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Cullin-1

 CUL1_ARATH              Reviewed;         738 AA.
Q94AH6; O22770; Q56W31;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
02-DEC-2020, entry version 146.
RecName: Full=Cullin-1;
Name=CUL1; OrderedLocusNames=At4g02570; ORFNames=T10P11.26;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=12058059; DOI=10.1091/mbc.e02-02-0077;
Shen W.-H., Parmentier Y., Hellmann H., Lechner E., Dong A., Masson J.,
Granier F., Lepiniec L., Estelle M., Genschik P.;
"Null mutation of AtCUL1 causes arrest in early embryogenesis in
Arabidopsis.";
Mol. Biol. Cell 13:1916-1928(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=10617198; DOI=10.1038/47134;
Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
Martienssen R., McCombie W.R.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[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 [LARGE SCALE MRNA] OF 491-738.
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.
[6]
INTERACTION WITH TIR1, AND IDENTIFICATION IN A SCF(TIR1) COMPLEX.
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).
[7]
NEDDYLATION AT LYS-682, AND MUTAGENESIS OF LYS-682 AND LYS-712.
PubMed=10611386; DOI=10.1073/pnas.96.26.15342;
del Pozo J.C., Estelle M.;
"The Arabidopsis cullin AtCUL1 is modified by the ubiquitin-related protein
RUB1.";
Proc. Natl. Acad. Sci. U.S.A. 96:15342-15347(1999).
[8]
SUBCELLULAR LOCATION, AND INTERACTION WITH SKP1A; KIN10 AND KIN11.
PubMed=11387208; DOI=10.1093/emboj/20.11.2742;
Farras R., Ferrando A., Jasik J., Kleinow T., Oekresz L., Tiburcio A.,
Salchert K., del Pozo C., Schell J., Koncz C.;
"SKP1-SnRK protein kinase interactions mediate proteasomal binding of a
plant SCF ubiquitin ligase.";
EMBO J. 20:2742-2756(2001).
[9]
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).
[10]
INTERACTION WITH SKP1A; SKP1B; RBX1A AND RBX1B.
PubMed=12381738; DOI=10.1074/jbc.m204254200;
Lechner E., Xie D., Grava S., Pigaglio E., Planchais S., Murray J.A.H.,
Parmentier Y., Mutterer J., Dubreucq B., Shen W.-H., Genschik P.;
"The AtRbx1 protein is part of plant SCF complexes, and its down-regulation
causes severe growth and developmental defects.";
J. Biol. Chem. 277:50069-50080(2002).
[11]
NEDDYLATION, AND DENEDDYLATION BY THE CSN COMPLEX.
PubMed=11854419; DOI=10.1091/mbc.01-08-0427;
Wang X., Kang D., Feng S., Serino G., Schwechheimer C., Wei N.;
"CSN1 N-terminal-dependent activity is required for Arabidopsis development
but not for Rub1/Nedd8 deconjugation of cullins: a structure-function study
of CSN1 subunit of COP9 signalosome.";
Mol. Biol. Cell 13:646-655(2002).
[12]
INTERACTION WITH SKIP14; FBW2/SKIP18; SKIP19/FBL20 AND SKIP28/MEE11.
PubMed=12795696; DOI=10.1046/j.1365-313x.2003.01768.x;
Risseeuw E.P., Daskalchuk T.E., Banks T.W., Liu E., Cotelesage J.,
Hellmann H., Estelle M., Somers D.E., Crosby W.L.;
"Protein interaction analysis of SCF ubiquitin E3 ligase subunits from
Arabidopsis.";
Plant J. 34:753-767(2003).
[13]
FUNCTION, INTERACTION WITH CAND1, AND MUTAGENESIS OF LYS-682.
PubMed=15208391; DOI=10.1105/tpc.021949;
Feng S., Shen Y., Sullivan J.A., Rubio V., Xiong Y., Sun T.P., Deng X.W.;
"Arabidopsis CAND1, an unmodified CUL1-interacting protein, is involved in
multiple developmental pathways controlled by ubiquitin/proteasome-mediated
protein Degradation.";
Plant Cell 16:1870-1882(2004).
[14]
INTERACTION WITH DOR.
PubMed=18835996; DOI=10.1104/pp.108.126912;
Zhang Y., Xu W., Li Z., Deng X.W., Wu W., Xue Y.;
"F-box protein DOR functions as a novel inhibitory factor for abscisic
acid-induced stomatal closure under drought stress in Arabidopsis.";
Plant Physiol. 148:2121-2133(2008).
-!- FUNCTION: Involved in ubiquitination and subsequent proteasomal
degradation of target proteins. Regulator of mitotic processes which
plays a role during gametogenesis and embryogenesis. Together with
SKP1, RBX1 and a F-box protein, it forms a SCF complex. The functional
specificity of this complex depends of the type of F-box protein.
SCF(UFO) is implicated in floral organ development. SCF(TIR1) is
involved in auxin signaling pathway. SCF(COI1) regulates responses to
jasmonates. SCF(EID1) and SCF(AFR) are implicated in phytochrome A
light signaling. SCF(ADO1/ZTL), SCF(ADO2/LKP2), SCF(ADO3/FKF1) are
related to the circadian clock. SCF(ORE9) seems to be involved in
senescence. SCF(EBF1/EBF2) may regulate ethylene signaling.
{ECO:0000269|PubMed:12058059, ECO:0000269|PubMed:15208391}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Part of E3 ubiquitin ligase SCF complexes such as SCF(TIR1)
and SCF(COI1). SCF(TIR1) is composed of CUL1, SKP1 (SKP1A or SKP1B),
RBX1 (RBX1A or RBX1B) and TIR1, while SCF(COI1) is composed of CUL1,
SKP1, RBX1 and COI1. A SNF1-related protein kinase (KIN10 and KIN11)
can also be part of these SCF complexes. SCF(TIR1) is able to interact
with the COP9 signalosome (CSN) complex. Interacts directly with some
F-box proteins such as DOR, SKIP14, FBW2/SKIP18, SKIP19/FBL20 and
SKIP28/MEE11. Interacts with CAND1. {ECO:0000269|PubMed:10398681,
ECO:0000269|PubMed:11337587, ECO:0000269|PubMed:11387208,
ECO:0000269|PubMed:12381738, ECO:0000269|PubMed:12795696,
ECO:0000269|PubMed:15208391, ECO:0000269|PubMed:18835996}.
-!- INTERACTION:
Q94AH6; P43288: ASK1; NbExp=2; IntAct=EBI-532411, EBI-4463633;
Q94AH6; Q8L5Y6: CAND1; NbExp=7; IntAct=EBI-532411, EBI-602912;
Q94AH6; O04197: COI1; NbExp=3; IntAct=EBI-532411, EBI-401159;
Q94AH6; Q9SKK0: EBF1; NbExp=4; IntAct=EBI-532411, EBI-401198;
Q94AH6; Q38825: IAA7; NbExp=5; IntAct=EBI-532411, EBI-602959;
Q94AH6; Q940X7: RBX1A; NbExp=6; IntAct=EBI-532411, EBI-532404;
Q94AH6; Q39255: SKP1A; NbExp=7; IntAct=EBI-532411, EBI-532357;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton,
spindle. Cytoplasm, cytoskeleton, phragmoplast. Note=Mainly nuclear
during interphase and preprophase, but also weakly cytoplasmic during
interphase. Associated to mitotic spindle during metaphase, and to the
phragmoplast during telophase.
-!- TISSUE SPECIFICITY: Expressed constitutively in roots, seedlings,
stems, leaves and flowers. {ECO:0000269|PubMed:12058059}.
-!- DEVELOPMENTAL STAGE: Strong accumulation in embryos (at protein level).
{ECO:0000269|PubMed:12058059}.
-!- PTM: Neddylated (rubylated). Deneddylation occurs upon interaction with
the COP9 signalosome (CSN) complex. {ECO:0000269|PubMed:10611386,
ECO:0000269|PubMed:11854419}.
-!- SIMILARITY: Belongs to the cullin family. {ECO:0000255|PROSITE-
ProRule:PRU00330}.
-!- SEQUENCE CAUTION:
Sequence=AAC78267.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=CAB80750.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AJ318017; CAC85264.1; -; mRNA.
EMBL; AC002330; AAC78267.1; ALT_SEQ; Genomic_DNA.
EMBL; AL161494; CAB80750.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002687; AEE82194.1; -; Genomic_DNA.
EMBL; CP002687; AEE82195.1; -; Genomic_DNA.
EMBL; CP002687; AEE82196.1; -; Genomic_DNA.
EMBL; CP002687; AEE82197.1; -; Genomic_DNA.
EMBL; AY046030; AAK76704.1; -; mRNA.
EMBL; AY133878; AAM91812.1; -; mRNA.
EMBL; AK222216; BAD95380.1; -; mRNA.
PIR; T01092; T01092.
RefSeq; NP_001031575.1; NM_001036498.3.
RefSeq; NP_001031576.1; NM_001036499.1.
RefSeq; NP_001190661.1; NM_001203732.1.
RefSeq; NP_567243.1; NM_116491.3.
SMR; Q94AH6; -.
BioGRID; 10962; 47.
ComplexPortal; CPX-1339; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1A.
ComplexPortal; CPX-1343; SCF(TIR1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1A.
ComplexPortal; CPX-1429; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-SKP1B.
ComplexPortal; CPX-1430; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK3.
ComplexPortal; CPX-1431; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK4.
ComplexPortal; CPX-1432; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK5.
ComplexPortal; CPX-1433; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK6.
ComplexPortal; CPX-1434; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK7.
ComplexPortal; CPX-1435; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK8.
ComplexPortal; CPX-1436; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK9.
ComplexPortal; CPX-1437; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK10.
ComplexPortal; CPX-1438; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK11.
ComplexPortal; CPX-1439; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK12.
ComplexPortal; CPX-1440; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK13.
ComplexPortal; CPX-1441; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK14.
ComplexPortal; CPX-1442; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK15.
ComplexPortal; CPX-1443; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK16.
ComplexPortal; CPX-1444; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK17.
ComplexPortal; CPX-1445; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK18.
ComplexPortal; CPX-1446; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK19.
ComplexPortal; CPX-1447; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK20.
ComplexPortal; CPX-1448; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1A-ASK21.
ComplexPortal; CPX-1449; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1A.
ComplexPortal; CPX-1450; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-SKP1B.
ComplexPortal; CPX-1451; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK3.
ComplexPortal; CPX-1452; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK4.
ComplexPortal; CPX-1453; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK5.
ComplexPortal; CPX-1454; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK6.
ComplexPortal; CPX-1455; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK7.
ComplexPortal; CPX-1456; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK8.
ComplexPortal; CPX-1457; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK9.
ComplexPortal; CPX-1458; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK10.
ComplexPortal; CPX-1459; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK11.
ComplexPortal; CPX-1460; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK12.
ComplexPortal; CPX-1461; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK13.
ComplexPortal; CPX-1462; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK14.
ComplexPortal; CPX-1463; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK15.
ComplexPortal; CPX-1464; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK16.
ComplexPortal; CPX-1465; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK17.
ComplexPortal; CPX-1466; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK18.
ComplexPortal; CPX-1467; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK19.
ComplexPortal; CPX-1468; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK20.
ComplexPortal; CPX-1469; SCF(COI1) ubiquitin ligase complex, variant CUL1-RBX1B-ASK21.
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.
DIP; DIP-33346N; -.
IntAct; Q94AH6; 36.
STRING; 3702.AT4G02570.4; -.
PaxDb; Q94AH6; -.
PRIDE; Q94AH6; -.
ProteomicsDB; 220459; -.
EnsemblPlants; AT4G02570.1; AT4G02570.1; AT4G02570.
EnsemblPlants; AT4G02570.2; AT4G02570.2; AT4G02570.
EnsemblPlants; AT4G02570.3; AT4G02570.3; AT4G02570.
EnsemblPlants; AT4G02570.4; AT4G02570.4; AT4G02570.
GeneID; 825648; -.
Gramene; AT4G02570.1; AT4G02570.1; AT4G02570.
Gramene; AT4G02570.2; AT4G02570.2; AT4G02570.
Gramene; AT4G02570.3; AT4G02570.3; AT4G02570.
Gramene; AT4G02570.4; AT4G02570.4; AT4G02570.
KEGG; ath:AT4G02570; -.
Araport; AT4G02570; -.
TAIR; locus:2132377; AT4G02570.
eggNOG; KOG2166; Eukaryota.
HOGENOM; CLU_004747_3_0_1; -.
InParanoid; Q94AH6; -.
OMA; VITPEYW; -.
OrthoDB; 1040292at2759; -.
PhylomeDB; Q94AH6; -.
UniPathway; UPA00143; -.
PRO; PR:Q94AH6; -.
Proteomes; UP000006548; Chromosome 4.
ExpressionAtlas; Q94AH6; baseline and differential.
Genevisible; Q94AH6; AT.
GO; GO:0000794; C:condensed nuclear chromosome; IDA:TAIR.
GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IDA:TAIR.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0009524; C:phragmoplast; IDA:TAIR.
GO; GO:0005819; C:spindle; IDA:TAIR.
GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
GO; GO:0009734; P:auxin-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
GO; GO:0009873; P:ethylene-activated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0009867; P:jasmonic acid mediated signaling pathway; TAS:TAIR.
GO; GO:0048366; P:leaf development; IMP:TAIR.
GO; GO:0010087; P:phloem or xylem histogenesis; IMP:TAIR.
GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:TAIR.
GO; GO:0009733; P:response to auxin; IMP:TAIR.
GO; GO:0009753; P:response to jasmonic acid; IMP:TAIR.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR016157; Cullin_CS.
InterPro; IPR016158; Cullin_homology.
InterPro; IPR036317; Cullin_homology_sf.
InterPro; IPR001373; Cullin_N.
InterPro; IPR019559; Cullin_neddylation_domain.
InterPro; IPR016159; Cullin_repeat-like_dom_sf.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00888; Cullin; 1.
Pfam; PF10557; Cullin_Nedd8; 1.
SMART; SM00182; CULLIN; 1.
SMART; SM00884; Cullin_Nedd8; 1.
SUPFAM; SSF46785; SSF46785; 1.
SUPFAM; SSF74788; SSF74788; 1.
SUPFAM; SSF75632; SSF75632; 1.
PROSITE; PS01256; CULLIN_1; 1.
PROSITE; PS50069; CULLIN_2; 1.
1: Evidence at protein level;
Auxin signaling pathway; Cell cycle; Cytoplasm; Cytoskeleton;
Developmental protein; Ethylene signaling pathway; Isopeptide bond;
Nucleus; Reference proteome; Ubl conjugation; Ubl conjugation pathway.
CHAIN 1..738
/note="Cullin-1"
/id="PRO_0000119804"
CROSSLNK 682
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in NEDD8)"
/evidence="ECO:0000269|PubMed:10611386"
MUTAGEN 682
/note="K->M: No neddylation."
/evidence="ECO:0000269|PubMed:10611386,
ECO:0000269|PubMed:15208391"
MUTAGEN 712
/note="K->M: No change in neddylation."
/evidence="ECO:0000269|PubMed:10611386"
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


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EIAAB05270 CAND1,Cullin-associated and neddylation-dissociated protein 1,Cullin-associated NEDD8-dissociated protein 1,Homo sapiens,Human,KIAA0829,p120 CAND1,TBP-interacting protein 120A,TBP-interacting protein
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EIAAB05273 Cand2,Cullin-associated and neddylation-dissociated protein 2,Cullin-associated NEDD8-dissociated protein 2,p120 CAND2,Rat,Rattus norvegicus,TBP-interacting protein 120B,TBP-interacting protein b,TBP-
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Pathways :
WP1411: Cell Division: First embryonic mitosis
WP428: Wnt Signaling Pathway
WP1355: One Carbon Metabolism
WP426: Urea cycle and metabolism of amino groups
WP1351: Apoptosis
WP79: Tryptophan metabolism
WP1321: Myometrial Relaxation and Contraction Pathways
WP1039: Glutathione metabolism
WP1449: Regulation of toll-like receptor signaling pathway
WP785: Wnt Signaling Pathway
WP2085: miRNAs involved in DDR
WP1367: TGF-beta Receptor Signaling Pathway
WP2359: Parkin-Ubiquitin Proteasomal System pathway
WP1345: T Cell Receptor Signaling Pathway
WP1330: estrogen signalling
WP730: Glutathione and one carbon metabolism
WP1338: Peptide GPCRs
WP411: mRNA processing
WP1393: Cell cycle
WP938: Complement and Coagulation Cascades
WP1386: Integrin-mediated cell adhesion
WP1347: Triacylglyceride Synthesis
WP163: Cytoplasmic Ribosomal Proteins
WP2233: Immune responses in the epidermis
WP1016: Wnt Signaling Pathway

Related Genes :
[CAND1 KIAA0829 TIP120 TIP120A] Cullin-associated NEDD8-dissociated protein 1 (Cullin-associated and neddylation-dissociated protein 1) (TBP-interacting protein of 120 kDa A) (TBP-interacting protein 120A) (p120 CAND1)
[Cand1 Tip120 Tip120a] Cullin-associated NEDD8-dissociated protein 1 (Cullin-associated and neddylation-dissociated protein 1) (TBP-interacting protein of 120 kDa A) (TBP-interacting protein 120A) (p120 CAND1)
[CAND1 ETA2 HVE At2g02560 T8K22.14] Cullin-associated NEDD8-dissociated protein 1 (Cullin-associated and neddylation-dissociated protein 1) (AtCAND1) (Protein ENHANCER OF TIR1-1 AUXIN RESISTANCE 2) (Protein HEMIVENATA)
[RTT101 CUL8 YJL047C J1166] Cullin-8 (Cullin-C) (Regulator of Ty1 transposition protein 101)
[DCUN1D1 DCN1 DCUN1L1 RP42 SCCRO] DCN1-like protein 1 (DCNL1) (DCUN1 domain-containing protein 1) (Defective in cullin neddylation protein 1-like protein 1) (Squamous cell carcinoma-related oncogene)
[CUL1] Cullin-1 (CUL-1)
[CUL5 VACM1] Cullin-5 (CUL-5) (Vasopressin-activated calcium-mobilizing receptor 1) (VACM-1)
[DCUN1D2 C13orf17 DCUN1L2] DCN1-like protein 2 (DCNL2) (DCUN1 domain-containing protein 2) (Defective in cullin neddylation protein 1-like protein 2)
[Cul1] Cullin-1 (CUL-1)
[DCUN1D5 SCCRO5] DCN1-like protein 5 (DCNL5) (DCUN1 domain-containing protein 5) (Defective in cullin neddylation protein 1-like protein 5) (Squamous cell carcinoma-related oncogene 5)
[Cul1 cul-1 lin19 CG1877] Cullin homolog 1 (Lin-19 homolog protein)
[Cul5 Vacm1] Cullin-5 (CUL-5) (Vasopressin-activated calcium-mobilizing receptor 1) (VACM-1)
[DCUN1D3 SCCRO3] DCN1-like protein 3 (DCNL3) (DCUN1 domain-containing protein 3) (Defective in cullin neddylation protein 1-like protein 3) (Squamous cell carcinoma-related oncogene 3)
[cul-1 lin-19 D2045.6] Cullin-1 (CUL-1) (Abnormal cell lineage protein 19)
[DCUN1D4 KIAA0276] DCN1-like protein 4 (DCNL4) (DCUN1 domain-containing protein 4) (Defective in cullin neddylation protein 1-like protein 4)
[CUL1 At4g02570 T10P11.26] Cullin-1
[CUL9 H7AP1 KIAA0708 PARC] Cullin-9 (CUL-9) (UbcH7-associated protein 1) (p53-associated parkin-like cytoplasmic protein)
[cul1 pcu1 SPAC17G6.12] Cullin-1 (Cul-1) (Cell division control 53 homolog)
[cul-3 Y108G3AL.1] Cullin-3 (CUL-3)
[Cul3 BG:DS07851.2 br34 CG11861 CG31829 CUL-3 Cul-3 cul-3 Cul-3-RF CUL3 cul3 Cullin3 dCul-3 dCul3 DMcul-3 Dmel\CG42616 gft guftagu l(2)06430 l(2)35Cd l(2)br34 l35Cd mds CG42616 Dmel_CG42616] Cullin 3, isoform F (FI19425p1)
[CACUL1 C10orf46 CAC1] CDK2-associated and cullin domain-containing protein 1 (Cdk-associated cullin 1)
[candA-C AN2458] Cullin-associated NEDD8-dissociated protein 1, C-terminal part (Cullin-associated and neddylation-dissociated protein 1, C-terminal part)
[Cul3 BG:DS07851.2 br34 CG11861 CG31829 CUL-3 Cul-3 cul-3 CUL3 cul3 Cullin3 dCul-3 dCul3 DMcul-3 Dmel\CG42616 gft guftagu l(2)06430 l(2)35Cd l(2)br34 l35Cd mds CG42616 Dmel_CG42616] Cullin 3, isoform C (Cullin 3, isoform D) (Cullin 3, isoform E) (LD10516p)
[CUL3A CUL3 At1g26830 T2P11.2] Cullin-3A (AtCUL3a)
[culA cul1 DDB_G0291972] Cullin-1 (CUL-1) (Cullin-A)
[LAG2 YOL025W] Cullin-associated NEDD8-dissociated protein 1 homolog (CAND1 homolog) (Longevity-assurance protein 2)
[CUL3] CULLIN_2 domain-containing protein
[Dcun1d5] DCN1-like protein 5 (DCNL5) (DCUN1 domain-containing protein 5) (Defective in cullin neddylation protein 1-like protein 5) (Squamous cell carcinoma-related oncogene 5)
[CAND2 KIAA0667 TIP120B] Cullin-associated NEDD8-dissociated protein 2 (Cullin-associated and neddylation-dissociated protein 2) (Epididymis tissue protein Li 169) (TBP-interacting protein of 120 kDa B) (TBP-interacting protein 120B) (p120 CAND2)
[CUL3 KIAA0617] Cullin-3 (CUL-3)

Bibliography :
[34319780] Suppression of JAK-STAT signaling by Epstein-Barr virus tegument protein BGLF2 through recruitment of SHP1 phosphatase and promotion of STAT2 degradation.
[34299191] Cullin 1 (CUL1) Promotes Primary Ciliogenesis through the Induction of Ubiquitin-Proteasome-Dependent Dvl2 Degradation.
[34237211] A Hypoxia-Induced SCFFBXL1 E3 Ligase Ubiquitinates and Degrades the MEN1 Tumor Suppressor to Promote Colorectal Cancer Tumorigenesis.
[34183418] missense mutations suppress P53 and enhance cell growth.
[34107052] Proteolysis of γ-tubulin small complex proteins is mediated by the ubiquitin-proteasome system.
[34080964] CDK-associated Cullin 1 promotes Cell Proliferation and inhibits Cell Apoptosis in Human Glioblastoma.
[34060591] The parkinsonism-associated protein FBXO7 cooperates with the BAG6 complex in proteasome function and controls the subcellular localization of the complex.
[33442232] Targeting Protein Neddylation to Inactivate Cullin-RING Ligases by Gossypol: A Lucky Hit or a New Start?
[33360542] Arabidopsis F-box protein At1g08710 interacts with transcriptional protein ADA2b and imparts drought stress tolerance by negatively regulating seedling growth.
[33203912] Molecular variation in a functionally divergent homolog of FCA regulates flowering time in Arabidopsis thaliana.