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Protein

CBL-interacting serine/threonine-protein kinase 7

Gene

CIPK7

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). Phosphorylates the rice sucrose synthase (SuSy) in vitro in an allosteric manner. Involved in cold response.By similarity2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Cofactori

Mn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541ATPPROSITE-ProRule annotation
Active sitei149 – 1491Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi31 – 399ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • intracellular signal transduction Source: GO_Central
  • protein phosphorylation Source: GO_Central
  • response to cold 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:AT3G23000-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
CBL-interacting serine/threonine-protein kinase 7 (EC:2.7.11.1)
Alternative name(s):
SNF1-related kinase 3.10
SOS2-like protein kinase PKS7
Serine/threonine-protein kinase SR2
Short name:
AtSR2
Short name:
AtSRPK1
Gene namesi
Name:CIPK7
Synonyms:PKS7, SnRK3.10, SR2, SRPK1
Ordered Locus Names:At3g23000
ORF Names:MXC7.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G23000.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429CBL-interacting serine/threonine-protein kinase 7PRO_0000337210Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei171 – 1711PhosphoserineBy similarity
Modified residuei184 – 1841PhosphothreonineBy similarity

Post-translational modificationi

Autophosphorylated.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9XIW0.
PRIDEiQ9XIW0.

Expressioni

Tissue specificityi

Strongly expressed in leaves, but barely expressed in roots, stems or flowers.2 Publications

Inductioni

By sucrose, glucose and fructose. Repressed in roots by salt stress. Up-regulated by cold stress.3 Publications

Gene expression databases

GenevisibleiQ9XIW0. AT.

Interactioni

Subunit structurei

Interacts with CBL1, CBL2 and CBL3.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CBL1O814453EBI-1765255,EBI-974530

Protein-protein interaction databases

BioGridi7206. 7 interactions.
IntActiQ9XIW0. 6 interactions.
STRINGi3702.AT3G23000.1.

Structurei

3D structure databases

ProteinModelPortaliQ9XIW0.
SMRiQ9XIW0. Positions 22-421.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 280256Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini302 – 32625NAFPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni167 – 19529Activation loopBy similarityAdd
BLAST
Regioni330 – 36334PPIBy 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.
InParanoidiQ9XIW0.
OMAiEILEVAM.
PhylomeDBiQ9XIW0.

Family and domain databases

InterProiIPR011009. 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]
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.

Q9XIW0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESLPQPQNQ SSPATTPAKI LLGKYELGRR LGSGSFAKVH LARSIESDEL
60 70 80 90 100
VAVKIIEKKK TIESGMEPRI IREIDAMRRL RHHPNILKIH EVMATKSKIY
110 120 130 140 150
LVMELASGGE LFSKVLRRGR LPESTARRYF QQLASALRFS HQDGVAHRDV
160 170 180 190 200
KPQNLLLDEQ GNLKVSDFGL SALPEHLQNG LLHTACGTPA YTAPEVISRR
210 220 230 240 250
GYDGAKADAW SCGVILFVLL VGDVPFDDSN IAAMYRKIHR RDYRFPSWIS
260 270 280 290 300
KQAKSIIYQM LDPNPVTRMS IETVMKTNWF KKSLETSEFH RNVFDSEVEM
310 320 330 340 350
KSSVNSITAF DLISLSSGLD LSGLFEAKKK KERRFTAKVS GVEVEEKAKM
360 370 380 390 400
IGEKLGYVVK KKMMKKEGEV KVVGLGRGRT VIVVEAVELT VDVVVVEVKV
410 420
VEGEEDDSRW SDLITELEDI VLSWHNDIM
Length:429
Mass (Da):48,266
Last modified:November 1, 1999 - v1
Checksum:i5D6703058ACF4A75
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251Y → H in BAB11738 (PubMed:11212922).Curated
Sequence conflicti224 – 2241V → A in AAK96877 (PubMed:14593172).Curated
Sequence conflicti336 – 3361T → P in AAK96877 (PubMed:14593172).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF290192 mRNA. Translation: AAK16682.1.
AB035148 mRNA. Translation: BAB11738.1.
AB027153 mRNA. Translation: BAA77716.2.
AF339148 mRNA. Translation: AAK26846.1.
AB026655 Genomic DNA. Translation: BAB02091.1.
CP002686 Genomic DNA. Translation: AEE76704.1.
AY054686 mRNA. Translation: AAK96877.1.
BT020492 mRNA. Translation: AAW38993.1.
BT028967 mRNA. Translation: ABI54342.1.
RefSeqiNP_188940.1. NM_113200.2.
UniGeneiAt.389.
At.71615.

Genome annotation databases

EnsemblPlantsiAT3G23000.1; AT3G23000.1; AT3G23000.
GeneIDi821874.
GrameneiAT3G23000.1; AT3G23000.1; AT3G23000.
KEGGiath:AT3G23000.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF290192 mRNA. Translation: AAK16682.1.
AB035148 mRNA. Translation: BAB11738.1.
AB027153 mRNA. Translation: BAA77716.2.
AF339148 mRNA. Translation: AAK26846.1.
AB026655 Genomic DNA. Translation: BAB02091.1.
CP002686 Genomic DNA. Translation: AEE76704.1.
AY054686 mRNA. Translation: AAK96877.1.
BT020492 mRNA. Translation: AAW38993.1.
BT028967 mRNA. Translation: ABI54342.1.
RefSeqiNP_188940.1. NM_113200.2.
UniGeneiAt.389.
At.71615.

3D structure databases

ProteinModelPortaliQ9XIW0.
SMRiQ9XIW0. Positions 22-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi7206. 7 interactions.
IntActiQ9XIW0. 6 interactions.
STRINGi3702.AT3G23000.1.

Proteomic databases

PaxDbiQ9XIW0.
PRIDEiQ9XIW0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G23000.1; AT3G23000.1; AT3G23000.
GeneIDi821874.
GrameneiAT3G23000.1; AT3G23000.1; AT3G23000.
KEGGiath:AT3G23000.

Organism-specific databases

TAIRiAT3G23000.

Phylogenomic databases

eggNOGiKOG0583. Eukaryota.
COG0515. LUCA.
HOGENOMiHOG000233016.
InParanoidiQ9XIW0.
OMAiEILEVAM.
PhylomeDBiQ9XIW0.

Enzyme and pathway databases

BioCyciARA:AT3G23000-MONOMER.

Miscellaneous databases

PROiQ9XIW0.

Gene expression databases

GenevisibleiQ9XIW0. AT.

Family and domain databases

InterProiIPR011009. 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]
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], INTERACTION WITH CBL2 AND CBL3.
  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], FUNCTION, AUTOPHOSPHORYLATION, INDUCTION.
    Strain: cv. Columbia.
  3. "Arabidopsis thaliana mRNA for a novel SNF1 related protein kinase (ATSRPK1), partial cds."
    Nanmori T., Matsuoka D., Kono T.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: cv. Columbia.
  5. "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.
    DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  6. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  7. "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.
  8. "Arabidopsis ORF clones."
    Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.
    Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  9. Cited for: GENE FAMILY, NOMENCLATURE.
  10. "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.
  11. "CIPK7 is involved in cold response by interacting with CBL1 in Arabidopsis thaliana."
    Huang C., Ding S., Zhang H., Du H., An L.
    Plant Sci. 181:57-64(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CBL1, INDUCTION BY COLD, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCIPK7_ARATH
AccessioniPrimary (citable) accession number: Q9XIW0
Secondary accession number(s): Q93Y18, Q9FZN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 1, 1999
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

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. 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.