Reviewed, UniProtKB/Swiss-Prot P14682 (UBC3_YEAST)

Names and origin

Protein names

Recommended name:
    Ubiquitin-conjugating enzyme E2-34 kDa
    EC=6.3.2.19
Alternative name(s):
    Ubiquitin-protein ligase
    Ubiquitin carrier protein
    Cell division control protein 34
    E3 ubiquitin ligase complex SCF subunit CDC34

Gene names

Name:	CDC34
Synonyms:	DNA6, UBC3
Ordered Locus Names:	YDR054C
ORF Names:	YD9609.08C, D4211

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	295 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.4 Ref.5 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.4 Ref.5
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.5 Ref.6
Subcellular location	Cytoplasm. Nucleus. Ref.7
Domain	The acidic C-terminal extension is essential for the cell cycle function.
Miscellaneous	Present with 8170 molecules/cell in log phase SD medium. Ref.8
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA replication Ubl conjugation pathway
Cellular component	Cytoplasm Nucleus
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	DNA replication Inferred from electronic annotation. Source: UniProtKB-KW G1/S transition of mitotic cell cycle Traceable author statement. Source: SGD G2/M transition of mitotic cell cycle Inferred from genetic interaction. Source: SGD SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from direct assay. Source: SGD cell division Inferred from electronic annotation. Source: UniProtKB-KW protein autoubiquitination Inferred from direct assay. Source: SGD protein polyubiquitination Inferred from direct assay. Source: SGD protein ubiquitination during ubiquitin-dependent protein catabolic process Inferred from direct assay. Source: SGD regulation of protein metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	SCF ubiquitin ligase complex Inferred from direct assay. Source: SGD cytoplasm Inferred from direct assay. Source: SGD nucleus Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein homodimerization activity Inferred from direct assay. Source: SGD ubiquitin-protein ligase activity Ref.1 Inferred from direct assay. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDC53	Q12018	1	EBI-19730,EBI-4321

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 295	295	Ubiquitin-conjugating enzyme E2-34 kDa		PRO_0000082541
Regions
	Compositional bias	191 – 289	99	Asp/Glu-rich (acidic)
Sites
	Active site	95	1	Glycyl thioester intermediate By similarity
Amino acid modifications
	Modified residue	10	1	Phosphoserine Ref.9
	Modified residue	182	1	Phosphoserine Ref.9
	Modified residue	186	1	Phosphoserine Ref.9
	Modified residue	188	1	Phosphoserine Ref.9
	Modified residue	292	1	Phosphoserine Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P14682-1 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: 1CE3E0C3AB1436DC	FASTA	295	34,065
	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

References

	« Hide 'large scale' referencesShow '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: 2842867] [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: 8789263] [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: 9169867] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	"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: 9312054] [Abstract] Cited for: FUNCTION.
[5]	"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: 9499404] [Abstract] Cited for: FUNCTION, SUBUNIT.
[6]	"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: 10385629] [Abstract] Cited for: INTERACTION WITH HRT1.
[7]	"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: 14562095] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-182; SER-186; SER-188 AND SER-292, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M21877 Genomic DNA. Translation: AAA35188.1. X84162 Genomic DNA. Translation: CAA58970.1. Z74350 Genomic DNA. Translation: CAA98872.1. Z49209 Genomic DNA. Translation: CAA89083.1.
PIR	A41241.
RefSeq	NP_010339.1.
3D structure databases
HSSP	HSSP built from PDB template 1PZV based on UniProtKB P34477.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1618N.
IntAct	P14682. 5 interactions.
Proteomic databases
PeptideAtlas	P14682.
Genome annotation databases
Ensembl	YDR054C. Saccharomyces cerevisiae. [Contig view]
GeneID	851624.
GenomeReviews	Gene locus YDR054C in contig Z71256_GR.
KEGG	sce:YDR054C.
NMPDR	fig|4932.3.peg.1084.
Organism-specific databases
CYGD	YDR054c.
SGD	S000002461. CDC34.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P14682.
OMA	P14682. CISILHQ.
Enzyme and pathway databases
BRENDA	6.3.2.19. 250.
Gene expression databases
ArrayExpress	P14682.
GermOnline	YDR054C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR016135. UBQ-conjugat/RWD-like. IPR000608. UBQ-conjugat_E2. [Graphical view]
Gene3D	G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.
Pfam	PF00179. UQ_con. 1 hit. [Graphical view]
ProDom	PD000461. UBQ_conjugat. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00212. UBCc. 1 hit. [Graphical view]
PROSITE	PS00183. UBIQUITIN_CONJUGAT_1. 1 hit. PS50127. UBIQUITIN_CONJUGAT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	969160.

Entry information

Entry name

UBC3_YEAST

Accession

Primary (citable) accession number: P14682

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	June 16, 2009
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)