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UniProtKB/Swiss-Prot entry P52490


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

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Entry information
Entry name UBC13_YEAST
Primary accession number P52490
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 76)
Name and origin of the protein
Protein name Ubiquitin-conjugating enzyme E2 13
Synonyms EC 6.3.2.19
Ubiquitin-protein ligase 13
Ubiquitin carrier protein 13
Gene name
Name: UBC13
OrderedLocusNames: YDR092W
ORFNames: YD6652.04
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 200912 / DF5;
DOI=10.1074/jbc.271.5.2789; PubMed=8576256 [NCBI, ExPASy, EBI, Israel, Japan]
Matuschewski K., Hauser H.P., Treier M., Jentsch S.;
"Identification of a novel family of ubiquitin-conjugating enzymes with distinct amino-terminal extensions.";
J. Biol. Chem. 271:2789-2794(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204511 / S288c / AB972;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[4]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MMS2, AND MUTAGENESIS OF GLU-55.
DOI=10.1016/S0092-8674(01)00387-7; PubMed=11440714 [NCBI, ExPASy, EBI, Israel, Japan]
VanDemark A.P., Hofmann R.M., Tsui C., Pickart C.M., Wolberger C.;
"Molecular insights into polyubiquitin chain assembly: crystal structure of the Mms2/Ubc13 heterodimer.";
Cell 105:711-720(2001).
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
X99443; CAA67806.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z50111; CAA90451.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S58092; S58092.
RefSeq NP_010377.1; -.
3D structure databases
PDB
1JAT; X-ray; 1.60 A; A=2-153.[ExPASy / RCSB / EBI]
1JBB; X-ray; 2.00 A; A/B=1-153.[ExPASy / RCSB / EBI]
2GMI; X-ray; 2.50 A; A=1-152.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1JAT; -.
1JBB; -.
2GMI; -.
ModBase P52490.
Protein-protein interaction databases
DIP DIP:5486N; -.
IntAct P52490; -.
Organism-specific databases
CYGD YDR092w; -.
SGD S000002499; UBC13.
Yeast-GFP YDR092W.
Gene expression databases
ArrayExpress P52490; -.
GermOnline YDR092W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from SGD).
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0031371; Cellular component: ubiquitin conjugating enzyme complex (inferred from physical interaction from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006301; Biological process: postreplication repair (inferred from genetic interaction from SGD).
GO:0006513; Biological process: protein monoubiquitination (traceable author statement from SGD).
GO:0000209; Biological process: protein polyubiquitination (inferred from direct assay from SGD).
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 P52490.
Proteomic databases
PeptideAtlas P52490; -.
Genome annotation databases
Ensembl YDR092W; Saccharomyces cerevisiae. [Contig view]
GeneID 851666; -.
GenomeReviews Z71256_GR; YDR092W.
KEGG sce:YDR092W; -.
NMPDR fig|4932.3.peg.1123; -.
Phylogenomic databases
HOGENOM P52490; -.
Other
LinkHub P52490; -.
ProtoNet P52490.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Ligase; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   153  153     Ubiquitin-conjugating enzyme E2 13. PRO_0000082565
ACT_SITE   87    87        Glycyl thioester intermediate. 
MUTAGEN   55    55        E->A: Strongly reduces MMS2 binding and interferes with error-free DNA repair. 
MUTAGEN   81    81        D->R: Abolishes ubiquitin chain elongation. No effect on thioester formation at the active site. 
MUTAGEN   110   110        A->R: Lowers rate of ubiquitin chain elongation. No effect on thioester formation at the active site. 
HELIX   6    17  12      
STRAND   23    28  6      
STRAND   31    40  10      
TURN   46    49  4      
STRAND   50    57  8      
TURN   60    64  5      
STRAND   68    71  4      
HELIX   89    91  3      
TURN   92    94  3      
HELIX   101   113  13      
HELIX   126   131  6      
HELIX   133   147  15      
STRAND   148   150  3      
Sequence information
Length: 153 AA [This is the length of the unprocessed precursor] Molecular weight: 17468 Da [This is the MW of the unprocessed precursor] CRC64: 445558F8F193275B [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASLPKRIIK ETEKLVSDPV PGITAEPHDD NLRYFQVTIE GPEQSPYEDG IFELELYLPD 

        70         80         90        100        110        120 
DYPMEAPKVR FLTKIYHPNI DRLGRICLDV LKTNWSPALQ IRTVLLSIQA LLASPNPNDP 

       130        140        150 
LANDVAEDWI KNEQGAKAKA REWTKLYAKK KPE 

P52490 in FASTA format

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