporter SOS1. CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner. Phosphorylates CBL1, CBL4 and CBL10.4 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Cofactori

    Manganese.1 Publication

    Kineticsi

    1. KM=131.2 µM for synthetic substrate1 Publication

    Vmax=1304 pmol/min/mg enzyme1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei40 – 401ATPPROSITE-ProRule annotation
    Active sitei134 – 1341Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi17 – 259ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. protein kinase activity Source: TAIR
    4. protein serine/threonine kinase activity Source: UniProtKB-KW

    GO - Biological processi

    1. response to salt stress Source: TAIR
    2. signal transduction Source: InterPro

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Manganese, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciARA:AT5G35410-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    CBL-interacting serine/threonine-protein kinase 24 (EC:2.7.11.1)
    Alternative name(s):
    Protein SALT OVERLY SENSITIVE 2
    SNF1-related kinase 3.11
    Gene namesi
    Name:CIPK24
    Synonyms:SnRK3.11, SOS2
    Ordered Locus Names:At5g35410
    ORF Names:F6I13.1, K21B8.3
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 5

    Organism-specific databases

    TAIRiAT5G35410.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Targeted to the cell membrane when interacting with CBL1 or CBL5 and to the tonoplast when interacting with CBL2 orCBL10.

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell
    2. plant-type vacuole membrane Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi40 – 401K → N: Abolishes autophosphorylation. 1 Publication
    Mutagenesisi156 – 1561S → D: Increases kinase activity. 1 Publication
    Mutagenesisi168 – 1681T → D: Increases kinase activity. 1 Publication
    Mutagenesisi175 – 1751Y → D: Increases kinase activity. 1 Publication
    Mutagenesisi197 – 1971G → E: Abolishes autophosphorylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 446446CBL-interacting serine/threonine-protein kinase 24PRO_0000085877Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei156 – 1561PhosphoserineBy similarity
    Modified residuei168 – 1681PhosphothreonineBy similarity
    Modified residuei169 – 1691PhosphothreonineBy similarity

    Post-translational modificationi

    Autophosphorylated.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9LDI3.
    PRIDEiQ9LDI3.

    Expressioni

    Inductioni

    Up-regulated in roots by salt stress.

    Gene expression databases

    GenevestigatoriQ9LDI3.

    Interactioni

    Subunit structurei

    Interacts with CBL1, CBL2, CBL4/SOS3, CBL5, CBL9, CBL10 and with the protein phosphatase 2C ABI2.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABI2O047194EBI-537551,EBI-537680
    CAM4P258542EBI-537551,EBI-1235664
    CAM7P592202EBI-537551,EBI-1236031
    CBL1O814453EBI-537551,EBI-974530
    CBL10Q7FRS85EBI-537551,EBI-2026616
    CBL10Q7FRS8-24EBI-537551,EBI-2026677
    CBL4O812239EBI-537551,EBI-537541
    CML9Q9S7442EBI-537551,EBI-1236048
    NDPK2O649033EBI-537551,EBI-349517

    Protein-protein interaction databases

    BioGridi18756. 20 interactions.
    DIPiDIP-34745N.
    IntActiQ9LDI3. 30 interactions.
    MINTiMINT-274819.
    STRINGi3702.AT5G35410.1-P.

    Structurei

    Secondary structure

    1
    446
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi312 – 3165
    Turni320 – 3223
    Helixi324 – 3285
    Beta strandi340 – 3434
    Helixi347 – 36014
    Beta strandi363 – 37614
    Helixi381 – 3833
    Beta strandi386 – 39510
    Beta strandi398 – 40811
    Helixi410 – 42314
    Turni425 – 4273

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EHBX-ray2.10D304-446[»]
    ProteinModelPortaliQ9LDI3.
    SMRiQ9LDI3. Positions 6-430.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9LDI3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 264254Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini305 – 32925NAFPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni152 – 17928Activation loopAdd
    BLAST
    Regioni336 – 36530PPIAdd
    BLAST

    Domaini

    The activation loop within the kinase domain is the target of phosphorylation/activation by upstream protein kinases. The PPI motif mediates the interaction with the ABI (abscisic acid-insensitive) phosphatases. The C-terminal part (309-446) of the protein is required for the phosphorylation of CBL, but is not involved in autophosphorylation.1 Publication

    Sequence similaritiesi

    Contains 1 NAF domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233016.
    InParanoidiQ9LDI3.
    OMAiNAFEMIT.
    PhylomeDBiQ9LDI3.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR018451. NAF/FISL_domain.
    IPR004041. NAF_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF03822. NAF. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50816. NAF. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9LDI3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTKKMRRVGK YEVGRTIGEG TFAKVKFARN TDTGDNVAIK IMAKSTILKN    50
    RMVDQIKREI SIMKIVRHPN IVRLYEVLAS PSKIYIVLEF VTGGELFDRI 100
    VHKGRLEESE SRKYFQQLVD AVAHCHCKGV YHRDLKPENL LLDTNGNLKV 150
    SDFGLSALPQ EGVELLRTTC GTPNYVAPEV LSGQGYDGSA ADIWSCGVIL 200
    FVILAGYLPF SETDLPGLYR KINAAEFSCP PWFSAEVKFL IHRILDPNPK 250
    TRIQIQGIKK DPWFRLNYVP IRAREEEEVN LDDIRAVFDG IEGSYVAENV 300
    ERNDEGPLMM NAFEMITLSQ GLNLSALFDR RQDFVKRQTR FVSRREPSEI 350
    IANIEAVANS MGFKSHTRNF KTRLEGLSSI KAGQLAVVIE IYEVAPSLFM 400
    VDVRKAAGET LEYHKFYKKL CSKLENIIWR ATEGIPKSEI LRTITF 446
    Length:446
    Mass (Da):50,635
    Last modified:October 1, 2000 - v1
    Checksum:i99FDF3A778E1093D
    GO

    Sequence cautioni

    The sequence AAF67384.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF237670 Genomic DNA. Translation: AAF62923.1.
    AF395081 mRNA. Translation: AAK72257.1.
    AB025611 Genomic DNA. Translation: BAA98146.1.
    AF262044 Genomic DNA. Translation: AAF67384.1. Sequence problems.
    CP002688 Genomic DNA. Translation: AED93966.1.
    AY099621 mRNA. Translation: AAM20472.1.
    BT002138 mRNA. Translation: AAN72149.1.
    RefSeqiNP_198391.1. NM_122932.4.
    UniGeneiAt.7930.

    Genome annotation databases

    EnsemblPlantsiAT5G35410.1; AT5G35410.1; AT5G35410.
    GeneIDi833502.
    KEGGiath:AT5G35410.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF237670 Genomic DNA. Translation: AAF62923.1 .
    AF395081 mRNA. Translation: AAK72257.1 .
    AB025611 Genomic DNA. Translation: BAA98146.1 .
    AF262044 Genomic DNA. Translation: AAF67384.1 . Sequence problems.
    CP002688 Genomic DNA. Translation: AED93966.1 .
    AY099621 mRNA. Translation: AAM20472.1 .
    BT002138 mRNA. Translation: AAN72149.1 .
    RefSeqi NP_198391.1. NM_122932.4.
    UniGenei At.7930.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EHB X-ray 2.10 D 304-446 [» ]
    ProteinModelPortali Q9LDI3.
    SMRi Q9LDI3. Positions 6-430.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 18756. 20 interactions.
    DIPi DIP-34745N.
    IntActi Q9LDI3. 30 interactions.
    MINTi MINT-274819.
    STRINGi 3702.AT5G35410.1-P.

    Proteomic databases

    PaxDbi Q9LDI3.
    PRIDEi Q9LDI3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT5G35410.1 ; AT5G35410.1 ; AT5G35410 .
    GeneIDi 833502.
    KEGGi ath:AT5G35410.

    Organism-specific databases

    TAIRi AT5G35410.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233016.
    InParanoidi Q9LDI3.
    OMAi NAFEMIT.
    PhylomeDBi Q9LDI3.

    Enzyme and pathway databases

    BioCyci ARA:AT5G35410-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q9LDI3.

    Gene expression databases

    Genevestigatori Q9LDI3.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR018451. NAF/FISL_domain.
    IPR004041. NAF_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF03822. NAF. 1 hit.
    PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS50816. NAF. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The Arabidopsis thaliana SOS2 gene encodes a protein kinase that is required for salt tolerance."
      Liu J., Ishitani M., Halfter U., Kim C.-S., Zhu J.-K.
      Proc. Natl. Acad. Sci. U.S.A. 97:3730-3734(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, MUTAGENESIS OF LYS-40 AND GLY-197.
      Strain: cv. Columbia.
    2. "Molecular characterization of the CIPK gene family from Arabidopsis thaliana."
      Weinl S., Albrecht V., Kudla J.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Structural analysis of Arabidopsis thaliana chromosome 5. XI."
      Kaneko T., Katoh T., Asamizu E., Sato S., Nakamura Y., Kotani H., Tabata S.
      Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    4. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
      Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
      , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
      Nature 408:823-826(2000) [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. "The Arabidopsis SOS2 protein kinase physically interacts with and is activated by the calcium-binding protein SOS3."
      Halfter U., Ishitani M., Zhu J.-K.
      Proc. Natl. Acad. Sci. U.S.A. 97:3735-3740(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CBL4, MUTAGENESIS OF THR-168.
    8. "Molecular characterization of functional domains in the protein kinase SOS2 that is required for plant salt tolerance."
      Guo Y., Halfter U., Ishitani M., Zhu J.-K.
      Plant Cell 13:1383-1400(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVATION DOMAINS.
    9. "Regulation of SOS1, a plasma membrane Na(+)/H(+) exchanger in Arabidopsis thaliana, by SOS2 and SOS3."
      Qiu Q.-S., Guo Y., Dietrich M.A., Schumaker K.S., Zhu J.-K.
      Proc. Natl. Acad. Sci. U.S.A. 99:8436-8441(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Biochemical characterization of the Arabidopsis protein kinase SOS2 that functions in salt tolerance."
      Gong D., Guo Y., Jagendorf A.T., Zhu J.-K.
      Plant Physiol. 130:256-264(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF SER-156 AND TYR-175.
    11. "A novel domain in the protein kinase SOS2 mediates interaction with the protein phosphatase 2C ABI2."
      Ohta M., Guo Y., Halfter U., Zhu J.-K.
      Proc. Natl. Acad. Sci. U.S.A. 100:11771-11776(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ABI2.
    12. Cited for: GENE FAMILY, NOMENCLATURE.
    13. "The protein kinase SOS2 activates the Arabidopsis H(+)/Ca(2+) antiporter CAX1 to integrate calcium transport and salt tolerance."
      Cheng N.-H., Pittman J.K., Zhu J.-K., Hirschi K.D.
      J. Biol. Chem. 279:2922-2926(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "Calcium sensors and their interacting protein kinases: genomics of the Arabidopsis and rice CBL-CIPK signaling networks."
      Kolukisaoglu U., Weinl S., Blazevic D., Batistic O., Kudla J.
      Plant Physiol. 134:43-58(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBL1 AND CBL9.
    15. "The calcium sensor CBL10 mediates salt tolerance by regulating ion homeostasis in Arabidopsis."
      Kim B.G., Waadt R., Cheong Y.H., Pandey G.K., Dominguez-Solis J.R., Schueltke S., Lee S.C., Kudla J., Luan S.
      Plant J. 52:473-484(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBL1; CBL2; CBL5 AND CBL10, SUBCELLULAR LOCATION.
    16. "Phosphorylation of calcineurin B-like (CBL) calcium sensor proteins by their CBL-interacting protein kinases (CIPKs) is required for full activity of CBL-CIPK complexes toward their target proteins."
      Hashimoto K., Eckert C., Anschuetz U., Scholz M., Held K., Waadt R., Reyer A., Hippler M., Becker D., Kudla J.
      J. Biol. Chem. 287:7956-7968(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION, INTERACTION WITH CBL1; CBL4 AND CBL10, DOMAIN.
    17. "The structure of the C-terminal domain of the protein kinase AtSOS2 bound to the calcium sensor AtSOS3."
      Sanchez-Barrena M.J., Fujii H., Angulo I., Martinez-Ripoll M., Zhu J.-K., Albert A.
      Mol. Cell 26:427-435(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 304-446 IN COMPLEX WITH SOS3, INTERACTION WITH SOS3 AND ABI2.

    Entry informationi

    Entry nameiCIPKO_ARATH
    AccessioniPrimary (citable) accession number: Q9LDI3
    Secondary accession number(s): Q9LKR2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 21, 2004
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 110 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