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UniProtKB/Swiss-Prot entry Q94AH6


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CUL1_ARATH
Primary accession number Q94AH6
Secondary accession numbers O22770 Q56W31
Integrated into Swiss-Prot on June 21, 2005
Sequence was last modified on December 1, 2001 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 55)
Name and origin of the protein
Protein name Cullin-1
Synonyms None
Gene name
Name: CUL1
OrderedLocusNames: At4g02570
ORFNames: T10P11.26
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
DOI=10.1091/mbc.E02-02-0077; PubMed=12058059 [NCBI, ExPASy, EBI, Israel, Japan]
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;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
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.
[5]
INTERACTION WITH TIR1, AND IDENTIFICATION IN A SCF(TIR1) COMPLEX.
DOI=10.1101/gad.13.13.1678; PubMed=10398681 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
NEDDYLATION AT LYS-682, AND MUTAGENESIS OF LYS-682 AND LYS-712.
DOI=10.1073/pnas.96.26.15342; PubMed=10611386 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
SUBCELLULAR LOCATION, AND INTERACTION WITH SKP1A; KIN10 AND KIN11.
DOI=10.1093/emboj/20.11.2742; PubMed=11387208 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
INTERACTION WITH THE CSN COMPLEX.
DOI=10.1126/science.1059776; PubMed=11337587 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
INTERACTION WITH SKP1A; SKP1B; RBX1A AND RBX1B.
DOI=10.1074/jbc.M204254200; PubMed=12381738 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
NEDDYLATION, AND DENEDDYLATION BY THE CSN COMPLEX.
DOI=10.1091/mbc.01-08-0427; PubMed=11854419 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
  • 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.
  • 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.
  • INTERACTION:
    Q8L5Y6:At2g02560; NbExp=3; IntAct=EBI-532411, EBI-602912;
    O04197:COI1; NbExp=2; IntAct=EBI-532411, EBI-401159;
    Q9SKK0:EBF1; NbExp=1; IntAct=EBI-532411, EBI-401198;
    Q708Y0:EBF2; NbExp=1; IntAct=EBI-532411, EBI-593623;
    Q9STX3:GID2; NbExp=1; IntAct=EBI-532411, EBI-619033;
    Q38825:IAA7; NbExp=3; IntAct=EBI-532411, EBI-602959;
    Q940X7:RBX1A; NbExp=6; IntAct=EBI-532411, EBI-532404;
    Q9SDY5:RCE1; NbExp=1; IntAct=EBI-532411, EBI-595116;
    Q39255:SKP1A; NbExp=4; IntAct=EBI-532411, EBI-532357;
  • SUBCELLULAR LOCATION: Nucleus. Cytoplasm. 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.
  • DEVELOPMENTAL STAGE: Strong accumulation in embryos (at protein level).
  • PTM: Neddylated. Deneddylated via its interaction with the COP9 signalosome (CSN) complex.
  • SIMILARITY: Belongs to the cullin family.
  • SEQUENCE CAUTION:
    • Sequence=AAC78267.1; Type=Erroneous gene model prediction;
    • Sequence=CAB80750.1; Type=Erroneous gene model prediction;
  • WEB RESOURCE: Name=PlantsUBQ; Note=A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants; URL="http://plantsubq.genomics.purdue.edu/";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ318017; CAC85264.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC002330; AAC78267.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161494; CAB80750.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY046030; AAK76704.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY133878; AAM91812.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK222216; BAD95380.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T01092; T01092.
RefSeq NP_001031575.1; -.
NP_001031576.1; -.
NP_567243.1; -.
UniGene At.24877
3D structure databases
HSSP Q9JLV5; 1IUY. [HSSP ENTRY / PDB]
ModBase Q94AH6.
Protein-protein interaction databases
IntAct Q94AH6; 36.
Organism-specific databases
TAIR At4g02570; -.
Gene expression databases
GermOnline AT4G02570; Arabidopsis thaliana.
Ontologies
GO
GO:0000794; Cellular component: condensed nuclear chromosome (inferred from direct assay from TAIR).
GO:0031461; Cellular component: cullin-RING ubiquitin ligase complex (inferred from electronic annotation from InterPro).
GO:0009524; Cellular component: phragmoplast (inferred from direct assay from TAIR).
GO:0005819; Cellular component: spindle (inferred from direct assay from TAIR).
GO:0031625; Molecular function: ubiquitin protein ligase binding (inferred from electronic annotation from InterPro).
GO:0009734; Biological process: auxin mediated signaling pathway (inferred from electronic annotation from UniProtKB-KW).
GO:0007049; Biological process: cell cycle (inferred from electronic annotation from UniProtKB-KW).
GO:0009793; Biological process: embryonic development ending in seed dormancy (inferred from mutant phenotype from TAIR).
GO:0009873; Biological process: ethylene mediated signaling pathway (inferred from electronic annotation from UniProtKB-KW).
GO:0009867; Biological process: jasmonic acid mediated signaling pathway (traceable author statement from TAIR).
GO:0042752; Biological process: regulation of circadian rhythm (inferred from mutant phenotype from TAIR).
GO:0010265; Biological process: SCF complex assembly (inferred from physical interaction from TAIR).
GO:0006511; Biological process: ubiquitin-dependent protein catabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR016157; Cullin_CS.
IPR016158; Cullin_homology.
IPR001373; Cullin_N.
IPR011991; Wing_hlx_DNA_bd.
Graphical view of domain structure.
Gene3D G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
Pfam PF00888; Cullin; 1.
Pfam graphical view of domain structure.
SMART SM00182; CULLIN; 1.
SMART graphical view of domain structure.
PROSITE PS01256; CULLIN_1; 1.
PS50069; CULLIN_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomics databases
PRIDE Q94AH6; -.
Genome annotation databases
GeneID 825648; -.
GenomeReviews CT486007_GR; AT4G02570.
KEGG ath:AT4G02570; -.
NMPDR fig|3702.1.peg.18072; -.
Other
ProtoNet Q94AH6.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Auxin signaling pathway; Cell cycle; Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein; Ethylene signaling pathway; Nucleus; Ubl conjugation; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   738  738     Cullin-1. PRO_0000119804
CROSSLNK   682   682        Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8). 
MUTAGEN   682   682        K->M: No neddylation. 
MUTAGEN   712   712        K->M: No change in neddylation. 
Sequence information
Length: 738 AA [This is the length of the unprocessed precursor] Molecular weight: 86302 Da [This is the MW of the unprocessed precursor] CRC64: 45041357DE8DAD8C [This is a checksum on the sequence]
        10         20         30         40         50         60 
MERKTIDLEQ GWDYMQTGIT KLKRILEGLN EPAFDSEQYM MLYTTIYNMC TQKPPHDYSQ 

        70         80         90        100        110        120 
QLYDKYREAF EEYINSTVLP ALREKHDEFM LRELFKRWSN HKVMVRWLSR FFYYLDRYFI 

       130        140        150        160        170        180 
ARRSLPPLNE VGLTCFRDLV YNELHSKVKQ AVIALVDKER EGEQIDRALL KNVLDIYVEI 

       190        200        210        220        230        240 
GMGQMERYEE DFESFMLQDT SSYYSRKASS WIQEDSCPDY MLKSEECLKK ERERVAHYLH 

       250        260        270        280        290        300 
SSSEPKLVEK VQHELLVVFA SQLLEKEHSG CRALLRDDKV DDLSRMYRLY HKILRGLEPV 

       310        320        330        340        350        360 
ANIFKQHVTA EGNALVQQAE DTATNQVANT ASVQEQVLIR KVIELHDKYM VYVTECFQNH 

       370        380        390        400        410        420 
TLFHKALKEA FEIFCNKTVA GSSSAELLAT FCDNILKKGG SEKLSDEAIE DTLEKVVKLL 

       430        440        450        460        470        480 
AYISDKDLFA EFYRKKLARR LLFDRSANDD HERSILTKLK QQCGGQFTSK MEGMVTDLTL 

       490        500        510        520        530        540 
ARENQNSFED YLGSNPAANP GIDLTVTVLT TGFWPSYKSF DINLPSEMIK CVEVFKGFYE 

       550        560        570        580        590        600 
TKTKHRKLTW IYSLGTCHIN GKFDQKAIEL IVSTYQAAVL LLFNTTDKLS YTEILAQLNL 

       610        620        630        640        650        660 
SHEDLVRLLH SLSCAKYKIL LKEPNTKTVS QNDAFEFNSK FTDRMRRIKI PLPPVDERKK 

       670        680        690        700        710        720 
VVEDVDKDRR YAIDAAIVRI MKSRKVLGHQ QLVSECVEQL SRMFKPDIKA IKKRMEDLIT 

       730 
RDYLERDKEN PNMFRYLA 

Q94AH6 in FASTA format

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