UB2D2_RAT
ID UB2D2_RAT Reviewed; 147 AA.
AC P62839; P51669;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
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-conjugating enzyme E2(17)KB 2;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 2;
DE AltName: Full=Ubiquitin-protein ligase D2;
GN Name=Ube2d2; Synonyms=Ubc4, Ubch4, Ubch5b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=7826319; DOI=10.1042/bj3050125;
RA Wing S.S., Jain P.;
RT "Molecular cloning, expression and characterization of a ubiquitin
RT conjugation enzyme (E2(17)kB) highly expressed in rat testis.";
RL Biochem. J. 305:125-132(1995).
RN [2]
RP FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18359941; DOI=10.1074/jbc.m800402200;
RA Grou C.P., Carvalho A.F., Pinto M.P., Wiese S., Piechura H., Meyer H.E.,
RA Warscheid B., Sa-Miranda C., Azevedo J.E.;
RT "Members of the E2D (UbcH5) family mediate the ubiquitination of the
RT conserved cysteine of Pex5p, the peroxisomal import receptor.";
RL J. Biol. Chem. 283:14190-14197(2008).
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 autoubiquitination of STUB1 and
CC TRAF6. Involved in the signal-induced conjugation and subsequent
CC degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and
CC degradation, MDM2-dependent degradation of p53/TP53 and the activation
CC of MAVS in the mitochondria by DDX58/RIG-I in response to viral
CC infection. Essential for viral activation of IRF3 (By similarity).
CC Mediates ubiquitination of PEX5. {ECO:0000250|UniProtKB:P62837,
CC ECO:0000269|PubMed:18359941}.
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 -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC {ECO:0000269|PubMed:7826319}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; U13176; AAA85101.1; -; mRNA.
DR PIR; S53359; S53359.
DR RefSeq; NP_001032369.1; NM_001037292.1.
DR AlphaFoldDB; P62839; -.
DR SMR; P62839; -.
DR BioGRID; 566013; 1.
DR iPTMnet; P62839; -.
DR PhosphoSitePlus; P62839; -.
DR SwissPalm; P62839; -.
DR jPOST; P62839; -.
DR PRIDE; P62839; -.
DR Ensembl; ENSRNOT00000095794; ENSRNOP00000088484; ENSRNOG00000069286.
DR GeneID; 641452; -.
DR KEGG; rno:641452; -.
DR UCSC; RGD:1591897; rat.
DR CTD; 7322; -.
DR RGD; 1591897; Ube2d2.
DR GeneTree; ENSGT00940000153169; -.
DR InParanoid; P62839; -.
DR OrthoDB; 1337945at2759; -.
DR Reactome; R-RNO-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-RNO-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-RNO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-RNO-8951664; Neddylation.
DR Reactome; R-RNO-9033241; Peroxisomal protein import.
DR Reactome; R-RNO-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:P62839; -.
DR Proteomes; UP000002494; Chromosome 18.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:RGD.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0016567; P:protein ubiquitination; ISO:RGD.
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 1: Evidence at protein 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_0000082464"
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
