UB2D2_XENLA
ID UB2D2_XENLA Reviewed; 147 AA.
AC P62840; P51669; Q5XGS3;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 4;
DE Short=xUBC4;
DE AltName: Full=Ubiquitin carrier protein D2;
DE AltName: Full=Ubiquitin-protein ligase D2;
GN Name=ube2d2; Synonyms=ubc4, ube2d3.1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Oocyte;
RA Karasawa A., Matushita H., Yagura T.;
RT "Molecular cloning of cDNAs encoding Xenopus ubiquitin-conjugating
RT enzyme(E2) and their expression in various Xenopus tissues.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NOMENCLATURE.
RX PubMed=18021256; DOI=10.1111/j.1432-0436.2007.00239.x;
RA Jean S., Moss T.;
RT "A ubiquitin-conjugating enzyme, ube2d3.2, regulates xMLK2 and pronephros
RT formation in Xenopus.";
RL Differentiation 76:431-441(2008).
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 ubiquitination of
CC p53/TP53. {ECO:0000255|PROSITE-ProRule:PRU00388}.
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. {ECO:0000250|UniProtKB:P62837}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AB105546; BAD06215.1; -; mRNA.
DR EMBL; BC084359; AAH84359.1; -; mRNA.
DR RefSeq; NP_001084434.1; NM_001090965.1.
DR RefSeq; XP_018098879.1; XM_018243390.1.
DR PDB; 3EB6; X-ray; 3.40 A; B=1-147.
DR PDBsum; 3EB6; -.
DR AlphaFoldDB; P62840; -.
DR SMR; P62840; -.
DR BioGRID; 100827; 2.
DR DNASU; 403384; -.
DR GeneID; 108706735; -.
DR GeneID; 403384; -.
DR KEGG; xla:108706735; -.
DR KEGG; xla:403384; -.
DR CTD; 108706735; -.
DR CTD; 403384; -.
DR Xenbase; XB-GENE-972284; ube2d3.L.
DR Xenbase; XB-GENE-17334432; ube2d3.S.
DR OMA; XVAFTTR; -.
DR OrthoDB; 1337945at2759; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; P62840; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 108706735; Expressed in gastrula and 19 other tissues.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
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 3D-structure; ATP-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..147
FT /note="Ubiquitin-conjugating enzyme E2 D2"
FT /id="PRO_0000082465"
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"
FT HELIX 2..15
FT /evidence="ECO:0007829|PDB:3EB6"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:3EB6"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:3EB6"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:3EB6"
FT TURN 58..62
FT /evidence="ECO:0007829|PDB:3EB6"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:3EB6"
FT TURN 87..92
FT /evidence="ECO:0007829|PDB:3EB6"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:3EB6"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:3EB6"
FT HELIX 131..145
FT /evidence="ECO:0007829|PDB:3EB6"
SQ SEQUENCE 147 AA; 16735 MW; C942BE7853CBC355 CRC64;
MALKRIHKEL NDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY
PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV
PEIARIYKTD REKYNRIARE WTQKYAM
