Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q94AH6

- CUL1_ARATH

UniProt

Q94AH6 - CUL1_ARATH

Protein

Cullin-1

Gene

CUL1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.2 Publications

    Pathwayi

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. auxin-activated signaling pathway Source: UniProtKB-KW
    2. cell cycle Source: UniProtKB-KW
    3. embryo development ending in seed dormancy Source: TAIR
    4. ethylene-activated signaling pathway Source: UniProtKB-KW
    5. jasmonic acid mediated signaling pathway Source: TAIR
    6. leaf development Source: TAIR
    7. phloem or xylem histogenesis Source: TAIR
    8. protein ubiquitination Source: UniProtKB-UniPathway
    9. regulation of circadian rhythm Source: TAIR
    10. response to auxin Source: TAIR
    11. response to jasmonic acid Source: TAIR
    12. SCF complex assembly Source: TAIR
    13. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Auxin signaling pathway, Cell cycle, Ethylene signaling pathway, Ubl conjugation pathway

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cullin-1
    Gene namesi
    Name:CUL1
    Ordered Locus Names:At4g02570
    ORF Names:T10P11.26
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    ProteomesiUP000006548: Chromosome 4

    Organism-specific databases

    TAIRiAT4G02570.

    Subcellular locationi

    Nucleus. Cytoplasm. Cytoplasmcytoskeletonspindle. Cytoplasmcytoskeletonphragmoplast
    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.

    GO - Cellular componenti

    1. condensed nuclear chromosome Source: TAIR
    2. cullin-RING ubiquitin ligase complex Source: InterPro
    3. cytoplasm Source: TAIR
    4. cytosol Source: TAIR
    5. nucleus Source: TAIR
    6. phragmoplast Source: TAIR
    7. spindle Source: TAIR
    8. ubiquitin ligase complex Source: TAIR

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi682 – 6821K → M: No neddylation. 2 Publications
    Mutagenesisi712 – 7121K → M: No change in neddylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 738738Cullin-1PRO_0000119804Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki682 – 682Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)

    Post-translational modificationi

    Neddylated (rubylated). Deneddylation occurs upon interaction with the COP9 signalosome (CSN) complex.2 Publications

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    PaxDbiQ94AH6.
    PRIDEiQ94AH6.

    Expressioni

    Tissue specificityi

    Expressed constitutively in roots, seedlings, stems, leaves and flowers.1 Publication

    Developmental stagei

    Strong accumulation in embryos (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ94AH6.
    GenevestigatoriQ94AH6.

    Interactioni

    Subunit structurei

    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 CAND1.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CAND1Q8L5Y68EBI-532411,EBI-602912
    COI1O041973EBI-532411,EBI-401159
    IAA7Q388255EBI-532411,EBI-602959
    RBX1AQ940X76EBI-532411,EBI-532404
    SKP1AQ392557EBI-532411,EBI-532357

    Protein-protein interaction databases

    BioGridi10962. 43 interactions.
    DIPiDIP-33346N.
    IntActiQ94AH6. 33 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ94AH6.
    SMRiQ94AH6. Positions 42-738.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the cullin family.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5647.
    HOGENOMiHOG000176712.
    InParanoidiQ94AH6.
    KOiK03347.
    OMAiYTTEWEN.
    PhylomeDBiQ94AH6.

    Family and domain databases

    Gene3Di1.10.10.10. 2 hits.
    InterProiIPR016157. Cullin_CS.
    IPR016158. Cullin_homology.
    IPR001373. Cullin_N.
    IPR019559. Cullin_neddylation_domain.
    IPR016159. Cullin_repeat-like_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00888. Cullin. 1 hit.
    PF10557. Cullin_Nedd8. 1 hit.
    [Graphical view]
    SMARTiSM00182. CULLIN. 1 hit.
    SM00884. Cullin_Nedd8. 1 hit.
    [Graphical view]
    SUPFAMiSSF74788. SSF74788. 1 hit.
    SSF75632. SSF75632. 1 hit.
    PROSITEiPS01256. CULLIN_1. 1 hit.
    PS50069. CULLIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q94AH6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MERKTIDLEQ GWDYMQTGIT KLKRILEGLN EPAFDSEQYM MLYTTIYNMC    50
    TQKPPHDYSQ QLYDKYREAF EEYINSTVLP ALREKHDEFM LRELFKRWSN 100
    HKVMVRWLSR FFYYLDRYFI ARRSLPPLNE VGLTCFRDLV YNELHSKVKQ 150
    AVIALVDKER EGEQIDRALL KNVLDIYVEI GMGQMERYEE DFESFMLQDT 200
    SSYYSRKASS WIQEDSCPDY MLKSEECLKK ERERVAHYLH SSSEPKLVEK 250
    VQHELLVVFA SQLLEKEHSG CRALLRDDKV DDLSRMYRLY HKILRGLEPV 300
    ANIFKQHVTA EGNALVQQAE DTATNQVANT ASVQEQVLIR KVIELHDKYM 350
    VYVTECFQNH TLFHKALKEA FEIFCNKTVA GSSSAELLAT FCDNILKKGG 400
    SEKLSDEAIE DTLEKVVKLL AYISDKDLFA EFYRKKLARR LLFDRSANDD 450
    HERSILTKLK QQCGGQFTSK MEGMVTDLTL ARENQNSFED YLGSNPAANP 500
    GIDLTVTVLT TGFWPSYKSF DINLPSEMIK CVEVFKGFYE TKTKHRKLTW 550
    IYSLGTCHIN GKFDQKAIEL IVSTYQAAVL LLFNTTDKLS YTEILAQLNL 600
    SHEDLVRLLH SLSCAKYKIL LKEPNTKTVS QNDAFEFNSK FTDRMRRIKI 650
    PLPPVDERKK VVEDVDKDRR YAIDAAIVRI MKSRKVLGHQ QLVSECVEQL 700
    SRMFKPDIKA IKKRMEDLIT RDYLERDKEN PNMFRYLA 738
    Length:738
    Mass (Da):86,302
    Last modified:December 1, 2001 - v1
    Checksum:i45041357DE8DAD8C
    GO

    Sequence cautioni

    The sequence AAC78267.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAB80750.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ318017 mRNA. Translation: CAC85264.1.
    AC002330 Genomic DNA. Translation: AAC78267.1. Sequence problems.
    AL161494 Genomic DNA. Translation: CAB80750.1. Sequence problems.
    CP002687 Genomic DNA. Translation: AEE82194.1.
    CP002687 Genomic DNA. Translation: AEE82195.1.
    CP002687 Genomic DNA. Translation: AEE82196.1.
    CP002687 Genomic DNA. Translation: AEE82197.1.
    AY046030 mRNA. Translation: AAK76704.1.
    AY133878 mRNA. Translation: AAM91812.1.
    AK222216 mRNA. Translation: BAD95380.1.
    PIRiT01092.
    RefSeqiNP_001031575.1. NM_001036498.2.
    NP_001031576.1. NM_001036499.1.
    NP_001190661.1. NM_001203732.1.
    NP_567243.1. NM_116491.2.
    UniGeneiAt.24877.
    At.67849.

    Genome annotation databases

    EnsemblPlantsiAT4G02570.1; AT4G02570.1; AT4G02570.
    AT4G02570.2; AT4G02570.2; AT4G02570.
    AT4G02570.3; AT4G02570.3; AT4G02570.
    AT4G02570.4; AT4G02570.4; AT4G02570.
    GeneIDi825648.
    KEGGiath:AT4G02570.

    Cross-referencesi

    Web resourcesi

    PlantsUBQ

    A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ318017 mRNA. Translation: CAC85264.1 .
    AC002330 Genomic DNA. Translation: AAC78267.1 . Sequence problems.
    AL161494 Genomic DNA. Translation: CAB80750.1 . Sequence problems.
    CP002687 Genomic DNA. Translation: AEE82194.1 .
    CP002687 Genomic DNA. Translation: AEE82195.1 .
    CP002687 Genomic DNA. Translation: AEE82196.1 .
    CP002687 Genomic DNA. Translation: AEE82197.1 .
    AY046030 mRNA. Translation: AAK76704.1 .
    AY133878 mRNA. Translation: AAM91812.1 .
    AK222216 mRNA. Translation: BAD95380.1 .
    PIRi T01092.
    RefSeqi NP_001031575.1. NM_001036498.2.
    NP_001031576.1. NM_001036499.1.
    NP_001190661.1. NM_001203732.1.
    NP_567243.1. NM_116491.2.
    UniGenei At.24877.
    At.67849.

    3D structure databases

    ProteinModelPortali Q94AH6.
    SMRi Q94AH6. Positions 42-738.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 10962. 43 interactions.
    DIPi DIP-33346N.
    IntActi Q94AH6. 33 interactions.

    Proteomic databases

    PaxDbi Q94AH6.
    PRIDEi Q94AH6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblPlantsi AT4G02570.1 ; AT4G02570.1 ; AT4G02570 .
    AT4G02570.2 ; AT4G02570.2 ; AT4G02570 .
    AT4G02570.3 ; AT4G02570.3 ; AT4G02570 .
    AT4G02570.4 ; AT4G02570.4 ; AT4G02570 .
    GeneIDi 825648.
    KEGGi ath:AT4G02570.

    Organism-specific databases

    TAIRi AT4G02570.

    Phylogenomic databases

    eggNOGi COG5647.
    HOGENOMi HOG000176712.
    InParanoidi Q94AH6.
    KOi K03347.
    OMAi YTTEWEN.
    PhylomeDBi Q94AH6.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    PROi Q94AH6.

    Gene expression databases

    ArrayExpressi Q94AH6.
    Genevestigatori Q94AH6.

    Family and domain databases

    Gene3Di 1.10.10.10. 2 hits.
    InterProi IPR016157. Cullin_CS.
    IPR016158. Cullin_homology.
    IPR001373. Cullin_N.
    IPR019559. Cullin_neddylation_domain.
    IPR016159. Cullin_repeat-like_dom.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00888. Cullin. 1 hit.
    PF10557. Cullin_Nedd8. 1 hit.
    [Graphical view ]
    SMARTi SM00182. CULLIN. 1 hit.
    SM00884. Cullin_Nedd8. 1 hit.
    [Graphical view ]
    SUPFAMi SSF74788. SSF74788. 1 hit.
    SSF75632. SSF75632. 1 hit.
    PROSITEi PS01256. CULLIN_1. 1 hit.
    PS50069. CULLIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      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.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    3. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    4. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      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.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
      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.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 491-738.
      Strain: cv. Columbia.
    6. "Identification of an SCF ubiquitin-ligase complex required for auxin response in Arabidopsis thaliana."
      Gray W.M., del Pozo J.C., Walker L., Hobbie L., Risseeuw E., Banks T., Crosby W.L., Yang M., Ma H., Estelle M.
      Genes Dev. 13:1678-1691(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TIR1, IDENTIFICATION IN A SCF(TIR1) COMPLEX.
    7. "The Arabidopsis cullin AtCUL1 is modified by the ubiquitin-related protein RUB1."
      del Pozo J.C., Estelle M.
      Proc. Natl. Acad. Sci. U.S.A. 96:15342-15347(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NEDDYLATION AT LYS-682, MUTAGENESIS OF LYS-682 AND LYS-712.
    8. "SKP1-SnRK protein kinase interactions mediate proteasomal binding of a plant SCF ubiquitin ligase."
      Farras R., Ferrando A., Jasik J., Kleinow T., Oekresz L., Tiburcio A., Salchert K., del Pozo C., Schell J., Koncz C.
      EMBO J. 20:2742-2756(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SKP1A; KIN10 AND KIN11.
    9. "Interactions of the COP9 signalosome with the E3 ubiquitin ligase SCF(TIR1) in mediating auxin response."
      Schwechheimer C., Serino G., Callis J., Crosby W.L., Lyapina S., Deshaies R.J., Gray W.M., Estelle M., Deng X.-W.
      Science 292:1379-1382(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THE CSN COMPLEX.
    10. "The AtRbx1 protein is part of plant SCF complexes, and its down-regulation causes severe growth and developmental defects."
      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.
      J. Biol. Chem. 277:50069-50080(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKP1A; SKP1B; RBX1A AND RBX1B.
    11. "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."
      Wang X., Kang D., Feng S., Serino G., Schwechheimer C., Wei N.
      Mol. Biol. Cell 13:646-655(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NEDDYLATION, DENEDDYLATION BY THE CSN COMPLEX.
    12. "Protein interaction analysis of SCF ubiquitin E3 ligase subunits from Arabidopsis."
      Risseeuw E.P., Daskalchuk T.E., Banks T.W., Liu E., Cotelesage J., Hellmann H., Estelle M., Somers D.E., Crosby W.L.
      Plant J. 34:753-767(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SKIP14; FBW2/SKIP18; SKIP19/FBL20 AND SKIP28/MEE11.
    13. "Arabidopsis CAND1, an unmodified CUL1-interacting protein, is involved in multiple developmental pathways controlled by ubiquitin/proteasome-mediated protein Degradation."
      Feng S., Shen Y., Sullivan J.A., Rubio V., Xiong Y., Sun T.P., Deng X.W.
      Plant Cell 16:1870-1882(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CAND1, MUTAGENESIS OF LYS-682.
    14. "F-box protein DOR functions as a novel inhibitory factor for abscisic acid-induced stomatal closure under drought stress in Arabidopsis."
      Zhang Y., Xu W., Li Z., Deng X.W., Wu W., Xue Y.
      Plant Physiol. 148:2121-2133(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DOR.

    Entry informationi

    Entry nameiCUL1_ARATH
    AccessioniPrimary (citable) accession number: Q94AH6
    Secondary accession number(s): O22770, Q56W31
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2005
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 102 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3