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Protein

RING-box protein 1

Gene

rbx-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. 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 (By similarity). Essential for meiosis, mitotic chromosomal condensation and cytokinesis. Involved in histone H3 phosphorylation.By similarity1 Publication

Pathway: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi44 – 441Zinc 1By similarity
Metal bindingi47 – 471Zinc 1By similarity
Metal bindingi55 – 551Zinc 2By similarity
Metal bindingi58 – 581Zinc 2By similarity
Metal bindingi70 – 701Zinc 2By similarity
Metal bindingi77 – 771Zinc 3By similarity
Metal bindingi79 – 791Zinc 3; via pros nitrogenBy similarity
Metal bindingi82 – 821Zinc 1; via pros nitrogenBy similarity
Metal bindingi84 – 841Zinc 2By similarity
Metal bindingi96 – 961Zinc 3By similarity
Metal bindingi99 – 991Zinc 3By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri44 – 10057RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • anterior/posterior axis specification, embryo Source: WormBase
  • cell division Source: UniProtKB-KW
  • mitotic nuclear division Source: UniProtKB-KW
  • positive regulation of metaphase/anaphase transition of meiotic cell cycle Source: WormBase
  • protein ubiquitination Source: UniProtKB-UniPathway
  • sister chromosome movement towards spindle pole involved in meiotic sister chromatid segregation Source: WormBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Cell cycle, Cell division, Meiosis, Mitosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_297004. degradation of DVL.
REACT_297277. Degradation of beta-catenin by the destruction complex.
REACT_297611. Hedgehog 'on' state.
REACT_317653. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
RING-box protein 1
Short name:
Rbx1
Alternative name(s):
Ce-rbx-1
Gene namesi
Name:rbx-1
ORF Names:ZK287.5
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
ProteomesiUP000001940 Componenti: Chromosome V

Organism-specific databases

WormBaseiZK287.5; CE06614; WBGene00004320; rbx-1.

Subcellular locationi

GO - Cellular componenti

  • Cul2-RING ubiquitin ligase complex Source: WormBase
  • cytoplasm Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 110110RING-box protein 1PRO_0000056016Add
BLAST

Proteomic databases

PaxDbiQ23457.

Expressioni

Tissue specificityi

Strongly expressed in the gonads of hermaphrodite animals.1 Publication

Developmental stagei

Expressed at high levels in eggs and adults, and at low levels in larva.1 Publication

Interactioni

Subunit structurei

Part of SCF complexes, which consist of a SKP1 or a SKP1-related protein, a cullin protein, and a F-box protein (By similarity). Interacts with csn-1 and csn-6.By similarity1 Publication

Protein-protein interaction databases

BioGridi44394. 4 interactions.
IntActiQ23457. 5 interactions.
MINTiMINT-4052036.
STRINGi6239.ZK287.5.1.

Structurei

3D structure databases

ProteinModelPortaliQ23457.
SMRiQ23457. Positions 21-110.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The RING-type zinc finger domain is essential for ubiquitin ligase activity. It coordinates an additional third zinc ion.

Sequence similaritiesi

Belongs to the RING-box family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri44 – 10057RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5194.
GeneTreeiENSGT00390000017058.
HOGENOMiHOG000171951.
InParanoidiQ23457.
KOiK03868.
OMAiARSVCPL.
OrthoDBiEOG7CG721.
PhylomeDBiQ23457.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR024766. Znf_RING_H2.
[Graphical view]
PfamiPF12678. zf-rbx1. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q23457-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQASDSTAM EVEEATNQTV KKRFEVKKWS AVALWAWDIQ VDNCAICRNH
60 70 80 90 100
IMDLCIECQA NQAAGLKDEC TVAWGNCNHA FHFHCISRWL KTRQVCPLDN
110
REWEFQKYGH
Length:110
Mass (Da):12,760
Last modified:November 1, 1996 - v1
Checksum:iEFE50F7684B30A56
GO

Sequence cautioni

The sequence BAB83695.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 32AQ → GP in BAB83695 (PubMed:14622138).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z70757 Genomic DNA. Translation: CAA94801.1.
AB077287 mRNA. Translation: BAB83695.1. Different initiation.
PIRiT27823.
RefSeqiNP_505496.1. NM_073095.5.
UniGeneiCel.7279.

Genome annotation databases

EnsemblMetazoaiZK287.5.1; ZK287.5.1; WBGene00004320.
ZK287.5.2; ZK287.5.2; WBGene00004320.
GeneIDi179358.
KEGGicel:CELE_ZK287.5.
UCSCiZK287.5.1. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z70757 Genomic DNA. Translation: CAA94801.1.
AB077287 mRNA. Translation: BAB83695.1. Different initiation.
PIRiT27823.
RefSeqiNP_505496.1. NM_073095.5.
UniGeneiCel.7279.

3D structure databases

ProteinModelPortaliQ23457.
SMRiQ23457. Positions 21-110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi44394. 4 interactions.
IntActiQ23457. 5 interactions.
MINTiMINT-4052036.
STRINGi6239.ZK287.5.1.

Proteomic databases

PaxDbiQ23457.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiZK287.5.1; ZK287.5.1; WBGene00004320.
ZK287.5.2; ZK287.5.2; WBGene00004320.
GeneIDi179358.
KEGGicel:CELE_ZK287.5.
UCSCiZK287.5.1. c. elegans.

Organism-specific databases

CTDi179358.
WormBaseiZK287.5; CE06614; WBGene00004320; rbx-1.

Phylogenomic databases

eggNOGiCOG5194.
GeneTreeiENSGT00390000017058.
HOGENOMiHOG000171951.
InParanoidiQ23457.
KOiK03868.
OMAiARSVCPL.
OrthoDBiEOG7CG721.
PhylomeDBiQ23457.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_297004. degradation of DVL.
REACT_297277. Degradation of beta-catenin by the destruction complex.
REACT_297611. Hedgehog 'on' state.
REACT_317653. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.

Miscellaneous databases

NextBioi905060.
PROiQ23457.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR024766. Znf_RING_H2.
[Graphical view]
PfamiPF12678. zf-rbx1. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "Caenorhabditis elegans RBX1 is essential for meiosis, mitotic chromosomal condensation and segregation, and cytokinesis."
    Sasagawa Y., Urano T., Kohara Y., Takahashi H., Higashitani A.
    Genes Cells 8:857-872(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-110, FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  3. "Neddylation and deneddylation of CUL-3 is required to target MEI-1/katanin for degradation at the meiosis-to-mitosis transition in C. elegans."
    Pintard L., Kurz T., Glaser S., Willis J.H., Peter M., Bowerman B.
    Curr. Biol. 13:911-921(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSN-1 AND CSN-6.

Entry informationi

Entry nameiRBX1_CAEEL
AccessioniPrimary (citable) accession number: Q23457
Secondary accession number(s): Q8WSQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Caution

It is uncertain whether Met-1 or Met-10 is the initiator.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.