RBX1_SALSA
ID RBX1_SALSA Reviewed; 108 AA.
AC Q8QG64;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=RING-box protein 1;
DE Short=Rbx1;
DE AltName: Full=Hyperosmotic protein 21;
DE Short=sHOP21;
GN Name=rbx1; Synonyms=hop21;
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Gill;
RX PubMed=12010746; DOI=10.1152/ajpregu.00571.2001;
RA Pan F., Zarate J., Bradley T.M.;
RT "A homolog of the E3 ubiquitin ligase Rbx1 is induced during hyperosmotic
RT stress of salmon.";
RL Am. J. Physiol. 282:R1643-R1653(2002).
CC -!- FUNCTION: E3 ubiquitin ligase component of multiple cullin-RING-based
CC E3 ubiquitin-protein ligase (CRLs) complexes which mediate the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins, including proteins involved in cell cycle progression, signal
CC transduction, transcription and transcription-coupled nucleotide
CC excision repair. CRLs complexes and arih1 collaborate in tandem to
CC mediate ubiquitination of target proteins, arih1 mediating addition of
CC the first ubiquitin on CRLs targets. The functional specificity of the
CC E3 ubiquitin-protein ligase complexes depends on the variable substrate
CC recognition components. {ECO:0000250|UniProtKB:P62877}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:P62877}.
CC -!- SUBUNIT: Part of SCF complexes, which consist of skp1, cul1, rbx1 and a
CC F-box protein. Interacts with ube2m (By similarity).
CC {ECO:0000250|UniProtKB:P62877}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in heart and kidney.
CC {ECO:0000269|PubMed:12010746}.
CC -!- INDUCTION: During hyperosmotic stress and thermal stress.
CC {ECO:0000269|PubMed:12010746}.
CC -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC ligase activity. It coordinates an additional third zinc ion.
CC {ECO:0000250|UniProtKB:P62877}.
CC -!- SIMILARITY: Belongs to the RING-box family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK29182.1; 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; AY027936; AAK29182.1; ALT_INIT; mRNA.
DR RefSeq; XP_014048765.1; XM_014193290.1.
DR AlphaFoldDB; Q8QG64; -.
DR SMR; Q8QG64; -.
DR STRING; 8030.ENSSSAP00000005050; -.
DR GeneID; 106601243; -.
DR KEGG; sasa:106601243; -.
DR OMA; RFDVKKW; -.
DR OrthoDB; 1587140at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000087266; Chromosome ssa03.
DR Bgee; ENSSSAG00000002531; Expressed in testis and 16 other tissues.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0031467; C:Cul7-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0061663; F:NEDD8 ligase activity; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
DR GO; GO:0045116; P:protein neddylation; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cytoplasm; Metal-binding; Nucleus; Reference proteome; Stress response;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..108
FT /note="RING-box protein 1"
FT /id="PRO_0000056015"
FT ZN_FING 53..98
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 45
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
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 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P62878"
SQ SEQUENCE 108 AA; 12318 MW; 44C3EA712CEDC7BB CRC64;
MAAAMDVDTP SATNSGASKK RFEVKKWNAV ALWAWDIVVD NCAICRNHIM DLCIECQANQ
ASATSEECTV AWGVCNHAFH FHCISRWLKT RQVCPLDNRE WEFQKYGH
