UB2D2_BOVIN
ID UB2D2_BOVIN Reviewed; 147 AA.
AC Q1RMX2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 114.
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 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=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-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
CC autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced
CC conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1
CC ubiquitination and degradation, MDM2-dependent degradation of p53/TP53
CC and the activation of MAVS in the mitochondria by DDX58/RIG-I in
CC response to viral infection. Essential for viral activation of IRF3.
CC {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; BC114654; AAI14655.1; -; mRNA.
DR RefSeq; NP_001039961.1; NM_001046496.1.
DR AlphaFoldDB; Q1RMX2; -.
DR SMR; Q1RMX2; -.
DR IntAct; Q1RMX2; 3.
DR STRING; 9913.ENSBTAP00000049292; -.
DR PaxDb; Q1RMX2; -.
DR PRIDE; Q1RMX2; -.
DR Ensembl; ENSBTAT00000055723; ENSBTAP00000049292; ENSBTAG00000004161.
DR GeneID; 541003; -.
DR KEGG; bta:541003; -.
DR CTD; 7322; -.
DR VEuPathDB; HostDB:ENSBTAG00000004161; -.
DR VGNC; VGNC:36580; UBE2D2.
DR eggNOG; KOG0417; Eukaryota.
DR GeneTree; ENSGT00940000153169; -.
DR HOGENOM; CLU_030988_13_3_1; -.
DR InParanoid; Q1RMX2; -.
DR OMA; VHFTTRI; -.
DR OrthoDB; 1337945at2759; -.
DR TreeFam; TF101108; -.
DR Reactome; R-BTA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-BTA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-BTA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-BTA-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000004161; Expressed in retropharyngeal lymph node and 103 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
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:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; IEA:Ensembl.
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:0000209; P:protein polyubiquitination; IBA:GO_Central.
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 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_0000245034"
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; 16735 MW; C942BE7853CBC355 CRC64;
MALKRIHKEL NDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY
PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV
PEIARIYKTD REKYNRIARE WTQKYAM
