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 27-MAR-2024, entry version 157. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.Q94AH6; -. DR PaxDb; 3702-AT4G02570-4; -. 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; AT4G02570; CUL1. DR eggNOG; KOG2166; Eukaryota. DR HOGENOM; CLU_004747_3_0_1; -. DR InParanoid; Q94AH6; -. DR OMA; AGFCDNI; -. DR OrthoDB; 21270at2759; -. DR PhylomeDB; Q94AH6; -. DR UniPathway; UPA00143; -. DR PRO; PR:Q94AH6; -. DR Proteomes; UP000006548; Chromosome 4. DR ExpressionAtlas; Q94AH6; baseline and differential. DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:TAIR. 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; IEA:InterPro. DR GO; GO:0009734; P:auxin-activated signaling pathway; NAS: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; IEA:UniProtKB-UniPathway. 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; 1.20.1310.10; Cullin Repeats; 4. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; CULLIN; 1. DR PANTHER; PTHR11932:SF138; CULLIN-1-RELATED; 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; SSF75632; Cullin homology domain; 1. DR SUPFAM; SSF74788; Cullin repeat-like; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS01256; CULLIN_1; 1. DR PROSITE; PS50069; CULLIN_2; 1. DR Genevisible; Q94AH6; AT. 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 //