(data stored in ACNUC26462 zone)

HOGENOM: ARATH_3_PE3950

ID   ARATH_3_PE3950                       STANDARD;      PRT;   512 AA.
AC   ARATH_3_PE3950; P92958; A6XGQ9; P92968; Q3E7R4;
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=SNF1-related protein kinase catalytic subunit alpha KIN11;
DE   Short=AKIN11; EC=2.7.11 1;AltName: Full=AKIN alpha-1; Short=AKINalpha1;
DE   (ARATH_3.PE3950).
GN   Name=KIN11; Synonyms=SNF1; OrderedLocusNames=At3g29160;
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_3.PE3950.
CC       Arabidopsis thaliana chromosome 3 TAIR10 full sequence 1..23459830
CC       annotated by Ensembl Genomes
CC   -!- ANNOTATIONS ORIGIN:KIN11_ARATH
CC   -!- FUNCTION: Catalytic subunit of the probable trimeric SNF1-related
CC       protein kinase (SnRK) complex, which may play a role in a signal
CC       transduction cascade regulating gene expression and carbohydrate
CC       metabolism in higher plants. The SnRK complex may also be involved
CC       in the regulation of fatty acid synthesis by phosphorylation of
CC       acetyl-CoA carboxylase and in assimilation of nitrogen by
CC       phosphorylating nitrate reductase. In vitro, KIN11 exhibits kinase
CC       activity on sucrose phosphate synthase and the kinase activity is
CC       inhibited by PRL1. May be a subunit of a SCF ubiquitin ligase
CC       complex and thus be involved in proteasomal ubiquitination.
CC       Involved in innate antiviral defenses.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- ENZYME REGULATION: Inactivated by the begomovirus AL2 protein or
CC       the curtovirus L2 protein.
CC   -!- SUBUNIT: Subunit of a probable heterotrimeric complex consisting
CC       of an alpha catalytic (KIN10 or KIN11) subunit, and a beta (KINB)
CC       and a gamma (KING or SNF4) non-catalytic regulatory subunits.
CC       Interacts with KINB2, KINB3, SNF4 and probably with KINB1 and
CC       KING1. Interacts with SKP1/ASK1, PAD1 and the N-terminus of PRL1.
CC       Potential subunit of a SCF ubiquitin ligase complex consisting of
CC       a SNF1-related protein kinase, SKP1 and CUL1. The association of
CC       the SCF complex with the proteasome may be mediated by PAD1 and
CC       seems to be inhibited by the interaction with PRL1. Interacts with
CC       the KIS domain of PTPKIS1. Interacts with the begomovirus AL2
CC       protein and the curtovirus L2 protein.
CC   -!- INTERACTION:
CC       Q9FEB5:f4F15.290; NbExp=2; IntAct=EBI-307202, EBI-307215;
CC       Q9SCY5:KINB2; NbExp=4; IntAct=EBI-307202, EBI-2042436;
CC       Q42384:PRL1; NbExp=2; IntAct=EBI-307202, EBI-1382964;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P92958-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P92958-2; Sequence=VSP_034567, VSP_034568;
CC         Note=Derived from EST data. No experimental confirmation
CC         available;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, shoots, flower buds,
CC       flowers, siliques and leaves.
CC   -!- INDUCTION: Induced by sucrose.
CC   -!- PTM: Autophosphorylated.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. SNF1 subfamily.
CC   -!- SIMILARITY: Contains 1 KA1 (kinase-associated) domain.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC   -!- SIMILARITY: Contains 1 UBA domain.
CC   -!- GENE_FAMILY: HOG000233016 [ FAMILY / ALN / TREE ]
DR   HOGENOM:Arabidopsis_thaliana;AT3G29160;AT3G29160.2;AT3G29160.2.
DR   EMBL; AB018121; - ;
DR   EMBL; AK317239; - ;
DR   EMBL; AY070468; - ;
DR   EMBL; AY149927; - ;
DR   EMBL; DQ778956; - ;
DR   EMBL; X94755; - ;
DR   EMBL; X99279; - ;
DR   UniProtKB/Swiss-Prot; P92958; A6XGQ9; P92968; Q3E7R4; -.
DR   EMBL; X94755; CAA64382.1; -; mRNA.
DR   EMBL; X99279; CAA67671.1; -; mRNA.
DR   EMBL; DQ778956; ABH11526.1; -; mRNA.
DR   EMBL; AB018121; BAB01993.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77542.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77543.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77544.1; -; Genomic_DNA.
DR   EMBL; AY070468; AAL49934.1; -; mRNA.
DR   EMBL; AY149927; AAN31081.1; -; mRNA.
DR   IPI; IPI00523787; -.
DR   IPI; IPI00548800; -.
DR   PIR; T52633; T52633.
DR   RefSeq; NP_566843.1; NM_113839.3.
DR   RefSeq; NP_974374.1; NM_202645.2.
DR   RefSeq; NP_974375.1; NM_202646.1.
DR   UniGene; At.184; -.
DR   ProteinModelPortal; P92958; -.
DR   SMR; P92958; 15-494.
DR   IntAct; P92958; 7.
DR   STRING; P92958; -.
DR   PRIDE; P92958; -.
DR   ProMEX; P92958; -.
DR   EnsemblPlants; AT3G29160.1; AT3G29160.1; AT3G29160.
DR   EnsemblPlants; AT3G29160.2; AT3G29160.2; AT3G29160.
DR   GeneID; 822566; -.
DR   GenomeReviews; BA000014_GR; AT3G29160.
DR   KEGG; ath:AT3G29160; -.
DR   NMPDR; fig|3702.1.peg.15221; -.
DR   TAIR; At3g29160; -.
DR   eggNOG; KOG0583; -.
DR   GeneTree; EPGT00050000000031; -.
DR   InParanoid; P92958; -.
DR   OMA; ATVTYYL; -.
DR   PhylomeDB; P92958; -.
DR   ProtClustDB; CLSN2688899; -.
DR   Genevestigator; P92958; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0044419; P:interspecies interaction between organisms; IEA:UniProtKB-KW.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR   GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR   InterPro; IPR001772; Kinase-assoc_KA1.
DR   InterPro; IPR011009; Kinase-like_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   InterPro; IPR000449; UBA/transl_elong_EF1B_N.
DR   InterPro; IPR015940; UBA/transl_elong_EF1B_N_euk.
DR   Pfam; PF02149; KA1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00627; UBA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF103243; Kinase-assoc_KA1; 1.
DR   SUPFAM; SSF56112; Kinase_like; 1.
DR   PROSITE; PS50032; KA1; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   HOGENOMDNA; ARATH_3.PE3950; -.
KW   AT3G29160pg.C_scaffold_1320000031; AT3G29160.2.C_scaffold_1320000031;
KW   B9DGQ3; AB018121; AK317239; AY070468; AY149927; DQ778956; X94755; X99279;
KW   Alternative splicing; Antiviral protein; ATP-binding;
KW   Carbohydrate metabolism; Complete proteome; Fatty acid biosynthesis;
KW   Host-virus interaction; Kinase; Lipid synthesis; Nitrate assimilation;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase; Ubl conjugation pathway.
SQ   SEQUENCE   512 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDHSSNRFGN NGVESILPNY KLGKTLGIGS FGKVKIAEHV VTGHKVAIKI LNRRKIKNME
     MEEKVRREIK ILRLFMHPHI IRQYEVIETT SDIYVVMEYV KSGELFDYIV EKGRLQEDEA
     RNFFQQIISG VEYCHRNMVV HRDLKPENLL LDSRCNIKIA DFGLSNVMRD GHFLKTSCGS
     PNYAAPEVIS GKLYAGPEVD VWSCGVILYA LLCGTLPFDD ENIPNLFKKI KGGIYTLPSH
     LSSEARDLIP RMLIVDPVKR ITIPEIRQHR WFQTHLPRYL AVSPPDTVEQ AKKINEEIVQ
     EVVNMGFDRN QVLESLRNRT QNDATVTYYL LLDNRFRVPS GYLESEFQET TDSGSNPMRT
     PEAGASPVGH WIPAHVDHYG LGARSQVPVD RKWALGLQSH AHPREIMNEV LKALQELNVC
     WKKIGHYNMK CRWVPGLADG QNTMVNNQLH FRDESSIIED DCAMTSPTVI KFELQLYKAR
     EEKYLLDIQR VNGPQFLFLD LCAAFLTELR VI
//

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