UBE2C_SPISO
ID UBE2C_SPISO Reviewed; 177 AA.
AC Q95044;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 25-MAY-2022, entry version 106.
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 Spisula solidissima (Atlantic surf-clam).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Heteroconchia; Euheterodonta; Imparidentia; Neoheterodontei;
OC Venerida; Mactroidea; Mactridae; Spisula.
OX NCBI_TaxID=6584;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8633058; DOI=10.1073/pnas.93.9.4294;
RA Aristarkhov A., Eytan E., Moghe A., Admon A., Hershko A., Ruderman J.V.;
RT "E2-C, a cyclin-selective ubiquitin carrier protein required for the
RT destruction of mitotic cyclins.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:4294-4299(1996).
RN [2]
RP MUTAGENESIS OF CYS-114.
RX PubMed=9122200; DOI=10.1073/pnas.94.6.2362;
RA Townsley F.M., Aristarkhov A., Beck S., Hershko A., Ruderman J.V.;
RT "Dominant-negative cyclin-selective ubiquitin carrier protein E2-C/UbcH10
RT blocks cells in metaphase.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:2362-2367(1997).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=10350465; DOI=10.1021/bi9901329;
RA Jiang F., Basavappa R.;
RT "Crystal structure of the cyclin-specific ubiquitin-conjugating enzyme from
RT clam, E2-C, at 2.0 A resolution.";
RL Biochemistry 38:6471-6478(1999).
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 is essential for the transition from metaphase to anaphase in mitosis.
CC Involved in both degradation of proteins responsible for maintaining
CC sister chromatid cohesion at the onset of anaphase and of mitotic
CC cyclins A and B at the exit of mitosis. Acts by initiating
CC polyubiquitin chains on APC/C substrates, leading to the degradation of
CC APC/C substrates by the proteasome and promoting mitotic exit.
CC {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; U52949; AAB06237.1; -; mRNA.
DR PDB; 2E2C; X-ray; 2.00 A; A=22-177.
DR PDBsum; 2E2C; -.
DR AlphaFoldDB; Q95044; -.
DR SMR; Q95044; -.
DR UniPathway; UPA00143; -.
DR EvolutionaryTrace; Q95044; -.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; Cell cycle; Cell division;
KW Direct protein sequencing; Mitosis; Nucleotide-binding; Transferase;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..177
FT /note="Ubiquitin-conjugating enzyme E2 C"
FT /id="PRO_0000082563"
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 COMPBIAS 13..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 114
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT MUTAGEN 114
FT /note="C->S: Inhibition of cyclin B degradation."
FT /evidence="ECO:0000269|PubMed:9122200"
FT HELIX 31..45
FT /evidence="ECO:0007829|PDB:2E2C"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:2E2C"
FT STRAND 59..67
FT /evidence="ECO:0007829|PDB:2E2C"
FT TURN 73..76
FT /evidence="ECO:0007829|PDB:2E2C"
FT STRAND 78..84
FT /evidence="ECO:0007829|PDB:2E2C"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:2E2C"
FT STRAND 95..100
FT /evidence="ECO:0007829|PDB:2E2C"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:2E2C"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:2E2C"
FT HELIX 128..138
FT /evidence="ECO:0007829|PDB:2E2C"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:2E2C"
FT HELIX 159..175
FT /evidence="ECO:0007829|PDB:2E2C"
SQ SEQUENCE 177 AA; 20134 MW; 06A454E798EE4F3A CRC64;
MSGQNIDPAA NQVRQKERPR DMTTSKERHS VSKRLQQELR TLLMSGDPGI TAFPDGDNLF
KWVATLDGPK DTVYESLKYK LTLEFPSDYP YKPPVVKFTT PCWHPNVDQS GNICLDILKE
NWTASYDVRT ILLSLQSLLG EPNNASPLNA QAADMWSNQT EYKKVLHEKY KTAQSDK
