ID A0A2K6BA20_MACNE Unreviewed; 877 AA.
AC A0A2K6BA20;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Ubiquitin-protein ligase E3A {ECO:0000256|PIRNR:PIRNR037201};
DE EC=2.3.2.26 {ECO:0000256|PIRNR:PIRNR037201};
GN Name=UBE3A {ECO:0000313|Ensembl:ENSMNEP00000008252.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000008252.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000008252.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and
CC transfers it to its substrates. {ECO:0000256|PIRNR:PIRNR037201}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000256|PIRNR:PIRNR037201};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|PIRNR:PIRNR037201}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR037201}.
CC Nucleus {ECO:0000256|PIRNR:PIRNR037201}.
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DR AlphaFoldDB; A0A2K6BA20; -.
DR STRING; 9545.ENSMNEP00000008252; -.
DR Ensembl; ENSMNET00000032417.1; ENSMNEP00000008252.1; ENSMNEG00000028458.1.
DR GeneTree; ENSGT00940000155050; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000028458; Expressed in skeletal muscle tissue and 12 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-UniRule.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR GO; GO:0050847; P:progesterone receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IEA:UniProtKB-UniRule.
DR GO; GO:0042752; P:regulation of circadian rhythm; IEA:Ensembl.
DR GO; GO:2000058; P:regulation of ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0032570; P:response to progesterone; IEA:Ensembl.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR Gene3D; 6.10.130.10; Ubiquitin-protein ligase E3A, N-terminal zinc-binding domain (AZUL); 1.
DR InterPro; IPR032353; AZUL.
DR InterPro; IPR042556; AZUL_sf.
DR InterPro; IPR044611; E3A/B/C-like.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR017134; UBE3A.
DR PANTHER; PTHR45700; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR PANTHER; PTHR45700:SF2; UBIQUITIN-PROTEIN LIGASE E3C; 1.
DR Pfam; PF16558; AZUL; 1.
DR Pfam; PF00632; HECT; 1.
DR PIRSF; PIRSF037201; Ubiquitin-protein_ligase_E6-AP; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR037201};
KW Nucleus {ECO:0000256|PIRNR:PIRNR037201};
KW Proteasome {ECO:0000256|PIRNR:PIRNR037201};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW Transferase {ECO:0000256|PIRNR:PIRNR037201};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PIRNR:PIRNR037201}.
FT DOMAIN 549..877
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 177..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 845
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 877 AA; 100774 MW; 6DBC4ECAE7598869 CRC64;
MQKRKPPIKP SDLVRLTTTR TACGKLKRAA AKHLIERYYH QLTEGCGNEA CTNEFCASCP
TFLRMDNNAA AIKALELYKI NAKLCDPHPS KKGASSAYLE NSKGAPNNSC SEIKMNKKGT
RIDFKDVTYL TEEKVYEILE LCREREDYSP LIRVIGRVFS SAEALVQSFR KVKQHTKEEL
KSLQAKDEDK DEDEKEKAAC SAAAMEEDSE ASSSRIGDSS QGDNNLQKVG PDDVSVDIDA
IRRVYTRLLS NEKIETAFLN ALVYLSPNVE CDLTYHNVYS RDPNYLNLFI IVMENRNLHS
PEYLEMALPL FCKAMSKLPL AAQGKLIRLW SKYNADQIRR MMETFQQLIT YKVISNEFNS
RNLVNDDDAI VAASKCLKMV YYANVVGGEV DTNHNEEDDE EPIPESSELT LQELLGEERR
NKKGPRVDPL ETELGVKTLD CRKPLIPFEE FINEPLNEVL EMDKDYTFFK VETENKFSFM
TCPFILNAVT KNLGLYYDNR IRMYSERRIT VLYSLVQGQQ LNPYLRLKVR RDHIIDDALV
RLEMIAMENP ADLKKQLYVE FEGEQGVDEG GVSKEFFQLV VEEIFNPDIG MFTYDESTKL
FWFNPSSFET EGQFTLIGIV LGLAIYNNCI LDVHFPMVVY RKLMGKKGTF RDLGDSHPVL
YQSLKDLLEY EGNVEDDMMI TFQISQTDLF GNPMMYDLKE NGDKIPITNE NRKEFVNLYS
DYILNKSVEK QFKAFRRGFH MVTNESPLKY LFRPEEIELL ICGSRNLDFQ ALEETTEYDG
GYTRDSVLIR EFWEIVHSFT DEQKRLFLQF TTGTDRAPVG GLGKLKMIIA KNGPDTERLP
TSHTCFNVLL LPEYSSKEKL KERLLKAITY AKGFGML
//
