UBE2S_MOUSE
ID UBE2S_MOUSE Reviewed; 223 AA.
AC Q921J4; Q3U4V7; Q8CF67;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
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-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;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, DBA/2J, and NOD; TISSUE=Spleen, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and Czech II; TISSUE=Mammary gland;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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; AK003078; BAC25019.1; -; mRNA.
DR EMBL; AK017648; BAC25523.1; -; mRNA.
DR EMBL; AK146276; BAE27035.1; -; mRNA.
DR EMBL; AK154026; BAE32323.1; -; mRNA.
DR EMBL; AK154067; BAE32353.1; -; mRNA.
DR EMBL; BC012255; AAH12255.1; -; mRNA.
DR EMBL; BC030171; AAH30171.1; -; mRNA.
DR EMBL; BC083323; AAH83323.1; -; mRNA.
DR CCDS; CCDS39743.1; -.
DR RefSeq; NP_598538.1; NM_133777.2.
DR AlphaFoldDB; Q921J4; -.
DR BMRB; Q921J4; -.
DR SMR; Q921J4; -.
DR IntAct; Q921J4; 2.
DR MINT; Q921J4; -.
DR STRING; 10090.ENSMUSP00000078459; -.
DR iPTMnet; Q921J4; -.
DR PhosphoSitePlus; Q921J4; -.
DR SwissPalm; Q921J4; -.
DR REPRODUCTION-2DPAGE; Q921J4; -.
DR EPD; Q921J4; -.
DR MaxQB; Q921J4; -.
DR PaxDb; Q921J4; -.
DR PeptideAtlas; Q921J4; -.
DR PRIDE; Q921J4; -.
DR ProteomicsDB; 298403; -.
DR DNASU; 77891; -.
DR Ensembl; ENSMUST00000079496; ENSMUSP00000078459; ENSMUSG00000060860.
DR GeneID; 77891; -.
DR KEGG; mmu:77891; -.
DR UCSC; uc009eyt.1; mouse.
DR CTD; 27338; -.
DR MGI; MGI:1925141; Ube2s.
DR VEuPathDB; HostDB:ENSMUSG00000060860; -.
DR eggNOG; KOG0423; Eukaryota.
DR GeneTree; ENSGT00940000157149; -.
DR HOGENOM; CLU_030988_5_3_1; -.
DR InParanoid; Q921J4; -.
DR OMA; QPAKCGA; -.
DR OrthoDB; 1412570at2759; -.
DR PhylomeDB; Q921J4; -.
DR TreeFam; TF101120; -.
DR Reactome; R-MMU-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-MMU-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-MMU-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-MMU-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-MMU-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-MMU-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-MMU-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR Reactome; R-MMU-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR Reactome; R-MMU-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-MMU-176412; Phosphorylation of the APC/C.
DR Reactome; R-MMU-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-MMU-68867; Assembly of the pre-replicative complex.
DR Reactome; R-MMU-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 77891; 6 hits in 74 CRISPR screens.
DR ChiTaRS; Ube2s; mouse.
DR PRO; PR:Q921J4; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q921J4; protein.
DR Bgee; ENSMUSG00000060860; Expressed in ventricular zone and 64 other tissues.
DR ExpressionAtlas; Q921J4; baseline and differential.
DR Genevisible; Q921J4; MM.
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:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:MGI.
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 1: Evidence at protein 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_0000082508"
FT DOMAIN 11..157
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 170..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 213
FT /note="K -> N (in Ref. 1; BAC25019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 223 AA; 24183 MW; 10816CE4377BC406 CRC64;
MNSNVENLPP HIIRLVYKEV TTLTADPPDG IKVFPNEEDL TDLQVTIEGP EGTPYAGGLF
RMKLLLGKDF PASPPKGYFL TKIFHPNVGP NGEICVNVLK RDWTAELGIR HVLLTIKCLL
IHPNPESALN EEAGRLLLEN YEEYAARARL LTEIHGGACS TSSGRAEATQ DLASGASASS
ADPMIPGVLG GAEGPMAKKH AGERDKKLAA KKKLDKKRAL RRL
