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 16-JUN-2009, entry version 45. DE RecName: Full=Ubiquitin-conjugating enzyme E2 D2; DE EC=6.3.2.19; DE AltName: Full=Ubiquitin-protein ligase D2; DE AltName: Full=Ubiquitin carrier protein D2; DE AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 2; DE AltName: Full=E2(17)KB 2; GN Name=Ube2d2; Synonyms=Ubc2e, Ubc4; 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 MEDLINE=95126893; 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). CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other CC proteins. Mediates the selective degradation of short-lived and CC abnormal proteins. Functions in the E6/E6-AP-induced CC ubiquitination of p53/TP53 (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP + CC diphosphate + protein N-ubiquityllysine. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC -!- SUBUNIT: Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin CC ligase complex and with E3 ubiquitin-protein ligase PJA2 (By CC similarity). CC -!- TISSUE SPECIFICITY: Highly expressed in testis. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. 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 IPI; IPI00204331; -. DR PIR; S53359; S53359. DR RefSeq; NP_001032369.1; -. DR UniGene; Rn.7390; -. DR HSSP; P15731; 1QCQ. DR SMR; P62839; 1-147. DR PRIDE; P62839; -. DR Ensembl; ENSRNOG00000013741; Rattus norvegicus. DR GeneID; 641452; -. DR KEGG; rno:641452; -. DR RGD; 1591897; Ube2d2. DR HOVERGEN; P62839; -. DR BRENDA; 6.3.2.19; 248. DR NextBio; 714693; -. DR ArrayExpress; P62839; -. DR GermOnline; ENSRNOG00000013741; Rattus norvegicus. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC. DR GO; GO:0043687; P:post-translational protein modification; IEA:InterPro. DR GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro. DR InterPro; IPR016135; UBQ-conjugat/RWD-like. DR InterPro; IPR000608; UBQ-conjugat_E2. DR Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1. DR Pfam; PF00179; UQ_con; 1. DR ProDom; PD000461; UBQ_conjugat; 1. DR SMART; SM00212; UBCc; 1. DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1. DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1. PE 2: Evidence at transcript level; KW ATP-binding; Ligase; Nucleotide-binding; Ubl conjugation pathway. FT CHAIN 1 147 Ubiquitin-conjugating enzyme E2 D2. FT /FTId=PRO_0000082464. FT ACT_SITE 85 85 Glycyl thioester intermediate (By FT similarity). SQ SEQUENCE 147 AA; 16735 MW; C942BE7853CBC355 CRC64; MALKRIHKEL NDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV PEIARIYKTD REKYNRIARE WTQKYAM //