ID   Q8NI42_HUMAN            Unreviewed;       203 AA.
AC   Q8NI42;
DT   01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
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:AAM21459.1};
RN   [1] {ECO:0000313|EMBL:AAM21459.1}
RP   NUCLEOTIDE SEQUENCE.
RA   D'Agata V., Scapagnini G., Cavallaro S.;
RT   "Functional and molecular diversity of parkin.";
RL   Submitted (MAY-2001) 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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
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DR   EMBL; AF381284; AAM21459.1; -; mRNA.
DR   AlphaFoldDB; Q8NI42; -.
DR   SMR; Q8NI42; -.
DR   PeptideAtlas; Q8NI42; -.
DR   UniPathway; UPA00143; -.
DR   GO; GO:0005829; C:cytosol; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IEA:InterPro.
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:UniProtKB-UniPathway.
DR   CDD; cd20340; BRcat_RBR_parkin; 1.
DR   CDD; cd16627; RING-HC_RBR_parkin; 1.
DR   Gene3D; 2.20.25.20; -; 1.
DR   InterPro; IPR047534; BRcat_RBR_parkin.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR003977; Parkin.
DR   InterPro; IPR041565; Parkin_Znf-RING.
DR   InterPro; IPR047535; RING-HC_RBR_parkin.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR041170; Znf-RING_14.
DR   PANTHER; PTHR11685:SF471; E3 UBIQUITIN-PROTEIN LIGASE PARKIN; 1.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF17976; zf-RING_12; 1.
DR   Pfam; PF17978; zf-RING_14; 1.
DR   PRINTS; PR01475; PARKIN.
DR   SMART; SM00647; IBR; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51873; TRIAD; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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}.
FT   DOMAIN          43..203
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
SQ   SEQUENCE   203 AA;  22192 MW;  F92E796F069DC818 CRC64;
     MSGECQSPHC PGTSAEFFFK CGAHPTSDKE TPVALHLIAT NSRNITCITC TDVRSPVLVF
     QCNSRHVICL DCFHLYCVTR LNDRQFVHDP QLGYSLPCVA GCPNSLIKEL HHFRILGEEQ
     YNRYQQYGAE ECVLQMGGVL CPRPGCGAGL LPEPDQRKVT CEGGNGLGCG FAFCRECKEA
     YHEGECSAVF EASGTTTQEA ACT
//