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   03-MAY-2023, entry version 109.
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   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24067:SF338; UBIQUITIN-CONJUGATING ENZYME E2C; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 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
//