ID A0A0G2JGL0_MOUSE Unreviewed; 148 AA. AC A0A0G2JGL0; DT 22-JUL-2015, integrated into UniProtKB/TrEMBL. DT 22-JUL-2015, sequence version 1. DT 27-NOV-2024, entry version 49. DE RecName: Full=Ubiquitin-conjugating enzyme E2 D3 {ECO:0000256|ARBA:ARBA00040338}; DE EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486}; DE EC=2.3.2.24 {ECO:0000256|ARBA:ARBA00039076}; DE AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme D3 {ECO:0000256|ARBA:ARBA00041314}; DE AltName: Full=E2 ubiquitin-conjugating enzyme D3 {ECO:0000256|ARBA:ARBA00041427}; DE AltName: Full=Ubiquitin carrier protein D3 {ECO:0000256|ARBA:ARBA00041862}; DE AltName: Full=Ubiquitin-protein ligase D3 {ECO:0000256|ARBA:ARBA00043109}; GN Name=Ube2d3 {ECO:0000313|Ensembl:ENSMUSP00000143606.2, GN ECO:0000313|MGI:MGI:1913355}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000143606.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000143606.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000143606.2, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RG Mouse Genome Sequencing Consortium; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0000313|Ensembl:ENSMUSP00000143606.2} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000143606.2}; RX PubMed=21750661; RA Church D.M., Schneider V.A., Graves T., Auger K., Cunningham F., Bouk N., RA Chen H.C., Agarwala R., McLaren W.M., Ritchie G.R., Albracht D., RA Kremitzki M., Rock S., Kotkiewicz H., Kremitzki C., Wollam A., Trani L., RA Fulton L., Fulton R., Matthews L., Whitehead S., Chow W., Torrance J., RA Dunn M., Harden G., Threadgold G., Wood J., Collins J., Heath P., RA Griffiths G., Pelan S., Grafham D., Eichler E.E., Weinstock G., RA Mardis E.R., Wilson R.K., Howe K., Flicek P., Hubbard T.; RT "Modernizing reference genome assemblies."; RL PLoS Biol. 9:e1001091-e1001091(2011). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000143606.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000143606.2}; RG Ensembl; RL Submitted (AUG-2024) to UniProtKB. 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:0000256|ARBA:ARBA00000485}; 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:0000256|ARBA:ARBA00035845}; CC -!- PATHWAY: Protein modification. {ECO:0000256|ARBA:ARBA00043952}. CC -!- SUBUNIT: Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin CC ligase complex; when Cullin is neddylated, the interaction between the CC E2 and the SCF complex is strengthened. Interacts with DAPK3. Interacts CC with BRCA1; the DNA damage checkpoint promotes the association with CC BRCA1 after ionizing radiation. Interacts non-covalently with CC ubiquitin. Interacts with E3 ubiquitin-protein ligase CBLC. Interacts CC with UBTD1. Interacts with RIGI and RNF135; involved in RIGI CC ubiquitination and activation. {ECO:0000256|ARBA:ARBA00046671}. CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family. CC {ECO:0000256|RuleBase:RU362109}. 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 AlphaFoldDB; A0A0G2JGL0; -. DR SMR; A0A0G2JGL0; -. DR Ensembl; ENSMUST00000197134.3; ENSMUSP00000143606.2; ENSMUSG00000078578.10. DR AGR; MGI:1913355; -. DR MGI; MGI:1913355; Ube2d3. DR VEuPathDB; HostDB:ENSMUSG00000078578; -. DR GeneTree; ENSGT00940000153169; -. DR OMA; RNCKEIL; -. DR OrthoDB; 5478564at2759; -. DR ChiTaRS; Ube2d3; mouse. DR Proteomes; UP000000589; Chromosome 3. DR Bgee; ENSMUSG00000078578; Expressed in undifferentiated genital tubercle and 260 other cell types or tissues. DR ExpressionAtlas; A0A0G2JGL0; baseline and differential. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR CDD; cd00195; UBCc; 1. DR FunFam; 3.10.110.10:FF:000101; Ubiquitin-conjugating enzyme E2 D2; 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:SF415; UBIQUITIN-CONJUGATING ENZYME E2 D3; 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 {ECO:0000256|RuleBase:RU362109}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU362109}; KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A0G2JGL0, KW ECO:0007829|ProteomicsDB:A0A0G2JGL0}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786, KW ECO:0000256|RuleBase:RU362109}. FT DOMAIN 1..147 FT /note="UBC core" FT /evidence="ECO:0000259|PROSITE:PS50127" FT ACT_SITE 85 FT /note="Glycyl thioester intermediate" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10133" SQ SEQUENCE 148 AA; 16785 MW; E73DC194DB6D4EFE CRC64; MALKRINKEL SDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV PEIARIYKTD RDKYNRLARE WTEKYAML //