UBE2S_BOVIN
ID UBE2S_BOVIN Reviewed; 223 AA.
AC Q1RML1; A6QLZ2;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 2.
DT 03-AUG-2022, entry version 111.
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 Name=UBE2S;
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, and Hereford; TISSUE=Fetal brain, and Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. Catalyzes 'Lys-11'-linked
CC polyubiquitination. Acts as an essential factor of the anaphase
CC promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin
CC ligase that controls progression through mitosis. Acts by specifically
CC elongating 'Lys-11'-linked polyubiquitin chains initiated by the E2
CC enzyme UBE2C/UBCH10 on APC/C substrates, enhancing the degradation of
CC APC/C substrates by the proteasome and promoting mitotic exit. Also
CC acts by elongating ubiquitin chains initiated by the E2 enzyme
CC UBE2D1/UBCH5 in vitro; it is however unclear whether UBE2D1/UBCH5 acts
CC as an E2 enzyme for the APC/C in vivo. Also involved in ubiquitination
CC and subsequent degradation of VHL, resulting in an accumulation of
CC HIF1A. In vitro able to promote polyubiquitination using all 7
CC ubiquitin Lys residues, except 'Lys-48'-linked polyubiquitination.
CC {ECO:0000250|UniProtKB:Q16763}.
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 -!- 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 and ANAPC4. Interacts with CDC20,
CC FZR1/CDH1 and VHL. {ECO:0000250|UniProtKB:Q16763}.
CC -!- PTM: Autoubiquitinated by the APC/C complex during G1, leading to its
CC degradation by the proteasome. {ECO:0000250|UniProtKB:Q16763}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; BC114838; AAI14839.1; -; mRNA.
DR EMBL; BC148138; AAI48139.1; -; mRNA.
DR RefSeq; NP_001069940.1; NM_001076472.2.
DR AlphaFoldDB; Q1RML1; -.
DR BMRB; Q1RML1; -.
DR SMR; Q1RML1; -.
DR STRING; 9913.ENSBTAP00000012136; -.
DR PaxDb; Q1RML1; -.
DR PRIDE; Q1RML1; -.
DR Ensembl; ENSBTAT00000012136; ENSBTAP00000012136; ENSBTAG00000009211.
DR GeneID; 617703; -.
DR KEGG; bta:617703; -.
DR CTD; 27338; -.
DR VEuPathDB; HostDB:ENSBTAG00000009211; -.
DR VGNC; VGNC:36595; UBE2S.
DR eggNOG; KOG0423; Eukaryota.
DR GeneTree; ENSGT00940000157149; -.
DR HOGENOM; CLU_030988_5_3_1; -.
DR InParanoid; Q1RML1; -.
DR OMA; QPAKCGA; -.
DR OrthoDB; 1412570at2759; -.
DR TreeFam; TF101120; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000009211; Expressed in granulosa cell and 107 other tissues.
DR ExpressionAtlas; Q1RML1; 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: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:0044314; P:protein K27-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0035519; P:protein K29-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0085020; P:protein K6-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0070534; P:protein K63-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 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Cell cycle; Cell division; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway.
FT CHAIN 1..223
FT /note="Ubiquitin-conjugating enzyme E2 S"
FT /id="PRO_0000245039"
FT DOMAIN 11..157
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 155..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 95
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q16763"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16763"
FT CONFLICT 186
FT /note="P -> T (in Ref. 1; AAI14839)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 223 AA; 23896 MW; C3D0FAEE6429E3EB CRC64;
MNSNVENLPP HIIRLVYKEV TTLTADPPDG IKVFPNEEDL TDLQVTIEGP EGTPYAGGLF
RMKLLLGKDF PASPPKGYFL TKIFHPNVGA NGEICVNVLK RDWTAELGIR HVLLTIKCLL
IHPNPESALN EEAGRLLLEN YEEYAARARL LTEIHGGAGG PSGGRPEPGR ATASGAAAST
ADPTAPGGPA GAEGPMAKKH AGERDKKLAA KKKTDKKRAL RRL
