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Q94AH6 (CUL1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cullin-1
Gene names
Name:CUL1
Ordered Locus Names:At4g02570
ORF Names:T10P11.26
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length738 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (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. Ref.1 Ref.13

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.6 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14

Subcellular location

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. Ref.1 Ref.8

Tissue specificity

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

Developmental stage

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

Post-translational modification

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

Sequence similarities

Belongs to the cullin family.

Sequence caution

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.

Ontologies

Keywords
   Biological processAuxin signaling pathway
Cell cycle
Ethylene signaling pathway
Ubl conjugation pathway
   Cellular componentCytoplasm
Cytoskeleton
Nucleus
   Molecular functionDevelopmental protein
   PTMIsopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSCF complex assembly

Inferred from physical interaction PubMed 15860010. Source: TAIR

auxin-activated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

embryo development ending in seed dormancy

Inferred from mutant phenotype PubMed 10654597. Source: TAIR

ethylene-activated signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

jasmonic acid mediated signaling pathway

Traceable author statement PubMed 15860010. Source: TAIR

leaf development

Inferred from mutant phenotype PubMed 23319550. Source: TAIR

phloem or xylem histogenesis

Inferred from mutant phenotype PubMed 23319550. Source: TAIR

protein ubiquitination

Inferred from electronic annotation. Source: UniProtKB-UniPathway

regulation of circadian rhythm

Inferred from mutant phenotype PubMed 18433436. Source: TAIR

response to auxin

Inferred from mutant phenotype PubMed 10654597. Source: TAIR

response to jasmonic acid

Inferred from mutant phenotype PubMed 15860010. Source: TAIR

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcondensed nuclear chromosome

Inferred from direct assay Ref.1. Source: TAIR

cullin-RING ubiquitin ligase complex

Inferred from electronic annotation. Source: InterPro

cytoplasm

Inferred from direct assay Ref.1PubMed 23319550. Source: TAIR

cytosol

Inferred from direct assay PubMed 21166475. Source: TAIR

nucleus

Inferred from direct assay Ref.8PubMed 23319550. Source: TAIR

phragmoplast

Inferred from direct assay Ref.8. Source: TAIR

spindle

Inferred from direct assay Ref.8. Source: TAIR

ubiquitin ligase complex

Inferred from physical interaction Ref.6. Source: TAIR

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 738738Cullin-1
PRO_0000119804

Amino acid modifications

Cross-link682Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) Ref.7

Experimental info

Mutagenesis6821K → M: No neddylation. Ref.7 Ref.13
Mutagenesis7121K → M: No change in neddylation. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Q94AH6 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 45041357DE8DAD8C

FASTA73886,302
        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 

« Hide

References

« Hide 'large scale' references
[1]"Null mutation of AtCUL1 causes arrest in early embryogenesis in Arabidopsis."
Shen W.-H., Parmentier Y., Hellmann H., Lechner E., Dong A., Masson J., Granier F., Lepiniec L., Estelle M., Genschik P.
Mol. Biol. Cell 13:1916-1928(2002) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

PlantsUBQ

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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT01092.
RefSeqNP_001031575.1. NM_001036498.2.
NP_001031576.1. NM_001036499.1.
NP_001190661.1. NM_001203732.1.
NP_567243.1. NM_116491.2.
UniGeneAt.24877.
At.67849.

3D structure databases

ProteinModelPortalQ94AH6.
SMRQ94AH6. Positions 42-738.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid10962. 43 interactions.
DIPDIP-33346N.
IntActQ94AH6. 33 interactions.

Proteomic databases

PaxDbQ94AH6.
PRIDEQ94AH6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G02570.1; AT4G02570.1; AT4G02570.
AT4G02570.2; AT4G02570.2; AT4G02570.
AT4G02570.3; AT4G02570.3; AT4G02570.
AT4G02570.4; AT4G02570.4; AT4G02570.
GeneID825648.
KEGGath:AT4G02570.

Organism-specific databases

TAIRAT4G02570.

Phylogenomic databases

eggNOGCOG5647.
HOGENOMHOG000176712.
InParanoidQ94AH6.
KOK03347.
OMALDEGHEN.
PhylomeDBQ94AH6.
ProtClustDBCLSN2689296.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ94AH6.
GenevestigatorQ94AH6.

Family and domain databases

Gene3D1.10.10.10. 2 hits.
InterProIPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTSM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMSSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ94AH6.

Entry information

Entry nameCUL1_ARATH
AccessionPrimary (citable) accession number: Q94AH6
Secondary accession number(s): O22770, Q56W31
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names