UBE2C_XENLA
ID UBE2C_XENLA Reviewed; 179 AA.
AC P56616; Q6DJN4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 C;
DE EC=2.3.2.23;
DE AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme C;
DE EC=2.3.2.24;
DE AltName: Full=E2 ubiquitin-conjugating enzyme C;
DE AltName: Full=UBC-X;
DE AltName: Full=Ubiquitin carrier protein C;
DE AltName: Full=Ubiquitin-protein ligase C;
GN Name=ube2c; Synonyms=ubch10, ubcx;
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, AND PROTEIN SEQUENCE OF 63-80 AND 99-108.
RX PubMed=8723350; DOI=10.1016/s0960-9822(02)00513-4;
RA Yu H., King R.W., Peters J.-M., Kirschner M.W.;
RT "Identification of a novel ubiquitin-conjugating enzyme involved in mitotic
RT cyclin degradation.";
RL Curr. Biol. 6:455-466(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. Acts as an essential factor of the anaphase promoting
CC complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that
CC controls progression through mitosis. Acts by initiating 'Lys-11'-
CC linked polyubiquitin chains on APC/C substrates, leading to the
CC degradation of APC/C substrates by the proteasome and promoting mitotic
CC exit. {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:O00762, 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:O00762};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Component of the APC/C complex.
CC {ECO:0000250|UniProtKB:O00762}.
CC -!- PTM: Autoubiquitinated by the APC/C complex, leading to its degradation
CC by the proteasome. {ECO:0000250|UniProtKB:O00762}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; BC075141; AAH75141.1; -; mRNA.
DR RefSeq; NP_001086346.1; NM_001092877.1.
DR AlphaFoldDB; P56616; -.
DR SMR; P56616; -.
DR DNASU; 444775; -.
DR GeneID; 444775; -.
DR KEGG; xla:444775; -.
DR CTD; 444775; -.
DR Xenbase; XB-GENE-17339936; ube2c.L.
DR OMA; WINQEEY; -.
DR OrthoDB; 1444506at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 444775; Expressed in oocyte and 19 other tissues.
DR GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010458; P:exit from mitosis; ISS:UniProtKB.
DR GO; GO:0010994; P:free ubiquitin chain polymerization; ISS:UniProtKB.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
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; Cell cycle; Cell division; Direct protein sequencing; Mitosis;
KW Nucleotide-binding; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..179
FT /note="Ubiquitin-conjugating enzyme E2 C"
FT /id="PRO_0000082562"
FT DOMAIN 30..179
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 114
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 179 AA; 19897 MW; 0F7C242CE55996BA CRC64;
MASQNVDPAA ASSVASRKGQ ESGTSAARGS VGKRLQQELM TLMMSGDKGI SAFPESDNLF
KWIGTIDGAV GTVYEDLRYK LSLEFPSGYP YNAPTVKFVT PCFHPNVDSH GNICLDILKD
KWSALYDVRT ILLSLQSLLG EPNNESPLNP YAAELWQNQT AYKKHLHEQY QKQVREKEI
