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   24-JAN-2024, entry version 176.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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; 10090-ENSMUSP00000022296; -.
DR   PeptideAtlas; P52482; -.
DR   ProteomicsDB; 297771; -.
DR   Pumba; P52482; -.
DR   Antibodypedia; 45210; 138 antibodies from 23 providers.
DR   DNASU; 22194; -.
DR   Ensembl; ENSMUST00000022296.7; ENSMUSP00000022296.7; ENSMUSG00000021774.14.
DR   GeneID; 22194; -.
DR   KEGG; mmu:22194; -.
DR   UCSC; uc007shu.1; mouse.
DR   AGR; MGI:107411; -.
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; IVFRTRI; -.
DR   OrthoDB; 5478564at2759; -.
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; 5 hits in 81 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 271 other cell types or tissues.
DR   ExpressionAtlas; P52482; baseline and differential.
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:0032020; P:ISG15-protein conjugation; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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; 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; PTHR24068; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24068:SF70; UBIQUITIN-CONJUGATING ENZYME E2 E1; 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; P52482; MM.
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
//