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 27-MAR-2024, entry version 171. 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; 18. DR ComplexPortal; CPX-3383; CBC-fem-1 Ubiquitin Ligase complex. DR IntAct; Q23457; 5. DR MINT; Q23457; -. DR STRING; 6239.ZK287.5.2; -. DR EPD; Q23457; -. DR PaxDb; 6239-ZK287-5-1; -. DR PeptideAtlas; 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 AGR; WB:WBGene00004320; -. 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; NACPLDN; -. DR OrthoDB; 3546417at2759; -. 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-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 cell types or 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 CDD; cd16485; mRING-H2-C3H2C2D_RBX1; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR024766; Znf_RING_H2. DR PANTHER; PTHR11210:SF2; E3 UBIQUITIN-PROTEIN LIGASE RBX1; 1. DR PANTHER; PTHR11210; RING BOX; 1. DR Pfam; PF12678; zf-rbx1; 1. DR SUPFAM; SSF57850; RING/U-box; 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 //