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   24-JAN-2024, entry version 104.
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; 9913-ENSBTAP00000053293; -.
DR   Ensembl; ENSBTAT00000070217.1; ENSBTAP00000058709.1; ENSBTAG00000043956.3.
DR   Ensembl; ENSBTAT00000070904.1; ENSBTAP00000074585.1; ENSBTAG00000043956.3.
DR   Ensembl; ENSBTAT00000077371.1; ENSBTAP00000068105.1; ENSBTAG00000043956.3.
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; 5478564at2759; -.
DR   Reactome; R-BTA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000043956; Expressed in Ammon's horn and 106 other cell types or 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   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24068:SF63; UBIQUITIN-CONJUGATING ENZYME E2 E3; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 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
//