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UniProtKB/Swiss-Prot entry P21734


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

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Entry information
Entry name UBC1_YEAST
Primary accession number P21734
Secondary accession numbers None
Integrated into Swiss-Prot on May 1, 1991
Sequence was last modified on May 1, 1991 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 90)
Name and origin of the protein
Protein name Ubiquitin-conjugating enzyme E2-24 kDa
Synonyms EC 6.3.2.19
Ubiquitin-protein ligase
Ubiquitin carrier protein
Gene name
Name: UBC1
OrderedLocusNames: YDR177W
ORFNames: YD9395.10
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].
PubMed=2265617 [NCBI, ExPASy, EBI, Israel, Japan]
Seufert W., McGrath J.P., Jeutsch S.;
"UBC1 encodes a novel member of an essential subfamily of yeast ubiquitin-conjugating enzymes involved in protein degradation.";
EMBO J. 9:4535-4541(1990).
[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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
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).
[5]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND STRUCTURE BY NMR IN COMPLEX WITH UBIQUITIN.
DOI=10.1016/S0969-2126(01)00657-8; PubMed=11591345 [NCBI, ExPASy, EBI, Israel, Japan]
Hamilton K.S., Ellison M.J., Barber K.R., Williams R.S., Huzil J.T., McKenna S., Ptak C., Glover M., Shaw G.S.;
"Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail.";
Structure 9:897-904(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
X56402; CAA39812.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z46727; CAA86682.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY557675; AAS56001.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S12493; S12493.
RefSeq NP_010462.1; -.
3D structure databases
PDB
1FXT; NMR; -; A=2-150.[ExPASy / RCSB / EBI]
1FZY; X-ray; 1.90 A; A/B=2-150.[ExPASy / RCSB / EBI]
1TTE; NMR; -; A=2-215.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1FXT; -.
1FZY; -.
1TTE; -.
ModBase P21734.
Protein-protein interaction databases
DIP DIP:6594N; -.
IntAct P21734; -.
Organism-specific databases
CYGD YDR177w; -.
SGD S000002584; UBC1.
Yeast-GFP YDR177W.
Gene expression databases
GermOnline YDR177W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0000502; Cellular component: proteasome complex (inferred from physical interaction from SGD).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0004842; Molecular function: ubiquitin-protein ligase activity (inferred from electronic annotation from EC).
GO:0006897; Biological process: endocytosis (traceable author statement from SGD).
GO:0030433; Biological process: ER-associated protein catabolic process (inferred from genetic interaction from SGD).
GO:0006513; Biological process: protein monoubiquitination (traceable author statement from SGD).
GO:0000209; Biological process: protein polyubiquitination (traceable author statement from SGD).
GO:0042787; Biological process: protein ubiquitination during ubiquitin-dependent protein catabolic process (inferred from mutant phenotype from SGD).
GO:0051246; Biological process: regulation of protein metabolic process (inferred from electronic annotation from InterPro).
GO:0006950; Biological process: response to stress (inferred from electronic annotation from UniProtKB-KW).
GO:0009847; Biological process: spore germination (traceable author statement from SGD).
GO:0016050; Biological process: vesicle organization (inferred from mutant phenotype from SGD).
QuickGo view.
Family and domain databases
InterPro IPR015368; UBA_C_fun.
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 PF09288; UBA_3; 1.
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 P21734.
Proteomic databases
PeptideAtlas P21734; -.
Genome annotation databases
Ensembl YDR177W; Saccharomyces cerevisiae. [Contig view]
GeneID 851757; -.
GenomeReviews Z71256_GR; YDR177W.
KEGG sce:YDR177W; -.
NMPDR fig|4932.3.peg.1212; -.
Phylogenomic databases
HOGENOM P21734; -.
Other
LinkHub P21734; -.
NextBio 969525; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Ligase; Stress response; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   215  215     Ubiquitin-conjugating enzyme E2-24 kDa. PRO_0000082525
ACT_SITE   88    88        Glycyl thioester intermediate (By similarity). 
HELIX   3    15  13      
HELIX   18    20  3      
STRAND   22    27  6      
STRAND   32    40  9      
TURN   46    49  4      
STRAND   51    57  7      
TURN   60    63  4      
STRAND   68    73  6      
TURN   82    84  3      
HELIX   90    92  3      
TURN   93    95  3      
HELIX   102   114  13      
HELIX   124   132  9      
HELIX   134   148  15      
HELIX   170   179  10      
HELIX   183   192  10      
HELIX   204   213  10      
Sequence information
Length: 215 AA [This is the length of the unprocessed precursor] Molecular weight: 24178 Da [This is the MW of the unprocessed precursor] CRC64: 899CC397A1285145 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSRAKRIMKE IQAVKDDPAA HITLEFVSES DIHHLKGTFL GPPGTPYEGG KFVVDIEVPM 

        70         80         90        100        110        120 
EYPFKPPKMQ FDTKVYHPNI SSVTGAICLD ILKNAWSPVI TLKSALISLQ ALLQSPEPND 

       130        140        150        160        170        180 
PQDAEVAQHY LRDRESFNKT AALWTRLYAS ETSNGQKGNV EESDLYGIDH DLIDEFESQG 

       190        200        210 
FEKDKIVEVL RRLGVKSLDP NDNNTANRII EELLK 

P21734 in FASTA format

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