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Database: UniProt
Entry: A0A0D9RGT6_CHLSB
LinkDB: A0A0D9RGT6_CHLSB
Original site: A0A0D9RGT6_CHLSB 
ID   A0A0D9RGT6_CHLSB        Unreviewed;       324 AA.
AC   A0A0D9RGT6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU201113};
DE            EC=2.3.2.27 {ECO:0000256|RuleBase:RU201113};
GN   Name=SIAH2 {ECO:0000313|Ensembl:ENSCSAP00000007825.1};
OS   Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000007825.1, ECO:0000313|Proteomes:UP000029965};
RN   [1] {ECO:0000313|Ensembl:ENSCSAP00000007825.1, ECO:0000313|Proteomes:UP000029965}
RP   NUCLEOTIDE SEQUENCE.
RA   Warren W., Wilson R.K.;
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCSAP00000007825.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: E3 ubiquitin-protein ligase that mediates ubiquitination and
CC       subsequent proteasomal degradation of target proteins. E3 ubiquitin
CC       ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the
CC       form of a thioester and then directly transfers the ubiquitin to
CC       targeted substrates. {ECO:0000256|RuleBase:RU201113}.
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         ECO:0000256|RuleBase:RU201113};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU201113}.
CC   -!- DOMAIN: The RING-type zinc finger domain is essential for ubiquitin
CC       ligase activity. {ECO:0000256|RuleBase:RU201113}.
CC   -!- DOMAIN: The SBD domain (substrate-binding domain) mediates the
CC       interaction with substrate proteins. It is related to the TRAF family.
CC       {ECO:0000256|RuleBase:RU201113}.
CC   -!- SIMILARITY: Belongs to the SINA (Seven in absentia) family.
CC       {ECO:0000256|ARBA:ARBA00009119, ECO:0000256|RuleBase:RU201113}.
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DR   EMBL; AQIB01076077; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_008006916.1; XM_008008725.1.
DR   AlphaFoldDB; A0A0D9RGT6; -.
DR   SMR; A0A0D9RGT6; -.
DR   STRING; 60711.ENSCSAP00000007825; -.
DR   Ensembl; ENSCSAT00000009715.1; ENSCSAP00000007825.1; ENSCSAG00000011630.1.
DR   GeneID; 103241474; -.
DR   KEGG; csab:103241474; -.
DR   CTD; 6478; -.
DR   eggNOG; KOG3002; Eukaryota.
DR   GeneTree; ENSGT00940000159812; -.
DR   OMA; AGHLVCK; -.
DR   OrthoDB; 222086at2759; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 103241474; 0 hits in 9 CRISPR screens.
DR   Proteomes; UP000029965; Chromosome 15.
DR   Bgee; ENSCSAG00000011630; Expressed in adrenal cortex and 7 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0042752; P:regulation of circadian rhythm; IEA:Ensembl.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   CDD; cd16752; RING-HC_SIAH2; 1.
DR   CDD; cd03829; Sina; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR   InterPro; IPR018121; 7-in-absentia-prot_TRAF-dom.
DR   InterPro; IPR004162; SINA-like_animal.
DR   InterPro; IPR008974; TRAF-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR013010; Znf_SIAH.
DR   PANTHER; PTHR45877; E3 UBIQUITIN-PROTEIN LIGASE SIAH2; 1.
DR   PANTHER; PTHR45877:SF4; E3 UBIQUITIN-PROTEIN LIGASE SIAH2; 1.
DR   Pfam; PF21362; Sina_RING; 1.
DR   Pfam; PF03145; Sina_TRAF; 1.
DR   Pfam; PF21361; Sina_ZnF; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49599; TRAF domain-like; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
DR   PROSITE; PS51081; ZF_SIAH; 1.
PE   3: Inferred from homology;
KW   Biological rhythms {ECO:0000256|ARBA:ARBA00023108};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU201113};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|RuleBase:RU201113};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU201113};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00455}.
FT   DOMAIN          80..115
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          133..193
FT                   /note="SIAH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51081"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..30
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   324 AA;  34615 MW;  2D5DD845666EC924 CRC64;
     MSRPSSTGPS ANKPCSKQPP PQPQHTPSPA APPAAATISA AGPGSSAVPA AAAVISGPGG
     GGGAGPVSPQ HHELTSLFEC PVCFDYVLPP ILQCQAGHLV CNQCRQKLSC CPTCRGALTP
     SIRNLAMEKV ASAVLFPCKY ATTGCSLTLH HTEKPEHEDI CEYRPYSCPC PGASCKWQGS
     LEAVMSHLMH AHKSITTLQG EDIVFLATDI NLPGAVDWVM MQSCFGHHFM LVLEKQEKYE
     GHQQFFAIVL LIGTRKQAEN FAYRLELNGN RRRLTWEATP RSIHDGVAAA IMNSDCLVFD
     TAIAHLFADN GNLGINVTIS TCCP
//
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