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P14682

- UBC3_YEAST

UniProt

P14682 - UBC3_YEAST

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Protein

Ubiquitin-conjugating enzyme E2-34 kDa

Gene

CDC34

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei95 – 951Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. protein homodimerization activity Source: SGD
  4. ubiquitin-protein transferase activity Source: SGD

GO - Biological processi

  1. cell division Source: UniProtKB-KW
  2. DNA replication Source: UniProtKB-KW
  3. G1/S transition of mitotic cell cycle Source: SGD
  4. G2/M transition of mitotic cell cycle Source: SGD
  5. protein autoubiquitination Source: SGD
  6. protein polyubiquitination Source: SGD
  7. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: SGD
  8. SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Cell division, DNA replication, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29663-MONOMER.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CDC34
Synonyms:DNA6, UBC3
Ordered Locus Names:YDR054C
ORF Names:D4211, YD9609.08C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome IV

Organism-specific databases

CYGDiYDR054c.
SGDiS000002461. CDC34.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. nucleus Source: SGD
  3. SCF ubiquitin ligase complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 295295Ubiquitin-conjugating enzyme E2-34 kDaPRO_0000082541Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei186 – 1861Phosphoserine1 Publication
Modified residuei282 – 2821Phosphoserine1 Publication
Modified residuei292 – 2921Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP14682.
PaxDbiP14682.
PeptideAtlasiP14682.

Expressioni

Gene expression databases

GenevestigatoriP14682.

Interactioni

Subunit structurei

Interacts with CDC53. Component of the E3 ubiquitin ligase complexes SCF with CDC53, SKP1/CBF3D, HRT1 and some F-box proteins like MET30 and CDC4.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC53Q120183EBI-19730,EBI-4321

Protein-protein interaction databases

BioGridi32107. 192 interactions.
DIPiDIP-1618N.
IntActiP14682. 6 interactions.
MINTiMINT-398866.
STRINGi4932.YDR054C.

Structurei

3D structure databases

ProteinModelPortaliP14682.
SMRiP14682. Positions 7-167.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi191 – 28999Asp/Glu-rich (acidic)Add
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
GeneTreeiENSGT00730000113586.
HOGENOMiHOG000233454.
InParanoidiP14682.
KOiK02207.
OMAiHKAEDES.
OrthoDBiEOG7SBP18.

Family and domain databases

Gene3Di3.10.110.10. 2 hits.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P14682 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSRKSTASS LLLRQYRELT DPKKAIPSFH IELEDDSNIF TWNIGVMVLN
60 70 80 90 100
EDSIYHGGFF KAQMRFPEDF PFSPPQFRFT PAIYHPNVYR DGRLCISILH
110 120 130 140 150
QSGDPMTDEP DAETWSPVQT VESVLISIVS LLEDPNINSP ANVDAAVDYR
160 170 180 190 200
KNPEQYKQRV KMEVERSKQD IPKGFIMPTS ESAYISQSKL DEPESNKDMA
210 220 230 240 250
DNFWYDSDLD DDENGSVILQ DDDYDDGNNH IPFEDDDVYN YNDNDDDDER
260 270 280 290
IEFEDDDDDD DDSIDNDSVM DRKQPHKAED ESEDVEDVER VSKKI
Length:295
Mass (Da):34,065
Last modified:April 1, 1990 - v1
Checksum:i1CE3E0C3AB1436DC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA41241.
RefSeqiNP_010339.1. NM_001180362.1.

Genome annotation databases

EnsemblFungiiYDR054C; YDR054C; YDR054C.
GeneIDi851624.
KEGGisce:YDR054C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A41241.
RefSeqi NP_010339.1. NM_001180362.1.

3D structure databases

ProteinModelPortali P14682.
SMRi P14682. Positions 7-167.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32107. 192 interactions.
DIPi DIP-1618N.
IntActi P14682. 6 interactions.
MINTi MINT-398866.
STRINGi 4932.YDR054C.

Proteomic databases

MaxQBi P14682.
PaxDbi P14682.
PeptideAtlasi P14682.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YDR054C ; YDR054C ; YDR054C .
GeneIDi 851624.
KEGGi sce:YDR054C.

Organism-specific databases

CYGDi YDR054c.
SGDi S000002461. CDC34.

Phylogenomic databases

eggNOGi COG5078.
GeneTreei ENSGT00730000113586.
HOGENOMi HOG000233454.
InParanoidi P14682.
KOi K02207.
OMAi HKAEDES.
OrthoDBi EOG7SBP18.

Enzyme and pathway databases

UniPathwayi UPA00143 .
BioCyci YEAST:G3O-29663-MONOMER.

Miscellaneous databases

NextBioi 969160.
PROi P14682.

Gene expression databases

Genevestigatori P14682.

Family and domain databases

Gene3Di 3.10.110.10. 2 hits.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. 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].

Entry informationi

Entry nameiUBC3_YEAST
AccessioniPrimary (citable) accession number: P14682
Secondary accession number(s): D6VS40
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: October 29, 2014
This is version 156 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8170 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3