(data stored in ACNUC26462 zone)

HOGENOM: ARATH_5_PE116

ID   ARATH_5_PE116                        STANDARD;      PRT;   442 AA.
AC   ARATH_5_PE116; Q9LZW4;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=CBL-interacting serine/threonine-protein kinase 14;
DE   EC=2.7.11.1;AltName: Full=SNF1-related kinase 3 15;AltName:
DE   Full=SOS2-like protein kinase PKS24;AltName:
DE   Full=Serine/threonine-protein kinase SR1; Short=AtSR1; (ARATH_5.PE116).
GN   Name=CIPK14; Synonyms=PKS24, SnRK3.15, SR1;
OS   ARABIDOPSIS THALIANA.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids;
OC   eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ARATH_5.PE116.
CC       Arabidopsis thaliana chromosome 5 TAIR10 full sequence 1..26975502
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:CIPKE_ARATH
CC   -!- FUNCTION: CIPK serine-threonine protein kinases interact with CBL
CC       proteins. Binding of a CBL protein to the regulatory NAF domain of
CC       CIPK protein lead to the activation of the kinase in a calcium-
CC       dependent manner (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- COFACTOR: Manganese (By similarity).
CC   -!- SUBUNIT: Interacts with CBL2.
CC   -!- INTERACTION:
CC       Q8LAS7:CBL2; NbExp=5; IntAct=EBI-307576, EBI-485991;
CC   -!- TISSUE SPECIFICITY: Predominant in roots, cauline leaves, and
CC       flowers.
CC   -!- DEVELOPMENTAL STAGE: First observed in imbibed seeds. Mostly
CC       localized in hopocotyls during germination and in seedlings. In
CC       mature plants, confined to vascular tissues of leaves and roots.
CC       In flowers, expressed in the vascular bundle of the stamen
CC       filament and in the stigma, where the filament joins the pistil.
CC   -!- INDUCTION: By light in a cytokinin-dependent manner and N(6)-
CC       benzylaminopurine (BA). Also induced by By sucrose, glucose and
CC       fructose.
CC   -!- DOMAIN: The activation loop within the kinase domain is the target
CC       of phosphorylation/activation by upstream protein kinases. The PPI
CC       motif mediates the interaction with the ABI (abscisic acid-
CC       insensitive) phosphatases (By similarity).
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. SNF1 subfamily.
CC   -!- SIMILARITY: Contains 1 NAF domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- GENE_FAMILY: HOG000233016 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Arabidopsis_thaliana;AT5G01820;AT5G01820.1;AT5G01820.1.
DR   EMBL; AB035147; - ;
DR   EMBL; AF295669; - ;
DR   EMBL; AF360189; - ;
DR   EMBL; AL162351; - ;
DR   EMBL; AY142684; - ;
DR   UniProtKB/Swiss-Prot; Q9LZW4; -.
DR   EMBL; AF295669; AAK16689.1; -; mRNA.
DR   EMBL; AB035147; BAB11737.1; -; mRNA.
DR   EMBL; AL162351; CAB82752.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED90397.1; -; Genomic_DNA.
DR   EMBL; AF360189; AAK25899.1; -; mRNA.
DR   EMBL; AY142684; AAN13222.1; -; mRNA.
DR   IPI; IPI00547217; -.
DR   PIR; T48203; T48203.
DR   RefSeq; NP_195802.1; NM_120260.2.
DR   UniGene; At.23738; -.
DR   PDB; 2ZFD; X-ray; 1.20 A; B=305-427.
DR   PDBsum; 2ZFD; -.
DR   ProteinModelPortal; Q9LZW4; -.
DR   SMR; Q9LZW4; 14-426.
DR   IntAct; Q9LZW4; 7.
DR   STRING; Q9LZW4; -.
DR   PRIDE; Q9LZW4; -.
DR   EnsemblPlants; AT5G01820.1; AT5G01820.1; AT5G01820.
DR   GeneID; 831765; -.
DR   GenomeReviews; BA000015_GR; AT5G01820.
DR   KEGG; ath:AT5G01820; -.
DR   NMPDR; fig|3702.1.peg.22252; -.
DR   TAIR; At5g01820; -.
DR   eggNOG; KOG0583; -.
DR   GeneTree; EPGT00050000000048; -.
DR   InParanoid; Q9LZW4; -.
DR   OMA; MYRKIYK; -.
DR   PhylomeDB; Q9LZW4; -.
DR   ProtClustDB; CLSN2916659; -.
DR   ArrayExpress; Q9LZW4; -.
DR   Genevestigator; Q9LZW4; -.
DR   GO; GO:0005773; C:vacuole; IDA:TAIR.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR018451; NAF/FISL_domain.
DR   InterPro; IPR004041; NAF_dom.
DR   InterPro; IPR000719; Prot_kinase_cat_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR017442; Se/Thr_kinase-like_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR002290; Ser/Thr_kinase_dom.
DR   Pfam; PF03822; NAF; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50816; NAF; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   HOGENOMDNA; ARATH_5.PE116; -.
KW   AT5G01820pg.C_scaffold_1320000031; AT5G01820.10C_scaffold_1320000031;
KW   AB035147; AF295669; AF360189; AL162351; AY142684;
KW   3D-structure; ATP-binding; Complete proteome; Kinase; Manganese;
KW   Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
SQ   SEQUENCE   442 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MVDSDPVEFP PENRRGQLFG KYEVGKLVGC GAFAKVYHGR STATGQSVAI KVVSKQRLQK
     GGLNGNIQRE IAIMHRLRHP SIVRLFEVLA TKSKIFFVME FAKGGELFAK VSKGRFCEDL
     SRRYFQQLIS AVGYCHSRGI FHRDLKPENL LLDEKLDLKI SDFGLSALTD QIRPDGLLHT
     LCGTPAYVAP EVLAKKGYDG AKIDIWSCGI ILFVLNAGYL PFNDHNLMVM YRKIYKGEFR
     IPKWTSPDLR RLLTRLLDTN PQTRITIEEI IHDPWFKQGY DDRMSKFHLE DSDMKLPADE
     TDSEMGARRM NAFDIISGSP GFNLSGLFGD ARKYDRVERF VSAWTAERVV ERLEEIVSAE
     NLTVAKKETW GMKIEGQKGN FAMVVEINQL TDELVMIEVR KRQRAAASGR DLWTDTLRPF
     FVELVHESDQ TDPEPTQVHT TS
//

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