RBX1_CAEEL
ID RBX1_CAEEL Reviewed; 110 AA.
AC Q23457; Q8WSQ1;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=RING-box protein 1;
DE Short=Rbx1;
DE AltName: Full=Ce-rbx-1;
GN Name=rbx-1; ORFNames=ZK287.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-110, FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=14622138; DOI=10.1046/j.1365-2443.2003.00682.x;
RA Sasagawa Y., Urano T., Kohara Y., Takahashi H., Higashitani A.;
RT "Caenorhabditis elegans RBX1 is essential for meiosis, mitotic chromosomal
RT condensation and segregation, and cytokinesis.";
RL Genes Cells 8:857-872(2003).
RN [3]
RP INTERACTION WITH CSN-1 AND CSN-6.
RX PubMed=12781129; DOI=10.1016/s0960-9822(03)00336-1;
RA Pintard L., Kurz T., Glaser S., Willis J.H., Peter M., Bowerman B.;
RT "Neddylation and deneddylation of CUL-3 is required to target MEI-1/katanin
RT for degradation at the meiosis-to-mitosis transition in C. elegans.";
RL Curr. Biol. 13:911-921(2003).
CC -!- FUNCTION: Component of the SCF (SKP1-CUL1-F-box protein) E3 ubiquitin
CC ligase complex, which mediates the ubiquitination and subsequent
CC proteasomal degradation of target proteins. Through the RING-type zinc
CC finger, seems to recruit the E2 ubiquitination enzyme to the complex
CC and brings it into close proximity to the substrate (By similarity).
CC Essential for meiosis, mitotic chromosomal condensation and
CC cytokinesis. Involved in histone H3 phosphorylation. {ECO:0000250,
CC ECO:0000269|PubMed:14622138}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Part of SCF complexes, which consist of a SKP1 or a SKP1-
CC related protein, a cullin protein, and a F-box protein (By similarity).
CC Interacts with csn-1 and csn-6. {ECO:0000250,
CC ECO:0000269|PubMed:12781129}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in the gonads of hermaphrodite
CC animals. {ECO:0000269|PubMed:14622138}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels in eggs and adults, and
CC at low levels in larva. {ECO:0000269|PubMed:14622138}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity. It coordinates an additional third zinc ion.
CC -!- SIMILARITY: Belongs to the RING-box family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-10 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB83695.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z70757; CAA94801.1; -; Genomic_DNA.
DR EMBL; AB077287; BAB83695.1; ALT_INIT; mRNA.
DR PIR; T27823; T27823.
DR RefSeq; NP_505496.1; NM_073095.5.
DR AlphaFoldDB; Q23457; -.
DR SMR; Q23457; -.
DR BioGRID; 44394; 17.
DR ComplexPortal; CPX-3383; CBC-fem-1 Ubiquitin Ligase complex.
DR IntAct; Q23457; 5.
DR MINT; Q23457; -.
DR STRING; 6239.ZK287.5.1; -.
DR EPD; Q23457; -.
DR PaxDb; Q23457; -.
DR PeptideAtlas; Q23457; -.
DR PRIDE; Q23457; -.
DR EnsemblMetazoa; ZK287.5.1; ZK287.5.1; WBGene00004320.
DR GeneID; 179358; -.
DR KEGG; cel:CELE_ZK287.5; -.
DR UCSC; ZK287.5.1; c. elegans.
DR CTD; 179358; -.
DR WormBase; ZK287.5; CE06614; WBGene00004320; rbx-1.
DR eggNOG; KOG2930; Eukaryota.
DR GeneTree; ENSGT00940000155618; -.
DR HOGENOM; CLU_115512_2_1_1; -.
DR InParanoid; Q23457; -.
DR OMA; RFDVKKW; -.
DR OrthoDB; 1587140at2759; -.
DR PhylomeDB; Q23457; -.
DR Reactome; R-CEL-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-CEL-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-CEL-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-CEL-4641258; Degradation of DVL.
DR Reactome; R-CEL-5632684; Hedgehog 'on' state.
DR Reactome; R-CEL-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-CEL-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-CEL-5696400; Dual Incision in GG-NER.
DR Reactome; R-CEL-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-CEL-6782135; Dual incision in TC-NER.
DR Reactome; R-CEL-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-CEL-68949; Orc1 removal from chromatin.
DR Reactome; R-CEL-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-CEL-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-CEL-8951664; Neddylation.
DR Reactome; R-CEL-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-CEL-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q23457; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00004320; Expressed in embryo and 7 other tissues.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:ComplexPortal.
DR GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0097602; F:cullin family protein binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; IMP:WormBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030238; P:male sex determination; IMP:ComplexPortal.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:UniProtKB.
DR GO; GO:1902104; P:positive regulation of metaphase/anaphase transition of meiotic cell cycle; IMP:WormBase.
DR GO; GO:0010623; P:programmed cell death involved in cell development; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0051759; P:sister chromosome movement towards spindle pole involved in meiotic sister chromatid segregation; IMP:WormBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
DR Pfam; PF12678; zf-rbx1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Developmental protein; Meiosis;
KW Metal-binding; Mitosis; Nucleus; Reference proteome;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..110
FT /note="RING-box protein 1"
FT /id="PRO_0000056016"
FT ZN_FING 44..100
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 55
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT CONFLICT 2..3
FT /note="AQ -> GP (in Ref. 2; BAB83695)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 110 AA; 12760 MW; EFE50F7684B30A56 CRC64;
MAQASDSTAM EVEEATNQTV KKRFEVKKWS AVALWAWDIQ VDNCAICRNH IMDLCIECQA
NQAAGLKDEC TVAWGNCNHA FHFHCISRWL KTRQVCPLDN REWEFQKYGH
