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UniProtKB/Swiss-Prot entry P51668

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

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Entry information
Entry name UB2D1_HUMAN
Primary accession number P51668
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    July 22, 2008 (Entry version 75)
Name and origin of the protein
Protein name Ubiquitin-conjugating enzyme E2 D1
Synonyms EC 6.3.2.19
Ubiquitin-protein ligase D1
Ubiquitin carrier protein D1
UbcH5
Ubiquitin-conjugating enzyme E2-17 kDa 1
E2(17)KB 1
UBC4/5 homolog
Stimulator of Fe transport
SFT
Gene name
Name: UBE2D1
Synonyms: SFT, UBCH5, UBCH5A
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].
PubMed=8090726 [NCBI, ExPASy, EBI, Israel, Japan]
Scheffner M., Huibregtse J.M., Howley P.M.;
"Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53.";
Proc. Natl. Acad. Sci. U.S.A. 91:8797-8801(1994).
[2]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
DOI=10.1182/blood-2002-07-2192; PubMed=12480712 [NCBI, ExPASy, EBI, Israel, Japan]
Gehrke S.G., Riedel H.-D., Herrmann T., Hadaschik B., Bents K., Veltkamp C., Stremmel W.;
"UbcH5A, a member of human E2 ubiquitin-conjugating enzymes, is closely related to SFT, a stimulator of iron transport, and is up-regulated in hereditary hemochromatosis.";
Blood 101:3288-3293(2003).
[3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Bone marrow, and Skin;
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).
[5]
 NUCLEOTIDE SEQUENCE [MRNA] OF 134-147, AND TISSUE SPECIFICITY.
DOI=10.1083/jcb.139.4.895; PubMed=9362508 [NCBI, ExPASy, EBI, Israel, Japan]
Gutierrez J.A., Yu J., Rivera S., Wessling-Resnick M.;
"Functional expression cloning and characterization of SFT, a stimulator of Fe transport.";
J. Cell Biol. 139:895-905(1997).
[6]
 ERRATUM.
Gutierrez J.A., Yu J., Rivera S., Wessling-Resnick M.;
J. Cell Biol. 147:205-205(1999).
[7]
 SUBUNIT OF A COMPLEX WITH SIAH1; CACYBP; SKP1; APC AND TBL1X.
DOI=10.1016/S1097-2765(01)00242-8; PubMed=11389839 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuzawa S., Reed J.C.;
"Siah-1, SIP, and Ebi collaborate in a novel pathway for beta-catenin degradation linked to p53 responses.";
Mol. Cell 7:915-926(2001).
Comments
  • FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53.
  • CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
  • PATHWAY: Protein modification; protein ubiquitination.
  • SUBUNIT: Component of a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X.
  • TISSUE SPECIFICITY: Ubiquitous. Up-regulated in livers of iron-overloaded patients with hereditary hemochromatosis.
  • SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
  • CAUTION: PubMed:9362508 cloned and sequenced SFT which consisted of UBE2D1 last coding exon along with intronic sequences on the 5'-end of this exon. A function in iron transport has been described.
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
X78140; CAA55019.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF257220; AAM81086.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ272367; CAC82177.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ293565; CAC82097.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007041; AAP35690.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005980; AAH05980.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015997; AAH15997.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF020761; -; NOT_ANNOTATED_CDS; mRNA.[EMBL / GenBank / DDBJ]
PIR I39202; I39202.
RefSeq NP_003329.1; -.
UniGene Hs.129683
3D structure databases
PDB
2C4P; X-ray; 2.35 A; A/B=1-147.[ExPASy / RCSB / EBI]
PDBsum 2C4P; -.
ModBase P51668.
Enzyme and pathway databases
Reactome REACT_152; Cell Cycle, Mitotic.
REACT_1538; Cell Cycle Checkpoints.
REACT_6844; Signaling by TGF beta.
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 HIX0008841; -.
HGNC HGNC:12474; UBE2D1.
GenAtlas UBE2D1.
MIM 602961; gene. [NCBI / EBI]
PharmGKB PA37124; -.
GeneCards P51668.
Gene expression databases
ArrayExpress P51668; -.
CleanEx HS_UBE2D1; -.
GermOnline ENSG00000072401; 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:0031145; Biological process: anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process (inferred from experiment from Reactome).
GO:0030509; Biological process: BMP signaling pathway (inferred from experiment from Reactome).
GO:0051436; Biological process: negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
GO:0031398; Biological process: positive regulation of protein ubiquitination (inferred from direct assay from UniProtKB).
GO:0051437; Biological process: positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
GO:0000209; Biological process: protein polyubiquitination (inferred from direct assay from UniProtKB).
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).
BLOCKS P51668.
Genome annotation databases
Ensembl ENSG00000072401; Homo sapiens. [Contig view]
GeneID 7321; -.
KEGG hsa:7321; -.
Phylogenomic databases
HOGENOM P51668; -.
HOVERGEN P51668; -.
Other
SOURCE UBE2D1; Homo sapiens.
ProtoNet P51668.
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   147  147     Ubiquitin-conjugating enzyme E2 D1. PRO_0000082460
ACT_SITE   85    85        Glycyl thioester intermediate (By similarity). 
HELIX   1    11  11      
TURN   12    15  4      
STRAND   19    26  8      
STRAND   29    38  10      
TURN   44    47  4      
STRAND   49    55  7      
TURN   58    61  4      
STRAND   66    69  4      
HELIX   87    89  3      
TURN   90    92  3      
HELIX   99   111  13      
HELIX   121   129  9      
HELIX   131   145  15      
Sequence information
Length: 147 AA [This is the length of the unprocessed precursor] Molecular weight: 16602 Da [This is the MW of the unprocessed precursor] CRC64: 2E96FD0179EE119D [This is a checksum on the sequence] 
        10         20         30         40         50         60 
MALKRIQKEL SDLQRDPPAH CSAGPVGDDL FHWQATIMGP PDSAYQGGVF FLTVHFPTDY 

        70         80         90        100        110        120 
PFKPPKIAFT TKIYHPNINS NGSICLDILR SQWSPALTVS KVLLSICSLL CDPNPDDPLV 

       130        140 
PDIAQIYKSD KEKYNRHARE WTQKYAM
P51668 in FASTA format

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