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 27-MAR-2024, entry version 126. 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 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 (By similarity). Mediates ubiquitination of PEX5. CC {ECO:0000250|UniProtKB:P62837, 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 Ensembl; ENSRNOT00000095794.1; ENSRNOP00000088484.1; ENSRNOG00000069286.1. DR Ensembl; ENSRNOT00065019874; ENSRNOP00065015229; ENSRNOG00065012223. DR KEGG; rno:641452; -. DR UCSC; RGD:1591897; rat. DR AGR; RGD:1591897; -. DR CTD; 7322; -. DR RGD; 1591897; Ube2d2. DR GeneTree; ENSGT00940000153169; -. DR InParanoid; P62839; -. DR OMA; VHFTTRI; -. DR OrthoDB; 5478564at2759; -. DR Reactome; R-RNO-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha. DR Reactome; R-RNO-5357905; Regulation of TNFR1 signaling. 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:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0051865; P:protein autoubiquitination; ISO:RGD. 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 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:SF330; UBIQUITIN-CONJUGATING ENZYME E2 D2; 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 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 //