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   16-JUN-2009, entry version 81.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 E1;
DE            EC=6.3.2.19;
DE   AltName: Full=Ubiquitin-protein ligase E1;
DE   AltName: Full=Ubiquitin carrier protein E1;
DE   AltName: Full=UbcM3;
GN   Name=Ube2e1; Synonyms=Ubce5, Ubcm3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=BALB/c; TISSUE=Brain;
RX   MEDLINE=96162026; 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
RT   with 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Mediates the selective degradation of short-lived and
CC       abnormal proteins.
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with RNF14.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
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DR   EMBL; X92665; CAA63353.1; -; mRNA.
DR   EMBL; BC003781; AAH03781.1; -; mRNA.
DR   IPI; IPI00127542; -.
DR   RefSeq; NP_033481.1; -.
DR   UniGene; Mm.4429; -.
DR   HSSP; P15731; 1QCQ.
DR   SMR; P52482; 46-193.
DR   PhosphoSite; P52482; -.
DR   Ensembl; ENSMUSG00000021774; Mus musculus.
DR   GeneID; 22194; -.
DR   KEGG; mmu:22194; -.
DR   MGI; MGI:107411; Ube2e1.
DR   HOGENOM; P52482; -.
DR   HOVERGEN; P52482; -.
DR   OMA; P52482; KETNAPK.
DR   BRENDA; 6.3.2.19; 244.
DR   NextBio; 302173; -.
DR   Bgee; P52482; -.
DR   GermOnline; ENSMUSG00000021774; Mus musculus.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IEA:EC.
DR   GO; GO:0019941; P:modification-dependent protein catabolic pr...; IEA:UniProtKB-KW.
DR   GO; GO:0043687; P:post-translational protein modification; IEA:InterPro.
DR   GO; GO:0051246; P:regulation of protein metabolic process; IEA:InterPro.
DR   InterPro; IPR016135; UBQ-conjugat/RWD-like.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   Gene3D; G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   ProDom; PD000461; UBQ_conjugat; 1.
DR   SMART; SM00212; UBCc; 1.
DR   PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR   PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Ligase; Nucleotide-binding; Ubl conjugation pathway.
FT   CHAIN         1    193       Ubiquitin-conjugating enzyme E2 E1.
FT                                /FTId=PRO_0000082471.
FT   COMPBIAS      9     18       Poly-Ser.
FT   ACT_SITE    131    131       Glycyl thioester intermediate (By
FT                                similarity).
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
//