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Database: UniProt
Entry: Q59FM8_HUMAN
LinkDB: Q59FM8_HUMAN
Original site: Q59FM8_HUMAN 
ID   Q59FM8_HUMAN            Unreviewed;       526 AA.
AC   Q59FM8;
DT   26-APR-2005, integrated into UniProtKB/TrEMBL.
DT   26-APR-2005, sequence version 1.
DT   24-JAN-2024, entry version 83.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE   Flags: Fragment;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD92669.1};
RN   [1] {ECO:0000313|EMBL:BAD92669.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Brain {ECO:0000313|EMBL:BAD92669.1};
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA   Ohara O., Nagase T., Kikuno R.F.;
RT   "Homo sapiens protein coding cDNA.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the RBR family. Ariadne subfamily.
CC       {ECO:0000256|ARBA:ARBA00005884}.
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DR   EMBL; AB209432; BAD92669.1; -; mRNA.
DR   AlphaFoldDB; Q59FM8; -.
DR   PeptideAtlas; Q59FM8; -.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd20343; BRcat_RBR_HHARI-like; 1.
DR   CDD; cd20356; Rcat_RBR_HHARI-like; 1.
DR   CDD; cd16626; RING-HC_RBR_HHARI; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045840; Ariadne.
DR   InterPro; IPR048962; ARIH1-like_UBL.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR11685:SF212; E3 UBIQUITIN-PROTEIN LIGASE ARIH1; 1.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF21235; ARI1_UBAl; 1.
DR   Pfam; PF19422; Ariadne; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF00097; zf-C3HC4; 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; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
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          151..362
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          155..203
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAD92669.1"
SQ   SEQUENCE   526 AA;  61363 MW;  BFBF96F8823849A6 CRC64;
     LRRAASGPLA PSLPPPRPPR RHQPSNANRR SWGGAAARGA GARPASGHQP EPEREPGPRR
     PRPLPASASV RRAPARRAMD SDEGYNYEFN EVIQNPATIT RILLSHFNWD KEKLMERYFD
     GNLEKLFAEC HVINPSKKSR TRQMNTRSSA QDMPCQICYL NYPNSYFTGL ECGHKFCMQC
     WSEYLTTKIM EEGMGQTISC PAHGCDILVD DNTVMRLITD SKVKLKYQHL ITNSFVECNR
     LLKWCPAPDC HHVVKVQYPD AKPVRCKCGR QFCFNCGENW HDPVKCKWLK KWIKKCDDDS
     ETSNWIAANT KECPKCHVTI EKDGGCNHMV CRNQNCKAEF CWVCLGPWEP HGSAWYNCNR
     YNEDDAKAAR DAQERSRAAL QRYLFYCNRY MNHMQSLRFE HKLYAQVKQK MEEMQQHNMS
     WIEVQFLKKA VDVLCQCRAT LMYTYVFAFY LKKNNQSIIF ENNQADLENA TEVLSGYLER
     DISQDSLQDI KQKVQDKYRY CESRRRVLLQ HVHEGYEKDL WEYIED
//
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