UBE2S_HUMAN
ID UBE2S_HUMAN Reviewed; 222 AA.
AC Q16763; Q9BTC1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 S;
DE EC=2.3.2.23 {ECO:0000269|PubMed:19820702, ECO:0000269|PubMed:19822757, ECO:0000269|PubMed:20061386};
DE AltName: Full=E2 ubiquitin-conjugating enzyme S;
DE AltName: Full=E2-EPF;
DE AltName: Full=Ubiquitin carrier protein S;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-24 kDa;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-EPF5;
DE AltName: Full=Ubiquitin-protein ligase S;
GN Name=UBE2S; Synonyms=E2EPF; ORFNames=OK/SW-cl.73;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Foreskin;
RX PubMed=1379239; DOI=10.1016/s0021-9258(19)49610-5;
RA Liu Z., Diaz L.A., Haas A.L., Giudice G.J.;
RT "cDNA cloning of a novel human ubiquitin carrier protein. An antigenic
RT domain specifically recognized by endemic pemphigus foliaceus
RT autoantibodies is encoded in a secondary reading frame of this human
RT epidermal transcript.";
RL J. Biol. Chem. 267:15829-15835(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Skin;
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).
RN [5]
RP FUNCTION, AND INTERACTION WITH VHL.
RX PubMed=16819549; DOI=10.1038/nm1440;
RA Jung C.R., Hwang K.S., Yoo J., Cho W.K., Kim J.M., Kim W.H., Im D.S.;
RT "E2-EPF UCP targets pVHL for degradation and associates with tumor growth
RT and metastasis.";
RL Nat. Med. 12:809-816(2006).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=19820702; DOI=10.1038/ncb1983;
RA Garnett M.J., Mansfeld J., Godwin C., Matsusaka T., Wu J., Russell P.,
RA Pines J., Venkitaraman A.R.;
RT "UBE2S elongates ubiquitin chains on APC/C substrates to promote mitotic
RT exit.";
RL Nat. Cell Biol. 11:1363-1369(2009).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INTERACTION WITH CDC20 AND FZR,
RP UBIQUITINATION, AND MUTAGENESIS OF CYS-95.
RX PubMed=19822757; DOI=10.1073/pnas.0907887106;
RA Williamson A., Wickliffe K.E., Mellone B.G., Song L., Karpen G.H., Rape M.;
RT "Identification of a physiological E2 module for the human anaphase-
RT promoting complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:18213-18218(2009).
RN [10]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20061386; DOI=10.1074/jbc.m109.089003;
RA David Y., Ziv T., Admon A., Navon A.;
RT "The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
RT preferred lysines.";
RL J. Biol. Chem. 285:8595-8604(2010).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF CYS-95.
RX PubMed=20622874; DOI=10.1038/nsmb.1873;
RA Bremm A., Freund S.M., Komander D.;
RT "Lys11-linked ubiquitin chains adopt compact conformations and are
RT preferentially hydrolyzed by the deubiquitinase Cezanne.";
RL Nat. Struct. Mol. Biol. 17:939-947(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 1-156.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human ubiquitin-conjugating enzyme E2S.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [15] {ECO:0007744|PDB:1ZDN}
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 1-156, FUNCTION, AND
RP AUTOUBIQUITINATION.
RX PubMed=22496338; DOI=10.1074/mcp.o111.013706;
RA Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J., Avvakumov G.V.,
RA Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K., Arrowsmith C.H.,
RA Raught B., Dhe-Paganon S.;
RT "A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
RT function screen.";
RL Mol. Cell. Proteomics 11:329-341(2012).
RN [16] {ECO:0007744|PDB:5L9T}
RP STRUCTURE BY ELECTRON MICROSCOPY (6.40 ANGSTROMS) IN COMPLEX WITH APC/C,
RP FUNCTION, INTERACTION WITH ANAPC2 AND ANAPC4, AND MUTAGENESIS OF LEU-222.
RX PubMed=27259151; DOI=10.1016/j.cell.2016.05.037;
RA Brown N.G., VanderLinden R., Watson E.R., Weissmann F., Ordureau A.,
RA Wu K.P., Zhang W., Yu S., Mercredi P.Y., Harrison J.S., Davidson I.F.,
RA Qiao R., Lu Y., Dube P., Brunner M.R., Grace C.R., Miller D.J.,
RA Haselbach D., Jarvis M.A., Yamaguchi M., Yanishevski D., Petzold G.,
RA Sidhu S.S., Kuhlman B., Kirschner M.W., Harper J.W., Peters J.M., Stark H.,
RA Schulman B.A.;
RT "Dual RING E3 architectures regulate multiubiquitination and ubiquitin
RT chain elongation by APC/C.";
RL Cell 165:1440-1453(2016).
RN [17] {ECO:0007744|PDB:5BNB}
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 1-156 IN COMPLEX WITH UBIQUITIN,
RP AND MUTAGENESIS OF LYS-117.
RX PubMed=26828794; DOI=10.1371/journal.pone.0147550;
RA Lorenz S., Bhattacharyya M., Feiler C., Rape M., Kuriyan J.;
RT "Crystal structure of a Ube2S-ubiquitin conjugate.";
RL PLoS ONE 11:E0147550-E0147550(2016).
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins (PubMed:22496338). Catalyzes
CC 'Lys-11'-linked polyubiquitination. Acts as an essential factor of the
CC anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated
CC ubiquitin ligase that controls progression through mitosis. Acts by
CC specifically elongating 'Lys-11'-linked polyubiquitin chains initiated
CC by the E2 enzyme UBE2C/UBCH10 on APC/C substrates, enhancing the
CC degradation of APC/C substrates by the proteasome and promoting mitotic
CC exit (PubMed:19820702, PubMed:19822757, PubMed:27259151). Also acts by
CC elongating ubiquitin chains initiated by the E2 enzyme UBE2D1/UBCH5 in
CC vitro; it is however unclear whether UBE2D1/UBCH5 acts as an E2 enzyme
CC for the APC/C in vivo. Also involved in ubiquitination and subsequent
CC degradation of VHL, resulting in an accumulation of HIF1A
CC (PubMed:16819549). In vitro able to promote polyubiquitination using
CC all 7 ubiquitin Lys residues, except 'Lys-48'-linked polyubiquitination
CC (PubMed:20061386, PubMed:20622874). {ECO:0000269|PubMed:16819549,
CC ECO:0000269|PubMed:19820702, ECO:0000269|PubMed:19822757,
CC ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:20622874,
CC ECO:0000269|PubMed:22496338, ECO:0000269|PubMed:27259151}.
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, ECO:0000269|PubMed:19820702,
CC ECO:0000269|PubMed:19822757, ECO:0000269|PubMed:20061386};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:19820702,
CC ECO:0000269|PubMed:19822757}.
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 (PubMed:27259151). Interacts
CC with CDC20, FZR1/CDH1 and VHL (PubMed:16819549, PubMed:19822757).
CC {ECO:0000269|PubMed:16819549, ECO:0000269|PubMed:19822757,
CC ECO:0000269|PubMed:27259151}.
CC -!- INTERACTION:
CC Q16763; Q9UJX6: ANAPC2; NbExp=4; IntAct=EBI-2339823, EBI-396211;
CC Q16763; P62879: GNB2; NbExp=3; IntAct=EBI-2339823, EBI-356942;
CC Q16763; P40337-2: VHL; NbExp=3; IntAct=EBI-2339823, EBI-12157263;
CC -!- PTM: Autoubiquitinated by the APC/C complex during G1, leading to its
CC degradation by the proteasome. {ECO:0000269|PubMed:19822757}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; M91670; AAA58446.1; -; mRNA.
DR EMBL; AB062397; BAB93484.1; -; mRNA.
DR EMBL; AC020922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004236; AAH04236.1; -; mRNA.
DR EMBL; BC007554; AAH07554.1; -; mRNA.
DR EMBL; BC065364; AAH65364.1; -; mRNA.
DR CCDS; CCDS33114.1; -.
DR RefSeq; NP_055316.2; NM_014501.2.
DR PDB; 1ZDN; X-ray; 1.93 A; A/B=1-156.
DR PDB; 5BNB; X-ray; 2.49 A; A/B/C/D=1-156.
DR PDB; 5L9T; EM; 6.40 A; T=1-222.
DR PDB; 6QH3; X-ray; 2.90 A; A/B=1-156.
DR PDB; 6QHK; X-ray; 1.96 A; A/B=1-156.
DR PDB; 6S96; X-ray; 2.18 A; A/B=1-156.
DR PDB; 6S98; X-ray; 1.55 A; A/B=1-156.
DR PDB; 7AHF; X-ray; 2.15 A; A/B=1-156.
DR PDBsum; 1ZDN; -.
DR PDBsum; 5BNB; -.
DR PDBsum; 5L9T; -.
DR PDBsum; 6QH3; -.
DR PDBsum; 6QHK; -.
DR PDBsum; 6S96; -.
DR PDBsum; 6S98; -.
DR PDBsum; 7AHF; -.
DR AlphaFoldDB; Q16763; -.
DR BMRB; Q16763; -.
DR SMR; Q16763; -.
DR BioGRID; 118150; 126.
DR DIP; DIP-52784N; -.
DR IntAct; Q16763; 23.
DR MINT; Q16763; -.
DR STRING; 9606.ENSP00000264552; -.
DR iPTMnet; Q16763; -.
DR MetOSite; Q16763; -.
DR PhosphoSitePlus; Q16763; -.
DR SwissPalm; Q16763; -.
DR BioMuta; UBE2S; -.
DR DMDM; 23829978; -.
DR EPD; Q16763; -.
DR jPOST; Q16763; -.
DR MassIVE; Q16763; -.
DR MaxQB; Q16763; -.
DR PaxDb; Q16763; -.
DR PeptideAtlas; Q16763; -.
DR PRIDE; Q16763; -.
DR ProteomicsDB; 61055; -.
DR Antibodypedia; 33096; 566 antibodies from 31 providers.
DR DNASU; 27338; -.
DR Ensembl; ENST00000264552.14; ENSP00000264552.8; ENSG00000108106.14.
DR GeneID; 27338; -.
DR KEGG; hsa:27338; -.
DR MANE-Select; ENST00000264552.14; ENSP00000264552.8; NM_014501.3; NP_055316.2.
DR UCSC; uc002qkx.2; human.
DR CTD; 27338; -.
DR DisGeNET; 27338; -.
DR GeneCards; UBE2S; -.
DR HGNC; HGNC:17895; UBE2S.
DR HPA; ENSG00000108106; Tissue enhanced (bone marrow, testis).
DR MIM; 610309; gene.
DR neXtProt; NX_Q16763; -.
DR OpenTargets; ENSG00000108106; -.
DR PharmGKB; PA134904441; -.
DR VEuPathDB; HostDB:ENSG00000108106; -.
DR eggNOG; KOG0423; Eukaryota.
DR GeneTree; ENSGT00940000157149; -.
DR InParanoid; Q16763; -.
DR OMA; QPAKCGA; -.
DR OrthoDB; 1412570at2759; -.
DR PhylomeDB; Q16763; -.
DR TreeFam; TF101120; -.
DR BRENDA; 2.3.2.23; 2681.
DR BRENDA; 2.3.2.24; 2681.
DR PathwayCommons; Q16763; -.
DR Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-HSA-176412; Phosphorylation of the APC/C.
DR Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
DR Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-HSA-9687136; Aberrant regulation of mitotic exit in cancer due to RB1 defects.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q16763; -.
DR SIGNOR; Q16763; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 27338; 264 hits in 1060 CRISPR screens.
DR ChiTaRS; UBE2S; human.
DR EvolutionaryTrace; Q16763; -.
DR GenomeRNAi; 27338; -.
DR Pharos; Q16763; Tbio.
DR PRO; PR:Q16763; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q16763; protein.
DR Bgee; ENSG00000108106; Expressed in ventricular zone and 98 other tissues.
DR ExpressionAtlas; Q16763; baseline and differential.
DR Genevisible; Q16763; HS.
DR GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0010997; F:anaphase-promoting complex binding; IPI:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0010458; P:exit from mitosis; IDA:UniProtKB.
DR GO; GO:0010994; P:free ubiquitin chain polymerization; IDA:UniProtKB.
DR GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0044314; P:protein K27-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0035519; P:protein K29-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0085020; P:protein K6-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB.
DR GO; GO:0036211; P:protein modification process; TAS:ProtInc.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..222
FT /note="Ubiquitin-conjugating enzyme E2 S"
FT /id="PRO_0000082507"
FT DOMAIN 11..157
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 156..222
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 MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MUTAGEN 95
FT /note="C->S: Loss of function."
FT /evidence="ECO:0000269|PubMed:19822757,
FT ECO:0000269|PubMed:20622874"
FT MUTAGEN 117
FT /note="K->A: Reduced ubiquitination activity."
FT /evidence="ECO:0000269|PubMed:26828794"
FT MUTAGEN 222
FT /note="L->A: Impairs polyubiquitination in the presence of
FT APC/C complex, decreasing affinity for substrate."
FT /evidence="ECO:0000269|PubMed:27259151"
FT CONFLICT 216
FT /note="K -> KRAL (in Ref. 1; AAA58446)"
FT /evidence="ECO:0000305"
FT HELIX 10..25
FT /evidence="ECO:0007829|PDB:6S98"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:6S98"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:7AHF"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:6S98"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:6S98"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:6S98"
FT TURN 68..72
FT /evidence="ECO:0007829|PDB:6S98"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:6S98"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:6S98"
FT HELIX 96..100
FT /evidence="ECO:0007829|PDB:6S98"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:6S98"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6S98"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:6S98"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:6S98"
SQ SEQUENCE 222 AA; 23845 MW; 2842DC3DCD2AFCB5 CRC64;
MNSNVENLPP HIIRLVYKEV TTLTADPPDG IKVFPNEEDL TDLQVTIEGP EGTPYAGGLF
RMKLLLGKDF PASPPKGYFL TKIFHPNVGA NGEICVNVLK RDWTAELGIR HVLLTIKCLL
IHPNPESALN EEAGRLLLEN YEEYAARARL LTEIHGGAGG PSGRAEAGRA LASGTEASST
DPGAPGGPGG AEGPMAKKHA GERDKKLAAK KKTDKKRALR RL
