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   02-SEP-2026, entry version 127.
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   FunCoup; Q1RML1; 4148.
DR   STRING; 9913.ENSBTAP00000058650; -.
DR   PaxDb; 9913-ENSBTAP00000058650; -.
DR   Ensembl; ENSBTAT00000012136.5; ENSBTAP00000012136.3; ENSBTAG00000009211.6.
DR   Ensembl; ENSBTAT00085082126; ENSBTAP00085038326; ENSBTAG00085024542.
DR   Ensembl; ENSBTAT00090017890; ENSBTAP00090008599; ENSBTAG00090009459.
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; 10069349at2759; -.
DR   Reactome; R-BTA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR   Reactome; R-BTA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR   Reactome; R-BTA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-BTA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-BTA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-BTA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-BTA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR   Reactome; R-BTA-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR   Reactome; R-BTA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR   Reactome; R-BTA-176412; Phosphorylation of the APC/C.
DR   Reactome; R-BTA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; R-BTA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-BTA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-BTA-68867; Assembly of the pre-replicative complex.
DR   Reactome; R-BTA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-BTA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Chromosome 18.
DR   Bgee; ENSBTAG00000009211; Expressed in granulosa cell and 107 other cell types or tissues.
DR   ExpressionAtlas; Q1RML1; baseline.
DR   GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
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: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   CDD; cd23804; UBCc_UBE2S; 1.
DR   FunFam; 3.10.110.10:FF:000034; Ubiquitin-conjugating enzyme E2 S; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR050113; Ub_conjugating_enzyme-E2-like.
DR   InterPro; IPR000608; UBC.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 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   2: Evidence at transcript level;
KW   Acetylation; Cell cycle; Cell division; Phosphoprotein; Reference proteome;
KW   Transferase; Ubl conjugation; 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   COMPBIAS        169..195
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..223
FT                   /note="Basic residues"
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
//