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Q38997

- KIN10_ARATH

UniProt

Q38997 - KIN10_ARATH

Protein

SNF1-related protein kinase catalytic subunit alpha KIN10

Gene

KIN10

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 2 (21 Nov 2003)
      Previous versions | rss
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    Functioni

    Catalytic subunit of the probable trimeric SNF1-related protein kinase (SnRK) complex, which may play a role in a signal transduction cascade regulating gene expression and carbohydrate metabolism in higher plants. The SnRK complex may also be involved in the regulation of fatty acid synthesis by phosphorylation of acetyl-CoA carboxylase and in assimilation of nitrogen by phosphorylating nitrate reductase. In vitro, KIN10 exhibits kinase activity on sucrose phosphate synthase and the kinase activity is inhibited by PRL1. May be a subunit of a SCF ubiquitin ligase complex and thus be involved in proteasomal ubiquitination. Phosphorylates GRIK1/SNAK2 and GRIK2/SNAK1 in vitro.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Activated by phosphorylation at Thr-198.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei71 – 711ATPPROSITE-ProRule annotation
    Active sitei165 – 1651Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi48 – 569ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein serine/threonine kinase activity Source: TAIR

    GO - Biological processi

    1. abscisic acid-activated signaling pathway Source: TAIR
    2. carbohydrate metabolic process Source: UniProtKB-KW
    3. detection of nutrient Source: TAIR
    4. developmental process involved in reproduction Source: TAIR
    5. fatty acid biosynthetic process Source: UniProtKB-KW
    6. nitrate assimilation Source: UniProtKB-KW
    7. organ senescence Source: TAIR
    8. primary root development Source: TAIR
    9. sugar mediated signaling pathway Source: TAIR
    10. vegetative phase change Source: TAIR

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Nitrate assimilation, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciARA:AT3G01090-MONOMER.
    ARA:GQT-1037-MONOMER.
    ARA:GQT-194-MONOMER.
    BRENDAi2.7.11.1. 399.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SNF1-related protein kinase catalytic subunit alpha KIN10 (EC:2.7.11.1)
    Short name:
    AKIN10
    Alternative name(s):
    AKIN alpha-2
    Short name:
    AKINalpha2
    Gene namesi
    Name:KIN10
    Synonyms:AK21, SKIN10, SNR2, SNRK1.1
    Ordered Locus Names:At3g01090
    ORF Names:T4P13.22
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G01090.

    Subcellular locationi

    GO - Cellular componenti

    1. nuclear ubiquitin ligase complex Source: TAIR

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi198 – 1981T → A: Abolishes phosphorylation by GRIK1 or GRIK2 leading to inactivation of the protein. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 535535SNF1-related protein kinase catalytic subunit alpha KIN10PRO_0000086128Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki43 – 43Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei187 – 1871PhosphoserineBy similarity
    Modified residuei198 – 1981Phosphothreonine; by GRIK1 or GRIK22 Publications

    Post-translational modificationi

    Autophosphorylated. Phosphorylated at Thr-198 by GRIK1/SNAK2 and GRIK2/SNAK1.2 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ38997.
    PRIDEiQ38997.

    Expressioni

    Inductioni

    Induced by sucrose.1 Publication

    Gene expression databases

    ArrayExpressiQ38997.
    GenevestigatoriQ38997.

    Interactioni

    Subunit structurei

    Subunit of a probable heterotrimeric complex consisting of an alpha catalytic (KIN10 or KIN11) subunit, and a beta (KINB) and a gamma (KING or SNF4) non-catalytic regulatory subunits. Interacts with KINB2, KINB3, SNF4 and probably with KINB1 and KING1. Interacts with SKP1/ASK1, PAD1, the N-terminus of PRL1 and the WD40 domain of 5PTase13. Potential subunit of a SCF ubiquitin ligase complex consisting of a SNF1-related protein kinase, SKP1 and CUL1. The association of the SCF complex with the proteasome may be mediated by PAD1 and seems to be inhibited by the interaction with PRL1. Interacts with DSP4.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GRIK1Q93V582EBI-2107143,EBI-6399184
    GRIK2Q5HZ382EBI-2107143,EBI-6399237
    KINB2Q9SCY53EBI-2107143,EBI-2042436
    PRL1Q423843EBI-2107143,EBI-1382964
    SNF4Q944A62EBI-2107143,EBI-2360649

    Protein-protein interaction databases

    BioGridi6592. 27 interactions.
    IntActiQ38997. 9 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ38997.
    SMRiQ38997. Positions 41-532.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 294253Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini315 – 35541UBAPROSITE-ProRule annotationAdd
    BLAST
    Domaini486 – 53449KA1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 KA1 (kinase-associated) domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 UBA domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233016.
    InParanoidiQ38997.
    KOiK07198.
    OMAiLPGLMEY.
    PhylomeDBiQ38997.

    Family and domain databases

    InterProiIPR028375. KA1/Ssp2_C.
    IPR001772. KA1_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    [Graphical view]
    PfamiPF02149. KA1. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00627. UBA. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    SM00165. UBA. 1 hit.
    [Graphical view]
    SUPFAMiSSF103243. SSF103243. 1 hit.
    SSF46934. SSF46934. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS50032. KA1. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50030. UBA. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q38997-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MFKRVDEFNL VSSTIDHRIF KSRMDGSGTG SRSGVESILP NYKLGRTLGI    50
    GSFGRVKIAE HALTGHKVAI KILNRRKIKN MEMEEKVRRE IKILRLFMHP 100
    HIIRLYEVIE TPTDIYLVME YVNSGELFDY IVEKGRLQED EARNFFQQII 150
    SGVEYCHRNM VVHRDLKPEN LLLDSKCNVK IADFGLSNIM RDGHFLKTSC 200
    GSPNYAAPEV ISGKLYAGPE VDVWSCGVIL YALLCGTLPF DDENIPNLFK 250
    KIKGGIYTLP SHLSPGARDL IPRMLVVDPM KRVTIPEIRQ HPWFQAHLPR 300
    YLAVPPPDTV QQAKKIDEEI LQEVINMGFD RNHLIESLRN RTQNDGTVTY 350
    YLILDNRFRA SSGYLGAEFQ ETMEGTPRMH PAESVASPVS HRLPGLMEYQ 400
    GVGLRSQYPV ERKWALGLQS RAHPREIMTE VLKALQDLNV CWKKIGHYNM 450
    KCRWVPNSSA DGMLSNSMHD NNYFGDESSI IENEAAVKSP NVVKFEIQLY 500
    KTRDDKYLLD LQRVQGPQFL FLDLCAAFLA QLRVL 535

    Note: No experimental confirmation available.

    Length:535
    Mass (Da):61,182
    Last modified:November 21, 2003 - v2
    Checksum:iFFFC383223FD8317
    GO
    Isoform 2 (identifier: Q38997-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: Missing.

    Show »
    Length:512
    Mass (Da):58,373
    Checksum:i5A18655A0AA506DF
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2323Missing in isoform 2. 2 PublicationsVSP_009001Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93023 Genomic DNA. Translation: AAA32736.1.
    X94757 mRNA. Translation: CAA64384.1.
    DQ778957 mRNA. Translation: ABH11527.1.
    AC008261 Genomic DNA. Translation: AAF26165.1.
    CP002686 Genomic DNA. Translation: AEE73607.1.
    CP002686 Genomic DNA. Translation: AEE73608.1.
    CP002686 Genomic DNA. Translation: AEE73609.1.
    AY093170 mRNA. Translation: AAM13169.1.
    BT010386 mRNA. Translation: AAQ56829.1.
    X79707 Genomic DNA. Translation: CAA56146.1.
    X86966 Genomic DNA. Translation: CAA60529.1.
    PIRiJC1446.
    RefSeqiNP_001118546.1. NM_001125074.1. [Q38997-2]
    NP_566130.1. NM_110974.4. [Q38997-2]
    NP_850488.1. NM_180157.1. [Q38997-1]
    UniGeneiAt.22965.

    Genome annotation databases

    EnsemblPlantsiAT3G01090.2; AT3G01090.2; AT3G01090. [Q38997-1]
    GeneIDi821259.
    KEGGiath:AT3G01090.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    PlantP kinase Classification PPC

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M93023 Genomic DNA. Translation: AAA32736.1 .
    X94757 mRNA. Translation: CAA64384.1 .
    DQ778957 mRNA. Translation: ABH11527.1 .
    AC008261 Genomic DNA. Translation: AAF26165.1 .
    CP002686 Genomic DNA. Translation: AEE73607.1 .
    CP002686 Genomic DNA. Translation: AEE73608.1 .
    CP002686 Genomic DNA. Translation: AEE73609.1 .
    AY093170 mRNA. Translation: AAM13169.1 .
    BT010386 mRNA. Translation: AAQ56829.1 .
    X79707 Genomic DNA. Translation: CAA56146.1 .
    X86966 Genomic DNA. Translation: CAA60529.1 .
    PIRi JC1446.
    RefSeqi NP_001118546.1. NM_001125074.1. [Q38997-2 ]
    NP_566130.1. NM_110974.4. [Q38997-2 ]
    NP_850488.1. NM_180157.1. [Q38997-1 ]
    UniGenei At.22965.

    3D structure databases

    ProteinModelPortali Q38997.
    SMRi Q38997. Positions 41-532.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 6592. 27 interactions.
    IntActi Q38997. 9 interactions.

    Proteomic databases

    PaxDbi Q38997.
    PRIDEi Q38997.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G01090.2 ; AT3G01090.2 ; AT3G01090 . [Q38997-1 ]
    GeneIDi 821259.
    KEGGi ath:AT3G01090.

    Organism-specific databases

    TAIRi AT3G01090.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233016.
    InParanoidi Q38997.
    KOi K07198.
    OMAi LPGLMEY.
    PhylomeDBi Q38997.

    Enzyme and pathway databases

    BioCyci ARA:AT3G01090-MONOMER.
    ARA:GQT-1037-MONOMER.
    ARA:GQT-194-MONOMER.
    BRENDAi 2.7.11.1. 399.

    Miscellaneous databases

    PROi Q38997.

    Gene expression databases

    ArrayExpressi Q38997.
    Genevestigatori Q38997.

    Family and domain databases

    InterProi IPR028375. KA1/Ssp2_C.
    IPR001772. KA1_dom.
    IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    IPR009060. UBA-like.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    [Graphical view ]
    Pfami PF02149. KA1. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00627. UBA. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    SM00165. UBA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103243. SSF103243. 1 hit.
    SSF46934. SSF46934. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS50032. KA1. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    PS50030. UBA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and expression of a gene from Arabidopsis thaliana encoding a protein related to SNF1 protein kinase."
      le Guen L., Thomas M., Bianchi M., Halford N.G., Kreis M.
      Gene 120:249-254(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Columbia.
    2. Lessard P., Kreis M., Thomas M.
      Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: cv. Columbia.
      Tissue: Seedling.
    3. "Functional differentiation of ubiquitin-interacting factors from Arabidopsis."
      Fu H.
      Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: cv. Columbia.
    4. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
      Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
      , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
      Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    5. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    6. "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] (ISOFORM 1).
      Strain: cv. Columbia.
    7. "Gene density and organization in a small region of the Arabidopsis thaliana genome."
      le Guen L., Thomas M., Kreis M.
      Mol. Gen. Genet. 245:390-396(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-42 (ISOFORM 2).
      Strain: cv. Columbia.
    8. "Differential accumulation of the transcripts of 22 novel protein kinase genes in Arabidopsis thaliana."
      Thuemmler F., Kirchner M., Teuber R., Dittrich P.
      Plant Mol. Biol. 29:551-565(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 167-221.
      Strain: cv. Eil-0.
      Tissue: Leaf.
    9. "Regulatory interaction of PRL1 WD protein with Arabidopsis SNF1-like protein kinases."
      Bhalerao R.P., Salchert K., Bako L., Oekresz L., Szabados L., Muranaka T., Machida Y., Schell J., Koncz C.
      Proc. Natl. Acad. Sci. U.S.A. 96:5322-5327(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION, INDUCTION, INTERACTION WITH PRL1.
    10. "Functional identification of an Arabidopsis Snf4 ortholog by screening for heterologous multicopy suppressors of snf4 deficiency in yeast."
      Kleinow T., Bhalerao R., Breuer F., Umeda M., Salchert K., Koncz C.
      Plant J. 23:115-122(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNF4.
    11. "SKP1-SnRK protein kinase interactions mediate proteasomal binding of a plant SCF ubiquitin ligase."
      Farras R., Ferrando A., Jasik J., Kleinow T., Oekresz L., Tiburcio A., Salchert K., del Pozo C., Schell J., Koncz C.
      EMBO J. 20:2742-2756(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SKP1 AND PAD1.
    12. "Detection of in vivo protein interactions between Snf1-related kinase subunits with intron-tagged epitope-labelling in plants cells."
      Ferrando A., Koncz-Kalman Z., Farras R., Tiburcio A., Schell J., Koncz C.
      Nucleic Acids Res. 29:3685-3693(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KINB2.
    13. "AKINbeta3, a plant specific SnRK1 protein, is lacking domains present in yeast and mammals non-catalytic beta-subunits."
      Gissot L., Polge C., Bouly J.P., Lemaitre T., Kreis M., Thomas M.
      Plant Mol. Biol. 56:747-759(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KINB3.
    14. "Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants."
      Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.
      Mol. Cell. Proteomics 6:601-610(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-43.
      Strain: cv. Landsberg erecta.
    15. "Interaction of the WD40 domain of a myoinositol polyphosphate 5-phosphatase with SnRK1 links inositol, sugar, and stress signaling."
      Ananieva E.A., Gillaspy G.E., Ely A., Burnette R.N., Erickson F.L.
      Plant Physiol. 148:1868-1882(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH 5PTASE13, SUBCELLULAR LOCATION.
    16. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
      Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
      Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Arabidopsis protein kinases GRIK1 and GRIK2 specifically activate SnRK1 by phosphorylating its activation loop."
      Shen W., Reyes M.I., Hanley-Bowdoin L.
      Plant Physiol. 150:996-1005(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-198, MUTAGENESIS OF THR-198, ENZYME REGULATION.
    18. "Cross-phosphorylation between Arabidopsis thaliana sucrose nonfermenting 1-related protein kinase 1 (AtSnRK1) and its activating kinase (AtSnAK) determines their catalytic activities."
      Crozet P., Jammes F., Valot B., Ambard-Bretteville F., Nessler S., Hodges M., Vidal J., Thomas M.
      J. Biol. Chem. 285:12071-12077(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF THR-198.

    Entry informationi

    Entry nameiKIN10_ARATH
    AccessioniPrimary (citable) accession number: Q38997
    Secondary accession number(s): A6XGR0
    , O04728, Q38987, Q39076, Q8RWD2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: November 21, 2003
    Last modified: October 1, 2014
    This is version 143 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