UniProt: A0A8B7QJ00

Database: UniProt
Entry: A0A8B7QJ00_HIPAR

LinkDB:  A0A8B7QJ00_HIPAR 
Original site:  A0A8B7QJ00_HIPAR

All links

Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   NCBI-Gene (1)   
Protein sequence (2)   
   RefSeq(pep) (2)   
Protein domain (17)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (3)   
   SMART (2)   
All databases (24)   

Download RDF

ID   A0A8B7QJ00_HIPAR        Unreviewed;       421 AA.
AC   A0A8B7QJ00;
DT   19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2022, sequence version 1.
DT   18-JUN-2025, entry version 19.
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_019487653.1,
GN   ECO:0000313|RefSeq:XP_019487661.1};
OS   Hipposideros armiger (Great Himalayan leaf-nosed bat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Rhinolophoidea;
OC   Hipposideridae; Hipposideros.
OX   NCBI_TaxID=186990 {ECO:0000313|Proteomes:UP000694851, ECO:0000313|RefSeq:XP_019487653.1};
RN   [1] {ECO:0000313|RefSeq:XP_019487653.1, ECO:0000313|RefSeq:XP_019487661.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_019487653.1,
RC   ECO:0000313|RefSeq:XP_019487661.1};
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}.
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_019487653.1; XM_019632108.1.
DR   RefSeq; XP_019487661.1; XM_019632116.1.
DR   GeneID; 109376241; -.
DR   CTD; 10425; -.
DR   OrthoDB; 10009520at2759; -.
DR   Proteomes; UP000694851; 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; 2.
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:UP000694851};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..421
FT                   /note="E3 ubiquitin-protein ligase ARIH2"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5044443225"
FT   DOMAIN          63..272
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          67..118
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          228..268
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   421 AA;  49569 MW;  5B7EEBFADFB83851 CRC64;
     MLTAISCILP MALVSHSVAK LILVNFHWQV AEILDRYKSN SSQLLVEARV QPNLSKHVSS
     AHPPHHCAVC MQFVRKENLL SLACQHQFCR SCWEQHCAVL VKDGVGVGVS CMAQDCPLRT
     PEDFVFPLLP NEELRDKYRR YLFRDYVESH YQLQLCPGAD CPMVIQVQEP RARRVQCNRC
     NEVFCFKCRQ MYHAPTDCAT IRKWLTKCAD DSETANYISA HTKDCPKCNI CIEKNGGCNH
     MQCSKCKHDF CWMCLGDWKT HGSEYYECSR YKENPDIVNQ SQQAQAREAL KKYLFYFERW
     ENHNKSLQLE AQTYQRIHEK IQERVMNNLG TWIDWQYLQN AAKLLAKCRY TLQYTYPYAY
     YMESGPRKKL FEYQQAQLEA EIENLSWKVE RADSYDRGDL ENQMHIAEQR RRTLLKDFHD
     T
//

DBGET integrated database retrieval system