ID   UB2D2_PIG               Reviewed;         147 AA.
AC   Q06AA9;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 88.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 D2;
DE            EC=2.3.2.23;
DE   AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme D2;
DE            EC=2.3.2.24;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme D2;
DE   AltName: Full=Ubiquitin carrier protein D2;
DE   AltName: Full=Ubiquitin-protein ligase D2;
GN   Name=UBE2D2; Synonyms=UBC4, UBCH4, UBCH5B;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Liu G.Y.;
RL   Submitted (AUG-2006) 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-48'-
CC       linked polyubiquitination. Mediates the selective degradation of short-
CC       lived and abnormal proteins. Functions in the E6/E6-AP-induced
CC       ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and SQSTM1
CC       and autoubiquitination of STUB1 and TRAF6. Involved in the signal-
CC       induced conjugation and subsequent degradation of NFKBIA, FBXW2-
CC       mediated GCM1 ubiquitination and degradation, MDM2-dependent
CC       degradation of p53/TP53 and the activation of MAVS in the mitochondria
CC       by RIGI in response to viral infection. Essential for viral activation
CC       of IRF3. {ECO:0000250|UniProtKB:P62837}.
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:0000250|UniProtKB:P62837, ECO:0000255|PROSITE-
CC         ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-
CC         cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.24; Evidence={ECO:0000250|UniProtKB:P62837};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBUNIT: Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin
CC       ligase complex. Interacts with CNOT4 (via RING domain). Interacts with
CC       E3 ubiquitin-protein ligases CBLC, PJA1 and PJA2. Interacts with
CC       PDZRN3. Interacts with PPP1R11. {ECO:0000250|UniProtKB:P62837,
CC       ECO:0000250|UniProtKB:P62838}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; DQ972955; ABI96191.1; -; mRNA.
DR   RefSeq; NP_001072141.1; NM_001078673.1.
DR   AlphaFoldDB; Q06AA9; -.
DR   SMR; Q06AA9; -.
DR   STRING; 9823.ENSSSCP00000057683; -.
DR   PaxDb; 9823-ENSSSCP00000009774; -.
DR   PeptideAtlas; Q06AA9; -.
DR   GeneID; 780418; -.
DR   KEGG; ssc:780418; -.
DR   CTD; 7323; -.
DR   eggNOG; KOG0417; Eukaryota.
DR   InParanoid; Q06AA9; -.
DR   OrthoDB; 5478564at2759; -.
DR   UniPathway; UPA00143; -.
DR   ChiTaRS; UBE2D2; pig.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000151; C:ubiquitin ligase complex; 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:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; IBA:GO_Central.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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:SF415; UBIQUITIN-CONJUGATING ENZYME E2 D3; 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   ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..147
FT                   /note="Ubiquitin-conjugating enzyme E2 D2"
FT                   /id="PRO_0000270203"
FT   DOMAIN          1..147
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        85
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   147 AA;  16737 MW;  A224647853CBC354 CRC64;
     MALKRIHKEL NDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY
     PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV
     PEIARIYKTD RDKYNRISRE WTQKYAM
//