ID A0A9F2R7P5_PYTBI Unreviewed; 489 AA.
AC A0A9F2R7P5;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 18-JUN-2025, entry version 12.
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|RefSeq:XP_007439124.1,
GN ECO:0000313|RefSeq:XP_007439125.1, ECO:0000313|RefSeq:XP_007439126.1};
OS Python bivittatus (Burmese python) (Python molurus bivittatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Henophidia; Pythonidae; Python.
OX NCBI_TaxID=176946 {ECO:0000313|Proteomes:UP000695026, ECO:0000313|RefSeq:XP_007439124.1};
RN [1] {ECO:0000313|RefSeq:XP_007439124.1, ECO:0000313|RefSeq:XP_007439125.1}
RP IDENTIFICATION.
RC TISSUE=Liver {ECO:0000313|RefSeq:XP_007439124.1,
RC ECO:0000313|RefSeq:XP_007439125.1};
RG RefSeq;
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}.
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DR RefSeq; XP_007439124.1; XM_007439062.2.
DR RefSeq; XP_007439125.1; XM_007439063.3.
DR RefSeq; XP_007439126.1; XM_007439064.2.
DR GeneID; 103063372; -.
DR KEGG; pbi:103063372; -.
DR CTD; 10425; -.
DR OMA; PYAYYMD; -.
DR OrthoDB; 10009520at2759; -.
DR Proteomes; UP000695026; Unplaced.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
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:UP000695026};
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; 57198 MW; FE55E1B992EA608D CRC64;
MSVDMNSQGS DSNEEDYDPN CDEEEDEDPG DIEGYYEGVA NDVEQQGADS FDPEEYQFTC
LTYRESESTL NEHMVRLASA LKVSHAVAKL VLVSFHWQIS EILERHTANS VQLLVEARVQ
PASFKHAVVH SSQHCAVCMQ LVRKENLLSL ACQHQFCRSC WEQHCTVLVK DGVGVGVSCM
AQDCLLRTPE DFVFPLLPSE ELKDKYRRYL FRDYVESHFQ 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
//
