UBE2S_DANRE
ID UBE2S_DANRE Reviewed; 221 AA.
AC Q4V908;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
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; ORFNames=zgc:114060;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 'Lys-11'-linked polyubiquitin chains initiated by the E2 enzyme
CC ube2c/ubch10 on APC/C substrates, enhancing the degradation of APC/C
CC 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: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; BC097122; AAH97122.1; -; mRNA.
DR RefSeq; NP_001020707.1; NM_001025536.1.
DR AlphaFoldDB; Q4V908; -.
DR SMR; Q4V908; -.
DR STRING; 7955.ENSDARP00000047451; -.
DR PaxDb; Q4V908; -.
DR Ensembl; ENSDART00000047452; ENSDARP00000047451; ENSDARG00000031775.
DR GeneID; 565498; -.
DR KEGG; dre:565498; -.
DR CTD; 27338; -.
DR ZFIN; ZDB-GENE-050913-92; ube2s.
DR eggNOG; KOG0423; Eukaryota.
DR GeneTree; ENSGT00940000157149; -.
DR HOGENOM; CLU_030988_5_3_1; -.
DR InParanoid; Q4V908; -.
DR OMA; QPAKCGA; -.
DR OrthoDB; 1412570at2759; -.
DR PhylomeDB; Q4V908; -.
DR TreeFam; TF101120; -.
DR Reactome; R-DRE-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-DRE-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-DRE-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-DRE-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-DRE-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-DRE-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-DRE-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-DRE-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-DRE-176412; Phosphorylation of the APC/C.
DR Reactome; R-DRE-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-DRE-2467813; Separation of Sister Chromatids.
DR Reactome; R-DRE-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-DRE-68867; Assembly of the pre-replicative complex.
DR Reactome; R-DRE-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-DRE-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-DRE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q4V908; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000031775; Expressed in cleaving embryo and 28 other tissues.
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 2: Evidence at transcript level;
KW ATP-binding; Cell cycle; Cell division; Nucleotide-binding;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..221
FT /note="Ubiquitin-conjugating enzyme E2 S"
FT /id="PRO_0000390429"
FT DOMAIN 11..157
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 158..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..207
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"
SQ SEQUENCE 221 AA; 24149 MW; 3E3B6C7E6AC6B26D CRC64;
MNSNVENLPP QVLRLVYKEV SALAADPPEG IKIYPSEEDI TELHTSIEGP EGTPYAGGVF
RMRLVLGKDF PAVPPRGYFL TKIFHPNVGH KGEICVNVLK RDWKAELGLR HVLLTIKCLL
IHPNPESALN EEAGKLLLED YKEYASRAHL LTEIHAMGGT SGAPQEPADG PQPKKHAGDP
NKRVVGAGLP TMGTGTNNSN ISNTNIVAKK KTDKKRALRR L
