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Q570C0

- TIR1_ARATH

UniProt

Q570C0 - TIR1_ARATH

Protein

Protein TRANSPORT INHIBITOR RESPONSE 1

Gene

TIR1

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 94 (01 Oct 2014)
      Sequence version 2 (21 Jun 2005)
      Previous versions | rss
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    Functioni

    Auxin receptor that mediates Aux/IAA proteins proteasomal degradation and auxin-regulated transcription. The SCF(TIR1) E3 ubiquitin ligase complex is involved in auxin-mediated signaling pathway that regulate root and hypocotyl growth, lateral root formation, cell elongation, and gravitropism. Appears to allow pericycle cells to overcome G2 arrest prior to lateral root development. Plays a role in ethylene signaling in roots. Confers sensitivity to the virulent bacterial pathogen P.syringae.8 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei74 – 741Myo-inositol hexakisphosphate2 Publications
    Sitei139 – 1391Interaction with auxin-responsive proteins
    Sitei165 – 1651Interaction with auxin-responsive proteins
    Binding sitei344 – 3441Myo-inositol hexakisphosphate2 Publications
    Sitei380 – 3801Interaction with auxin-responsive proteins
    Binding sitei436 – 4361Myo-inositol hexakisphosphate2 Publications
    Sitei489 – 4891Interaction with auxin-responsive proteins
    Binding sitei509 – 5091Myo-inositol hexakisphosphate2 Publications

    GO - Molecular functioni

    1. auxin binding Source: UniProtKB
    2. auxin receptor activity Source: UniProtKB
    3. inositol hexakisphosphate binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. ubiquitin-protein transferase activity Source: TAIR

    GO - Biological processi

    1. auxin-activated signaling pathway Source: UniProtKB
    2. cell cycle Source: UniProtKB-KW
    3. cellular response to phosphate starvation Source: TAIR
    4. defense response Source: UniProtKB-KW
    5. ethylene-activated signaling pathway Source: UniProtKB-KW
    6. lateral root formation Source: TAIR
    7. pollen maturation Source: TAIR
    8. response to auxin Source: TAIR
    9. response to molecule of bacterial origin Source: TAIR
    10. stamen development Source: TAIR

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Auxin signaling pathway, Cell cycle, Ethylene signaling pathway, Plant defense, Ubl conjugation pathway

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein TRANSPORT INHIBITOR RESPONSE 1
    Alternative name(s):
    Weak ethylene-insensitive protein 1
    Gene namesi
    Name:TIR1
    Synonyms:FBL1, WEI1
    Ordered Locus Names:At3g62980
    ORF Names:T20O10.80
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 3

    Organism-specific databases

    TAIRiAT3G62980.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell
    2. SCF ubiquitin ligase complex Source: TAIR

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Plant are deficient in a variety of auxin-regulated growth processes including lateral root formation, and hypocotyl and cell elongation.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101P → A: Abolishes SCF(TIR1) complex formation, altered auxin-mediated response and reduced affinity for auxin. 3 Publications
    Mutagenesisi33 – 331V → A: No affinity for auxin. 2 Publications
    Mutagenesisi35 – 351K → A: No affinity for auxin. 2 Publications
    Mutagenesisi147 – 1471G → D in tir1-1; insensitive to auxin ubiquitously and to ethylene in roots only. 2 Publications
    Mutagenesisi441 – 4411G → D in tir1-2; insensitive to auxin. 2 Publications
    Mutagenesisi574 – 59421Missing in tir1-101/wei1; insensitive to auxin ubiquitously and to ethylene in roots only. 1 PublicationAdd
    BLAST

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 594594Protein TRANSPORT INHIBITOR RESPONSE 1PRO_0000119965Add
    BLAST

    Proteomic databases

    PaxDbiQ570C0.
    PRIDEiQ570C0.

    Expressioni

    Tissue specificityi

    Expressed in roots, stems, leaves and flowers. In adult plants, mostly expressed in floral stigma, anther filaments, abscission zones and vascular tissues.2 Publications

    Developmental stagei

    Abundant expression in developing embryos. In young seedlings, expressed in root apical meristem, and expanding cotyledons and hypocotyls. In older seedlings, still expressed in root apical meristems, but also in lateral root primordia, stipules, shoot apical meristem and vascular tissues.1 Publication

    Inductioni

    Repressed by miR393a (microRNA) in response to flg-22 (flagellin-derived peptide 22).1 Publication

    Gene expression databases

    ArrayExpressiQ570C0.
    GenevestigatoriQ570C0.

    Interactioni

    Subunit structurei

    Interacts with auxin. Part of a SCF E3 ubiquitin ligase complex SCF(TIR1) composed of SKP1, CUL1, RBX1 and TIR1. SCF(TIR1) interacts with the COP9 signalosome (CSN) complex. Interacts with Aux/IAA proteins (IAA3, IAA7, IAA12 and IAA17) in an auxin-dependent manner. The interaction with IAA3, a negative regulator of auxin responses, is promoted by auxin, but repressed by juglon (5-hydroxy-1,4-naphthoquinone). Interactions with auxin-responsive proteins is inactivated by auxin antagonists.10 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IAA17P938302EBI-307183,EBI-632243
    IAA7Q388254EBI-307183,EBI-602959
    SKP1AQ392554EBI-307183,EBI-532357
    SKP1BQ9FHW74EBI-307183,EBI-604076

    Protein-protein interaction databases

    BioGridi10787. 18 interactions.
    DIPiDIP-31740N.
    IntActiQ570C0. 16 interactions.

    Structurei

    Secondary structure

    1
    594
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi11 – 199
    Helixi24 – 318
    Helixi35 – 4410
    Beta strandi47 – 526
    Helixi53 – 553
    Helixi58 – 647
    Beta strandi70 – 745
    Helixi78 – 825
    Helixi94 – 10310
    Beta strandi109 – 1146
    Helixi119 – 12810
    Beta strandi134 – 1396
    Beta strandi141 – 1444
    Helixi145 – 15410
    Beta strandi160 – 1623
    Beta strandi167 – 1693
    Helixi173 – 1786
    Beta strandi188 – 1903
    Helixi200 – 20910
    Beta strandi215 – 2173
    Helixi224 – 23310
    Beta strandi238 – 2414
    Helixi251 – 26212
    Beta strandi269 – 2713
    Helixi278 – 2847
    Helixi285 – 2884
    Beta strandi293 – 2953
    Helixi303 – 3108
    Beta strandi318 – 3225
    Helixi323 – 3253
    Helixi326 – 33611
    Beta strandi342 – 3465
    Beta strandi350 – 3523
    Helixi361 – 37010
    Beta strandi376 – 3827
    Helixi386 – 39510
    Beta strandi401 – 4088
    Turni414 – 4163
    Helixi421 – 43010
    Beta strandi436 – 4383
    Helixi445 – 45410
    Beta strandi460 – 4656
    Helixi470 – 47910
    Beta strandi485 – 4906
    Helixi495 – 5006
    Helixi502 – 5076
    Beta strandi508 – 5169
    Helixi520 – 52910
    Beta strandi533 – 5386
    Beta strandi540 – 5423
    Helixi544 – 5463
    Beta strandi554 – 5607
    Beta strandi573 – 5753

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2P1MX-ray1.80B1-594[»]
    2P1NX-ray2.50B/E1-594[»]
    2P1OX-ray1.90B1-594[»]
    2P1PX-ray2.21B1-594[»]
    2P1QX-ray1.91B1-594[»]
    3C6NX-ray2.60B1-594[»]
    3C6OX-ray2.70B1-594[»]
    3C6PX-ray2.70B1-594[»]
    ProteinModelPortaliQ570C0.
    SMRiQ570C0. Positions 10-576.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ570C0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini3 – 5048F-boxAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni81 – 822Interaction with auxin-responsive proteins
    Regioni113 – 1142Myo-inositol hexakisphosphate binding
    Regioni347 – 3526Interaction with auxin-responsive proteins
    Regioni401 – 4033Myo-inositol hexakisphosphate binding
    Regioni403 – 4042Auxin binding
    Regioni405 – 4095Interaction with auxin-responsive proteins
    Regioni438 – 4392Auxin binding
    Regioni464 – 4652Interaction with auxin-responsive proteins
    Regioni484 – 4852Myo-inositol hexakisphosphate binding

    Domaini

    The F-box is necessary for the interaction with SKP1.1 Publication

    Sequence similaritiesi

    Contains 1 F-box domain.Curated

    Phylogenomic databases

    eggNOGiNOG267823.
    HOGENOMiHOG000239805.
    InParanoidiQ570C0.
    KOiK14485.
    OMAiCEGLTSL.
    PhylomeDBiQ570C0.

    Family and domain databases

    InterProiIPR001810. F-box_dom.
    [Graphical view]
    PfamiPF12937. F-box-like. 1 hit.
    [Graphical view]
    SMARTiSM00256. FBOX. 1 hit.
    [Graphical view]
    SUPFAMiSSF81383. SSF81383. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q570C0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQKRIALSFP EEVLEHVFSF IQLDKDRNSV SLVCKSWYEI ERWCRRKVFI    50
    GNCYAVSPAT VIRRFPKVRS VELKGKPHFA DFNLVPDGWG GYVYPWIEAM 100
    SSSYTWLEEI RLKRMVVTDD CLELIAKSFK NFKVLVLSSC EGFSTDGLAA 150
    IAATCRNLKE LDLRESDVDD VSGHWLSHFP DTYTSLVSLN ISCLASEVSF 200
    SALERLVTRC PNLKSLKLNR AVPLEKLATL LQRAPQLEEL GTGGYTAEVR 250
    PDVYSGLSVA LSGCKELRCL SGFWDAVPAY LPAVYSVCSR LTTLNLSYAT 300
    VQSYDLVKLL CQCPKLQRLW VLDYIEDAGL EVLASTCKDL RELRVFPSEP 350
    FVMEPNVALT EQGLVSVSMG CPKLESVLYF CRQMTNAALI TIARNRPNMT 400
    RFRLCIIEPK APDYLTLEPL DIGFGAIVEH CKDLRRLSLS GLLTDKVFEY 450
    IGTYAKKMEM LSVAFAGDSD LGMHHVLSGC DSLRKLEIRD CPFGDKALLA 500
    NASKLETMRS LWMSSCSVSF GACKLLGQKM PKLNVEVIDE RGAPDSRPES 550
    CPVERVFIYR TVAGPRFDMP GFVWNMDQDS TMRFSRQIIT TNGL 594
    Length:594
    Mass (Da):66,799
    Last modified:June 21, 2005 - v2
    Checksum:i9E19ED5DABF40D07
    GO

    Sequence cautioni

    The sequence BAD94031.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti490 – 4901D → E in BAD94031. 1 PublicationCurated
    Sequence conflicti568 – 5681D → G in BAD94031. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF005047 Genomic DNA. Translation: AAB69175.1.
    AF005048 mRNA. Translation: AAB69176.1.
    AL163816 Genomic DNA. Translation: CAB87743.1.
    CP002686 Genomic DNA. Translation: AEE80419.1.
    BT001946 mRNA. Translation: AAN71945.1.
    EF598824 Genomic DNA. Translation: ABR04117.1.
    EF598825 Genomic DNA. Translation: ABR04118.1.
    EF598826 Genomic DNA. Translation: ABR04119.1.
    EF598827 Genomic DNA. Translation: ABR04120.1.
    EF598828 Genomic DNA. Translation: ABR04121.1.
    EF598829 Genomic DNA. Translation: ABR04122.1.
    EF598830 Genomic DNA. Translation: ABR04123.1.
    EF598831 Genomic DNA. Translation: ABR04124.1.
    EF598832 Genomic DNA. Translation: ABR04125.1.
    EF598833 Genomic DNA. Translation: ABR04126.1.
    EF598834 Genomic DNA. Translation: ABR04127.1.
    EF598835 Genomic DNA. Translation: ABR04128.1.
    EF598836 Genomic DNA. Translation: ABR04129.1.
    EF598837 Genomic DNA. Translation: ABR04130.1.
    EF598838 Genomic DNA. Translation: ABR04131.1.
    EF598839 Genomic DNA. Translation: ABR04132.1.
    EF598840 Genomic DNA. Translation: ABR04133.1.
    EF598841 Genomic DNA. Translation: ABR04134.1.
    EF598842 Genomic DNA. Translation: ABR04135.1.
    EF598843 Genomic DNA. Translation: ABR04136.1.
    EF598844 Genomic DNA. Translation: ABR04137.1.
    EF598845 Genomic DNA. Translation: ABR04138.1.
    EF598846 Genomic DNA. Translation: ABR04139.1.
    EF598847 Genomic DNA. Translation: ABR04140.1.
    AK220790 mRNA. Translation: BAD94031.1. Different initiation.
    EU550991 Genomic DNA. Translation: ACB31753.1.
    EU550992 Genomic DNA. Translation: ACB31754.1.
    EU550993 Genomic DNA. Translation: ACB31755.1.
    EU550994 Genomic DNA. Translation: ACB31756.1.
    EU550995 Genomic DNA. Translation: ACB31757.1.
    EU550996 Genomic DNA. Translation: ACB31758.1.
    EU550997 Genomic DNA. Translation: ACB31759.1.
    EU550998 Genomic DNA. Translation: ACB31760.1.
    EU550999 Genomic DNA. Translation: ACB31761.1.
    EU551000 Genomic DNA. Translation: ACB31762.1.
    EU551001 Genomic DNA. Translation: ACB31763.1.
    EU551002 Genomic DNA. Translation: ACB31764.1.
    EU551003 Genomic DNA. Translation: ACB31765.1.
    EU551004 Genomic DNA. Translation: ACB31766.1.
    EU551005 Genomic DNA. Translation: ACB31767.1.
    EU551006 Genomic DNA. Translation: ACB31768.1.
    EU551007 Genomic DNA. Translation: ACB31769.1.
    EU551008 Genomic DNA. Translation: ACB31770.1.
    EU551009 Genomic DNA. Translation: ACB31771.1.
    EU551010 Genomic DNA. Translation: ACB31772.1.
    EU551011 Genomic DNA. Translation: ACB31773.1.
    EU551012 Genomic DNA. Translation: ACB31774.1.
    EU551013 Genomic DNA. Translation: ACB31775.1.
    EU551014 Genomic DNA. Translation: ACB31776.1.
    PIRiT48087.
    RefSeqiNP_567135.1. NM_116163.3.
    UniGeneiAt.25594.

    Genome annotation databases

    EnsemblPlantsiAT3G62980.1; AT3G62980.1; AT3G62980.
    GeneIDi825473.
    KEGGiath:AT3G62980.

    Cross-referencesi

    Web resourcesi

    PlantsUBQ

    A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF005047 Genomic DNA. Translation: AAB69175.1 .
    AF005048 mRNA. Translation: AAB69176.1 .
    AL163816 Genomic DNA. Translation: CAB87743.1 .
    CP002686 Genomic DNA. Translation: AEE80419.1 .
    BT001946 mRNA. Translation: AAN71945.1 .
    EF598824 Genomic DNA. Translation: ABR04117.1 .
    EF598825 Genomic DNA. Translation: ABR04118.1 .
    EF598826 Genomic DNA. Translation: ABR04119.1 .
    EF598827 Genomic DNA. Translation: ABR04120.1 .
    EF598828 Genomic DNA. Translation: ABR04121.1 .
    EF598829 Genomic DNA. Translation: ABR04122.1 .
    EF598830 Genomic DNA. Translation: ABR04123.1 .
    EF598831 Genomic DNA. Translation: ABR04124.1 .
    EF598832 Genomic DNA. Translation: ABR04125.1 .
    EF598833 Genomic DNA. Translation: ABR04126.1 .
    EF598834 Genomic DNA. Translation: ABR04127.1 .
    EF598835 Genomic DNA. Translation: ABR04128.1 .
    EF598836 Genomic DNA. Translation: ABR04129.1 .
    EF598837 Genomic DNA. Translation: ABR04130.1 .
    EF598838 Genomic DNA. Translation: ABR04131.1 .
    EF598839 Genomic DNA. Translation: ABR04132.1 .
    EF598840 Genomic DNA. Translation: ABR04133.1 .
    EF598841 Genomic DNA. Translation: ABR04134.1 .
    EF598842 Genomic DNA. Translation: ABR04135.1 .
    EF598843 Genomic DNA. Translation: ABR04136.1 .
    EF598844 Genomic DNA. Translation: ABR04137.1 .
    EF598845 Genomic DNA. Translation: ABR04138.1 .
    EF598846 Genomic DNA. Translation: ABR04139.1 .
    EF598847 Genomic DNA. Translation: ABR04140.1 .
    AK220790 mRNA. Translation: BAD94031.1 . Different initiation.
    EU550991 Genomic DNA. Translation: ACB31753.1 .
    EU550992 Genomic DNA. Translation: ACB31754.1 .
    EU550993 Genomic DNA. Translation: ACB31755.1 .
    EU550994 Genomic DNA. Translation: ACB31756.1 .
    EU550995 Genomic DNA. Translation: ACB31757.1 .
    EU550996 Genomic DNA. Translation: ACB31758.1 .
    EU550997 Genomic DNA. Translation: ACB31759.1 .
    EU550998 Genomic DNA. Translation: ACB31760.1 .
    EU550999 Genomic DNA. Translation: ACB31761.1 .
    EU551000 Genomic DNA. Translation: ACB31762.1 .
    EU551001 Genomic DNA. Translation: ACB31763.1 .
    EU551002 Genomic DNA. Translation: ACB31764.1 .
    EU551003 Genomic DNA. Translation: ACB31765.1 .
    EU551004 Genomic DNA. Translation: ACB31766.1 .
    EU551005 Genomic DNA. Translation: ACB31767.1 .
    EU551006 Genomic DNA. Translation: ACB31768.1 .
    EU551007 Genomic DNA. Translation: ACB31769.1 .
    EU551008 Genomic DNA. Translation: ACB31770.1 .
    EU551009 Genomic DNA. Translation: ACB31771.1 .
    EU551010 Genomic DNA. Translation: ACB31772.1 .
    EU551011 Genomic DNA. Translation: ACB31773.1 .
    EU551012 Genomic DNA. Translation: ACB31774.1 .
    EU551013 Genomic DNA. Translation: ACB31775.1 .
    EU551014 Genomic DNA. Translation: ACB31776.1 .
    PIRi T48087.
    RefSeqi NP_567135.1. NM_116163.3.
    UniGenei At.25594.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2P1M X-ray 1.80 B 1-594 [» ]
    2P1N X-ray 2.50 B/E 1-594 [» ]
    2P1O X-ray 1.90 B 1-594 [» ]
    2P1P X-ray 2.21 B 1-594 [» ]
    2P1Q X-ray 1.91 B 1-594 [» ]
    3C6N X-ray 2.60 B 1-594 [» ]
    3C6O X-ray 2.70 B 1-594 [» ]
    3C6P X-ray 2.70 B 1-594 [» ]
    ProteinModelPortali Q570C0.
    SMRi Q570C0. Positions 10-576.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 10787. 18 interactions.
    DIPi DIP-31740N.
    IntActi Q570C0. 16 interactions.

    Proteomic databases

    PaxDbi Q570C0.
    PRIDEi Q570C0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT3G62980.1 ; AT3G62980.1 ; AT3G62980 .
    GeneIDi 825473.
    KEGGi ath:AT3G62980.

    Organism-specific databases

    GeneFarmi 4958.
    TAIRi AT3G62980.

    Phylogenomic databases

    eggNOGi NOG267823.
    HOGENOMi HOG000239805.
    InParanoidi Q570C0.
    KOi K14485.
    OMAi CEGLTSL.
    PhylomeDBi Q570C0.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    EvolutionaryTracei Q570C0.
    PROi Q570C0.

    Gene expression databases

    ArrayExpressi Q570C0.
    Genevestigatori Q570C0.

    Family and domain databases

    InterProi IPR001810. F-box_dom.
    [Graphical view ]
    Pfami PF12937. F-box-like. 1 hit.
    [Graphical view ]
    SMARTi SM00256. FBOX. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81383. SSF81383. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The TIR1 protein of Arabidopsis functions in auxin response and is related to human SKP2 and yeast grr1p."
      Ruegger M., Dewey E., Gray W.M., Hobbie L., Turner J., Estelle M.
      Genes Dev. 12:198-207(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, MUTAGENESIS OF GLY-147 AND GLY-441.
    2. "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.
    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 genetic architecture of shoot branching in Arabidopsis thaliana: a comparative assessment of candidate gene associations vs. quantitative trait locus mapping."
      Ehrenreich I.M., Stafford P.A., Purugganan M.D.
      Genetics 176:1223-1236(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 172-380.
      Strain: cv. Ag-0, cv. An-1, cv. Br-0, cv. C24, cv. Ct-1, cv. Cvi-1, cv. Edi-0, cv. Ga-0, cv. Kas-2, cv. Kin-0, cv. Landsberg erecta, cv. Ll-0, cv. Lz-0, cv. Ms-0, cv. Mt-0, cv. Nd-1, cv. Nok-3, cv. Oy-0, cv. Se-0, cv. Sorbo, cv. Tsu-1, cv. Van-0, cv. Wa-1 and cv. Wassilewskija.
    6. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
      , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 359-594.
      Strain: cv. Columbia.
    7. "Sequence variation of microRNAs and their binding sites in Arabidopsis."
      Ehrenreich I.M., Purugganan M.D.
      Plant Physiol. 146:1974-1982(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 429-579.
      Strain: cv. Ag-0, cv. An-1, cv. Bay-0, cv. Br-0, cv. C24, cv. Ct-1, cv. Cvi-0, cv. Edi-0, cv. Ei-2, cv. Ga-0, cv. Gy-0, cv. Kas-2, cv. Ll-0, cv. Mrk-0, cv. Ms-0, cv. Mt-0, cv. Nd-1, cv. Nok-3, cv. Oy-0, cv. Sorbo, cv. Wa-1, cv. Wassilewskija, cv. Wei-0 and cv. Wt-5.
    8. "Identification of an SCF ubiquitin-ligase complex required for auxin response in Arabidopsis thaliana."
      Gray W.M., del Pozo J.C., Walker L., Hobbie L., Risseeuw E., Banks T., Crosby W.L., Yang M., Ma H., Estelle M.
      Genes Dev. 13:1678-1691(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH SKP1A; SKP1B AND CUL1, DOMAIN, MUTAGENESIS OF PRO-10.
    9. Cited for: GENE FAMILY, NOMENCLATURE.
    10. "Auxin regulates SCF(TIR1)-dependent degradation of AUX/IAA proteins."
      Gray W.M., Kepinski S., Rouse D., Leyser O., Estelle M.
      Nature 414:271-276(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IAA7 AND IAA17.
    11. "Interactions of the COP9 signalosome with the E3 ubiquitin ligase SCF(TIR1) in mediating auxin response."
      Schwechheimer C., Serino G., Callis J., Crosby W.L., Lyapina S., Deshaies R.J., Gray W.M., Estelle M., Deng X.-W.
      Science 292:1379-1382(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THE CSN COMPLEX.
    12. "Role of the Arabidopsis RING-H2 protein RBX1 in RUB modification and SCF function."
      Gray W.M., Hellmann H., Dharmasiri S., Estelle M.
      Plant Cell 14:2137-2144(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBX1.
    13. "Regulation of Arabidopsis SHY2/IAA3 protein turnover."
      Tian Q., Nagpal P., Reed J.W.
      Plant J. 36:643-651(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IAA3.
    14. "Five components of the ethylene-response pathway identified in a screen for weak ethylene-insensitive mutants in Arabidopsis."
      Alonso J.M., Stepanova A.N., Solano R., Wisman E., Ferrari S., Ausubel F.M., Ecker J.R.
      Proc. Natl. Acad. Sci. U.S.A. 100:2992-2997(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF 574-TRP--LEU-594.
    15. "Plant development is regulated by a family of auxin receptor F box proteins."
      Dharmasiri N., Dharmasiri S., Weijers D., Lechner E., Yamada M., Hobbie L., Ehrismann J.S., Juergens G., Estelle M.
      Dev. Cell 9:109-119(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH IAA12; IAA7 AND SKP1A/ASK1.
    16. "The F-box protein TIR1 is an auxin receptor."
      Dharmasiri N., Dharmasiri S., Estelle M.
      Nature 435:441-445(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AUX/IAA PROTEINS AND AUXIN.
    17. "The Arabidopsis F-box protein TIR1 is an auxin receptor."
      Kepinski S., Leyser O.
      Nature 435:446-451(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AUX/IAA PROTEINS AND AUXIN, MUTAGENESIS OF PRO-10; VAL-33 AND LYS-35.
    18. "A plant miRNA contributes to antibacterial resistance by repressing auxin signaling."
      Navarro L., Dunoyer P., Jay F., Arnold B., Dharmasiri N., Estelle M., Voinnet O., Jones J.D.G.
      Science 312:436-439(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    19. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SKP1A; AUXIN; AUX/IAA POLYPEPTIDE SUBSTRATE; AUXIN ANALOGS AND MYO-INOSITOL HEXAKISPHOSPHATE.
    20. "Small-molecule agonists and antagonists of F-box protein-substrate interactions in auxin perception and signaling."
      Hayashi K., Tan X., Zheng N., Hatate T., Kimura Y., Kepinski S., Nozaki H.
      Proc. Natl. Acad. Sci. U.S.A. 105:5632-5637(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SKP1A; AUX/IAA POLYPEPTIDE; AUXIN; AUXIN AGONISTS; AUXIN ANTAGONISTS AND MYO-INOSITOL HEXAKISPHOSPHATE, FUNCTION.

    Entry informationi

    Entry nameiTIR1_ARATH
    AccessioniPrimary (citable) accession number: Q570C0
    Secondary accession number(s): A5YZP2, B2CVU0, O24660
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2005
    Last sequence update: June 21, 2005
    Last modified: October 1, 2014
    This is version 94 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The myo-inositol hexakisphosphate acts as a structural cofactor.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3