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UniProtKB/Swiss-Prot entry P51965

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name UB2E1_HUMAN
Primary accession number P51965
Secondary accession numbers None
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 86)
Name and origin of the protein
Protein name Ubiquitin-conjugating enzyme E2 E1
Synonyms EC 6.3.2.19
Ubiquitin-protein ligase E1
Ubiquitin carrier protein E1
UbcH6
Gene name
Name: UBE2E1
Synonyms: UBCH6
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1074/jbc.271.5.2795; PubMed=8576257 [NCBI, ExPASy, EBI, Israel, Japan]
Nuber U., Schwarz S., Kaiser P., Schneider R., Scheffner M.;
"Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-F1) and characterization of their interaction with E6-AP and RSP5.";
J. Biol. Chem. 271:2795-2800(1996).
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X92963; CAA63539.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009139; AAH09139.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_003332.1; -.
NP_872607.1; -.
UniGene Hs.164853
3D structure databases
PDB
1XR9; X-ray; 1.79 A; C=83-91.[ExPASy / RCSB / EBI]
3BZH; X-ray; 1.60 A; A=1-193.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1XR9; -.
3BZH; -.
ModBase P51965.
Protein-protein interaction databases
IntAct P51965; -.
PTM databases
PhosphoSite P51965; -.
Enzyme and pathway databases
Reactome REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_8017; APC-Cdc20 mediated degradation of Nek2A.
REACT_9035; APC/C:Cdh1-mediated degradation of Skp2.
Organism-specific databases
H-InvDB HIX0003129; -.
HGNC HGNC:12477; UBE2E1.
GenAtlas UBE2E1.
MIM 602916; gene. [NCBI / EBI]
PharmGKB PA37127; -.
GeneCards P51965.
Gene expression databases
CleanEx HS_UBE2E1; -.
GermOnline ENSG00000170142; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from experiment from Reactome).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0042296; Molecular function: ISG15 ligase activity (inferred from direct assay from HGNC).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004842; Molecular function: ubiquitin-protein ligase activity (traceable author statement from ProtInc).
GO:0031145; Biological process: anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process (inferred from experiment from Reactome).
GO:0032020; Biological process: ISG15-protein conjugation (inferred from direct assay from HGNC).
GO:0051436; Biological process: negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
GO:0051437; Biological process: positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
GO:0016567; Biological process: protein ubiquitination (inferred from direct assay from UniProtKB).
GO:0051246; Biological process: regulation of protein metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR016135; UBQ-conjugat/RWD-like.
IPR000608; UBQ-conjugat_E2.
Graphical view of domain structure.
Gene3D G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
PANTHER PTHR11621; UBQ-conjugat_E2; 1.
Pfam PF00179; UQ_con; 1.
Pfam graphical view of domain structure.
ProDom PD000461; UBQ_conjugat; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00212; UBCc; 1.
SMART graphical view of domain structure.
PROSITE PS00183; UBIQUITIN_CONJUGAT_1; 1.
PS50127; UBIQUITIN_CONJUGAT_2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet P51965.
Genome annotation databases
Ensembl ENSG00000170142; Homo sapiens. [Contig view]
GeneID 7324; -.
KEGG hsa:7324; -.
Phylogenomic databases
HOGENOM P51965; -.
HOVERGEN P51965; -.
Other
LinkHub P51965; -.
NextBio 28656; -.
SOURCE UBE2E1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Ligase; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   193  193     Ubiquitin-conjugating enzyme E2 E1. PRO_0000082470
COMPBIAS   9    18  10     Poly-Ser. 
ACT_SITE   131   131        Glycyl thioester intermediate (By similarity). 
HELIX   22    24  3      
HELIX   42    61  20      
STRAND   67    74  8      
STRAND   78    82  5      
STRAND   95   101  7      
TURN   104   108  5      
STRAND   112   117  6      
HELIX   133   135  3      
TURN   136   138  3      
HELIX   145   157  13      
HELIX   167   175  9      
HELIX   177   191  15      
Sequence information
Length: 193 AA [This is the length of the unprocessed precursor] Molecular weight: 21404 Da [This is the MW of the unprocessed precursor] CRC64: 2FBC50BE2A6A0008 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MSDDDSRAST SSSSSSSSNQ QTEKETNTPK KKESKVSMSK NSKLLSTSAK RIQKELADIT 

        70         80         90        100        110        120 
LDPPPNCSAG PKGDNIYEWR STILGPPGSV YEGGVFFLDI TFTPEYPFKP PKVTFRTRIY 

       130        140        150        160        170        180 
HCNINSQGVI CLDILKDNWS PALTISKVLL SICSLLTDCN PADPLVGSIA TQYMTNRAEH 

       190 
DRMARQWTKR YAT
P51965 in FASTA format

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