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Protein

CBL-interacting serine/threonine-protein kinase 14

Gene

CIPK14

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

Functioni

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 (By similarity).By similarity

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511ATPPROSITE-ProRule annotation
Active sitei144 – 1441Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi28 – 369ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Manganese, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT5G01820-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
CBL-interacting serine/threonine-protein kinase 14 (EC:2.7.11.1)
Alternative name(s):
SNF1-related kinase 3.15
SOS2-like protein kinase PKS24
Serine/threonine-protein kinase SR1
Short name:
AtSR1
Gene namesi
Name:CIPK14
Synonyms:PKS24, SnRK3.15, SR1
Ordered Locus Names:At5g01820
ORF Names:T20L15.90
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G01820.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

  • Note: Targeted to the tonoplast when interacting with CBL2 or CBL3 and to the cell membrane when interacting with CBL8.

GO - Cellular componenti

  • nucleus Source: UniProtKB-SubCell
  • plasmodesma Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi311 – 3111N → A: No effect on binding to CBL2. 1 Publication
Mutagenesisi313 – 3131F → A: Loss of binding to CBL2. 1 Publication
Mutagenesisi316 – 3161I → A: No effect on binding to CBL2. 1 Publication
Mutagenesisi319 – 3191S → A or D: No effect on binding to CBL2. 1 Publication
Mutagenesisi322 – 3221F → A: Loss of binding to CBL2. 1 Publication
Mutagenesisi324 – 3241L → A: No effect on binding to CBL2.
Mutagenesisi327 – 3271L → A: No effect on binding to CBL2. 1 Publication
Mutagenesisi328 – 3281F → A: No effect on binding to CBL2. 1 Publication
Mutagenesisi336 – 3361R → A: No effect on binding to CBL2.
Mutagenesisi339 – 3391R → A: No effect on binding to CBL2. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 442442CBL-interacting serine/threonine-protein kinase 14PRO_0000337216Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei166 – 1661PhosphoserineBy similarity
Modified residuei180 – 1801PhosphothreonineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9LZW4.
PRIDEiQ9LZW4.

PTM databases

iPTMnetiQ9LZW4.

Expressioni

Tissue specificityi

Predominant in roots, cauline leaves, and flowers.1 Publication

Developmental stagei

First observed in imbibed seeds. Mostly localized in hypocotyls during germination and in seedlings. In mature plants, confined to vascular tissues of leaves and roots. In flowers, expressed in the vascular bundle of the stamen filament and in the stigma, where the filament joins the pistil.1 Publication

Inductioni

By light in a cytokinin-dependent manner and N(6)-benzylaminopurine (BA). Also induced by sucrose, glucose and fructose.2 Publications

Gene expression databases

GenevisibleiQ9LZW4. AT.

Interactioni

Subunit structurei

Interacts with CBL2,CBL3 and CBL8.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBL2Q8LAS79EBI-307576,EBI-485991

Protein-protein interaction databases

BioGridi17041. 48 interactions.
IntActiQ9LZW4. 13 interactions.
STRINGi3702.AT5G01820.1.

Structurei

Secondary structure

1
442
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi312 – 3176Combined sources
Beta strandi322 – 3243Combined sources
Helixi325 – 3317Combined sources
Beta strandi338 – 3447Combined sources
Helixi346 – 35914Combined sources
Beta strandi363 – 3686Combined sources
Beta strandi371 – 3766Combined sources
Helixi377 – 3793Combined sources
Beta strandi381 – 3899Combined sources
Beta strandi391 – 3933Combined sources
Beta strandi395 – 40410Combined sources
Helixi412 – 4154Combined sources
Helixi417 – 4237Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZFDX-ray1.20B305-427[»]
ProteinModelPortaliQ9LZW4.
SMRiQ9LZW4. Positions 20-426.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9LZW4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 276255Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini305 – 32925NAFPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni162 – 19130Activation loopBy similarityAdd
BLAST
Regioni335 – 36531PPIBy similarityAdd
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 (By similarity).By similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0583. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000233016.
InParanoidiQ9LZW4.
OMAiEIAIMHR.
PhylomeDBiQ9LZW4.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR018451. NAF/FISL_domain.
IPR004041. NAF_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
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.

Q9LZW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDSDPVEFP PENRRGQLFG KYEVGKLVGC GAFAKVYHGR STATGQSVAI
60 70 80 90 100
KVVSKQRLQK GGLNGNIQRE IAIMHRLRHP SIVRLFEVLA TKSKIFFVME
110 120 130 140 150
FAKGGELFAK VSKGRFCEDL SRRYFQQLIS AVGYCHSRGI FHRDLKPENL
160 170 180 190 200
LLDEKLDLKI SDFGLSALTD QIRPDGLLHT LCGTPAYVAP EVLAKKGYDG
210 220 230 240 250
AKIDIWSCGI ILFVLNAGYL PFNDHNLMVM YRKIYKGEFR IPKWTSPDLR
260 270 280 290 300
RLLTRLLDTN PQTRITIEEI IHDPWFKQGY DDRMSKFHLE DSDMKLPADE
310 320 330 340 350
TDSEMGARRM NAFDIISGSP GFNLSGLFGD ARKYDRVERF VSAWTAERVV
360 370 380 390 400
ERLEEIVSAE NLTVAKKETW GMKIEGQKGN FAMVVEINQL TDELVMIEVR
410 420 430 440
KRQRAAASGR DLWTDTLRPF FVELVHESDQ TDPEPTQVHT TS
Length:442
Mass (Da):50,298
Last modified:October 1, 2000 - v1
Checksum:i319532FEFB7244C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF295669 mRNA. Translation: AAK16689.1.
AB035147 mRNA. Translation: BAB11737.1.
AL162351 Genomic DNA. Translation: CAB82752.1.
CP002688 Genomic DNA. Translation: AED90397.1.
AF360189 mRNA. Translation: AAK25899.1.
AY142684 mRNA. Translation: AAN13222.1.
PIRiT48203.
RefSeqiNP_195802.1. NM_120260.2.
UniGeneiAt.23738.

Genome annotation databases

EnsemblPlantsiAT5G01820.1; AT5G01820.1; AT5G01820.
GeneIDi831765.
GrameneiAT5G01820.1; AT5G01820.1; AT5G01820.
KEGGiath:AT5G01820.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF295669 mRNA. Translation: AAK16689.1.
AB035147 mRNA. Translation: BAB11737.1.
AL162351 Genomic DNA. Translation: CAB82752.1.
CP002688 Genomic DNA. Translation: AED90397.1.
AF360189 mRNA. Translation: AAK25899.1.
AY142684 mRNA. Translation: AAN13222.1.
PIRiT48203.
RefSeqiNP_195802.1. NM_120260.2.
UniGeneiAt.23738.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZFDX-ray1.20B305-427[»]
ProteinModelPortaliQ9LZW4.
SMRiQ9LZW4. Positions 20-426.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi17041. 48 interactions.
IntActiQ9LZW4. 13 interactions.
STRINGi3702.AT5G01820.1.

PTM databases

iPTMnetiQ9LZW4.

Proteomic databases

PaxDbiQ9LZW4.
PRIDEiQ9LZW4.

Protocols and materials databases

DNASUi831765.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G01820.1; AT5G01820.1; AT5G01820.
GeneIDi831765.
GrameneiAT5G01820.1; AT5G01820.1; AT5G01820.
KEGGiath:AT5G01820.

Organism-specific databases

TAIRiAT5G01820.

Phylogenomic databases

eggNOGiKOG0583. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000233016.
InParanoidiQ9LZW4.
OMAiEIAIMHR.
PhylomeDBiQ9LZW4.

Enzyme and pathway databases

BioCyciARA:AT5G01820-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9LZW4.
PROiQ9LZW4.

Gene expression databases

GenevisibleiQ9LZW4. AT.

Family and domain databases

InterProiIPR020636. Ca/CaM-dep_Ca-dep_prot_Kinase.
IPR011009. Kinase-like_dom.
IPR018451. NAF/FISL_domain.
IPR004041. NAF_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PANTHERiPTHR24347. PTHR24347. 1 hit.
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 NAF domain defines a novel protein-protein interaction module conserved in Ca(2+)-regulated kinases."
    Albrecht V., Ritz O., Linder S., Harter K., Kudla J.
    EMBO J. 20:1051-1063(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Two novel genes encoding SNF-1 related protein kinases from Arabidopsis thaliana: differential accumulation of AtSR1 and AtSR2 transcripts in response to cytokinins and sugars, and phosphorylation of sucrose synthase by AtSR2."
    Chikano H., Ogawa M., Ikeda Y., Koizumi N., Kusano T., Sano H.
    Mol. Gen. Genet. 264:674-681(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
    Strain: cv. Columbia.
  3. "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.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "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.
  6. "An Arabidopsis SNF1-related protein kinase, AtSR1, interacts with a calcium-binding protein, AtCBL2, of which transcripts respond to light."
    Nozawa A., Koizumi N., Sano H.
    Plant Cell Physiol. 42:976-981(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBL2, TISSUE SPECIFICITY.
  7. Cited for: GENE FAMILY, NOMENCLATURE.
  8. "Sugar responsible and tissue specific expression of a gene encoding AtCIPK14, an Arabidopsis CBL-interacting protein kinase."
    Lee E.-J., Iai H., Sano H., Koizumi N.
    Biosci. Biotechnol. Biochem. 69:242-245(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, DEVELOPMENTAL STAGE.
  9. "CBL-mediated targeting of CIPKs facilitates the decoding of calcium signals emanating from distinct cellular stores."
    Batistic O., Waadt R., Steinhorst L., Held K., Kudla J.
    Plant J. 61:211-222(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CBL2; CBL3 AND CBL8.
  10. "The crystal structure of plant-specific calcium-binding protein AtCBL2 in complex with the regulatory domain of AtCIPK14."
    Akaboshi M., Hashimoto H., Ishida H., Saijo S., Koizumi N., Sato M., Shimizu T.
    J. Mol. Biol. 377:246-257(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 305-427 IN COMPLEX WITH CBL2, MUTAGENESIS OF ASN-311; PHE-313; ILE-316; SER-319; PHE-322; LEU-327; PHE-328 AND ARG-339.

Entry informationi

Entry nameiCIPKE_ARATH
AccessioniPrimary (citable) accession number: Q9LZW4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 119 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

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 one 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.