UB2D2_MOUSE
ID UB2D2_MOUSE Reviewed; 147 AA.
AC P62838; P51669;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 154.
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, Ube2d2a;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Richardson P., Zon L.I.;
RT "Cloning of a murine ubiquitin conjugating enzyme.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH PJA1.
RC STRAIN=129/SvJ;
RX PubMed=12036302; DOI=10.1006/geno.2002.6770;
RA Yu P., Chen Y., Tagle D.A., Cai T.;
RT "PJA1, encoding a RING-H2 finger ubiquitin ligase, is a novel human X
RT chromosome gene abundantly expressed in brain.";
RL Genomics 79:869-874(2002).
RN [4]
RP INTERACTION WITH PDZRN3.
RX PubMed=17576800; DOI=10.1083/jcb.200610060;
RA Lu Z., Je H.S., Young P., Gross J., Lu B., Feng G.;
RT "Regulation of synaptic growth and maturation by a synapse-associated E3
RT ubiquitin ligase at the neuromuscular junction.";
RL J. Cell Biol. 177:1077-1089(2007).
RN [5]
RP INTERACTION WITH PPP1R11.
RX PubMed=27805901; DOI=10.7554/elife.18496;
RA McKelvey A.C., Lear T.B., Dunn S.R., Evankovich J., Londino J.D.,
RA Bednash J.S., Zhang Y., McVerry B.J., Liu Y., Chen B.B.;
RT "RING finger E3 ligase PPP1R11 regulates TLR2 signaling and innate
RT immunity.";
RL Elife 5:0-0(2016).
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
CC autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced
CC conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1
CC ubiquitination and degradation, MDM2-dependent degradation of p53/TP53
CC and the activation of MAVS in the mitochondria by DDX58/RIG-I in
CC response to viral infection. Essential for viral activation of IRF3.
CC {ECO:0000250|UniProtKB:P62837}.
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 (PubMed:27805901).
CC {ECO:0000250|UniProtKB:P62837, ECO:0000269|PubMed:12036302,
CC ECO:0000269|PubMed:17576800, ECO:0000269|PubMed:27805901}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; U62483; AAB05772.1; -; mRNA.
DR EMBL; BC003923; AAH03923.1; -; mRNA.
DR CCDS; CCDS50254.1; -.
DR RefSeq; NP_064296.1; NM_019912.2.
DR AlphaFoldDB; P62838; -.
DR BMRB; P62838; -.
DR SMR; P62838; -.
DR BioGRID; 208052; 14.
DR IntAct; P62838; 1.
DR MINT; P62838; -.
DR STRING; 10090.ENSMUSP00000132446; -.
DR iPTMnet; P62838; -.
DR PhosphoSitePlus; P62838; -.
DR SwissPalm; P62838; -.
DR EPD; P62838; -.
DR jPOST; P62838; -.
DR PaxDb; P62838; -.
DR PeptideAtlas; P62838; -.
DR PRIDE; P62838; -.
DR ProteomicsDB; 297770; -.
DR Antibodypedia; 7407; 391 antibodies from 31 providers.
DR DNASU; 56550; -.
DR Ensembl; ENSMUST00000167406; ENSMUSP00000131206; ENSMUSG00000091896.
DR Ensembl; ENSMUST00000170693; ENSMUSP00000132446; ENSMUSG00000091896.
DR GeneID; 56550; -.
DR KEGG; mmu:56550; -.
DR UCSC; uc012bbj.1; mouse.
DR CTD; 56550; -.
DR MGI; MGI:1930715; Ube2d2a.
DR VEuPathDB; HostDB:ENSMUSG00000091896; -.
DR eggNOG; KOG0417; Eukaryota.
DR GeneTree; ENSGT00940000153169; -.
DR HOGENOM; CLU_030988_13_3_1; -.
DR InParanoid; P62838; -.
DR OMA; VHFTTRI; -.
DR OrthoDB; 1337945at2759; -.
DR PhylomeDB; P62838; -.
DR TreeFam; TF101108; -.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-202424; Downstream TCR signaling.
DR Reactome; R-MMU-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-MMU-8951664; Neddylation.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR Reactome; R-MMU-937041; IKK complex recruitment mediated by RIP1.
DR Reactome; R-MMU-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 56550; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Ube2d2a; mouse.
DR PRO; PR:P62838; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P62838; protein.
DR Bgee; ENSMUSG00000091896; Expressed in gonadal ridge and 250 other tissues.
DR ExpressionAtlas; P62838; baseline and differential.
DR Genevisible; P62838; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
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_0000082463"
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
