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P14682 (UBC3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2-34 kDa

EC=6.3.2.19
Alternative name(s):
Cell division control protein 34
E3 ubiquitin ligase complex SCF subunit CDC34
Ubiquitin carrier protein
Ubiquitin-protein ligase
Gene names
Name:CDC34
Synonyms:DNA6, UBC3
Ordered Locus Names:YDR054C
ORF Names:D4211, YD9609.08C
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the covalent attachment of ubiquitin to other proteins. Capable, in vitro, to ubiquitinate histone H2A. Ref.1 Ref.5 Ref.6

Mediates the initiation of DNA replication (transition of G1 to S phase in cell cycle). Essential component of the E3 ubiquitin ligase complex SCF (SKP1-CUL1-F-box protein), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Involved in the regulation of methionine biosynthesis genes and in the degradation of CDC6 together with CDC4 and CDC53. Ref.1 Ref.5 Ref.6

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with CDC53. Component of the E3 ubiquitin ligase complexes SCF with CDC53, SKP1/CBF3D, HRT1 and some F-box proteins like MET30 and CDC4. Ref.6 Ref.7

Subcellular location

Cytoplasm. Nucleus Ref.8.

Domain

The acidic C-terminal extension is essential for the cell cycle function.

Miscellaneous

Present with 8170 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA replication
Ubl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

G1/S transition of mitotic cell cycle

Traceable author statement PubMed 9346231. Source: SGD

G2/M transition of mitotic cell cycle

Inferred from genetic interaction PubMed 7954792PubMed 9736614. Source: SGD

SCF-dependent proteasomal ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 9346238PubMed 9346239. Source: SGD

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

protein autoubiquitination

Inferred from direct assay PubMed 8383676. Source: SGD

protein polyubiquitination

Inferred from direct assay PubMed 1848239. Source: SGD

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from direct assay PubMed 9346238PubMed 9346239. Source: SGD

   Cellular_componentSCF ubiquitin ligase complex

Inferred from direct assay PubMed 9346238. Source: SGD

cytoplasm

Inferred from direct assay PubMed 11080155. Source: SGD

nucleus

Inferred from direct assay PubMed 11080155PubMed 8164658. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.6. Source: IntAct

protein homodimerization activity

Inferred from direct assay PubMed 7929378. Source: SGD

ubiquitin-protein transferase activity

Inferred from direct assay Ref.1. Source: SGD

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CDC53Q120183EBI-19730,EBI-4321

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295Ubiquitin-conjugating enzyme E2-34 kDa
PRO_0000082541

Regions

Compositional bias191 – 28999Asp/Glu-rich (acidic)

Sites

Active site951Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue1861Phosphoserine Ref.10
Modified residue2821Phosphoserine Ref.11
Modified residue2921Phosphoserine Ref.10

Sequences

Sequence LengthMass (Da)Tools
P14682 [UniParc].

Last modified April 1, 1990. Version 1.
Checksum: 1CE3E0C3AB1436DC

FASTA29534,065
        10         20         30         40         50         60 
MSSRKSTASS LLLRQYRELT DPKKAIPSFH IELEDDSNIF TWNIGVMVLN EDSIYHGGFF 

        70         80         90        100        110        120 
KAQMRFPEDF PFSPPQFRFT PAIYHPNVYR DGRLCISILH QSGDPMTDEP DAETWSPVQT 

       130        140        150        160        170        180 
VESVLISIVS LLEDPNINSP ANVDAAVDYR KNPEQYKQRV KMEVERSKQD IPKGFIMPTS 

       190        200        210        220        230        240 
ESAYISQSKL DEPESNKDMA DNFWYDSDLD DDENGSVILQ DDDYDDGNNH IPFEDDDVYN 

       250        260        270        280        290 
YNDNDDDDER IEFEDDDDDD DDSIDNDSVM DRKQPHKAED ESEDVEDVER VSKKI 

« Hide

References

« Hide 'large scale' references
[1]"The yeast cell cycle gene CDC34 encodes a ubiquitin-conjugating enzyme."
Goebl M.G., Yochem J., Jentsch S., McGrath J.P., Varshavsky A., Byers B.
Science 241:1331-1335(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"Nucleotide sequence analysis of a 32,500 bp region of the right arm of Saccharomyces cerevisiae chromosome IV."
Brandt P., Ramlow S., Otto B., Bloecker H.
Yeast 12:85-90(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
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. expand/collapse author list , 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.
Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"The Cdc4/34/53 pathway targets Cdc6p for proteolysis in budding yeast."
Drury L.S., Perkins G., Diffley J.F.
EMBO J. 16:5966-5976(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Cdc53 is a scaffold protein for multiple Cdc34/Skp1/F-box protein complexes that regulate cell division and methionine biosynthesis in yeast."
Patton E.E., Willems A.R., Sa D., Kuras L., Thomas D., Craig K.L., Tyers M.
Genes Dev. 12:692-705(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[7]"Cdc53/cullin and the essential Hrt1 RING-H2 subunit of SCF define a ubiquitin ligase module that activates the E2 enzyme Cdc34."
Seol J.H., Feldman R.M.R., Zachariae W., Shevchenko A., Correll C.C., Lyapina S., Chi Y., Galova M., Claypool J., Sandmeyer S., Nasmyth K., Shevchenko A., Deshaies R.J.
Genes Dev. 13:1614-1626(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HRT1.
[8]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[10]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND SER-292, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-282, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M21877 Genomic DNA. Translation: AAA35188.1.
X84162 Genomic DNA. Translation: CAA58970.1.
Z74350 Genomic DNA. Translation: CAA98872.1.
Z49209 Genomic DNA. Translation: CAA89083.1.
BK006938 Genomic DNA. Translation: DAA11900.1.
PIRA41241.
RefSeqNP_010339.1. NM_001180362.1.

3D structure databases

ProteinModelPortalP14682.
SMRP14682. Positions 7-167.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32107. 181 interactions.
DIPDIP-1618N.
IntActP14682. 6 interactions.
MINTMINT-398866.
STRING4932.YDR054C.

Proteomic databases

MaxQBP14682.
PaxDbP14682.
PeptideAtlasP14682.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR054C; YDR054C; YDR054C.
GeneID851624.
KEGGsce:YDR054C.

Organism-specific databases

CYGDYDR054c.
SGDS000002461. CDC34.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00730000113586.
HOGENOMHOG000233454.
KOK02207.
OMAHKAEDES.
OrthoDBEOG7SBP18.

Enzyme and pathway databases

BioCycYEAST:G3O-29663-MONOMER.
UniPathwayUPA00143.

Gene expression databases

GenevestigatorP14682.

Family and domain databases

Gene3D3.10.110.10. 2 hits.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio969160.
PROP14682.

Entry information

Entry nameUBC3_YEAST
AccessionPrimary (citable) accession number: P14682
Secondary accession number(s): D6VS40
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 9, 2014
This is version 153 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome IV

Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways