Reviewed, UniProtKB/Swiss-Prot P53861 (ELOA1_YEAST)

Names and origin

Protein names

Recommended name:
    Elongin-A

Gene names

Name:	ELA1
Ordered Locus Names:	YNL230C
ORF Names:	N1161

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	379 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Subunit structure	Forms a complex with SKP1-like protein ELC1.
Miscellaneous	Present with 815 molecules/cell in log phase SD medium. Ref.5 In contrast to other members of the family it does not integrate a functional E3 ubiquitin complex.
Sequence similarities	Belongs to the ELA1 family. Contains 1 F-box domain.

Ontologies

Keywords
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein ubiquitination during ubiquitin-dependent protein catabolic process Inferred from mutant phenotype. Source: SGD regulation of transcription Inferred from electronic annotation. Source: InterPro
Cellular component	Cul3-RING ubiquitin ligase complex Inferred from mutant phenotype. Source: SGD integral to membrane Inferred from electronic annotation. Source: InterPro nucleus Inferred from electronic annotation. Source: InterPro
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HAT1	Q12341	1	EBI-29191,EBI-8176

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 379	379	Elongin-A		PRO_0000203386
Regions
	Domain	19 – 63	45	F-box
	Region	1 – 143	143	ELC1-binding
Amino acid modifications
	Modified residue	278	1	Phosphoserine Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P53861-1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 293F68C0AC709889	FASTA	379	43,981
	10 20 30 40 50 60 MKSLQTLCEI SLMRNHSNIQ SVSNVPYHLL KRILQKVKIP QLLKLEKSNV LLIFDDDELW 70 80 90 100 110 120 LEFLRQDFPT NVHEQFVSKR DIICKYYFDF VKENDIELYH SNQDLLKSCV RQSVVKDIRN 130 140 150 160 170 180 NKYRIPYRML YSKYQQEVEK KQEESAERLR LEMQKLQQER EKKQTIVVDH TVYFKKRNTK 190 200 210 220 230 240 KTTRLHNEPH SQLYMKSLKD HESRLKHFKD GGFNIAKRHA QRVAFGGQAG GQSSSPKKGP 250 260 270 280 290 300 LSIKPEPVKV NRQMDNVTAE KKDVTQPITP VKKRRSESPS IFLNRKKPAL FRPTPKTNAA 310 320 330 340 350 360 GSRPHTTAIT NDHRTTSHPY PHKDVVTSIS SVTANPVTKG HKKKKSGIFV RNAGSDGDSF 370 PHVTATGPTT RPYIYEPRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The DNA sequence of cosmid 14-5 from chromosome XIV reveals 21 open reading frames including a novel gene encoding a globin-like domain." Pandolfo D., de Antoni A., Lanfranchi G., Valle G. Yeast 12:1071-1076(1996) [PubMed: 8896273] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications." Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J. , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J. Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"Binding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin C." Botuyan M.V., Koth C.M., Mer G., Chakrabartty A., Conaway J.W., Conaway R.C., Edwards A.M., Arrowsmith C.H., Chazin W.J. Proc. Natl. Acad. Sci. U.S.A. 96:9033-9038(1999) [PubMed: 10430890] [Abstract] Cited for: INTERACTION WITH ELC1.
[4]	"Elongin from Saccharomyces cerevisiae." Koth C.M., Botuyan M.V., Moreland R.J., Jansma D.B., Conaway J.W., Conaway R.C., Chazin W.J., Friesen J.D., Arrowsmith C.H., Edwards A.M. J. Biol. Chem. 275:11174-11180(2000) [PubMed: 10753924] [Abstract] Cited for: IDENTIFICATION OF THE ELA1-ELC1 COMPLEX.
[5]	"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].
[6]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z69381 Genomic DNA. Translation: CAA93368.1. Z71506 Genomic DNA. Translation: CAA96135.1.
PIR	S63196.
RefSeq	NP_014169.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4281N.
IntAct	P53861. 32 interactions.
Proteomic databases
PeptideAtlas	P53861.
PRIDE	P53861.
Genome annotation databases
Ensembl	YNL230C. Saccharomyces cerevisiae. [Contig view]
GeneID	855491.
GenomeReviews	Gene locus YNL230C in contig Y13139_GR.
KEGG	sce:YNL230C.
NMPDR	fig|4932.3.peg.5234.
Organism-specific databases
CYGD	YNL230c.
SGD	S000005174. ELA1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P53861.
OMA	P53861. NTSPVRH.
Gene expression databases
GermOnline	YNL230C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001810. F-box. IPR010684. RNA_pol_II_trans_fac_SIII_A. [Graphical view]
Pfam	PF06881. Elongin_A. 1 hit. [Graphical view]
PROSITE	PS50181. FBOX. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	979475.

Entry information

Entry name

ELOA1_YEAST

Accession

Primary (citable) accession number: P53861

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)