Reviewed, UniProtKB/Swiss-Prot Q94AH6 (CUL1_ARATH)

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) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	738 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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
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.
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. Ref.1 Ref.7
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. Deneddylated via its 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
Gene Ontology (GO)
Biological process	SCF complex assembly Inferred from physical interaction. Source: TAIR auxin mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW cell cycle Inferred from electronic annotation. Source: UniProtKB-KW embryonic development ending in seed dormancy Inferred from mutant phenotype. Source: TAIR ethylene mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW jasmonic acid mediated signaling pathway Traceable author statement. Source: TAIR regulation of circadian rhythm Inferred from mutant phenotype. Source: TAIR ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	condensed nuclear chromosome Ref.1 Inferred from direct assay. Source: TAIR cullin-RING ubiquitin ligase complex Inferred from electronic annotation. Source: InterPro phragmoplast Ref.7 Inferred from direct assay. Source: TAIR spindle Ref.7 Inferred from direct assay. Source: TAIR
Molecular function	ubiquitin protein ligase binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
At2g02560	Q8L5Y6	6	EBI-532411,EBI-602912
At2g31470	Q5BPS3	1	EBI-532411,EBI-2042375
COI1	O04197	2	EBI-532411,EBI-401159
EBF1	Q9SKK0	1	EBI-532411,EBI-401198
EBF2	Q708Y0	1	EBI-532411,EBI-593623
GID2	Q9STX3	1	EBI-532411,EBI-619033
IAA7	Q38825	4	EBI-532411,EBI-602959
RBX1A	Q940X7	6	EBI-532411,EBI-532404
RCE1	Q9SDY5	1	EBI-532411,EBI-595116
SKP1A	Q39255	4	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.6 Ref.10
Experimental info
	Mutagenesis	682	1	K → M: No neddylation. Ref.6
	Mutagenesis	712	1	K → M: No change in neddylation. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q94AH6-1 [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: 12058059] [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: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"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.
[5]	"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: 10398681] [Abstract] Cited for: INTERACTION WITH TIR1, IDENTIFICATION IN A SCF(TIR1) COMPLEX.
[6]	"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: 10611386] [Abstract] Cited for: NEDDYLATION AT LYS-682, MUTAGENESIS OF LYS-682 AND LYS-712.
[7]	"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: 11387208] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SKP1A; KIN10 AND KIN11.
[8]	"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: 11337587] [Abstract] Cited for: INTERACTION WITH THE CSN COMPLEX.
[9]	"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: 12381738] [Abstract] Cited for: INTERACTION WITH SKP1A; SKP1B; RBX1A AND RBX1B.
[10]	"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: 11854419] [Abstract] Cited for: NEDDYLATION, DENEDDYLATION BY THE CSN COMPLEX.
[11]	"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: 12795696] [Abstract] Cited for: INTERACTION WITH SKIP14; FBW2/SKIP18; SKIP19/FBL20 AND SKIP28/MEE11.
[12]	"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: 18835996] [Abstract] Cited for: INTERACTION WITH DOR.

Web resources

PlantsUBQ

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ318017 mRNA. Translation: CAC85264.1. AC002330 Genomic DNA. Translation: AAC78267.1. Sequence problems. AL161494 Genomic DNA. Translation: CAB80750.1. Sequence problems. AY046030 mRNA. Translation: AAK76704.1. AY133878 mRNA. Translation: AAM91812.1. AK222216 mRNA. Translation: BAD95380.1.
IPI	IPI00524614.
PIR	T01092.
RefSeq	NP_001031575.1. NP_001031576.1. NP_567243.1.
UniGene	At.24877 At.67849
3D structure databases
HSSP	HSSP built from PDB template 1IUY based on UniProtKB Q9JLV5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q94AH6. 35 interactions.
Proteomic databases
PRIDE	Q94AH6.
Genome annotation databases
GeneID	825648.
GenomeReviews	Gene locus AT4G02570 in contig CT486007_GR.
KEGG	ath:AT4G02570.
NMPDR	fig|3702.1.peg.18072.
Organism-specific databases
TAIR	At4g02570.
Phylogenomic databases
OMA	Q94AH6. EDAASNK.
Gene expression databases
GermOnline	AT4G02570. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR016157. Cullin_CS. IPR016158. Cullin_homology. IPR001373. Cullin_N. IPR019559. Cullin_neddylation_domain. IPR011991. Wing_hlx_DNA_bd. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
Pfam	PF00888. Cullin. 1 hit. PF10557. Cullin_Nedd8. 1 hit. [Graphical view]
SMART	SM00182. CULLIN. 1 hit. [Graphical view]
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:	June 16, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)