UniProt: A0A7J7WC69

Database: UniProt
Entry: A0A7J7WC69_PIPKU

LinkDB:  A0A7J7WC69_PIPKU 
Original site:  A0A7J7WC69_PIPKU

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (9)   
   Pfam (3)   
   PROSITE (3)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (22)   

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ID   A0A7J7WC69_PIPKU        Unreviewed;       351 AA.
AC   A0A7J7WC69;
DT   07-APR-2021, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 1.
DT   18-JUN-2025, entry version 17.
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   ORFNames=mPipKuh1_000967 {ECO:0000313|EMBL:KAF6334808.1};
OS   Pipistrellus kuhlii (Kuhl's pipistrelle).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Vespertilionidae;
OC   Pipistrellus.
OX   NCBI_TaxID=59472 {ECO:0000313|EMBL:KAF6334808.1, ECO:0000313|Proteomes:UP000558488};
RN   [1] {ECO:0000313|EMBL:KAF6334808.1, ECO:0000313|Proteomes:UP000558488}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MPipKuh1 {ECO:0000313|EMBL:KAF6334808.1};
RC   TISSUE=Flight muscle {ECO:0000313|EMBL:KAF6334808.1};
RX   PubMed=32699395;
RA   Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA   Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA   Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA   Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA   Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA   Vernes S.C., Myers E.W., Teeling E.C.;
RT   "Six reference-quality genomes reveal evolution of bat adaptations.";
RL   Nature 583:578-584(2020).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAF6334808.1}.
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DR   EMBL; JACAGB010000011; KAF6334808.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A7J7WC69; -.
DR   Proteomes; UP000558488; Unassembled WGS sequence.
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   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:UP000558488};
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          1..202
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          158..198
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   351 AA;  41781 MW;  1992DBAFCD2906AB CRC64;
     MQFVRKENLL SLACQHQFCR SCWEQHCSVL VKDGVGVGVS CMAQDCPLRT PEDFVFPLLP
     NEELRDKYRR YLFRDHVESH YQLQLCPGAD CPMVIQVQEP RARRVQCSRC SEVFCFKCRQ
     MYHAPTDCAT IRKWLTKCAD DSETANYISA HTKDCPKCNI CIEKNGGCNH MQCSKCKHDF
     CWMCLGDWKT HGSEYYECSR YKENPDIVNQ SQQAQAREAL KKYLFYFERW ENHNKSLQLE
     AQTYQRIHEK IQERVMNNLG TWIDWQYLQN AAKLLAKCRY TLQYTYPYAY YMESGPRKKL
     FEYQQAQLEA EIENLSWKVE RADSYDRGDL ENQMHIAEQR RRTLLKDFHD T
//

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