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Q570C0 (TIR1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein TRANSPORT INHIBITOR RESPONSE 1
Alternative name(s):
Weak ethylene-insensitive protein 1
Gene names
Name:TIR1
Synonyms:FBL1, WEI1
Ordered Locus Names:At3g62980
ORF Names:T20O10.80
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length594 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.8 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.20

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17

Subcellular location

Nucleus Ref.15.

Tissue specificity

Expressed in roots, stems, leaves and flowers. In adult plants, mostly expressed in floral stigma, anther filaments, abscission zones and vascular tissues. Ref.1 Ref.8

Developmental stage

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. Ref.8

Induction

Repressed by miR393a (microRNA) in response to flg-22 (flagellin-derived peptide 22). Ref.18

Domain

The F-box is necessary for the interaction with SKP1. Ref.8

Disruption phenotype

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

Miscellaneous

The myo-inositol hexakisphosphate acts as a structural cofactor.

Sequence similarities

Contains 1 F-box domain.

Sequence caution

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

Ontologies

Keywords
   Biological processAuxin signaling pathway
Cell cycle
Ethylene signaling pathway
Plant defense
Ubl conjugation pathway
   Cellular componentNucleus
   Molecular functionDevelopmental protein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processauxin-activated signaling pathway

Inferred from mutant phenotype Ref.20. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to phosphate starvation

Inferred from expression pattern PubMed 19106375. Source: TAIR

defense response

Inferred from electronic annotation. Source: UniProtKB-KW

ethylene-activated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

lateral root formation

Inferred from mutant phenotype Ref.1. Source: TAIR

pollen maturation

Inferred from genetic interaction PubMed 18628351. Source: TAIR

response to auxin

Inferred from mutant phenotype Ref.1. Source: TAIR

response to molecule of bacterial origin

Inferred from expression pattern Ref.18. Source: TAIR

stamen development

Inferred from genetic interaction PubMed 18628351. Source: TAIR

   Cellular_componentSCF ubiquitin ligase complex

Inferred from direct assay Ref.8. Source: TAIR

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionauxin binding

Inferred from direct assay Ref.19Ref.20. Source: UniProtKB

auxin receptor activity

Inferred from direct assay Ref.16. Source: UniProtKB

inositol hexakisphosphate binding

Inferred from direct assay Ref.19. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.19. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred by curator Ref.8. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 594594Protein TRANSPORT INHIBITOR RESPONSE 1
PRO_0000119965

Regions

Domain3 – 5048F-box
Region81 – 822Interaction with auxin-responsive proteins
Region113 – 1142Myo-inositol hexakisphosphate binding
Region347 – 3526Interaction with auxin-responsive proteins
Region401 – 4033Myo-inositol hexakisphosphate binding
Region403 – 4042Auxin binding
Region405 – 4095Interaction with auxin-responsive proteins
Region438 – 4392Auxin binding
Region464 – 4652Interaction with auxin-responsive proteins
Region484 – 4852Myo-inositol hexakisphosphate binding

Sites

Binding site741Myo-inositol hexakisphosphate
Binding site3441Myo-inositol hexakisphosphate
Binding site4361Myo-inositol hexakisphosphate
Binding site5091Myo-inositol hexakisphosphate
Site1391Interaction with auxin-responsive proteins
Site1651Interaction with auxin-responsive proteins
Site3801Interaction with auxin-responsive proteins
Site4891Interaction with auxin-responsive proteins

Experimental info

Mutagenesis101P → A: Abolishes SCF(TIR1) complex formation, altered auxin-mediated response and reduced affinity for auxin. Ref.8 Ref.17
Mutagenesis331V → A: No affinity for auxin. Ref.17
Mutagenesis351K → A: No affinity for auxin. Ref.17
Mutagenesis1471G → D in tir1-1; insensitive to auxin ubiquitously and to ethylene in roots only. Ref.1
Mutagenesis4411G → D in tir1-2; insensitive to auxin. Ref.1
Mutagenesis574 – 59421Missing in tir1-101/wei1; insensitive to auxin ubiquitously and to ethylene in roots only. Ref.14
Sequence conflict4901D → E in BAD94031. Ref.6
Sequence conflict5681D → G in BAD94031. Ref.6

Secondary structure

..................................................................................................... 594
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q570C0 [UniParc].

Last modified June 21, 2005. Version 2.
Checksum: 9E19ED5DABF40D07

FASTA59466,799
        10         20         30         40         50         60 
MQKRIALSFP EEVLEHVFSF IQLDKDRNSV SLVCKSWYEI ERWCRRKVFI GNCYAVSPAT 

        70         80         90        100        110        120 
VIRRFPKVRS VELKGKPHFA DFNLVPDGWG GYVYPWIEAM SSSYTWLEEI RLKRMVVTDD 

       130        140        150        160        170        180 
CLELIAKSFK NFKVLVLSSC EGFSTDGLAA IAATCRNLKE LDLRESDVDD VSGHWLSHFP 

       190        200        210        220        230        240 
DTYTSLVSLN ISCLASEVSF SALERLVTRC PNLKSLKLNR AVPLEKLATL LQRAPQLEEL 

       250        260        270        280        290        300 
GTGGYTAEVR PDVYSGLSVA LSGCKELRCL SGFWDAVPAY LPAVYSVCSR LTTLNLSYAT 

       310        320        330        340        350        360 
VQSYDLVKLL CQCPKLQRLW VLDYIEDAGL EVLASTCKDL RELRVFPSEP FVMEPNVALT 

       370        380        390        400        410        420 
EQGLVSVSMG CPKLESVLYF CRQMTNAALI TIARNRPNMT RFRLCIIEPK APDYLTLEPL 

       430        440        450        460        470        480 
DIGFGAIVEH CKDLRRLSLS GLLTDKVFEY IGTYAKKMEM LSVAFAGDSD LGMHHVLSGC 

       490        500        510        520        530        540 
DSLRKLEIRD CPFGDKALLA NASKLETMRS LWMSSCSVSF GACKLLGQKM PKLNVEVIDE 

       550        560        570        580        590 
RGAPDSRPES CPVERVFIYR TVAGPRFDMP GFVWNMDQDS TMRFSRQIIT TNGL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"F-box proteins in Arabidopsis."
Xiao W., Jang J.-C.
Trends Plant Sci. 5:454-457(2000) [PubMed] [Europe PMC] [Abstract]
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]"Mechanism of auxin perception by the TIR1 ubiquitin ligase."
Tan X., Calderon-Villalobos L.I.A., Sharon M., Zheng C., Robinson C.V., Estelle M., Zheng N.
Nature 446:640-645(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

PlantsUBQ

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT48087.
RefSeqNP_567135.1. NM_116163.3.
UniGeneAt.25594.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalQ570C0.
SMRQ570C0. Positions 10-576.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid10787. 18 interactions.
DIPDIP-31740N.
IntActQ570C0. 16 interactions.

Proteomic databases

PaxDbQ570C0.
PRIDEQ570C0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT3G62980.1; AT3G62980.1; AT3G62980.
GeneID825473.
KEGGath:AT3G62980.

Organism-specific databases

GeneFarm4958.
TAIRAT3G62980.

Phylogenomic databases

eggNOGNOG267823.
HOGENOMHOG000239805.
InParanoidQ570C0.
KOK14485.
OMACEGLTSL.
PhylomeDBQ570C0.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ570C0.
GenevestigatorQ570C0.

Family and domain databases

InterProIPR001810. F-box_dom.
[Graphical view]
PfamPF12937. F-box-like. 1 hit.
[Graphical view]
SMARTSM00256. FBOX. 1 hit.
[Graphical view]
SUPFAMSSF81383. SSF81383. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ570C0.
PROQ570C0.

Entry information

Entry nameTIR1_ARATH
AccessionPrimary (citable) accession number: Q570C0
Secondary accession number(s): A5YZP2, B2CVU0, O24660
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: June 21, 2005
Last modified: July 9, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names