CUL1_ARATH
ID CUL1_ARATH Reviewed; 738 AA.
AC Q94AH6; O22770; Q56W31;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 149.
DE RecName: Full=Cullin-1;
GN Name=CUL1; OrderedLocusNames=At4g02570; ORFNames=T10P11.26;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12058059; DOI=10.1091/mbc.e02-02-0077;
RA Shen W.-H., Parmentier Y., Hellmann H., Lechner E., Dong A., Masson J.,
RA Granier F., Lepiniec L., Estelle M., Genschik P.;
RT "Null mutation of AtCUL1 causes arrest in early embryogenesis in
RT Arabidopsis.";
RL Mol. Biol. Cell 13:1916-1928(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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=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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 491-738.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH TIR1, AND IDENTIFICATION IN A SCF(TIR1) COMPLEX.
RX PubMed=10398681; DOI=10.1101/gad.13.13.1678;
RA Gray W.M., del Pozo J.C., Walker L., Hobbie L., Risseeuw E., Banks T.,
RA Crosby W.L., Yang M., Ma H., Estelle M.;
RT "Identification of an SCF ubiquitin-ligase complex required for auxin
RT response in Arabidopsis thaliana.";
RL Genes Dev. 13:1678-1691(1999).
RN [7]
RP NEDDYLATION AT LYS-682, AND MUTAGENESIS OF LYS-682 AND LYS-712.
RX PubMed=10611386; DOI=10.1073/pnas.96.26.15342;
RA del Pozo J.C., Estelle M.;
RT "The Arabidopsis cullin AtCUL1 is modified by the ubiquitin-related protein
RT RUB1.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:15342-15347(1999).
RN [8]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SKP1A; KIN10 AND KIN11.
RX PubMed=11387208; DOI=10.1093/emboj/20.11.2742;
RA Farras R., Ferrando A., Jasik J., Kleinow T., Oekresz L., Tiburcio A.,
RA Salchert K., del Pozo C., Schell J., Koncz C.;
RT "SKP1-SnRK protein kinase interactions mediate proteasomal binding of a
RT plant SCF ubiquitin ligase.";
RL EMBO J. 20:2742-2756(2001).
RN [9]
RP INTERACTION WITH THE CSN COMPLEX.
RX PubMed=11337587; DOI=10.1126/science.1059776;
RA Schwechheimer C., Serino G., Callis J., Crosby W.L., Lyapina S.,
RA Deshaies R.J., Gray W.M., Estelle M., Deng X.-W.;
RT "Interactions of the COP9 signalosome with the E3 ubiquitin ligase
RT SCF(TIR1) in mediating auxin response.";
RL Science 292:1379-1382(2001).
RN [10]
RP INTERACTION WITH SKP1A; SKP1B; RBX1A AND RBX1B.
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 [11]
RP NEDDYLATION, AND DENEDDYLATION BY THE CSN COMPLEX.
RX PubMed=11854419; DOI=10.1091/mbc.01-08-0427;
RA Wang X., Kang D., Feng S., Serino G., Schwechheimer C., Wei N.;
RT "CSN1 N-terminal-dependent activity is required for Arabidopsis development
RT but not for Rub1/Nedd8 deconjugation of cullins: a structure-function study
RT of CSN1 subunit of COP9 signalosome.";
RL Mol. Biol. Cell 13:646-655(2002).
RN [12]
RP INTERACTION WITH SKIP14; FBW2/SKIP18; SKIP19/FBL20 AND SKIP28/MEE11.
RX PubMed=12795696; DOI=10.1046/j.1365-313x.2003.01768.x;
RA Risseeuw E.P., Daskalchuk T.E., Banks T.W., Liu E., Cotelesage J.,
RA Hellmann H., Estelle M., Somers D.E., Crosby W.L.;
RT "Protein interaction analysis of SCF ubiquitin E3 ligase subunits from
RT Arabidopsis.";
RL Plant J. 34:753-767(2003).
RN [13]
RP FUNCTION, INTERACTION WITH CAND1, AND MUTAGENESIS OF LYS-682.
RX PubMed=15208391; DOI=10.1105/tpc.021949;
RA Feng S., Shen Y., Sullivan J.A., Rubio V., Xiong Y., Sun T.P., Deng X.W.;
RT "Arabidopsis CAND1, an unmodified CUL1-interacting protein, is involved in
RT multiple developmental pathways controlled by ubiquitin/proteasome-mediated
RT protein Degradation.";
RL Plant Cell 16:1870-1882(2004).
RN [14]
RP INTERACTION WITH DOR.
RX PubMed=18835996; DOI=10.1104/pp.108.126912;
RA Zhang Y., Xu W., Li Z., Deng X.W., Wu W., Xue Y.;
RT "F-box protein DOR functions as a novel inhibitory factor for abscisic
RT acid-induced stomatal closure under drought stress in Arabidopsis.";
RL Plant Physiol. 148:2121-2133(2008).
CC -!- FUNCTION: Involved in ubiquitination and subsequent proteasomal
CC degradation of target proteins. Regulator of mitotic processes which
CC plays a role during gametogenesis and embryogenesis. Together with
CC SKP1, RBX1 and a F-box protein, it forms a SCF complex. The functional
CC specificity of this complex depends of the type of F-box protein.
CC SCF(UFO) is implicated in floral organ development. SCF(TIR1) is
CC involved in auxin signaling pathway. SCF(COI1) regulates responses to
CC jasmonates. SCF(EID1) and SCF(AFR) are implicated in phytochrome A
CC light signaling. SCF(ADO1/ZTL), SCF(ADO2/LKP2), SCF(ADO3/FKF1) are
CC related to the circadian clock. SCF(ORE9) seems to be involved in
CC senescence. SCF(EBF1/EBF2) may regulate ethylene signaling.
CC {ECO:0000269|PubMed:12058059, ECO:0000269|PubMed:15208391}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of E3 ubiquitin ligase SCF complexes such as SCF(TIR1)
CC and SCF(COI1). SCF(TIR1) is composed of CUL1, SKP1 (SKP1A or SKP1B),
CC RBX1 (RBX1A or RBX1B) and TIR1, while SCF(COI1) is composed of CUL1,
CC SKP1, RBX1 and COI1. A SNF1-related protein kinase (KIN10 and KIN11)
CC can also be part of these SCF complexes. SCF(TIR1) is able to interact
CC with the COP9 signalosome (CSN) complex. Interacts directly with some
CC F-box proteins such as DOR, SKIP14, FBW2/SKIP18, SKIP19/FBL20 and
CC SKIP28/MEE11. Interacts with CAND1. {ECO:0000269|PubMed:10398681,
CC ECO:0000269|PubMed:11337587, ECO:0000269|PubMed:11387208,
CC ECO:0000269|PubMed:12381738, ECO:0000269|PubMed:12795696,
CC ECO:0000269|PubMed:15208391, ECO:0000269|PubMed:18835996}.
CC -!- INTERACTION:
CC Q94AH6; P43288: ASK1; NbExp=2; IntAct=EBI-532411, EBI-4463633;
CC Q94AH6; Q8L5Y6: CAND1; NbExp=7; IntAct=EBI-532411, EBI-602912;
CC Q94AH6; O04197: COI1; NbExp=3; IntAct=EBI-532411, EBI-401159;
CC Q94AH6; Q9SKK0: EBF1; NbExp=4; IntAct=EBI-532411, EBI-401198;
CC Q94AH6; Q38825: IAA7; NbExp=5; IntAct=EBI-532411, EBI-602959;
CC Q94AH6; Q940X7: RBX1A; NbExp=6; IntAct=EBI-532411, EBI-532404;
CC Q94AH6; Q39255: SKP1A; NbExp=7; IntAct=EBI-532411, EBI-532357;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton,
CC spindle. Cytoplasm, cytoskeleton, phragmoplast. Note=Mainly nuclear
CC during interphase and preprophase, but also weakly cytoplasmic during
CC interphase. Associated to mitotic spindle during metaphase, and to the
CC phragmoplast during telophase.
CC -!- TISSUE SPECIFICITY: Expressed constitutively in roots, seedlings,
CC stems, leaves and flowers. {ECO:0000269|PubMed:12058059}.
CC -!- DEVELOPMENTAL STAGE: Strong accumulation in embryos (at protein level).
CC {ECO:0000269|PubMed:12058059}.
CC -!- PTM: Neddylated (rubylated). Deneddylation occurs upon interaction with
CC the COP9 signalosome (CSN) complex. {ECO:0000269|PubMed:10611386,
CC ECO:0000269|PubMed:11854419}.
CC -!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00330}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC78267.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80750.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ318017; CAC85264.1; -; mRNA.
DR EMBL; AC002330; AAC78267.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161494; CAB80750.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82194.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82195.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82196.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82197.1; -; Genomic_DNA.
DR EMBL; AY046030; AAK76704.1; -; mRNA.
DR EMBL; AY133878; AAM91812.1; -; mRNA.
DR EMBL; AK222216; BAD95380.1; -; mRNA.
DR PIR; T01092; T01092.
DR RefSeq; NP_001031575.1; NM_001036498.3.
DR RefSeq; NP_001031576.1; NM_001036499.1.
DR RefSeq; NP_001190661.1; NM_001203732.1.
DR RefSeq; NP_567243.1; NM_116491.3.
DR AlphaFoldDB; Q94AH6; -.
DR SMR; Q94AH6; -.
DR BioGRID; 10962; 47.
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-1449; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1A.
DR ComplexPortal; CPX-1450; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1B.
DR ComplexPortal; CPX-1451; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK3.
DR ComplexPortal; CPX-1452; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK4.
DR ComplexPortal; CPX-1453; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK5.
DR ComplexPortal; CPX-1454; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK6.
DR ComplexPortal; CPX-1455; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK7.
DR ComplexPortal; CPX-1456; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK8.
DR ComplexPortal; CPX-1457; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK9.
DR ComplexPortal; CPX-1458; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK10.
DR ComplexPortal; CPX-1459; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK11.
DR ComplexPortal; CPX-1460; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK12.
DR ComplexPortal; CPX-1461; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK13.
DR ComplexPortal; CPX-1462; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK14.
DR ComplexPortal; CPX-1463; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK15.
DR ComplexPortal; CPX-1464; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK16.
DR ComplexPortal; CPX-1465; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK17.
DR ComplexPortal; CPX-1466; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK18.
DR ComplexPortal; CPX-1467; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK19.
DR ComplexPortal; CPX-1468; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK20.
DR ComplexPortal; CPX-1469; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-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-1535; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1A.
DR ComplexPortal; CPX-1536; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1B.
DR ComplexPortal; CPX-1537; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK3.
DR ComplexPortal; CPX-1538; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK4.
DR ComplexPortal; CPX-1539; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK5.
DR ComplexPortal; CPX-1540; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK6.
DR ComplexPortal; CPX-1541; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK7.
DR ComplexPortal; CPX-1542; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK8.
DR ComplexPortal; CPX-1543; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK9.
DR ComplexPortal; CPX-1544; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK10.
DR ComplexPortal; CPX-1545; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK11.
DR ComplexPortal; CPX-1546; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK12.
DR ComplexPortal; CPX-1547; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK13.
DR ComplexPortal; CPX-1548; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK14.
DR ComplexPortal; CPX-1549; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK15.
DR ComplexPortal; CPX-1550; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK16.
DR ComplexPortal; CPX-1551; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK17.
DR ComplexPortal; CPX-1552; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK18.
DR ComplexPortal; CPX-1553; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK19.
DR ComplexPortal; CPX-1554; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK20.
DR ComplexPortal; CPX-1555; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK21.
DR DIP; DIP-33346N; -.
DR IntAct; Q94AH6; 36.
DR STRING; 3702.AT4G02570.4; -.
DR PaxDb; Q94AH6; -.
DR PRIDE; Q94AH6; -.
DR ProteomicsDB; 220459; -.
DR EnsemblPlants; AT4G02570.1; AT4G02570.1; AT4G02570.
DR EnsemblPlants; AT4G02570.2; AT4G02570.2; AT4G02570.
DR EnsemblPlants; AT4G02570.3; AT4G02570.3; AT4G02570.
DR EnsemblPlants; AT4G02570.4; AT4G02570.4; AT4G02570.
DR GeneID; 825648; -.
DR Gramene; AT4G02570.1; AT4G02570.1; AT4G02570.
DR Gramene; AT4G02570.2; AT4G02570.2; AT4G02570.
DR Gramene; AT4G02570.3; AT4G02570.3; AT4G02570.
DR Gramene; AT4G02570.4; AT4G02570.4; AT4G02570.
DR KEGG; ath:AT4G02570; -.
DR Araport; AT4G02570; -.
DR TAIR; locus:2132377; AT4G02570.
DR eggNOG; KOG2166; Eukaryota.
DR HOGENOM; CLU_004747_3_0_1; -.
DR InParanoid; Q94AH6; -.
DR OMA; DSFKERM; -.
DR OrthoDB; 1040292at2759; -.
DR PhylomeDB; Q94AH6; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q94AH6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q94AH6; baseline and differential.
DR Genevisible; Q94AH6; AT.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:TAIR.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:ComplexPortal.
DR GO; GO:0005819; C:spindle; IDA:TAIR.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0009734; P:auxin-activated signaling pathway; IC:ComplexPortal.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0009867; P:jasmonic acid mediated signaling pathway; IMP:ComplexPortal.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IMP:TAIR.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IMP:TAIR.
DR GO; GO:0010265; P:SCF complex assembly; IMP:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR045093; Cullin.
DR InterPro; IPR016157; Cullin_CS.
DR InterPro; IPR016158; Cullin_homology.
DR InterPro; IPR036317; Cullin_homology_sf.
DR InterPro; IPR001373; Cullin_N.
DR InterPro; IPR019559; Cullin_neddylation_domain.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11932; PTHR11932; 1.
DR Pfam; PF00888; Cullin; 1.
DR Pfam; PF10557; Cullin_Nedd8; 1.
DR SMART; SM00182; CULLIN; 1.
DR SMART; SM00884; Cullin_Nedd8; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF74788; SSF74788; 1.
DR SUPFAM; SSF75632; SSF75632; 1.
DR PROSITE; PS01256; CULLIN_1; 1.
DR PROSITE; PS50069; CULLIN_2; 1.
PE 1: Evidence at protein level;
KW Auxin signaling pathway; Cell cycle; Cytoplasm; Cytoskeleton;
KW Developmental protein; Ethylene signaling pathway; Isopeptide bond;
KW Nucleus; Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..738
FT /note="Cullin-1"
FT /id="PRO_0000119804"
FT CROSSLNK 682
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in NEDD8)"
FT /evidence="ECO:0000269|PubMed:10611386"
FT MUTAGEN 682
FT /note="K->M: No neddylation."
FT /evidence="ECO:0000269|PubMed:10611386,
FT ECO:0000269|PubMed:15208391"
FT MUTAGEN 712
FT /note="K->M: No change in neddylation."
FT /evidence="ECO:0000269|PubMed:10611386"
SQ SEQUENCE 738 AA; 86302 MW; 45041357DE8DAD8C CRC64;
MERKTIDLEQ GWDYMQTGIT KLKRILEGLN EPAFDSEQYM MLYTTIYNMC TQKPPHDYSQ
QLYDKYREAF EEYINSTVLP ALREKHDEFM LRELFKRWSN HKVMVRWLSR FFYYLDRYFI
ARRSLPPLNE VGLTCFRDLV YNELHSKVKQ AVIALVDKER EGEQIDRALL KNVLDIYVEI
GMGQMERYEE DFESFMLQDT SSYYSRKASS WIQEDSCPDY MLKSEECLKK ERERVAHYLH
SSSEPKLVEK VQHELLVVFA SQLLEKEHSG CRALLRDDKV DDLSRMYRLY HKILRGLEPV
ANIFKQHVTA EGNALVQQAE DTATNQVANT ASVQEQVLIR KVIELHDKYM VYVTECFQNH
TLFHKALKEA FEIFCNKTVA GSSSAELLAT FCDNILKKGG SEKLSDEAIE DTLEKVVKLL
AYISDKDLFA EFYRKKLARR LLFDRSANDD HERSILTKLK QQCGGQFTSK MEGMVTDLTL
ARENQNSFED YLGSNPAANP GIDLTVTVLT TGFWPSYKSF DINLPSEMIK CVEVFKGFYE
TKTKHRKLTW IYSLGTCHIN GKFDQKAIEL IVSTYQAAVL LLFNTTDKLS YTEILAQLNL
SHEDLVRLLH SLSCAKYKIL LKEPNTKTVS QNDAFEFNSK FTDRMRRIKI PLPPVDERKK
VVEDVDKDRR YAIDAAIVRI MKSRKVLGHQ QLVSECVEQL SRMFKPDIKA IKKRMEDLIT
RDYLERDKEN PNMFRYLA
