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Protein TRANSPORT INHIBITOR RESPONSE 1 (Weak ethylene-insensitive protein 1)

 TIR1_ARATH              Reviewed;         594 AA.
Q570C0; A5YZP2; B2CVU0; O24660;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 2.
02-JUN-2021, entry version 141.
RecName: Full=Protein TRANSPORT INHIBITOR RESPONSE 1;
AltName: Full=Weak ethylene-insensitive protein 1;
Name=TIR1; Synonyms=FBL1, WEI1; OrderedLocusNames=At3g62980;
ORFNames=T20O10.80;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, DISRUPTION PHENOTYPE,
TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-147 AND GLY-441.
PubMed=9436980; DOI=10.1101/gad.12.2.198;
Ruegger M., Dewey E., Gray W.M., Hobbie L., Turner J., Estelle M.;
"The TIR1 protein of Arabidopsis functions in auxin response and is related
to human SKP2 and yeast grr1p.";
Genes Dev. 12:198-207(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
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.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana reference
genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[5]
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;
PubMed=17435248; DOI=10.1534/genetics.107.071928;
Ehrenreich I.M., Stafford P.A., Purugganan M.D.;
"The genetic architecture of shoot branching in Arabidopsis thaliana: a
comparative assessment of candidate gene associations vs. quantitative
trait locus mapping.";
Genetics 176:1223-1236(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 359-594.
STRAIN=cv. Columbia;
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.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
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;
PubMed=18305205; DOI=10.1104/pp.108.116582;
Ehrenreich I.M., Purugganan M.D.;
"Sequence variation of microRNAs and their binding sites in Arabidopsis.";
Plant Physiol. 146:1974-1982(2008).
[8]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH SKP1A;
SKP1B AND CUL1, DOMAIN, AND MUTAGENESIS OF PRO-10.
PubMed=10398681; DOI=10.1101/gad.13.13.1678;
Gray W.M., del Pozo J.C., Walker L., Hobbie L., Risseeuw E., Banks T.,
Crosby W.L., Yang M., Ma H., Estelle M.;
"Identification of an SCF ubiquitin-ligase complex required for auxin
response in Arabidopsis thaliana.";
Genes Dev. 13:1678-1691(1999).
[9]
GENE FAMILY, AND NOMENCLATURE.
PubMed=11077244; DOI=10.1016/s1360-1385(00)01769-6;
Xiao W., Jang J.-C.;
"F-box proteins in Arabidopsis.";
Trends Plant Sci. 5:454-457(2000).
[10]
INTERACTION WITH IAA7 AND IAA17.
PubMed=11713520; DOI=10.1038/35104500;
Gray W.M., Kepinski S., Rouse D., Leyser O., Estelle M.;
"Auxin regulates SCF(TIR1)-dependent degradation of AUX/IAA proteins.";
Nature 414:271-276(2001).
[11]
INTERACTION WITH THE CSN COMPLEX.
PubMed=11337587; DOI=10.1126/science.1059776;
Schwechheimer C., Serino G., Callis J., Crosby W.L., Lyapina S.,
Deshaies R.J., Gray W.M., Estelle M., Deng X.-W.;
"Interactions of the COP9 signalosome with the E3 ubiquitin ligase
SCF(TIR1) in mediating auxin response.";
Science 292:1379-1382(2001).
[12]
INTERACTION WITH RBX1.
PubMed=12215511; DOI=10.1105/tpc.003178;
Gray W.M., Hellmann H., Dharmasiri S., Estelle M.;
"Role of the Arabidopsis RING-H2 protein RBX1 in RUB modification and SCF
function.";
Plant Cell 14:2137-2144(2002).
[13]
INTERACTION WITH IAA3.
PubMed=14617065; DOI=10.1046/j.1365-313x.2003.01909.x;
Tian Q., Nagpal P., Reed J.W.;
"Regulation of Arabidopsis SHY2/IAA3 protein turnover.";
Plant J. 36:643-651(2003).
[14]
FUNCTION, AND MUTAGENESIS OF 574-TRP--LEU-594.
PubMed=12606727; DOI=10.1073/pnas.0438070100;
Alonso J.M., Stepanova A.N., Solano R., Wisman E., Ferrari S.,
Ausubel F.M., Ecker J.R.;
"Five components of the ethylene-response pathway identified in a screen
for weak ethylene-insensitive mutants in Arabidopsis.";
Proc. Natl. Acad. Sci. U.S.A. 100:2992-2997(2003).
[15]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH IAA12; IAA7 AND
SKP1A/ASK1.
PubMed=15992545; DOI=10.1016/j.devcel.2005.05.014;
Dharmasiri N., Dharmasiri S., Weijers D., Lechner E., Yamada M., Hobbie L.,
Ehrismann J.S., Juergens G., Estelle M.;
"Plant development is regulated by a family of auxin receptor F box
proteins.";
Dev. Cell 9:109-119(2005).
[16]
FUNCTION, AND INTERACTION WITH AUX/IAA PROTEINS AND AUXIN.
PubMed=15917797; DOI=10.1038/nature03543;
Dharmasiri N., Dharmasiri S., Estelle M.;
"The F-box protein TIR1 is an auxin receptor.";
Nature 435:441-445(2005).
[17]
FUNCTION, INTERACTION WITH AUX/IAA PROTEINS AND AUXIN, AND MUTAGENESIS OF
PRO-10; VAL-33 AND LYS-35.
PubMed=15917798; DOI=10.1038/nature03542;
Kepinski S., Leyser O.;
"The Arabidopsis F-box protein TIR1 is an auxin receptor.";
Nature 435:446-451(2005).
[18]
FUNCTION, AND INDUCTION.
PubMed=16627744; DOI=10.1126/science.1126088;
Navarro L., Dunoyer P., Jay F., Arnold B., Dharmasiri N., Estelle M.,
Voinnet O., Jones J.D.G.;
"A plant miRNA contributes to antibacterial resistance by repressing auxin
signaling.";
Science 312:436-439(2006).
[19]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH SKP1A; AUXIN; AUX/IAA
POLYPEPTIDE SUBSTRATE; AUXIN ANALOGS AND MYO-INOSITOL HEXAKISPHOSPHATE.
PubMed=17410169; DOI=10.1038/nature05731;
Tan X., Calderon-Villalobos L.I.A., Sharon M., Zheng C., Robinson C.V.,
Estelle M., Zheng N.;
"Mechanism of auxin perception by the TIR1 ubiquitin ligase.";
Nature 446:640-645(2007).
[20]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SKP1A; AUX/IAA
POLYPEPTIDE; AUXIN; AUXIN AGONISTS; AUXIN ANTAGONISTS AND MYO-INOSITOL
HEXAKISPHOSPHATE, AND FUNCTION.
PubMed=18391211; DOI=10.1073/pnas.0711146105;
Hayashi K., Tan X., Zheng N., Hatate T., Kimura Y., Kepinski S., Nozaki H.;
"Small-molecule agonists and antagonists of F-box protein-substrate
interactions in auxin perception and signaling.";
Proc. Natl. Acad. Sci. U.S.A. 105:5632-5637(2008).
-!- 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.
{ECO:0000269|PubMed:10398681, ECO:0000269|PubMed:12606727,
ECO:0000269|PubMed:15917797, ECO:0000269|PubMed:15917798,
ECO:0000269|PubMed:15992545, ECO:0000269|PubMed:16627744,
ECO:0000269|PubMed:18391211, ECO:0000269|PubMed:9436980}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:10398681,
ECO:0000269|PubMed:11337587, ECO:0000269|PubMed:11713520,
ECO:0000269|PubMed:12215511, ECO:0000269|PubMed:14617065,
ECO:0000269|PubMed:15917797, ECO:0000269|PubMed:15917798,
ECO:0000269|PubMed:15992545, ECO:0000269|PubMed:17410169,
ECO:0000269|PubMed:18391211}.
-!- INTERACTION:
Q570C0; Q9SU81: At4g29700; NbExp=3; IntAct=EBI-307183, EBI-25530262;
Q570C0; P93830: IAA17; NbExp=2; IntAct=EBI-307183, EBI-632243;
Q570C0; Q38822: IAA3; NbExp=3; IntAct=EBI-307183, EBI-307174;
Q570C0; Q38825: IAA7; NbExp=8; IntAct=EBI-307183, EBI-602959;
Q570C0; Q39255: SKP1A; NbExp=11; IntAct=EBI-307183, EBI-532357;
Q570C0; Q9FHW7: SKP1B; NbExp=7; IntAct=EBI-307183, EBI-604076;
Q570C0; Q93Z00: TCP14; NbExp=3; IntAct=EBI-307183, EBI-4424563;
Q570C0; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-307183, EBI-15192297;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15992545}.
-!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves and flowers. In
adult plants, mostly expressed in floral stigma, anther filaments,
abscission zones and vascular tissues. {ECO:0000269|PubMed:10398681,
ECO:0000269|PubMed:9436980}.
-!- 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. {ECO:0000269|PubMed:10398681}.
-!- INDUCTION: Repressed by miR393a (microRNA) in response to flg-22
(flagellin-derived peptide 22). {ECO:0000269|PubMed:16627744}.
-!- DOMAIN: The F-box is necessary for the interaction with SKP1.
{ECO:0000269|PubMed:10398681}.
-!- DISRUPTION PHENOTYPE: Plant are deficient in a variety of auxin-
regulated growth processes including lateral root formation, and
hypocotyl and cell elongation. {ECO:0000269|PubMed:9436980}.
-!- MISCELLANEOUS: The myo-inositol hexakisphosphate acts as a structural
cofactor.
-!- SEQUENCE CAUTION:
Sequence=BAD94031.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF005047; AAB69175.1; -; Genomic_DNA.
EMBL; AF005048; AAB69176.1; -; mRNA.
EMBL; AL163816; CAB87743.1; -; Genomic_DNA.
EMBL; CP002686; AEE80419.1; -; Genomic_DNA.
EMBL; BT001946; AAN71945.1; -; mRNA.
EMBL; EF598824; ABR04117.1; -; Genomic_DNA.
EMBL; EF598825; ABR04118.1; -; Genomic_DNA.
EMBL; EF598826; ABR04119.1; -; Genomic_DNA.
EMBL; EF598827; ABR04120.1; -; Genomic_DNA.
EMBL; EF598828; ABR04121.1; -; Genomic_DNA.
EMBL; EF598829; ABR04122.1; -; Genomic_DNA.
EMBL; EF598830; ABR04123.1; -; Genomic_DNA.
EMBL; EF598831; ABR04124.1; -; Genomic_DNA.
EMBL; EF598832; ABR04125.1; -; Genomic_DNA.
EMBL; EF598833; ABR04126.1; -; Genomic_DNA.
EMBL; EF598834; ABR04127.1; -; Genomic_DNA.
EMBL; EF598835; ABR04128.1; -; Genomic_DNA.
EMBL; EF598836; ABR04129.1; -; Genomic_DNA.
EMBL; EF598837; ABR04130.1; -; Genomic_DNA.
EMBL; EF598838; ABR04131.1; -; Genomic_DNA.
EMBL; EF598839; ABR04132.1; -; Genomic_DNA.
EMBL; EF598840; ABR04133.1; -; Genomic_DNA.
EMBL; EF598841; ABR04134.1; -; Genomic_DNA.
EMBL; EF598842; ABR04135.1; -; Genomic_DNA.
EMBL; EF598843; ABR04136.1; -; Genomic_DNA.
EMBL; EF598844; ABR04137.1; -; Genomic_DNA.
EMBL; EF598845; ABR04138.1; -; Genomic_DNA.
EMBL; EF598846; ABR04139.1; -; Genomic_DNA.
EMBL; EF598847; ABR04140.1; -; Genomic_DNA.
EMBL; AK220790; BAD94031.1; ALT_INIT; mRNA.
EMBL; EU550991; ACB31753.1; -; Genomic_DNA.
EMBL; EU550992; ACB31754.1; -; Genomic_DNA.
EMBL; EU550993; ACB31755.1; -; Genomic_DNA.
EMBL; EU550994; ACB31756.1; -; Genomic_DNA.
EMBL; EU550995; ACB31757.1; -; Genomic_DNA.
EMBL; EU550996; ACB31758.1; -; Genomic_DNA.
EMBL; EU550997; ACB31759.1; -; Genomic_DNA.
EMBL; EU550998; ACB31760.1; -; Genomic_DNA.
EMBL; EU550999; ACB31761.1; -; Genomic_DNA.
EMBL; EU551000; ACB31762.1; -; Genomic_DNA.
EMBL; EU551001; ACB31763.1; -; Genomic_DNA.
EMBL; EU551002; ACB31764.1; -; Genomic_DNA.
EMBL; EU551003; ACB31765.1; -; Genomic_DNA.
EMBL; EU551004; ACB31766.1; -; Genomic_DNA.
EMBL; EU551005; ACB31767.1; -; Genomic_DNA.
EMBL; EU551006; ACB31768.1; -; Genomic_DNA.
EMBL; EU551007; ACB31769.1; -; Genomic_DNA.
EMBL; EU551008; ACB31770.1; -; Genomic_DNA.
EMBL; EU551009; ACB31771.1; -; Genomic_DNA.
EMBL; EU551010; ACB31772.1; -; Genomic_DNA.
EMBL; EU551011; ACB31773.1; -; Genomic_DNA.
EMBL; EU551012; ACB31774.1; -; Genomic_DNA.
EMBL; EU551013; ACB31775.1; -; Genomic_DNA.
EMBL; EU551014; ACB31776.1; -; Genomic_DNA.
PIR; T48087; T48087.
RefSeq; NP_567135.1; NM_116163.4.
PDB; 2P1M; X-ray; 1.80 A; B=1-594.
PDB; 2P1N; X-ray; 2.50 A; B/E=1-594.
PDB; 2P1O; X-ray; 1.90 A; B=1-594.
PDB; 2P1P; X-ray; 2.21 A; B=1-594.
PDB; 2P1Q; X-ray; 1.91 A; B=1-594.
PDB; 3C6N; X-ray; 2.60 A; B=1-594.
PDB; 3C6O; X-ray; 2.70 A; B=1-594.
PDB; 3C6P; X-ray; 2.70 A; B=1-594.
PDBsum; 2P1M; -.
PDBsum; 2P1N; -.
PDBsum; 2P1O; -.
PDBsum; 2P1P; -.
PDBsum; 2P1Q; -.
PDBsum; 3C6N; -.
PDBsum; 3C6O; -.
PDBsum; 3C6P; -.
SMR; Q570C0; -.
BioGRID; 10787; 24.
ComplexPortal; CPX-1343; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1A.
ComplexPortal; CPX-1515; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1B.
ComplexPortal; CPX-1516; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK3.
ComplexPortal; CPX-1517; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK4.
ComplexPortal; CPX-1518; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK5.
ComplexPortal; CPX-1519; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK6.
ComplexPortal; CPX-1520; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK7.
ComplexPortal; CPX-1521; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK8.
ComplexPortal; CPX-1522; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK9.
ComplexPortal; CPX-1523; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK10.
ComplexPortal; CPX-1524; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK11.
ComplexPortal; CPX-1525; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK12.
ComplexPortal; CPX-1526; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK13.
ComplexPortal; CPX-1527; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK14.
ComplexPortal; CPX-1528; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK15.
ComplexPortal; CPX-1529; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK16.
ComplexPortal; CPX-1530; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK17.
ComplexPortal; CPX-1531; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK18.
ComplexPortal; CPX-1532; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK19.
ComplexPortal; CPX-1533; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK20.
ComplexPortal; CPX-1534; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK21.
ComplexPortal; CPX-1535; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1A.
ComplexPortal; CPX-1536; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1B.
ComplexPortal; CPX-1537; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK3.
ComplexPortal; CPX-1538; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK4.
ComplexPortal; CPX-1539; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK5.
ComplexPortal; CPX-1540; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK6.
ComplexPortal; CPX-1541; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK7.
ComplexPortal; CPX-1542; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK8.
ComplexPortal; CPX-1543; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK9.
ComplexPortal; CPX-1544; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK10.
ComplexPortal; CPX-1545; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK11.
ComplexPortal; CPX-1546; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK12.
ComplexPortal; CPX-1547; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK13.
ComplexPortal; CPX-1548; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK14.
ComplexPortal; CPX-1549; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK15.
ComplexPortal; CPX-1550; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK16.
ComplexPortal; CPX-1551; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK17.
ComplexPortal; CPX-1552; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK18.
ComplexPortal; CPX-1553; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK19.
ComplexPortal; CPX-1554; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK20.
ComplexPortal; CPX-1555; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK21.
ComplexPortal; CPX-1557; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-SKP1A.
ComplexPortal; CPX-1558; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-SKP1B.
ComplexPortal; CPX-1559; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK3.
ComplexPortal; CPX-1560; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK4.
ComplexPortal; CPX-1561; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK5.
ComplexPortal; CPX-1562; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK6.
ComplexPortal; CPX-1563; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK7.
ComplexPortal; CPX-1564; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK8.
ComplexPortal; CPX-1565; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK9.
ComplexPortal; CPX-1566; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK10.
ComplexPortal; CPX-1567; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK11.
ComplexPortal; CPX-1568; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK12.
ComplexPortal; CPX-1569; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK13.
ComplexPortal; CPX-1570; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK14.
ComplexPortal; CPX-1571; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK15.
ComplexPortal; CPX-1572; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK16.
ComplexPortal; CPX-1573; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK17.
ComplexPortal; CPX-1574; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK18.
ComplexPortal; CPX-1575; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK19.
ComplexPortal; CPX-1576; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK20.
ComplexPortal; CPX-1577; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK21.
ComplexPortal; CPX-1578; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-SKP1A.
ComplexPortal; CPX-1579; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-SKP1B.
ComplexPortal; CPX-1580; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK3.
ComplexPortal; CPX-1581; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK4.
ComplexPortal; CPX-1582; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK5.
ComplexPortal; CPX-1583; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK6.
ComplexPortal; CPX-1584; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK7.
ComplexPortal; CPX-1585; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK8.
ComplexPortal; CPX-1586; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK9.
ComplexPortal; CPX-1587; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK10.
ComplexPortal; CPX-1588; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK11.
ComplexPortal; CPX-1589; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK12.
ComplexPortal; CPX-1590; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK13.
ComplexPortal; CPX-1591; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK14.
ComplexPortal; CPX-1592; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK15.
ComplexPortal; CPX-1593; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK16.
ComplexPortal; CPX-1594; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK17.
ComplexPortal; CPX-1595; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK18.
ComplexPortal; CPX-1596; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK19.
ComplexPortal; CPX-1597; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK20.
ComplexPortal; CPX-1598; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1B-ASK21.
DIP; DIP-31740N; -.
ELM; Q570C0; -.
IntAct; Q570C0; 21.
STRING; 3702.AT3G62980.1; -.
iPTMnet; Q570C0; -.
PaxDb; Q570C0; -.
PRIDE; Q570C0; -.
ProteomicsDB; 232425; -.
EnsemblPlants; AT3G62980.1; AT3G62980.1; AT3G62980.
GeneID; 825473; -.
Gramene; AT3G62980.1; AT3G62980.1; AT3G62980.
KEGG; ath:AT3G62980; -.
Araport; AT3G62980; -.
TAIR; locus:2099237; AT3G62980.
eggNOG; KOG1947; Eukaryota.
HOGENOM; CLU_022456_1_0_1; -.
InParanoid; Q570C0; -.
OMA; WIEAMAT; -.
OrthoDB; 1282076at2759; -.
PhylomeDB; Q570C0; -.
UniPathway; UPA00143; -.
EvolutionaryTrace; Q570C0; -.
PRO; PR:Q570C0; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q570C0; baseline and differential.
Genevisible; Q570C0; AT.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:TAIR.
GO; GO:0010011; F:auxin binding; IDA:UniProtKB.
GO; GO:0038198; F:auxin receptor activity; IDA:UniProtKB.
GO; GO:0000822; F:inositol hexakisphosphate binding; IDA:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IC:TAIR.
GO; GO:0009734; P:auxin-activated signaling pathway; IMP:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0010311; P:lateral root formation; IMP:TAIR.
GO; GO:0010152; P:pollen maturation; IGI:TAIR.
GO; GO:0009733; P:response to auxin; IMP:TAIR.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0048443; P:stamen development; IGI:TAIR.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR041567; COI1_F-box.
InterPro; IPR036047; F-box-like_dom_sf.
InterPro; IPR001810; F-box_dom.
InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR041101; Transp_inhibit.
Pfam; PF18511; F-box_5; 1.
Pfam; PF18791; Transp_inhibit; 1.
SMART; SM00256; FBOX; 1.
SMART; SM00367; LRR_CC; 6.
SUPFAM; SSF81383; SSF81383; 1.
1: Evidence at protein level;
3D-structure; Auxin signaling pathway; Cell cycle; Developmental protein;
Ethylene signaling pathway; Nucleus; Plant defense; Reference proteome;
Ubl conjugation pathway.
CHAIN 1..594
/note="Protein TRANSPORT INHIBITOR RESPONSE 1"
/id="PRO_0000119965"
DOMAIN 3..50
/note="F-box"
REGION 81..82
/note="Interaction with auxin-responsive proteins"
REGION 113..114
/note="Myo-inositol hexakisphosphate binding"
REGION 347..352
/note="Interaction with auxin-responsive proteins"
REGION 401..403
/note="Myo-inositol hexakisphosphate binding"
REGION 403..404
/note="Auxin binding"
REGION 405..409
/note="Interaction with auxin-responsive proteins"
REGION 438..439
/note="Auxin binding"
REGION 464..465
/note="Interaction with auxin-responsive proteins"
REGION 484..485
/note="Myo-inositol hexakisphosphate binding"
BINDING 74
/note="Myo-inositol hexakisphosphate"
/evidence="ECO:0000269|PubMed:17410169,
ECO:0000269|PubMed:18391211"
BINDING 344
/note="Myo-inositol hexakisphosphate"
/evidence="ECO:0000269|PubMed:17410169,
ECO:0000269|PubMed:18391211"
BINDING 436
/note="Myo-inositol hexakisphosphate"
/evidence="ECO:0000269|PubMed:17410169,
ECO:0000269|PubMed:18391211"
BINDING 509
/note="Myo-inositol hexakisphosphate"
/evidence="ECO:0000269|PubMed:17410169,
ECO:0000269|PubMed:18391211"
SITE 139
/note="Interaction with auxin-responsive proteins"
SITE 165
/note="Interaction with auxin-responsive proteins"
SITE 380
/note="Interaction with auxin-responsive proteins"
SITE 489
/note="Interaction with auxin-responsive proteins"
MUTAGEN 10
/note="P->A: Abolishes SCF(TIR1) complex formation, altered
auxin-mediated response and reduced affinity for auxin."
/evidence="ECO:0000269|PubMed:10398681,
ECO:0000269|PubMed:15917798"
MUTAGEN 33
/note="V->A: No affinity for auxin."
/evidence="ECO:0000269|PubMed:15917798"
MUTAGEN 35
/note="K->A: No affinity for auxin."
/evidence="ECO:0000269|PubMed:15917798"
MUTAGEN 147
/note="G->D: In tir1-1; insensitive to auxin ubiquitously
and to ethylene in roots only."
/evidence="ECO:0000269|PubMed:9436980"
MUTAGEN 441
/note="G->D: In tir1-2; insensitive to auxin."
/evidence="ECO:0000269|PubMed:9436980"
MUTAGEN 574..594
/note="Missing: In tir1-101/wei1; insensitive to auxin
ubiquitously and to ethylene in roots only."
/evidence="ECO:0000269|PubMed:12606727"
CONFLICT 490
/note="D -> E (in Ref. 6; BAD94031)"
/evidence="ECO:0000305"
CONFLICT 568
/note="D -> G (in Ref. 6; BAD94031)"
/evidence="ECO:0000305"
HELIX 11..19
/evidence="ECO:0007829|PDB:2P1M"
HELIX 24..31
/evidence="ECO:0007829|PDB:2P1M"
HELIX 35..44
/evidence="ECO:0007829|PDB:2P1M"
STRAND 47..52
/evidence="ECO:0007829|PDB:2P1M"
HELIX 53..55
/evidence="ECO:0007829|PDB:2P1N"
HELIX 58..64
/evidence="ECO:0007829|PDB:2P1M"
STRAND 70..74
/evidence="ECO:0007829|PDB:2P1M"
HELIX 78..82
/evidence="ECO:0007829|PDB:2P1M"
HELIX 94..103
/evidence="ECO:0007829|PDB:2P1M"
STRAND 109..114
/evidence="ECO:0007829|PDB:2P1M"
HELIX 119..128
/evidence="ECO:0007829|PDB:2P1M"
STRAND 134..139
/evidence="ECO:0007829|PDB:2P1M"
STRAND 141..144
/evidence="ECO:0007829|PDB:2P1M"
HELIX 145..154
/evidence="ECO:0007829|PDB:2P1M"
STRAND 160..162
/evidence="ECO:0007829|PDB:2P1M"
STRAND 167..169
/evidence="ECO:0007829|PDB:2P1M"
HELIX 173..178
/evidence="ECO:0007829|PDB:2P1M"
STRAND 188..190
/evidence="ECO:0007829|PDB:2P1M"
HELIX 200..209
/evidence="ECO:0007829|PDB:2P1M"
STRAND 215..217
/evidence="ECO:0007829|PDB:2P1M"
HELIX 224..233
/evidence="ECO:0007829|PDB:2P1M"
STRAND 238..241
/evidence="ECO:0007829|PDB:2P1M"
HELIX 251..262
/evidence="ECO:0007829|PDB:2P1M"
STRAND 269..271
/evidence="ECO:0007829|PDB:2P1M"
HELIX 278..284
/evidence="ECO:0007829|PDB:2P1M"
HELIX 285..288
/evidence="ECO:0007829|PDB:2P1M"
STRAND 293..295
/evidence="ECO:0007829|PDB:2P1M"
HELIX 303..310
/evidence="ECO:0007829|PDB:2P1M"
STRAND 318..322
/evidence="ECO:0007829|PDB:2P1M"
HELIX 323..325
/evidence="ECO:0007829|PDB:2P1M"
HELIX 326..336
/evidence="ECO:0007829|PDB:2P1M"
STRAND 342..346
/evidence="ECO:0007829|PDB:2P1M"
STRAND 350..352
/evidence="ECO:0007829|PDB:3C6N"
HELIX 361..370
/evidence="ECO:0007829|PDB:2P1M"
STRAND 376..382
/evidence="ECO:0007829|PDB:2P1M"
HELIX 386..395
/evidence="ECO:0007829|PDB:2P1M"
STRAND 401..408
/evidence="ECO:0007829|PDB:2P1M"
TURN 414..416
/evidence="ECO:0007829|PDB:2P1M"
HELIX 421..430
/evidence="ECO:0007829|PDB:2P1M"
STRAND 436..438
/evidence="ECO:0007829|PDB:2P1M"
HELIX 445..454
/evidence="ECO:0007829|PDB:2P1M"
STRAND 460..465
/evidence="ECO:0007829|PDB:2P1M"
HELIX 470..479
/evidence="ECO:0007829|PDB:2P1M"
STRAND 485..490
/evidence="ECO:0007829|PDB:2P1M"
HELIX 495..500
/evidence="ECO:0007829|PDB:2P1M"
HELIX 502..507
/evidence="ECO:0007829|PDB:2P1M"
STRAND 508..516
/evidence="ECO:0007829|PDB:2P1M"
HELIX 520..529
/evidence="ECO:0007829|PDB:2P1M"
STRAND 533..538
/evidence="ECO:0007829|PDB:2P1M"
STRAND 540..542
/evidence="ECO:0007829|PDB:2P1M"
HELIX 544..546
/evidence="ECO:0007829|PDB:2P1M"
STRAND 554..560
/evidence="ECO:0007829|PDB:2P1M"
STRAND 573..575
/evidence="ECO:0007829|PDB:2P1M"
SEQUENCE 594 AA; 66799 MW; 9E19ED5DABF40D07 CRC64;
MQKRIALSFP EEVLEHVFSF IQLDKDRNSV SLVCKSWYEI ERWCRRKVFI GNCYAVSPAT
VIRRFPKVRS VELKGKPHFA DFNLVPDGWG GYVYPWIEAM SSSYTWLEEI RLKRMVVTDD
CLELIAKSFK NFKVLVLSSC EGFSTDGLAA IAATCRNLKE LDLRESDVDD VSGHWLSHFP
DTYTSLVSLN ISCLASEVSF SALERLVTRC PNLKSLKLNR AVPLEKLATL LQRAPQLEEL
GTGGYTAEVR PDVYSGLSVA LSGCKELRCL SGFWDAVPAY LPAVYSVCSR LTTLNLSYAT
VQSYDLVKLL CQCPKLQRLW VLDYIEDAGL EVLASTCKDL RELRVFPSEP FVMEPNVALT
EQGLVSVSMG CPKLESVLYF CRQMTNAALI TIARNRPNMT RFRLCIIEPK APDYLTLEPL
DIGFGAIVEH CKDLRRLSLS GLLTDKVFEY IGTYAKKMEM LSVAFAGDSD LGMHHVLSGC
DSLRKLEIRD CPFGDKALLA NASKLETMRS LWMSSCSVSF GACKLLGQKM PKLNVEVIDE
RGAPDSRPES CPVERVFIYR TVAGPRFDMP GFVWNMDQDS TMRFSRQIIT TNGL


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WP1713: Two-component system
WP1672: Mismatch repair
WP211: BMP signaling pathway
WP1892: Protein folding
WP1049: G Protein Signaling Pathways
WP1676: Non-homologous end-joining
WP2203: TSLP Signaling Pathway
WP1685: Peptidoglycan biosynthesis
WP2272: Pathogenic Escherichia coli infection
WP931: G Protein Signaling Pathways
WP1624: Bacterial secretion system
WP1909: Signal regulatory protein (SIRP) family interactions
WP1650: Fluorobenzoate degradation
WP1165: G Protein Signaling Pathways
WP1692: Protein export
WP2324: AGE/RAGE pathway
WP1700: Selenoamino acid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1438: Influenza A virus infection
WP210: Cytoplasmic Ribosomal Proteins

Related Genes :
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[EIN2 CKR1 ORE3 At5g03280 F12E4.10 MOK16.19] Ethylene-insensitive protein 2 (AtEIN2) (EIN-2) (Cytokinin-resistant protein AtCKR1) (Protein ORESARA 3) [Cleaved into: EIN2-CEND (EIN2C)]
[ABI4 ERF052 GIN6 ISI3 SAN5 SIS5 SUN6 At2g40220 T7M7.16] Ethylene-responsive transcription factor ABI4 (ERF ABI4) (Protein ABSCISIC ACID INSENSITIVE 4) (Protein GLUCOSE INSENSITIVE 6) (Protein IMPAIRED SUCROSE INDUCTION 3) (Protein SALOBRENO 5) (Protein SUCROSE UNCOUPLED 6) (Protein SUGAR INSENSITIVE 5)
[XRN4 AIN1 EIN5 At1g54490 F20D21.30] 5'-3' exoribonuclease 4 (EC 3.1.13.-) (Protein ACC INSENSITIVE 1) (Protein ETHYLENE INSENSITIVE 5) (Protein EXORIBONUCLEASE 4)
[BIG ASA1 CRM1 DOC1 GA6 LPR1 TIR3 UMB1 At3g02260 F14P3.9] Auxin transport protein BIG (Protein ATTENUATED SHADE AVOIDANCE 1) (Protein CORYMBOSA1) (Protein DARK OVER-EXPRESSION OF CAB 1) (Protein LOW PHOSPHATE-RESISTANT ROOT 1) (Protein TRANSPORT INHIBITOR RESPONSE 3) (Protein UMBRELLA 1)
[COI1 FBL2 At2g39940 T28M21.10] Coronatine-insensitive protein 1 (COI-1) (F-box/LRR-repeat protein 2) (AtCOI1) (AtFBL2)
[ABI1 At4g26080 F20B18.190] Protein phosphatase 2C 56 (AtPP2C56) (EC 3.1.3.16) (Protein ABSCISIC ACID-INSENSITIVE 1) (Protein phosphatase 2C ABI1) (PP2C ABI1)
[PP2AA1 EER1 RCN1 REGA At1g25490 F2J7.19] Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform (AtA alpha) (PP2A, subunit A, alpha isoform) (PR-65 A) (Protein ROOTS CURL IN NAPHTHYLPHTHALAMIC ACID 1) (Protein enhancer of ethylene-response 1)
[ETR1 At1g66340 T27F4.9] Ethylene receptor 1 (AtETR1) (EC 2.7.13.3) (Protein ETHYLENE RESPONSE 1) (Protein ETR1)
[ARF7 BIP IAA21 IAA23 IAA25 NPH4 TIR5 At5g20730 T1M15.130] Auxin response factor 7 (Auxin-responsive protein IAA21/IAA23/IAA25) (Protein BIPOSTO) (Protein NON-PHOTOTROPIC HYPOCOTYL 4) (Protein TRANSPORT INHIBITOR RESPONSE 5)
[RUS1 WXR3 At3g45890 F16L2.10] Protein root UVB sensitive 1, chloroplastic (Protein WEAK AUXIN RESPONSE 3)
[ERF4 ERF-4 ERF078 RAP2-5 At3g15210 K7L4.1] Ethylene-responsive transcription factor 4 (AtERF4) (Ethylene-responsive element-binding factor 4) (EREBP-4) (Protein RELATED TO APETALA2 5)
[AOX1A AOX1 HSR3 At3g22370 MCB17.11] Ubiquinol oxidase 1a, mitochondrial (EC 1.10.3.11) (Alternative oxidase 1a)
[SLAC1 CDI3 OZS1 RCD3 At1g12480 F5O11.23 T12C24.3] Guard cell S-type anion channel SLAC1 (Protein CARBON DIOXIDE INSENSITIVE 3) (Protein OZONE-SENSITIVE 1) (Protein RADICAL-INDUCED CELL DEATH 3) (Protein SLOW ANION CHANNEL-ASSOCIATED 1)
[ERF1B ERF092 ERF1 At3g23240 K14B15.15] Ethylene-responsive transcription factor 1B (AtERF1B) (Ethylene-responsive element-binding factor 1B) (EREBP-1B)
[JAR1 FIN219 At2g46370 F11C10.6] Jasmonoyl--L-amino acid synthetase JAR1 (EC 6.3.2.52) (Jasmonate-amino acid synthetase JAR1) (Jasmonic acid-amido synthetase JAR1) (Protein FAR-RED INSENSITIVE 219) (Protein JASMONATE RESISTANT 1)
[ERF1A ERF-1 ERF100 At4g17500 dl4785w FCAALL.123] Ethylene-responsive transcription factor 1A (AtERF1A) (Ethylene-responsive element-binding factor 1A) (EREBP-1A)
[RUS2 WXR1 At2g31190 F16D14.3] Protein root UVB sensitive 2, chloroplastic (Protein WEAK AUXIN RESPONSE 1)
[ORF1ab orf1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[WSS1 YHR134W] DNA-dependent metalloprotease WSS1 (EC 3.4.24.-) (DNA damage response protein WSS1) (SUMO-dependent isopeptidase WSS1) (Weak suppressor of SMT3 protein 1)
[ABI2 PP2C77 At5g57050 MHM17.19] Protein phosphatase 2C 77 (AtPP2C77) (EC 3.1.3.16) (Protein ABSCISIC ACID-INSENSITIVE 2) (Protein phosphatase 2C ABI2) (PP2C ABI2)
[orf1ab ORF1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[CAMTA3 CMTA3 SARD3 SR1 At2g22300 T26C19.4] Calmodulin-binding transcription activator 3 (AtCAMTA3) (Ethylene-induced calmodulin-binding protein 1) (EICBP1) (Ethylene-induced calmodulin-binding protein a) (EICBP.a) (Protein SAR-DEFICIENT 3) (Signal-responsive protein 1) (AtSR1)
[SLC29A2 DER12 ENT2 HNP36] Equilibrative nucleoside transporter 2 (36 kDa nucleolar protein HNP36) (Delayed-early response protein 12) (Equilibrative nitrobenzylmercaptopurine riboside-insensitive nucleoside transporter) (Equilibrative NBMPR-insensitive nucleoside transporter) (Hydrophobic nucleolar protein, 36 kDa) (Nucleoside transporter, ei-type) (Solute carrier family 29 member 2)
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Host translation inhibitor nsp1 (Leader protein) (Non-structural protein 1) (nsp1); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL2-PRO) (Papain-like protease) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.69) (Main protease) (Mpro) (Non-structural protein 5) (nsp5) (SARS coronavirus main proteinase); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (Non-structural protein 12) (nsp12); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (Non-structural protein 13) (nsp13); Proofreading exoribonuclease (ExoN) (EC 3.1.13.-) (Guanine-N7 methyltransferase) (Non-structural protein 14) (nsp14); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (Non-structural protein 15) (nsp15); 2'-O-methyltransferase (EC 2.1.1.-) (Non-structural protein 16) (nsp16)]
[] Replicase polyprotein 1a (pp1a) (ORF1a polyprotein) [Cleaved into: Host translation inhibitor nsp1 (Leader protein) (Non-structural protein 1) (nsp1); Non-structural protein 2 (nsp2) (p65 homolog); Non-structural protein 3 (nsp3) (EC 3.4.19.12) (EC 3.4.22.-) (PL2-PRO) (Papain-like protease) (Papain-like proteinase) (PL-PRO); Non-structural protein 4 (nsp4); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.69) (Main protease) (Mpro) (Non-structural protein 5) (nsp5) (SARS coronavirus main proteinase); Non-structural protein 6 (nsp6); Non-structural protein 7 (nsp7); Non-structural protein 8 (nsp8); Non-structural protein 9 (nsp9); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL); Non-structural protein 11 (nsp11)]
[NPR1 NIM1 SAI1 At1g64280 F15H21.6] Regulatory protein NPR1 (BTB/POZ domain-containing protein NPR1) (Non-inducible immunity protein 1) (Nim1) (Nonexpresser of PR genes 1) (Salicylic acid insensitive 1) (Sai1)
[Oprm1 Mor Oprm] Mu-type opioid receptor (M-OR-1) (MOR-1)
[ORF1ab orf1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[EPPIN SPINLW1 WAP7 WFDC7] Eppin (Cancer/testis antigen 71) (CT71) (Epididymal protease inhibitor) (Protease inhibitor WAP7) (Serine protease inhibitor-like with Kunitz and WAP domains 1) (WAP four-disulfide core domain protein 7)

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