ID   UB2E1_HUMAN             Reviewed;         193 AA.
AC   P51965;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   07-JUL-2009, entry version 95.
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=UbcH6;
GN   Name=UBE2E1; Synonyms=UBCH6;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=96162027; PubMed=8576257; DOI=10.1074/jbc.271.5.2795;
RA   Nuber U., Schwarz S., Kaiser P., Schneider R., Scheffner M.;
RT   "Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-
RT   F1) and characterization of their interaction with E6-AP and RSP5.";
RL   J. Biol. Chem. 271:2795-2800(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
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).
RN   [3]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
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   -!- INTERACTION:
CC       Q99942:RNF5; NbExp=1; IntAct=EBI-348546, EBI-348482;
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
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DR   EMBL; X92963; CAA63539.1; -; mRNA.
DR   EMBL; BC009139; AAH09139.1; -; mRNA.
DR   IPI; IPI00021346; -.
DR   RefSeq; NP_003332.1; -.
DR   RefSeq; NP_872607.1; -.
DR   UniGene; Hs.164853; -.
DR   PDB; 1XR9; X-ray; 1.79 A; C=83-91.
DR   PDB; 3BZH; X-ray; 1.60 A; A=1-193.
DR   PDBsum; 1XR9; -.
DR   PDBsum; 3BZH; -.
DR   IntAct; P51965; 3.
DR   PhosphoSite; P51965; -.
DR   PRIDE; P51965; -.
DR   Ensembl; ENSG00000170142; Homo sapiens.
DR   GeneID; 7324; -.
DR   KEGG; hsa:7324; -.
DR   UCSC; uc003cch.1; human.
DR   GeneCards; GC03P023822; -.
DR   H-InvDB; HIX0003129; -.
DR   HGNC; HGNC:12477; UBE2E1.
DR   MIM; 602916; gene.
DR   PharmGKB; PA37127; -.
DR   HOGENOM; P51965; -.
DR   HOVERGEN; P51965; -.
DR   OMA; P51965; KETNAPK.
DR   BRENDA; 6.3.2.19; 247.
DR   Reactome; REACT_152; Cell Cycle, Mitotic.
DR   Reactome; REACT_1538; Cell Cycle Checkpoints.
DR   Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; REACT_8017; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; REACT_9035; APC/C:Cdh1-mediated degradation of Skp2.
DR   NextBio; 28656; -.
DR   Bgee; P51965; -.
DR   CleanEx; HS_UBE2E1; -.
DR   GermOnline; ENSG00000170142; Homo sapiens.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; EXP:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042296; F:ISG15 ligase activity; IDA:HGNC.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; TAS:ProtInc.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent protea...; EXP:Reactome.
DR   GO; GO:0032020; P:ISG15-protein conjugation; IDA:HGNC.
DR   GO; GO:0051436; P:negative regulation of ubiquitin-protein li...; EXP:Reactome.
DR   GO; GO:0051437; P:positive regulation of ubiquitin-protein li...; EXP:Reactome.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Ligase;
KW   Nucleotide-binding; Ubl conjugation pathway.
FT   CHAIN         1    193       Ubiquitin-conjugating enzyme E2 E1.
FT                                /FTId=PRO_0000082470.
FT   COMPBIAS      9     18       Poly-Ser.
FT   ACT_SITE    131    131       Glycyl thioester intermediate (By
FT                                similarity).
FT   HELIX        22     24
FT   HELIX        42     61
FT   STRAND       67     74
FT   STRAND       78     82
FT   STRAND       95    101
FT   TURN        104    108
FT   STRAND      112    117
FT   HELIX       133    135
FT   TURN        136    138
FT   HELIX       145    157
FT   HELIX       167    175
FT   HELIX       177    191
SQ   SEQUENCE   193 AA;  21404 MW;  2FBC50BE2A6A0008 CRC64;
     MSDDDSRAST SSSSSSSSNQ QTEKETNTPK KKESKVSMSK NSKLLSTSAK RIQKELADIT
     LDPPPNCSAG PKGDNIYEWR STILGPPGSV YEGGVFFLDI TFTPEYPFKP PKVTFRTRIY
     HCNINSQGVI CLDILKDNWS PALTISKVLL SICSLLTDCN PADPLVGSIA TQYMTNRAEH
     DRMARQWTKR YAT
//