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Protein

Calcium-dependent protein kinase 11

Gene

CPK11

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

Functioni

May play a role in signal transduction pathways that involve calcium as a second messenger. Functions as regulator of the calcium-mediated abscisic acid (ABA) signaling pathway. Phosphorylates ABA-responsive transcription factors ABF1 and ABF4 in vitro.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Activated by calcium. Autophosphorylation may play an important role in the regulation of the kinase activity (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei55 – 551ATPPROSITE-ProRule annotation
Active sitei150 – 1501Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi32 – 409ATPPROSITE-ProRule annotation
Calcium bindingi340 – 351121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi376 – 387122PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi412 – 423123PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi446 – 457124PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium ion binding Source: InterPro
  3. calmodulin-dependent protein kinase activity Source: TAIR
  4. protein kinase activity Source: TAIR
  5. protein serine/threonine kinase activity Source: TAIR

GO - Biological processi

  1. positive regulation of abscisic acid-activated signaling pathway Source: TAIR
  2. protein autophosphorylation Source: TAIR
  3. protein phosphorylation Source: TAIR
  4. regulation of inward rectifier potassium channel activity Source: TAIR
  5. regulation of pollen tube growth Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, Calcium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciARA:AT1G35670-MONOMER.
ReactomeiREACT_184938. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_190945. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_190953. Tristetraprolin (TTP) destabilizes mRNA.
REACT_220111. Regulation of HSF1-mediated heat shock response.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-dependent protein kinase 11 (EC:2.7.11.1)
Alternative name(s):
Calcium-dependent protein kinase isoform CDPK2
Short name:
AtCDPK2
Gene namesi
Name:CPK11
Synonyms:CDPK2
Ordered Locus Names:At1g35670
ORF Names:F15O4.8
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G35670.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: TAIR
  2. nucleus Source: TAIR
  3. plasma membrane Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mutant cpk11-2 shows reduced ABA and salt responsiveness in seed germination.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi150 – 1501D → A: Loss of activity. 1 Publication
Mutagenesisi171 – 1711D → A: Loss of activity. 1 Publication
Mutagenesisi306 – 3061F → A: Constitutive activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495Calcium-dependent protein kinase 11PRO_0000304513Add
BLAST

Proteomic databases

PaxDbiQ39016.
PRIDEiQ39016.

Expressioni

Inductioni

By drought and high-slat stress, but not by low-temperature, heat stress or abscisic acid treatment.1 Publication

Gene expression databases

ExpressionAtlasiQ39016. baseline and differential.
GenevestigatoriQ39016.

Interactioni

Subunit structurei

Interacts with Di19.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ADF3Q9ZSK45EBI-979321,EBI-2009725
At1g52740Q9C9449EBI-979321,EBI-1537419
At3g26510Q27GK55EBI-979321,EBI-2297208
At5g52550Q940C26EBI-979321,EBI-2298422
BT2Q94BN07EBI-979321,EBI-540986
CHLPQ9CA675EBI-979321,EBI-2298544
DI19-1Q3908325EBI-979321,EBI-979339
dl3455wO233386EBI-979321,EBI-2296482
F5I14.18O044824EBI-979321,EBI-2298606
MTACP2O808004EBI-979321,EBI-2298689
TOC33O236804EBI-979321,EBI-639377

Protein-protein interaction databases

BioGridi25703. 26 interactions.
IntActiQ39016. 24 interactions.
MINTiMINT-1788888.

Structurei

3D structure databases

ProteinModelPortaliQ39016.
SMRiQ39016. Positions 22-488.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 284259Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini327 – 36236EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini363 – 39836EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini399 – 43436EF-hand 3PROSITE-ProRule annotationAdd
BLAST
Domaini435 – 46834EF-hand 4PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni290 – 32031Autoinhibitory domainBy similarityAdd
BLAST

Domaini

There is 3 contiguous domains conserved in the CDPK subfamily: a kinase domain, an autoinhibitory (junction) domain and a calmodulin-like domain. The autoinhibitory domain (290-320) inactivates kinase activity under calcium-free conditions (By similarity).By similarity

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. CDPK subfamily.PROSITE-ProRule annotation
Contains 4 EF-hand domains.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233030.
InParanoidiQ39016.
KOiK13412.
OMAiTVLPYQT.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13499. EF-hand_7. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q39016-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
METKPNPRRP SNTVLPYQTP RLRDHYLLGK KLGQGQFGTT YLCTEKSTSA
60 70 80 90 100
NYACKSIPKR KLVCREDYED VWREIQIMHH LSEHPNVVRI KGTYEDSVFV
110 120 130 140 150
HIVMEVCEGG ELFDRIVSKG HFSEREAVKL IKTILGVVEA CHSLGVMHRD
160 170 180 190 200
LKPENFLFDS PKDDAKLKAT DFGLSVFYKP GQYLYDVVGS PYYVAPEVLK
210 220 230 240 250
KCYGPEIDVW SAGVILYILL SGVPPFWAET ESGIFRQILQ GKLDFKSDPW
260 270 280 290 300
PTISEAAKDL IYKMLERSPK KRISAHEALC HPWIVDEQAA PDKPLDPAVL
310 320 330 340 350
SRLKQFSQMN KIKKMALRVI AERLSEEEIG GLKELFKMID TDNSGTITFE
360 370 380 390 400
ELKAGLKRVG SELMESEIKS LMDAADIDNS GTIDYGEFLA ATLHMNKMER
410 420 430 440 450
EENLVAAFSY FDKDGSGYIT IDELQSACTE FGLCDTPLDD MIKEIDLDND
460 470 480 490
GKIDFSEFTA MMRKGDGVGR SRTMMKNLNF NIADAFGVDG EKSDD
Length:495
Mass (Da):55,916
Last modified:May 3, 2011 - v2
Checksum:i2DD0ED8C234EF2F7
GO

Sequence cautioni

The sequence AAF79386.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti403 – 4031N → I in BAA04830 (PubMed:8078458).Curated
Sequence conflicti410 – 4101Y → D in BAA04830 (PubMed:8078458).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21806 mRNA. Translation: BAA04830.1.
AC007887 Genomic DNA. Translation: AAF79386.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE31822.1.
AY050981 mRNA. Translation: AAK93658.1.
AY113986 mRNA. Translation: AAM45034.1.
PIRiS46284.
RefSeqiNP_174807.1. NM_103271.3.
UniGeneiAt.24141.

Genome annotation databases

EnsemblPlantsiAT1G35670.1; AT1G35670.1; AT1G35670.
GeneIDi840471.
KEGGiath:AT1G35670.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21806 mRNA. Translation: BAA04830.1.
AC007887 Genomic DNA. Translation: AAF79386.1. Sequence problems.
CP002684 Genomic DNA. Translation: AEE31822.1.
AY050981 mRNA. Translation: AAK93658.1.
AY113986 mRNA. Translation: AAM45034.1.
PIRiS46284.
RefSeqiNP_174807.1. NM_103271.3.
UniGeneiAt.24141.

3D structure databases

ProteinModelPortaliQ39016.
SMRiQ39016. Positions 22-488.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi25703. 26 interactions.
IntActiQ39016. 24 interactions.
MINTiMINT-1788888.

Proteomic databases

PaxDbiQ39016.
PRIDEiQ39016.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G35670.1; AT1G35670.1; AT1G35670.
GeneIDi840471.
KEGGiath:AT1G35670.

Organism-specific databases

TAIRiAT1G35670.

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233030.
InParanoidiQ39016.
KOiK13412.
OMAiTVLPYQT.

Enzyme and pathway databases

BioCyciARA:AT1G35670-MONOMER.
ReactomeiREACT_184938. Synthesis of Leukotrienes (LT) and Eoxins (EX).
REACT_190945. Butyrate Response Factor 1 (BRF1) destabilizes mRNA.
REACT_190953. Tristetraprolin (TTP) destabilizes mRNA.
REACT_220111. Regulation of HSF1-mediated heat shock response.

Gene expression databases

ExpressionAtlasiQ39016. baseline and differential.
GenevestigatoriQ39016.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF13499. EF-hand_7. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 4 hits.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS00018. EF_HAND_1. 4 hits.
PS50222. EF_HAND_2. 4 hits.
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. "Two genes that encode Ca(2+)-dependent protein kinases are induced by drought and high-salt stresses in Arabidopsis thaliana."
    Urao T., Katagiri T., Mizoguchi T., Yamaguchi-Shinozaki K., Hayashida N., Shinozaki K.
    Mol. Gen. Genet. 244:331-340(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION.
  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. "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.
  5. "The CDPK superfamily of protein kinases."
    Harmon A.C., Gribskov M., Gubrium E., Harper J.F.
    New Phytol. 151:175-183(2001)
    Cited for: GENE FAMILY, NOMENCLATURE.
  6. "Calcium signaling through protein kinases. The Arabidopsis calcium-dependent protein kinase gene family."
    Cheng S.-H., Willmann M.R., Chen H.-C., Sheen J.
    Plant Physiol. 129:469-485(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE.
  7. Cited for: GENE FAMILY, NOMENCLATURE.
  8. "A novel yeast two-hybrid approach to identify CDPK substrates: characterization of the interaction between AtCPK11 and AtDi19, a nuclear zinc finger protein."
    Rodriguez Milla M.A., Uno Y., Chang I.-F., Townsend J., Maher E.A., Quilici D., Cushman J.C.
    FEBS Lett. 580:904-911(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DI19, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-150; ASP-171 AND PHE-306.
  9. "Two calcium-dependent protein kinases, CPK4 and CPK11, regulate abscisic acid signal transduction in Arabidopsis."
    Zhu S.-Y., Yu X.-C., Wang X.-J., Zhao R., Li Y., Fan R.-C., Shang Y., Du S.-Y., Wang X.-F., Wu F.-Q., Xu Y.-H., Zhang X.-Y., Zhang D.-P.
    Plant Cell 19:3019-3036(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiCDPKB_ARATH
AccessioniPrimary (citable) accession number: Q39016
Secondary accession number(s): Q949P0, Q9LQH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: May 3, 2011
Last modified: January 7, 2015
This is version 122 of the entry and version 2 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

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.