Reviewed, UniProtKB/Swiss-Prot Q940X7 (RBX1A_ARATH)

Names and origin

Protein names

Recommended name:
    RING-box protein 1a
Alternative name(s):
    RBX1a-At
    At-Rbx1;1
    RBX1-2
    Protein RING of cullins 1

Gene names

Name:	RBX1A
Synonyms:	ROC1
Ordered Locus Names:	At5g20570
ORF Names:	F7C8.160

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	118 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The SCF complex plays a crucial role in regulating response to auxin and is essential for growth and development. Through the RING-type zinc finger, seems to recruit the E2 ubiquitination enzyme, to the complex and brings it into close proximity to the substrate. Promotes the neddylation of CUL1. Ref.6 Ref.7 Ref.8
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Part of SCF complexes, which consist of a SKP1-related protein, a cullin, a RBX protein and a F-box protein. Part of a SCF complex with ASK1 or ASK2 and CUL1. Part of a SCF complex with CUL1 and TIR1. Interacts with CUL1 and CUL4. Component of the CUL4-RBX1-CDD complex. Ref.6 Ref.7
Subcellular location	Cytoplasm By similarity. Nucleus By similarity.
Tissue specificity	Widely expressed. Expressed in shoot, siliques, meristem, flowers, floral buds, open flowers, leaves, stems, roots, germinal seeds and seedlings in dark. Expressed at a higher level in tissues containing actively dividing cells. Ref.6 Ref.7
Domain	The RING-type zinc finger domain is essential for ubiquitin ligase activity. It coordinates an additional third zinc ion.
Sequence similarities	Belongs to the RING-box family. Contains 1 RING-type zinc finger.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Domain	Zinc-finger
Ligand	Metal-binding Zinc
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW protein ubiquitination Ref.6 Traceable author statement. Source: TAIR response to auxin stimulus Ref.6 Inferred from mutant phenotype. Source: TAIR
Cellular component	Cul3-RING ubiquitin ligase complex Inferred from physical interaction. Source: TAIR SCF ubiquitin ligase complex Ref.6 Inferred from physical interaction. Source: TAIR cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	protein binding Ref.6 Ref.7 Ref.8 Ref.9 Inferred from physical interaction. Source: IntAct zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CUL1	Q94AH6	6	EBI-532404,EBI-532411
cul3a	Q9ZVH4	4	EBI-532404,EBI-531362
cul3B	Q711G4	3	EBI-532404,EBI-541687
DET1	Q9ZNU6	1	EBI-532404,EBI-2029363	From a different organism.
RCE1	Q9SDY5	2	EBI-532404,EBI-595116
TIR1	Q570C0	1	EBI-532404,EBI-307183

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 118	118	RING-box protein 1a		PRO_0000056019
Regions
	Zinc finger	63 – 108	46	RING-type
Sites
	Metal binding	52	1	Zinc 1 By similarity
	Metal binding	55	1	Zinc 1 By similarity
	Metal binding	63	1	Zinc 3 By similarity
	Metal binding	66	1	Zinc 3 By similarity
	Metal binding	78	1	Zinc 3 By similarity
	Metal binding	85	1	Zinc 2 By similarity
	Metal binding	87	1	Zinc 2 By similarity
	Metal binding	90	1	Zinc 1 By similarity
	Metal binding	92	1	Zinc 3 By similarity
	Metal binding	93	1	Zinc 1 By similarity
	Metal binding	104	1	Zinc 2 By similarity
	Metal binding	107	1	Zinc 2 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q940X7-1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 19947BF06F442A82	FASTA	118	13,238
	10 20 30 40 50 60 MATLDSDVTM IPAGEASSSV AASSSNKKAK RFEIKKWSAV ALWAWDIVVD NCAICRNHIM 70 80 90 100 110 DLCIECQANQ ASATSEECTV AWGVCNHAFH FHCISRWLKT RQVCPLDNSE WEFQKYGH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Oekresz L. Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F. Nature 408:823-826(2000) [PubMed: 11130714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"Functional annotation of a full-length Arabidopsis cDNA collection." Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K. Science 296:141-145(2002) [PubMed: 11910074] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[5]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	"Role of the Arabidopsis RING-H2 protein RBX1 in RUB modification and SCF function." Gray W.M., Hellmann H., Dharmasiri S., Estelle M. Plant Cell 14:2137-2144(2002) [PubMed: 12215511] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, IDENTIFICATION IN A SCF COMPLEX WITH CUL1 AND TIR1, INTERACTION WITH CUL1.
[7]	"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: FUNCTION, TISSUE SPECIFICITY, IDENTIFICATION IN SCF COMPLEX, INTERACTION WITH CUL1; CUL4; ASK1 AND ASK2.
[8]	"The RUB/Nedd8 conjugation pathway is required for early development in Arabidopsis." Dharmasiri S., Dharmasiri N., Hellmann H., Estelle M. EMBO J. 22:1762-1770(2003) [PubMed: 12682009] [Abstract] Cited for: FUNCTION.
[9]	"Arabidopsis CULLIN4 forms an E3 ubiquitin ligase with RBX1 and the CDD complex in mediating light control of development." Chen H., Shen Y., Tang X., Yu L., Wang J., Guo L., Zhang Y., Zhang H., Feng S., Strickland E., Zheng N., Deng X.-W. Plant Cell 18:1991-2004(2006) [PubMed: 16844902] [Abstract] Cited for: IDENTIFICATION IN THE CUL4-RBX1-CDD E3 LIGASE COMPLEX.

Web resources

PlantsUBQ

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

Cross-references

Sequence databases
EMBLGenBankDDBJ	AY052401 mRNA. Translation: AAL13435.1. AF296833 Genomic DNA. No translation available. AK118181 mRNA. Translation: BAC42804.1. AY072430 mRNA. Translation: AAL62422.1. AY114719 mRNA. Translation: AAM48038.1. AY086913 mRNA. Translation: AAM64477.1.
IPI	IPI00545980.
RefSeq	NP_568396.1.
UniGene	At.46369 At.69564
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q940X7. 10 interactions.
Proteomic databases
PRIDE	Q940X7.
Genome annotation databases
GeneID	832179.
GenomeReviews	Gene locus AT5G20570 in contig BA000015_GR.
KEGG	ath:AT5G20570.
NMPDR	fig|3702.1.peg.24267.
Organism-specific databases
TAIR	At5g20570.
Phylogenomic databases
OMA	Q940X7. RIECQAN.
Gene expression databases
ArrayExpress	Q940X7.
GermOnline	AT5G20570. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR018957. Znf_C3HC4_RING-type. IPR001841. Znf_RING. [Graphical view]
Pfam	PF00097. zf-C3HC4. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

RBX1A_ARATH

Accession

Primary (citable) accession number: Q940X7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	December 1, 2001
Last modified:	June 16, 2009
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)