UBE2S_BRAFL
ID UBE2S_BRAFL Reviewed; 213 AA.
AC C3Z724;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 S;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme S;
DE AltName: Full=Ubiquitin carrier protein S;
DE AltName: Full=Ubiquitin-protein ligase S;
GN ORFNames=BRAFLDRAFT_259979;
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82; TISSUE=Testis;
RX PubMed=18563158; DOI=10.1038/nature06967;
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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 specifically elongating
CC polyubiquitin chains initiated by the E2 enzyme UBCH10 on APC/C
CC substrates, enhancing the degradation of APC/C substrates by the
CC proteasome and promoting mitotic exit. {ECO:0000255|PROSITE-
CC 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:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC ProRule:PRU10133};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; GG666590; EEN51620.1; -; Genomic_DNA.
DR RefSeq; XP_002595608.1; XM_002595562.1.
DR AlphaFoldDB; C3Z724; -.
DR SMR; C3Z724; -.
DR STRING; 7739.XP_002595608.1; -.
DR eggNOG; KOG0423; Eukaryota.
DR InParanoid; C3Z724; -.
DR OMA; QPAKCGA; -.
DR OrthoDB; 1412570at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001554; Partially assembled WGS sequence.
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: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:1904668; P:positive regulation of ubiquitin protein ligase activity; ISS:UniProtKB.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Nucleotide-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..213
FT /note="Ubiquitin-conjugating enzyme E2 S"
FT /id="PRO_0000390435"
FT DOMAIN 13..159
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 157..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 97
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 213 AA; 23522 MW; 0729D63B1B091D5D CRC64;
MSGSSNVENL SPQIIRQVAK EVLDLANHPP EGVKVFPNEQ DITDVQATIE GPGGTPYEGG
QFKIKLSLGK DFPQTPPKGF FLTKIFHPNV AKNGEICVNT LKKDWKADLG LKHILLTIKC
LLIYPNPESA LNEEAGKLLL EQYDNYSERA RMMTEIHAKP TTKTAPTKNE ETNCPSTSGT
QSTSEGPMAK KHAGDKNAAE KKKKEKKRAL RRL
