GenomeNet

Database: UniProt
Entry: A0A670YUX9_PSETE
LinkDB: A0A670YUX9_PSETE
Original site: A0A670YUX9_PSETE 
ID   A0A670YUX9_PSETE        Unreviewed;       489 AA.
AC   A0A670YUX9;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   18-JUN-2025, entry version 22.
DE   RecName: Full=E3 ubiquitin-protein ligase ARIH2 {ECO:0000256|ARBA:ARBA00070157};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE   AltName: Full=Triad1 protein {ECO:0000256|ARBA:ARBA00080593};
GN   Name=ARIH2 {ECO:0000313|Ensembl:ENSPTXP00000014759.1};
OS   Pseudonaja textilis (Eastern brown snake).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Hydrophiinae; Pseudonaja.
OX   NCBI_TaxID=8673 {ECO:0000313|Ensembl:ENSPTXP00000014759.1, ECO:0000313|Proteomes:UP000472273};
RN   [1] {ECO:0000313|Ensembl:ENSPTXP00000014759.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2025) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC       {ECO:0000256|ARBA:ARBA00005884}.
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   RefSeq; XP_026573694.1; XM_026717909.1.
DR   RefSeq; XP_026573695.1; XM_026717910.1.
DR   RefSeq; XP_026573696.1; XM_026717911.1.
DR   AlphaFoldDB; A0A670YUX9; -.
DR   Ensembl; ENSPTXT00000015223.1; ENSPTXP00000014759.1; ENSPTXG00000010213.1.
DR   GeneID; 113447621; -.
DR   GeneTree; ENSGT00940000154875; -.
DR   OMA; PYAYYMD; -.
DR   OrthoDB; 10009520at2759; -.
DR   Proteomes; UP000472273; Unplaced.
DR   GO; GO:0031466; C:Cul5-RING ubiquitin ligase complex; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IEA:Ensembl.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0071425; P:hematopoietic stem cell proliferation; IEA:Ensembl.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:Ensembl.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; IEA:Ensembl.
DR   CDD; cd20344; BRcat_RBR_TRIAD1; 1.
DR   CDD; cd20360; Rcat_RBR_TRIAD1; 1.
DR   CDD; cd16773; RING-HC_RBR_TRIAD1; 1.
DR   FunFam; 1.20.120.1750:FF:000004; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 2.20.25.20:FF:000005; RBR-type E3 ubiquitin transferase; 1.
DR   FunFam; 3.30.40.10:FF:000098; RBR-type E3 ubiquitin transferase; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 2.20.25.20; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045840; Ariadne.
DR   InterPro; IPR047555; BRcat_RBR_TRIAD1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR047556; Rcat_RBR_TRIAD1.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00184; RING; 2.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000472273};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
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          131..340
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          296..336
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..11
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..31
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   489 AA;  57232 MW;  2124F6C7866ABA9D CRC64;
     MSVDMNSQGS DSNEEDYDPN CDEEEDEDPG DIEGYYEGVA NDVEQQGADS FDPEEYQFTC
     LTYKESESTL NEHMVRLASA LKVSHAVAKL VLVSFHWQIS EILERHTSNS VQLLVEARVQ
     PASFKHAMVH SSQHCAVCMQ LVRKENLLSL ACQHQFCRSC WEQHCTVLVK DGVGVGVSCM
     AQDCLLRTPE DFVFPLLPSE ELKDKYRRYL FRDYIESHFQ LQLCPGADCP MVIQVQEPKA
     RRVQCNRCNE VFCFKCRQMY HAPTDCATIR KWLTKCADDS ETANYISAHT KDCPKCNICI
     EKNGGCNHMQ CSKCKHDFCW MCLGDWKTHG SEYYECSRYK ENPDIVNQSQ QAQAREALKK
     YLFYFERWEN HNKSLQLEAQ TYQRIQEKIQ ERVMNNLGTW IDWQYLQNAA KLLAKCRYTL
     QYTYPYAYYM ESGPRKKLFE YQQAQLEAEI ENLSWKVERA DSYDRGDLEN QMHIAEQRRR
     TLLKDFHDT
//
DBGET integrated database retrieval system