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UniProtKB/Swiss-Prot entry Q940X7


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name RBX1A_ARATH
Primary accession number Q940X7
Secondary accession numbers None
Integrated into Swiss-Prot on October 3, 2003
Sequence was last modified on December 1, 2001 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 61)
Name and origin of the protein
Protein name RING-box protein 1a
Synonyms RBX1a-At
At-Rbx1;1
RBX1-2
Protein RING of cullins 1
Gene name
Name: RBX1A
Synonyms: ROC1
OrderedLocusNames: At5g20570
ORFNames: F7C8.160
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Oekresz L.;
Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048507; PubMed=11130714 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
Nature 408:823-826(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1071006; PubMed=11910074 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Functional annotation of a full-length Arabidopsis cDNA collection.";
Science 296:141-145(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.;
"Full-length cDNA from Arabidopsis thaliana.";
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, TISSUE SPECIFICITY, IDENTIFICATION IN A SCF COMPLEX WITH CUL1 AND TIR1, AND INTERACTION WITH CUL1.
DOI=10.1105/tpc.003178; PubMed=12215511 [NCBI, ExPASy, EBI, Israel, Japan]
Gray W.M., Hellmann H., Dharmasiri S., Estelle M.;
"Role of the Arabidopsis RING-H2 protein RBX1 in RUB modification and SCF function.";
Plant Cell 14:2137-2144(2002).
[7]
FUNCTION, TISSUE SPECIFICITY, IDENTIFICATION IN SCF COMPLEX, AND INTERACTION WITH CUL1; CUL4; ASK1 AND ASK2.
DOI=10.1074/jbc.M204254200; PubMed=12381738 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The AtRbx1 protein is part of plant SCF complexes, and its down-regulation causes severe growth and developmental defects.";
J. Biol. Chem. 277:50069-50080(2002).
[8]
FUNCTION.
DOI=10.1093/emboj/cdg190; PubMed=12682009 [NCBI, ExPASy, EBI, Israel, Japan]
Dharmasiri S., Dharmasiri N., Hellmann H., Estelle M.;
"The RUB/Nedd8 conjugation pathway is required for early development in Arabidopsis.";
EMBO J. 22:1762-1770(2003).
[9]
IDENTIFICATION IN THE CUL4-RBX1-CDD E3 LIGASE COMPLEX.
DOI=10.1105/tpc.106.043224; PubMed=16844902 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Arabidopsis CULLIN4 forms an E3 ubiquitin ligase with RBX1 and the CDD complex in mediating light control of development.";
Plant Cell 18:1991-2004(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY052401; AAL13435.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF296833; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
AK118181; BAC42804.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY072430; AAL62422.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY114719; AAM48038.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY086913; AAM64477.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_568396.1; -.
UniGene At.46369
3D structure databases
ModBase Q940X7.
Protein-protein interaction databases
IntAct Q940X7; -.
Organism-specific databases
TAIR At5g20570; -.
Gene expression databases
ArrayExpress Q940X7; -.
GermOnline AT5G20570; Arabidopsis thaliana.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR001841; Znf_RING.
IPR013083; Znf_RING/FYVE/PHD.
Graphical view of domain structure.
Gene3D G3DSA:3.30.40.10; Znf_RING/FYVE/PHD; 1.
Pfam PF00097; zf-C3HC4; 1.
Pfam graphical view of domain structure.
SMART SM00184; RING; 1.
SMART graphical view of domain structure.
PROSITE PS50089; ZF_RING_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q940X7.
Genome annotation databases
GeneID 832179; -.
GenomeReviews BA000015_GR; AT5G20570.
KEGG ath:AT5G20570; -.
NMPDR fig|3702.1.peg.24267; -.
Other
ProtoNet Q940X7.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Metal-binding; Nucleus; Ubl conjugation pathway; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   118  118     RING-box protein 1a. PRO_0000056019
ZN_FING   63   108  46     RING-type. 
METAL   52    52        Zinc 1 (By similarity). 
METAL   55    55        Zinc 1 (By similarity). 
METAL   63    63        Zinc 3 (By similarity). 
METAL   66    66        Zinc 3 (By similarity). 
METAL   78    78        Zinc 3 (By similarity). 
METAL   85    85        Zinc 2 (By similarity). 
METAL   87    87        Zinc 2 (By similarity). 
METAL   90    90        Zinc 1 (By similarity). 
METAL   92    92        Zinc 3 (By similarity). 
METAL   93    93        Zinc 1 (By similarity). 
METAL   104   104        Zinc 2 (By similarity). 
METAL   107   107        Zinc 2 (By similarity). 
Sequence information
Length: 118 AA [This is the length of the unprocessed precursor] Molecular weight: 13238 Da [This is the MW of the unprocessed precursor] CRC64: 19947BF06F442A82 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATLDSDVTM IPAGEASSSV AASSSNKKAK RFEIKKWSAV ALWAWDIVVD NCAICRNHIM 

        70         80         90        100        110 
DLCIECQANQ ASATSEECTV AWGVCNHAFH FHCISRWLKT RQVCPLDNSE WEFQKYGH 

Q940X7 in FASTA format

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