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UniProtKB/Swiss-Prot entry P62837


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

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Entry information
Entry name UB2D2_HUMAN
Primary accession number P62837
Secondary accession number P51669
Integrated into Swiss-Prot on August 16, 2004
Sequence was last modified on August 16, 2004 (Sequence version 1)
Annotations were last modified on    November 4, 2008 (Entry version 57)
Name and origin of the protein
Protein name Ubiquitin-conjugating enzyme E2 D2
Synonyms EC 6.3.2.19
Ubiquitin-protein ligase D2
Ubiquitin carrier protein D2
Ubiquitin-conjugating enzyme E2-17 kDa 2
E2(17)KB 2
Gene name
Name: UBE2D2
Synonyms: UBC4, UBCH5B
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.270.51.30408; PubMed=8530467 [NCBI, ExPASy, EBI, Israel, Japan]
Jensen J.P., Bates P.W., Yang M., Vierstra R.D., Weissman A.M.;
"Identification of a family of closely related human ubiquitin conjugating enzymes.";
J. Biol. Chem. 270:30408-30414(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7724550 [NCBI, ExPASy, EBI, Israel, Japan]
Rolfe M., Beer-Romero P., Glass S., Eckstein J., Berdo I., Theodoras A., Pagano M., Draetta G.;
"Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP).";
Proc. Natl. Acad. Sci. U.S.A. 92:3264-3268(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
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).
[4]
PROTEIN SEQUENCE OF 73-90, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
[5]
INTERACTION WITH SCF COMPLEX.
DOI=10.1038/sj.onc.1203647; PubMed=10918611 [NCBI, ExPASy, EBI, Israel, Japan]
Strack P., Caligiuri M., Pelletier M., Boisclair M., Theodoras A., Beer-Romero P., Glass S., Parsons T., Copeland R.A., Auger K.R., Benfield P., Brizuela L., Rolfe M.;
"SCF(beta-TRCP) and phosphorylation dependent ubiquitination of I kappa B alpha catalyzed by Ubc3 and Ubc4.";
Oncogene 19:3529-3536(2000).
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
U39317; AAA91460.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L40146; AAC41750.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC033349; AAH33349.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR I59365; I59365.
RefSeq NP_003330.1; -.
NP_862821.1; -.
UniGene Hs.108332
3D structure databases
PDB
1UR6; NMR; -; A=1-147.[ExPASy / RCSB / EBI]
1W4U; NMR; -; A=1-147.[ExPASy / RCSB / EBI]
2C4O; X-ray; 1.94 A; A/B/C/D=1-147.[ExPASy / RCSB / EBI]
2CLW; X-ray; 1.95 A; A/B/C/D=1-147.[ExPASy / RCSB / EBI]
2ESK; X-ray; 1.36 A; A=1-147.[ExPASy / RCSB / EBI]
2ESO; X-ray; 1.50 A; A=1-147.[ExPASy / RCSB / EBI]
2ESP; X-ray; 1.52 A; A=1-147.[ExPASy / RCSB / EBI]
2ESQ; X-ray; 1.44 A; A=1-147.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1UR6; -.
1W4U; -.
2C4O; -.
2CLW; -.
2ESK; -.
2ESO; -.
2ESP; -.
2ESQ; -.
ModBase P62837.
Protein-protein interaction databases
IntAct P62837; -.
Organism-specific databases
H-InvDB HIX0005224; -.
HIX0006636; -.
HIX0019025; -.
HIX0028451; -.
HGNC HGNC:12475; UBE2D2.
GenAtlas UBE2D2.
MIM 602962; gene. [NCBI / EBI]
PharmGKB PA37125; -.
GeneCards P62837.
Gene expression databases
ArrayExpress P62837; -.
CleanEx HS_UBE2D2; -.
GermOnline ENSG00000131508; Homo sapiens.
Ontologies
GO
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:0016567; Biological process: protein ubiquitination (inferred from direct assay from UniProtKB).
GO:0006511; Biological process: ubiquitin-dependent protein catabolic process (traceable author statement from ProtInc).
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 P62837.
ProtoNet P62837.
Genome annotation databases
Ensembl ENSG00000131508; Homo sapiens. [Contig view]
GeneID 7322; -.
KEGG hsa:7322; -.
Phylogenomic databases
HOVERGEN P62837; -.
Other
LinkHub P62837; -.
NextBio 28630; -.
SOURCE UBE2D2; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Ligase; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   147  147     Ubiquitin-conjugating enzyme E2 D2. PRO_0000082462
ACT_SITE   85    85        Glycyl thioester intermediate (By similarity). 
CONFLICT   128   128        K -> Q (in Ref. 2; AAC41750). 
HELIX   1    15  15      
STRAND   19    28  10      
STRAND   32    38  7      
TURN   44    47  4      
STRAND   49    55  7      
TURN   58    61  4      
STRAND   66    71  6      
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: 16735 Da [This is the MW of the unprocessed precursor] CRC64: C942BE7853CBC355 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MALKRIHKEL NDLARDPPAQ CSAGPVGDDM FHWQATIMGP NDSPYQGGVF FLTIHFPTDY 

        70         80         90        100        110        120 
PFKPPKVAFT TRIYHPNINS NGSICLDILR SQWSPALTIS KVLLSICSLL CDPNPDDPLV 

       130        140 
PEIARIYKTD REKYNRIARE WTQKYAM 

P62837 in FASTA format

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