UB2E1_MOUSE
ID UB2E1_MOUSE Reviewed; 193 AA.
AC P52482;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 E1;
DE EC=2.3.2.23;
DE AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme E1;
DE EC=2.3.2.24;
DE AltName: Full=E2 ubiquitin-conjugating enzyme E1;
DE AltName: Full=UbcM3;
DE AltName: Full=Ubiquitin carrier protein E1;
DE AltName: Full=Ubiquitin-protein ligase E1;
GN Name=Ube2e1; Synonyms=Ubce5, Ubcm3;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=8576256; DOI=10.1074/jbc.271.5.2789;
RA Matuschewski K., Hauser H.P., Treier M., Jentsch S.;
RT "Identification of a novel family of ubiquitin-conjugating enzymes with
RT distinct amino-terminal extensions.";
RL J. Biol. Chem. 271:2789-2794(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Mammary tumor;
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=Brain, Kidney, Liver, Lung, Pancreas, 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 the covalent
CC attachment of ISG15 to other proteins. Mediates the selective
CC degradation of short-lived and abnormal proteins. In vitro also
CC catalyzes 'Lys-48'-linked polyubiquitination.
CC {ECO:0000250|UniProtKB:P51965}.
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:0000250|UniProtKB:P51965, ECO:0000255|PROSITE-
CC ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-
CC cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.24; Evidence={ECO:0000250|UniProtKB:P51965};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SUBUNIT: Interacts with RNF14.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51965}.
CC -!- PTM: ISGylation suppresses ubiquitin E2 enzyme activity.
CC {ECO:0000250|UniProtKB:P51965}.
CC -!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:P51965}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; X92665; CAA63353.1; -; mRNA.
DR EMBL; BC003781; AAH03781.1; -; mRNA.
DR CCDS; CCDS26837.1; -.
DR RefSeq; NP_033481.1; NM_009455.3.
DR AlphaFoldDB; P52482; -.
DR SMR; P52482; -.
DR BioGRID; 204406; 5.
DR IntAct; P52482; 1.
DR STRING; 10090.ENSMUSP00000022296; -.
DR iPTMnet; P52482; -.
DR PhosphoSitePlus; P52482; -.
DR SwissPalm; P52482; -.
DR EPD; P52482; -.
DR jPOST; P52482; -.
DR PaxDb; P52482; -.
DR PeptideAtlas; P52482; -.
DR PRIDE; P52482; -.
DR ProteomicsDB; 297771; -.
DR Antibodypedia; 45210; 119 antibodies from 22 providers.
DR DNASU; 22194; -.
DR Ensembl; ENSMUST00000022296; ENSMUSP00000022296; ENSMUSG00000021774.
DR GeneID; 22194; -.
DR KEGG; mmu:22194; -.
DR UCSC; uc007shu.1; mouse.
DR CTD; 7324; -.
DR MGI; MGI:107411; Ube2e1.
DR VEuPathDB; HostDB:ENSMUSG00000021774; -.
DR eggNOG; KOG0417; Eukaryota.
DR GeneTree; ENSGT00940000156415; -.
DR HOGENOM; CLU_030988_14_4_1; -.
DR InParanoid; P52482; -.
DR OMA; MYSSINT; -.
DR OrthoDB; 1337945at2759; -.
DR PhylomeDB; P52482; -.
DR TreeFam; TF101117; -.
DR BRENDA; 2.3.2.B8; 3474.
DR Reactome; R-MMU-1169408; ISG15 antiviral mechanism.
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-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 22194; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Ube2e1; mouse.
DR PRO; PR:P52482; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P52482; protein.
DR Bgee; ENSMUSG00000021774; Expressed in otic placode and 268 other tissues.
DR ExpressionAtlas; P52482; baseline and differential.
DR Genevisible; P52482; MM.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042296; F:ISG15 transferase activity; ISO:MGI.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0033523; P:histone H2B ubiquitination; ISO:MGI.
DR GO; GO:0010390; P:histone monoubiquitination; ISO:MGI.
DR GO; GO:0032020; P:ISG15-protein conjugation; ISO:MGI.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR GO; GO:0016567; P:protein ubiquitination; IGI:MGI.
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; Isopeptide bond; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P51965"
FT CHAIN 2..193
FT /note="Ubiquitin-conjugating enzyme E2 E1"
FT /id="PRO_0000082471"
FT DOMAIN 47..193
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P51965"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ISG15)"
FT /evidence="ECO:0000250|UniProtKB:P51965"
SQ SEQUENCE 193 AA; 21333 MW; B535B3095EF6C445 CRC64;
MSDDDSRAST SSSSSSSSNQ QTEKEGSTPK KKESKVSMSK NSKLLSTSAK RIQKELADIT
LDPPPNCSAG PKGDNIYEWR STILGPPGSV YEGGVFFLDI TFTPEYPFKP PKVTFRTRIY
HCNINSQGVI CLDILKDNWS PALTISKVLL SICSLLTDCN PADPLVGSIA TQYMTNRAEH
DRMARQWTKR YAT
