UB2E3_BOVIN
ID UB2E3_BOVIN Reviewed; 207 AA.
AC Q2T9X7;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 E3;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme E3;
DE AltName: Full=Ubiquitin carrier protein E3;
DE AltName: Full=Ubiquitin-protein ligase E3;
GN Name=UBE2E3;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and
CC 'Lys-48'-, as well as 'Lys-63'-linked polyubiquitination. Participates
CC in the regulation of transepithelial sodium transport in renal cells.
CC May be involved in cell growth arrest. {ECO:0000250|UniProtKB:Q969T4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC ProRule:PRU10133};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: The ubiquitin-loaded form interacts specifically with
CC importin-11 (IPO11), leading to its import into the nucleus. Interacts
CC with NEDD4L. {ECO:0000250|UniProtKB:P52483}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q969T4}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q969T4}. Note=Shuttles between the nucleus and
CC cytoplasm in a IPO11-dependent manner. {ECO:0000250|UniProtKB:Q969T4}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; BC111218; AAI11219.1; -; mRNA.
DR RefSeq; NP_001073251.1; NM_001079783.1.
DR AlphaFoldDB; Q2T9X7; -.
DR SMR; Q2T9X7; -.
DR STRING; 9913.ENSBTAP00000053293; -.
DR PaxDb; Q2T9X7; -.
DR Ensembl; ENSBTAT00000070217; ENSBTAP00000058709; ENSBTAG00000043956.
DR Ensembl; ENSBTAT00000070904; ENSBTAP00000074585; ENSBTAG00000043956.
DR Ensembl; ENSBTAT00000077371; ENSBTAP00000068105; ENSBTAG00000043956.
DR GeneID; 534349; -.
DR KEGG; bta:534349; -.
DR CTD; 10477; -.
DR VEuPathDB; HostDB:ENSBTAG00000043956; -.
DR VGNC; VGNC:56154; UBE2E3.
DR eggNOG; KOG0417; Eukaryota.
DR GeneTree; ENSGT00940000155392; -.
DR InParanoid; Q2T9X7; -.
DR OMA; GDRAKHD; -.
DR OrthoDB; 1337945at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000043956; Expressed in Ammon's horn and 106 other tissues.
DR ExpressionAtlas; Q2T9X7; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cytoplasm; Growth regulation; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q969T4"
FT CHAIN 2..207
FT /note="Ubiquitin-conjugating enzyme E2 E3"
FT /id="PRO_0000245036"
FT DOMAIN 61..207
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 145
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q969T4"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q969T4"
SQ SEQUENCE 207 AA; 22913 MW; 821CB1382478DC9F CRC64;
MSSDRQRSDD ESPSTSSGSS DADQRDPAAP EPEEQEERKP SATQQKKNTK LSSKTTAKLS
TSAKRIQKEL AEITLDPPPN CSAGPKGDNI YEWRSTILGP PGSVYEGGVF FLDITFSSDY
PFKPPKVTFR TRIYHCNINS QGVICLDILK DNWSPALTIS KVLLSICSLL TDCNPADPLV
GSIATQYLTN RAEHDRIARQ WTKRYAT
