ID A0A3B5Q158_XIPMA Unreviewed; 110 AA.
AC A0A3B5Q158;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 28-JAN-2026, entry version 34.
DE RecName: Full=RING-box protein 2 {ECO:0000256|ARBA:ARBA00069656};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.32 {ECO:0000256|ARBA:ARBA00044971};
DE AltName: Full=RING finger protein 7 {ECO:0000256|ARBA:ARBA00078874};
DE AltName: Full=Sensitive to apoptosis gene protein {ECO:0000256|ARBA:ARBA00083543};
OS Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Xiphophorus.
OX NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000024557.1, ECO:0000313|Proteomes:UP000002852};
RN [1] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA Walter R., Schartl M., Warren W.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000002852}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX PubMed=23542700; DOI=10.1038/ng.2604;
RA Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA Postlethwait J.H., Warren W.C.;
RT "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT evolutionary adaptation and several complex traits.";
RL Nat. Genet. 45:567-572(2013).
RN [3] {ECO:0000313|Ensembl:ENSXMAP00000024557.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000024557.1};
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [4] {ECO:0000313|Ensembl:ENSXMAP00000024557.1}
RP IDENTIFICATION.
RC STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000024557.1};
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-[NEDD8-protein]-yl-[E2 NEDD8-conjugating enzyme]-L-cysteine
CC + [cullin]-L-lysine = [E2 NEDD8-conjugating enzyme]-L-cysteine +
CC N(6)-[NEDD8-protein]-yl-[cullin]-L-lysine.; EC=2.3.2.32;
CC Evidence={ECO:0000256|ARBA:ARBA00044896};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein neddylation.
CC {ECO:0000256|ARBA:ARBA00005032}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBUNIT: Catalytic component of multiple cullin-5-RING E3 ubiquitin-
CC protein ligase complexes (ECS complexes, also named CRL5 complexes)
CC composed of CUL5, Elongin BC (ELOB and ELOC), RNF7/RBX2 and a variable
CC SOCS box domain-containing protein as substrate-specific recognition
CC component. Also interacts (with lower preference) with CUL1, CUL2,
CC CUL3, CUL4A and CUL4B; additional evidence is however required to
CC confirm this result in vivo. Interacts with UBE2F. Interacts with
CC CSNK2B, the interaction is not affected by phosphorylation by CK2. May
CC also interact with DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and DCUN1D5.
CC {ECO:0000256|ARBA:ARBA00062884}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the RING-box family.
CC {ECO:0000256|ARBA:ARBA00009273}.
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DR RefSeq; XP_005803419.1; XM_005803362.2.
DR AlphaFoldDB; A0A3B5Q158; -.
DR FunCoup; A0A3B5Q158; 1093.
DR STRING; 8083.ENSXMAP00000024557; -.
DR Ensembl; ENSXMAT00000036605.1; ENSXMAP00000024557.1; ENSXMAG00000026480.1.
DR GeneID; 102218703; -.
DR KEGG; xma:102218703; -.
DR CTD; 9616; -.
DR GeneTree; ENSGT00940000155481; -.
DR InParanoid; A0A3B5Q158; -.
DR OMA; RQNNRCP; -.
DR OrthoDB; 8962942at2759; -.
DR Proteomes; UP000002852; Unassembled WGS sequence.
DR GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IEA:UniProtKB-ARBA.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-ARBA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0061663; F:NEDD8 ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:UniProtKB-ARBA.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:UniProtKB-ARBA.
DR CDD; cd16466; RING-H2_RBX2; 1.
DR FunFam; 3.30.40.10:FF:000156; RING-box protein 2 isoform X1; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR051031; RING-box_E3_Ubiquitin_Ligase.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR024766; Znf_RING_H2.
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 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002852};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 58..100
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 110 AA; 12434 MW; 49C1E48B68C80A21 CRC64;
MDDGDEPGLV LSHSTSSGSK SGGDKMFSLK KWNAVAMWSW DVECDTCAIC RVQVMDACLR
CQAENKQEDC VVVWGECNHS FHNCCMSLWV KQNNRCPLCQ QDWVVQRIGK
//
