UBE2C_BOVIN
ID UBE2C_BOVIN Reviewed; 179 AA.
AC Q32PA5;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=Ubiquitin carrier protein C;
DE AltName: Full=Ubiquitin-protein ligase C;
GN Name=UBE2C; Synonyms=UBCH10;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and
CC 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the
CC anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated
CC ubiquitin ligase that controls progression through mitosis. Acts by
CC initiating 'Lys-11'-linked polyubiquitin chains on APC/C substrates,
CC leading to the degradation of APC/C substrates by the proteasome and
CC promoting mitotic exit. {ECO:0000250|UniProtKB:O00762}.
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, composed of at least 14
CC distinct subunits that assemble into a complex of at least 19 chains
CC with a combined molecular mass of around 1.2 MDa. Within this complex,
CC directly interacts with ANAPC2. {ECO:0000250|UniProtKB:O00762}.
CC -!- PTM: Autoubiquitinated by the APC/C complex, leading to its degradation
CC by the proteasome. Its degradation plays a central role in APC/C
CC regulation, allowing cyclin-A accumulation before S phase entry. APC/C
CC substrates inhibit the autoubiquitination of UBE2C/UBCH10 but not its
CC E2 function, hence APC/C remaining active until its substrates have
CC been destroyed. {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; BC108195; AAI08196.1; -; mRNA.
DR RefSeq; NP_001032526.1; NM_001037449.2.
DR AlphaFoldDB; Q32PA5; -.
DR SMR; Q32PA5; -.
DR STRING; 9913.ENSBTAP00000022264; -.
DR PaxDb; Q32PA5; -.
DR PRIDE; Q32PA5; -.
DR Ensembl; ENSBTAT00000079595; ENSBTAP00000061332; ENSBTAG00000016746.
DR GeneID; 506962; -.
DR KEGG; bta:506962; -.
DR CTD; 11065; -.
DR VEuPathDB; HostDB:ENSBTAG00000016746; -.
DR VGNC; VGNC:36578; UBE2C.
DR eggNOG; KOG0421; Eukaryota.
DR GeneTree; ENSGT00930000150941; -.
DR HOGENOM; CLU_030988_9_2_1; -.
DR InParanoid; Q32PA5; -.
DR OMA; HPNVDMS; -.
DR OrthoDB; 1444506at2759; -.
DR TreeFam; TF101116; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000016746; Expressed in oocyte and 108 other tissues.
DR ExpressionAtlas; Q32PA5; baseline and differential.
DR GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
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:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cell cycle; Cell division; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O00762"
FT CHAIN 2..179
FT /note="Ubiquitin-conjugating enzyme E2 C"
FT /id="PRO_0000245040"
FT DOMAIN 30..175
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"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O00762"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00762"
SQ SEQUENCE 179 AA; 19608 MW; 19F9F5F63A3C97A0 CRC64;
MASQNRDPVA ASVAAARKGA EPSGGAARGP VGKRLQQELM TLMMSGDKGI SAFPESDNLF
KWVGTIHGAA GTVYEDLRYK LSLEFPSGYP YNAPTVKFLT PCYHPNVDTQ GNICLDILKD
KWSALYDVRT ILLSIQSLLG EPNIDSPLNT HAAELWKNPT AFKKYLQETY SKQVSSQDP
