ID   UBE2S_RAT               Reviewed;         223 AA.
AC   B5DFI8;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   24-JAN-2024, entry version 98.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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; CH474075; EDL75864.1; -; Genomic_DNA.
DR   EMBL; BC169077; AAI69077.1; -; mRNA.
DR   RefSeq; NP_001099694.1; NM_001106224.2.
DR   AlphaFoldDB; B5DFI8; -.
DR   BMRB; B5DFI8; -.
DR   SMR; B5DFI8; -.
DR   STRING; 10116.ENSRNOP00000022977; -.
DR   PhosphoSitePlus; B5DFI8; -.
DR   PaxDb; 10116-ENSRNOP00000022977; -.
DR   Ensembl; ENSRNOT00000022977.6; ENSRNOP00000022977.4; ENSRNOG00000016930.6.
DR   Ensembl; ENSRNOT00055024439; ENSRNOP00055019964; ENSRNOG00055014224.
DR   Ensembl; ENSRNOT00060045303; ENSRNOP00060037608; ENSRNOG00060026151.
DR   Ensembl; ENSRNOT00065055518; ENSRNOP00065045684; ENSRNOG00065032252.
DR   GeneID; 292588; -.
DR   KEGG; rno:292588; -.
DR   UCSC; RGD:1564746; rat.
DR   AGR; RGD:1564746; -.
DR   CTD; 27338; -.
DR   RGD; 1564746; Ube2s.
DR   eggNOG; KOG0423; Eukaryota.
DR   GeneTree; ENSGT00940000157149; -.
DR   HOGENOM; CLU_030988_5_3_1; -.
DR   InParanoid; B5DFI8; -.
DR   OMA; QPAKCGA; -.
DR   OrthoDB; 179223at2759; -.
DR   PhylomeDB; B5DFI8; -.
DR   TreeFam; TF101120; -.
DR   Reactome; R-RNO-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR   Reactome; R-RNO-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR   Reactome; R-RNO-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-RNO-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-RNO-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-RNO-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-RNO-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR   Reactome; R-RNO-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR   Reactome; R-RNO-176412; Phosphorylation of the APC/C.
DR   Reactome; R-RNO-179409; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR   Reactome; R-RNO-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-RNO-68867; Assembly of the pre-replicative complex.
DR   Reactome; R-RNO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-RNO-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:B5DFI8; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Proteomes; UP000234681; Chromosome 1.
DR   Bgee; ENSRNOG00000016930; Expressed in testis and 20 other cell types or tissues.
DR   GO; GO:0005680; C:anaphase-promoting complex; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0010997; F:anaphase-promoting complex binding; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:RGD.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:RGD.
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; 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:SF154; UBIQUITIN-CONJUGATING ENZYME E2 G2; 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.
DR   Genevisible; B5DFI8; RN.
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_0000390428"
FT   DOMAIN          11..157
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   REGION          159..223
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..184
FT                   /note="Polar 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"
SQ   SEQUENCE   223 AA;  24215 MW;  EB3C7AE437689AD5 CRC64;
     MNSNVENLPP HIIRLVYKEV TTLTADPPDG IKVFPNEEDL TDLQVTIEGP EGTPYAGGLF
     RMKLLLGKDF PASPPKGYFL TKIFHPNVGP NGEICVNVLK RDWTAELGIR HVLLTIKCLL
     IHPNPESALN EEAGRLLLEN YEEYAARARL LTEIHGGACS TSSGRAEASR DLASGASASS
     TDPMTPGVLG GAEGPMAKKH AGERDKKLAA KKKLDKKRAL RRL
//