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Protein

CBL-interacting serine/threonine-protein kinase 24

Gene

CIPK24

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Mn2+1 Publication

Kineticsi

  1. KM=131.2 µM for synthetic substrate1 Publication
  1. 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

  • ATP binding Source: UniProtKB-KW
  • protein kinase activity Source: TAIR
  • protein serine/threonine kinase activity Source: GO_Central

GO - Biological processi

  • intracellular signal transduction Source: GO_Central
  • protein phosphorylation Source: GO_Central
  • response to salt stress Source: TAIR
Complete GO annotation...

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 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G35410.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: GO_Central
  • plant-type vacuole membrane Source: TAIR
Complete GO annotation...

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

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
Beta strandi11 – 133Combined sources
Beta strandi24 – 307Combined sources
Turni31 – 344Combined sources
Beta strandi35 – 439Combined sources
Helixi44 – 485Combined sources
Helixi53 – 6513Combined sources
Beta strandi77 – 793Combined sources
Beta strandi81 – 888Combined sources
Beta strandi92 – 954Combined sources
Helixi97 – 1037Combined sources
Helixi108 – 12720Combined sources
Turni137 – 1393Combined sources
Beta strandi140 – 1423Combined sources
Beta strandi148 – 1503Combined sources
Beta strandi173 – 1764Combined sources
Helixi178 – 1825Combined sources
Helixi188 – 20518Combined sources
Beta strandi212 – 2143Combined sources
Helixi215 – 22410Combined sources
Helixi235 – 24410Combined sources
Turni249 – 2513Combined sources
Helixi255 – 2606Combined sources
Helixi262 – 2654Combined sources
Helixi281 – 2866Combined sources
Helixi312 – 3165Combined sources
Turni320 – 3223Combined sources
Helixi324 – 3285Combined sources
Beta strandi340 – 3434Combined sources
Helixi347 – 36014Combined sources
Beta strandi363 – 37614Combined sources
Helixi381 – 3833Combined sources
Beta strandi386 – 39510Combined sources
Beta strandi398 – 40811Combined sources
Helixi410 – 42314Combined sources
Turni425 – 4273Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EHBX-ray2.10D304-446[»]
4D28X-ray3.30A/B/C/D1-446[»]
ProteinModelPortaliQ9LDI3.
SMRiQ9LDI3. Positions 7-289, 305-430.
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.
OMAiKTKIYII.
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.
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

        10         20         30         40         50
MTKKMRRVGK YEVGRTIGEG TFAKVKFARN TDTGDNVAIK IMAKSTILKN
60 70 80 90 100
RMVDQIKREI SIMKIVRHPN IVRLYEVLAS PSKIYIVLEF VTGGELFDRI
110 120 130 140 150
VHKGRLEESE SRKYFQQLVD AVAHCHCKGV YHRDLKPENL LLDTNGNLKV
160 170 180 190 200
SDFGLSALPQ EGVELLRTTC GTPNYVAPEV LSGQGYDGSA ADIWSCGVIL
210 220 230 240 250
FVILAGYLPF SETDLPGLYR KINAAEFSCP PWFSAEVKFL IHRILDPNPK
260 270 280 290 300
TRIQIQGIKK DPWFRLNYVP IRAREEEEVN LDDIRAVFDG IEGSYVAENV
310 320 330 340 350
ERNDEGPLMM NAFEMITLSQ GLNLSALFDR RQDFVKRQTR FVSRREPSEI
360 370 380 390 400
IANIEAVANS MGFKSHTRNF KTRLEGLSSI KAGQLAVVIE IYEVAPSLFM
410 420 430 440
VDVRKAAGET LEYHKFYKKL CSKLENIIWR ATEGIPKSEI LRTITF
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. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EHBX-ray2.10D304-446[»]
4D28X-ray3.30A/B/C/D1-446[»]
ProteinModelPortaliQ9LDI3.
SMRiQ9LDI3. Positions 7-289, 305-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiQ9LDI3.
PRIDEiQ9LDI3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT5G35410.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233016.
InParanoidiQ9LDI3.
OMAiKTKIYII.
PhylomeDBiQ9LDI3.

Enzyme and pathway databases

BioCyciARA:AT5G35410-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9LDI3.
PROiQ9LDI3.

Gene expression databases

GenevestigatoriQ9LDI3.

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.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 29, 2015
This is version 116 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.