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Protein

Cullin-1

Gene

CUL1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 - 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. ubiquitin-dependent protein catabolic process Source: InterPro
Complete GO annotation...

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 Componenti: 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
Complete GO annotation...

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

ExpressionAtlasiQ94AH6. baseline and differential.
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.
OMAiWVYSQSR.
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

        10         20         30         40         50
MERKTIDLEQ GWDYMQTGIT KLKRILEGLN EPAFDSEQYM MLYTTIYNMC
60 70 80 90 100
TQKPPHDYSQ QLYDKYREAF EEYINSTVLP ALREKHDEFM LRELFKRWSN
110 120 130 140 150
HKVMVRWLSR FFYYLDRYFI ARRSLPPLNE VGLTCFRDLV YNELHSKVKQ
160 170 180 190 200
AVIALVDKER EGEQIDRALL KNVLDIYVEI GMGQMERYEE DFESFMLQDT
210 220 230 240 250
SSYYSRKASS WIQEDSCPDY MLKSEECLKK ERERVAHYLH SSSEPKLVEK
260 270 280 290 300
VQHELLVVFA SQLLEKEHSG CRALLRDDKV DDLSRMYRLY HKILRGLEPV
310 320 330 340 350
ANIFKQHVTA EGNALVQQAE DTATNQVANT ASVQEQVLIR KVIELHDKYM
360 370 380 390 400
VYVTECFQNH TLFHKALKEA FEIFCNKTVA GSSSAELLAT FCDNILKKGG
410 420 430 440 450
SEKLSDEAIE DTLEKVVKLL AYISDKDLFA EFYRKKLARR LLFDRSANDD
460 470 480 490 500
HERSILTKLK QQCGGQFTSK MEGMVTDLTL ARENQNSFED YLGSNPAANP
510 520 530 540 550
GIDLTVTVLT TGFWPSYKSF DINLPSEMIK CVEVFKGFYE TKTKHRKLTW
560 570 580 590 600
IYSLGTCHIN GKFDQKAIEL IVSTYQAAVL LLFNTTDKLS YTEILAQLNL
610 620 630 640 650
SHEDLVRLLH SLSCAKYKIL LKEPNTKTVS QNDAFEFNSK FTDRMRRIKI
660 670 680 690 700
PLPPVDERKK VVEDVDKDRR YAIDAAIVRI MKSRKVLGHQ QLVSECVEQL
710 720 730
SRMFKPDIKA IKKRMEDLIT RDYLERDKEN PNMFRYLA
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. Curated
The sequence CAB80750.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

Proteomic databases

PaxDbiQ94AH6.
PRIDEiQ94AH6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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.

Organism-specific databases

TAIRiAT4G02570.

Phylogenomic databases

eggNOGiCOG5647.
HOGENOMiHOG000176712.
InParanoidiQ94AH6.
KOiK03347.
OMAiWVYSQSR.
PhylomeDBiQ94AH6.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiQ94AH6.

Gene expression databases

ExpressionAtlasiQ94AH6. baseline and differential.
GenevestigatoriQ94AH6.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (MAR-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(2002) [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 (FEB-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(1998) [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(1998) [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(2000) [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(2000) [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(2001) [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(2001) [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(2002) [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(2003) [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(2007) [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: April 1, 2015
This is version 105 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.