RBX1A_ARATH
ID RBX1A_ARATH Reviewed; 118 AA.
AC Q940X7;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=RING-box protein 1a;
DE AltName: Full=At-Rbx1;1;
DE AltName: Full=Protein RING of cullins 1;
DE AltName: Full=RBX1-2;
DE AltName: Full=RBX1a-At;
GN Name=RBX1A; Synonyms=ROC1; OrderedLocusNames=At5g20570; ORFNames=F7C8.160;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Oekresz L.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, IDENTIFICATION IN A SCF COMPLEX WITH CUL1 AND
RP TIR1, AND INTERACTION WITH CUL1.
RX PubMed=12215511; DOI=10.1105/tpc.003178;
RA Gray W.M., Hellmann H., Dharmasiri S., Estelle M.;
RT "Role of the Arabidopsis RING-H2 protein RBX1 in RUB modification and SCF
RT function.";
RL Plant Cell 14:2137-2144(2002).
RN [8]
RP FUNCTION, TISSUE SPECIFICITY, IDENTIFICATION IN SCF COMPLEX, AND
RP INTERACTION WITH CUL1; CUL4; ASK1 AND ASK2.
RX PubMed=12381738; DOI=10.1074/jbc.m204254200;
RA Lechner E., Xie D., Grava S., Pigaglio E., Planchais S., Murray J.A.H.,
RA Parmentier Y., Mutterer J., Dubreucq B., Shen W.-H., Genschik P.;
RT "The AtRbx1 protein is part of plant SCF complexes, and its down-regulation
RT causes severe growth and developmental defects.";
RL J. Biol. Chem. 277:50069-50080(2002).
RN [9]
RP FUNCTION.
RX PubMed=12682009; DOI=10.1093/emboj/cdg190;
RA Dharmasiri S., Dharmasiri N., Hellmann H., Estelle M.;
RT "The RUB/Nedd8 conjugation pathway is required for early development in
RT Arabidopsis.";
RL EMBO J. 22:1762-1770(2003).
RN [10]
RP IDENTIFICATION IN THE CUL4-RBX1-CDD E3 LIGASE COMPLEX.
RX PubMed=16844902; DOI=10.1105/tpc.106.043224;
RA Chen H., Shen Y., Tang X., Yu L., Wang J., Guo L., Zhang Y., Zhang H.,
RA Feng S., Strickland E., Zheng N., Deng X.-W.;
RT "Arabidopsis CULLIN4 forms an E3 ubiquitin ligase with RBX1 and the CDD
RT complex in mediating light control of development.";
RL Plant Cell 18:1991-2004(2006).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin
CC ligase complex, which mediates the ubiquitination and subsequent
CC proteasomal degradation of target proteins. The SCF complex plays a
CC crucial role in regulating response to auxin and is essential for
CC growth and development. Through the RING-type zinc finger, seems to
CC recruit the E2 ubiquitination enzyme, to the complex and brings it into
CC close proximity to the substrate. Promotes the neddylation of CUL1.
CC {ECO:0000269|PubMed:12215511, ECO:0000269|PubMed:12381738,
CC ECO:0000269|PubMed:12682009}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of SCF complexes, which consist of a SKP1-related
CC protein, a cullin, a RBX protein and a F-box protein. Part of a SCF
CC complex with ASK1 or ASK2 and CUL1. Part of a SCF complex with CUL1 and
CC TIR1. Interacts with CUL1 and CUL4. Component of the CUL4-RBX1-CDD
CC complex. {ECO:0000269|PubMed:12215511, ECO:0000269|PubMed:12381738,
CC ECO:0000269|PubMed:16844902}.
CC -!- INTERACTION:
CC Q940X7; Q94AH6: CUL1; NbExp=6; IntAct=EBI-532404, EBI-532411;
CC Q940X7; Q9ZVH4: CUL3A; NbExp=4; IntAct=EBI-532404, EBI-531362;
CC Q940X7; Q9C9L0: CUL3B; NbExp=3; IntAct=EBI-532404, EBI-541687;
CC Q940X7; Q8LGH4: CUL4; NbExp=3; IntAct=EBI-532404, EBI-541750;
CC Q940X7; Q9SDY5: RCE1; NbExp=2; IntAct=EBI-532404, EBI-595116;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q940X7-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in shoot, siliques,
CC meristem, flowers, floral buds, open flowers, leaves, stems, roots,
CC germinal seeds and seedlings in dark. Expressed at a higher level in
CC tissues containing actively dividing cells.
CC {ECO:0000269|PubMed:12215511, ECO:0000269|PubMed:12381738}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity. It coordinates an additional third zinc ion.
CC -!- SIMILARITY: Belongs to the RING-box family. {ECO:0000305}.
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DR EMBL; AY052401; AAL13435.1; -; mRNA.
DR EMBL; AF296833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92859.1; -; Genomic_DNA.
DR EMBL; AK118181; BAC42804.1; -; mRNA.
DR EMBL; AY072430; AAL62422.1; -; mRNA.
DR EMBL; AY114719; AAM48038.1; -; mRNA.
DR EMBL; AY086913; AAM64477.1; -; mRNA.
DR RefSeq; NP_568396.1; NM_122064.3. [Q940X7-1]
DR AlphaFoldDB; Q940X7; -.
DR SMR; Q940X7; -.
DR BioGRID; 17454; 12.
DR ComplexPortal; CPX-1339; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1A.
DR ComplexPortal; CPX-1343; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1A.
DR ComplexPortal; CPX-1429; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1B.
DR ComplexPortal; CPX-1430; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK3.
DR ComplexPortal; CPX-1431; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK4.
DR ComplexPortal; CPX-1432; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK5.
DR ComplexPortal; CPX-1433; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK6.
DR ComplexPortal; CPX-1434; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK7.
DR ComplexPortal; CPX-1435; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK8.
DR ComplexPortal; CPX-1436; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK9.
DR ComplexPortal; CPX-1437; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK10.
DR ComplexPortal; CPX-1438; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK11.
DR ComplexPortal; CPX-1439; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK12.
DR ComplexPortal; CPX-1440; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK13.
DR ComplexPortal; CPX-1441; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK14.
DR ComplexPortal; CPX-1442; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK15.
DR ComplexPortal; CPX-1443; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK16.
DR ComplexPortal; CPX-1444; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK17.
DR ComplexPortal; CPX-1445; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK18.
DR ComplexPortal; CPX-1446; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK19.
DR ComplexPortal; CPX-1447; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK20.
DR ComplexPortal; CPX-1448; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK21.
DR ComplexPortal; CPX-1471; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-SKP1A.
DR ComplexPortal; CPX-1472; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-SKP1B.
DR ComplexPortal; CPX-1473; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK3.
DR ComplexPortal; CPX-1474; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK4.
DR ComplexPortal; CPX-1475; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK5.
DR ComplexPortal; CPX-1476; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK6.
DR ComplexPortal; CPX-1477; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK7.
DR ComplexPortal; CPX-1478; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK8.
DR ComplexPortal; CPX-1479; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK9.
DR ComplexPortal; CPX-1480; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK10.
DR ComplexPortal; CPX-1481; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK11.
DR ComplexPortal; CPX-1482; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK12.
DR ComplexPortal; CPX-1483; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK13.
DR ComplexPortal; CPX-1484; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK14.
DR ComplexPortal; CPX-1485; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK15.
DR ComplexPortal; CPX-1486; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK16.
DR ComplexPortal; CPX-1487; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK17.
DR ComplexPortal; CPX-1488; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK18.
DR ComplexPortal; CPX-1489; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK19.
DR ComplexPortal; CPX-1490; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK20.
DR ComplexPortal; CPX-1491; SCF(COI1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK21.
DR ComplexPortal; CPX-1515; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1B.
DR ComplexPortal; CPX-1516; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK3.
DR ComplexPortal; CPX-1517; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK4.
DR ComplexPortal; CPX-1518; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK5.
DR ComplexPortal; CPX-1519; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK6.
DR ComplexPortal; CPX-1520; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK7.
DR ComplexPortal; CPX-1521; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK8.
DR ComplexPortal; CPX-1522; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK9.
DR ComplexPortal; CPX-1523; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK10.
DR ComplexPortal; CPX-1524; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK11.
DR ComplexPortal; CPX-1525; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK12.
DR ComplexPortal; CPX-1526; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK13.
DR ComplexPortal; CPX-1527; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK14.
DR ComplexPortal; CPX-1528; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK15.
DR ComplexPortal; CPX-1529; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK16.
DR ComplexPortal; CPX-1530; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK17.
DR ComplexPortal; CPX-1531; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK18.
DR ComplexPortal; CPX-1532; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK19.
DR ComplexPortal; CPX-1533; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK20.
DR ComplexPortal; CPX-1534; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK21.
DR ComplexPortal; CPX-1557; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-SKP1A.
DR ComplexPortal; CPX-1558; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-SKP1B.
DR ComplexPortal; CPX-1559; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK3.
DR ComplexPortal; CPX-1560; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK4.
DR ComplexPortal; CPX-1561; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK5.
DR ComplexPortal; CPX-1562; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK6.
DR ComplexPortal; CPX-1563; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK7.
DR ComplexPortal; CPX-1564; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK8.
DR ComplexPortal; CPX-1565; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK9.
DR ComplexPortal; CPX-1566; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK10.
DR ComplexPortal; CPX-1567; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK11.
DR ComplexPortal; CPX-1568; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK12.
DR ComplexPortal; CPX-1569; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK13.
DR ComplexPortal; CPX-1570; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK14.
DR ComplexPortal; CPX-1571; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK15.
DR ComplexPortal; CPX-1572; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK16.
DR ComplexPortal; CPX-1573; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK17.
DR ComplexPortal; CPX-1574; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK18.
DR ComplexPortal; CPX-1575; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK19.
DR ComplexPortal; CPX-1576; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK20.
DR ComplexPortal; CPX-1577; SCF(TIR1) ubiquitin ligase complex, variant CUL2-RBX1A-ASK21.
DR IntAct; Q940X7; 10.
DR iPTMnet; Q940X7; -.
DR PRIDE; Q940X7; -.
DR EnsemblPlants; AT5G20570.1; AT5G20570.1; AT5G20570. [Q940X7-1]
DR GeneID; 832179; -.
DR Gramene; AT5G20570.1; AT5G20570.1; AT5G20570. [Q940X7-1]
DR KEGG; ath:AT5G20570; -.
DR Araport; AT5G20570; -.
DR HOGENOM; CLU_115512_2_2_1; -.
DR InParanoid; Q940X7; -.
DR OMA; FELEGPC; -.
DR PhylomeDB; Q940X7; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q940X7; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q940X7; baseline and differential.
DR Genevisible; Q940X7; AT.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:ComplexPortal.
DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IC:ComplexPortal.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:ComplexPortal.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0009733; P:response to auxin; IC:ComplexPortal.
DR GO; GO:0009753; P:response to jasmonic acid; IMP:ComplexPortal.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR Pfam; PF12678; zf-rbx1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..118
FT /note="RING-box protein 1a"
FT /id="PRO_0000056019"
FT ZN_FING 63..108
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 52
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 104
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ SEQUENCE 118 AA; 13238 MW; 19947BF06F442A82 CRC64;
MATLDSDVTM IPAGEASSSV AASSSNKKAK RFEIKKWSAV ALWAWDIVVD NCAICRNHIM
DLCIECQANQ ASATSEECTV AWGVCNHAFH FHCISRWLKT RQVCPLDNSE WEFQKYGH
