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 09-DEC-2015, entry version 90. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY. RC TISSUE=Testis; RX PubMed=7826319; 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., RA Meyer H.E., 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- CC 48'-linked polyubiquitination. Mediates the selective degradation CC of short-lived and abnormal proteins. Functions in the E6/E6-AP- CC induced ubiquitination of p53/TP53. Mediates autoubiquitination of CC STUB1 and TRAF6. Involved in the signal-induced conjugation and CC subsequent degradation of NFKBIA, FBXW2-mediated GCM1 CC ubiquitination and degradation, MDM2-dependent degradation of CC p53/TP53 and the activation of MAVS in the mitochondria by CC DDX58/RIG-I in response to viral infection. Essential for viral CC activation of IRF3 (By similarity). Mediates ubiquitination of CC PEX5. {ECO:0000250|UniProtKB:P62837, ECO:0000269|PubMed:18359941}. CC -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating CC enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine CC = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 CC ubiquitin-conjugating enzyme]-L-cysteine. CC {ECO:0000250|UniProtKB:P62837, ECO:0000255|PROSITE- CC ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}. CC -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating CC enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin- CC activating enzyme]-L-cysteine + N(6)-monoubiquitinyl-[acceptor CC protein]-L-lysine. {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 CC with E3 ubiquitin-protein ligases CBLC, PJA1 and PJA2. Interacts CC with PDZRN3. {ECO:0000250|UniProtKB:P62837}. 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 UniGene; Rn.7390; -. DR ProteinModelPortal; P62839; -. DR SMR; P62839; 1-147. DR BioGrid; 566013; 1. DR STRING; 10116.ENSRNOP00000060962; -. DR PhosphoSite; P62839; -. DR PaxDb; P62839; -. DR PRIDE; P62839; -. DR GeneID; 641452; -. DR KEGG; rno:641452; -. DR UCSC; RGD:1591897; rat. DR CTD; 7322; -. DR RGD; 1591897; Ube2d2. DR eggNOG; KOG0417; Eukaryota. DR eggNOG; COG5078; LUCA. DR HOGENOM; HOG000233455; -. DR HOVERGEN; HBG063308; -. DR InParanoid; P62839; -. DR KO; K06689; -. DR UniPathway; UPA00143; -. DR NextBio; 714693; -. DR PRO; PR:P62839; -. DR Proteomes; UP000002494; Unplaced. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB. DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB. 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; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transferase; Ubl conjugation pathway. FT CHAIN 1 147 Ubiquitin-conjugating enzyme E2 D2. FT /FTId=PRO_0000082464. FT ACT_SITE 85 85 Glycyl thioester intermediate. FT {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 //