Q94AH6 (CUL1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cullin-1

Gene names

Name:	CUL1
Ordered Locus Names:	At4g02570
ORF Names:	T10P11.26

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	738 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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. 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 process	Auxin signaling pathway Cell cycle Ethylene signaling pathway Ubl conjugation pathway
Cellular component	Cytoplasm Cytoskeleton Nucleus
Molecular function	Developmental protein
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	SCF complex assembly Inferred from physical interaction PubMed 15860010. Source: TAIR auxin mediated 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 mediated 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 stimulus Inferred from mutant phenotype PubMed 10654597. Source: TAIR ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	condensed nuclear chromosome Inferred from direct assay Ref.1. Source: TAIR cullin-RING ubiquitin ligase complex Inferred from electronic annotation. Source: InterPro cytosol Inferred from direct assay PubMed 21166475. 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...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CAND1	Q8L5Y6	8	EBI-532411,EBI-602912
COI1	O04197	3	EBI-532411,EBI-401159
IAA7	Q38825	5	EBI-532411,EBI-602959
RBX1A	Q940X7	6	EBI-532411,EBI-532404
SKP1A	Q39255	7	EBI-532411,EBI-532357

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 738	738	Cullin-1		PRO_0000119804
Amino acid modifications
	Cross-link	682		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) Ref.7
Experimental info
	Mutagenesis	682	1	K → M: No neddylation. Ref.7 Ref.13
	Mutagenesis	712	1	K → M: No change in neddylation. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Q94AH6 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 45041357DE8DAD8C	FASTA	738	86,302
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
+	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.
IPI	IPI00524614.
PIR	T01092.
RefSeq	NP_001031575.1. NM_001036498.2. NP_001031576.1. NM_001036499.1. NP_001190661.1. NM_001203732.1. NP_567243.1. NM_116491.2.
UniGene	At.24877. At.67849.
3D structure databases
ProteinModelPortal	Q94AH6.
SMR	Q94AH6. Positions 42-738.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q94AH6. 33 interactions.
Proteomic databases
PaxDb	Q94AH6.
PRIDE	Q94AH6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G02570.1; AT4G02570.1; AT4G02570. AT4G02570.2; AT4G02570.2; AT4G02570. AT4G02570.3; AT4G02570.3; AT4G02570. AT4G02570.4; AT4G02570.4; AT4G02570.
GeneID	825648.
KEGG	ath:AT4G02570.
Organism-specific databases
TAIR	At4g02570.
Phylogenomic databases
eggNOG	COG5647.
HOGENOM	HOG000176712.
InParanoid	Q94AH6.
KO	K03347.
OMA	LDEGHEN.
PhylomeDB	Q94AH6.
ProtClustDB	CLSN2689296.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	Q94AH6.
Genevestigator	Q94AH6.
GermOnline	AT4G02570. Arabidopsis thaliana.
Family and domain databases
Gene3D	1.10.10.10. 2 hits.
InterPro	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]
Pfam	PF00888. Cullin. 1 hit. PF10557. Cullin_Nedd8. 1 hit. [Graphical view]
SMART	SM00182. CULLIN. 1 hit. SM00884. Cullin_Nedd8. 1 hit. [Graphical view]
SUPFAM	SSF75632. Cullin_homology. 1 hit. SSF74788. Cullin_repeat-like. 1 hit.
PROSITE	PS01256. CULLIN_1. 1 hit. PS50069. CULLIN_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CUL1_ARATH

Accession

Primary (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:	May 1, 2013
This is version 92 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program