Replication factor A protein 2 - Saccharomyces cerevisiae (Baker's yeast)

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Reviewed, UniProtKB/Swiss-Prot P26754 (RFA2_YEAST)

Last modified November 24, 2009. Version 90. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Replication factor A protein 2
      Short name=RF-A protein 2
Alternative name(s):
    Replication protein A 36 kDa subunit
    DNA-binding protein BUF1

Gene names

Name:	RFA2
Synonyms:	BUF1
Ordered Locus Names:	YNL312W
ORF Names:	N0368

Organism

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

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	273 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Binds to single-stranded sequences participating in DNA replication in addition to those mediating transcriptional repression (URS1) and activation (CAR1). Stimulates the activity of a cognate strand exchange protein (SEP1). It cooperates with T-AG and DNA topoisomerase I to unwind template DNA containing the simian virus 40 origin of DNA replication.
Subunit structure	Heterotrimer of 69, 36, and 13 kDa chains. The DNA-binding activity may reside exclusively on the 69 kDa subunit. Interacts with MCM10. Ref.6
Subcellular location	Nucleus.
Post-translational modification	Phosphorylated in a cell-cycle-dependent manner (from the S phase until mitosis). Ref.7 Ref.8 Ref.9 Ref.10 The N-terminus is blocked.
Miscellaneous	Present with 6080 molecules/cell in log phase SD medium. Ref.5

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Ontologies

Keywords
Biological process	DNA replication
Cellular component	Nucleus
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA unwinding during replication Inferred from direct assay. Source: SGD double-strand break repair via homologous recombination Inferred from genetic interaction. Source: SGD establishment of protein localization Inferred from mutant phenotype. Source: SGD heteroduplex formation Inferred from direct assay. Source: SGD nucleotide-excision repair Inferred from direct assay. Source: SGD protein ubiquitination Inferred from physical interaction. Source: SGD reciprocal meiotic recombination Inferred from physical interaction. Source: SGD telomere maintenance via recombination Inferred from physical interaction. Source: SGD telomere maintenance via telomerase Inferred from mutant phenotype. Source: SGD
Cellular component	DNA replication factor A complex Inferred from direct assay. Source: SGD chromosome, telomeric region Inferred from mutant phenotype. Source: SGD condensed nuclear chromosome Inferred from direct assay. Source: SGD
Molecular function	double-stranded DNA binding Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct sequence-specific DNA binding Inferred from direct assay. Source: SGD single-stranded DNA binding Inferred from direct assay. Source: SGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
RNR1	P21524	1	EBI-14976,EBI-15234
RNR2	P09938	1	EBI-14976,EBI-15240

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 273

273

Replication factor A protein 2

PRO_0000097275

Regions

Compositional bias

1 – 30

Gly/Ser-rich

Amino acid modifications

Modified residue

Phosphoserine Ref.10

Modified residue

120

Phosphotyrosine Ref.10

Modified residue

122

Phosphoserine Ref.7 Ref.8 Ref.10

Modified residue

189

Phosphoserine Ref.9 Ref.10

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Sequences

Sequence

Length

Mass (Da)

Tools

P26754-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: F6087501E4E28CC1
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FASTA

273

29,936

        10         20         30         40         50         60 
MATYQPYNEY SSVTGGGFEN SESRPGSGES ETNTRVNTLT PVTIKQILES KQDIQDGPFV 

        70         80         90        100        110        120 
SHNQELHHVC FVGVVRNITD HTANIFLTIE DGTGQIEVRK WSEDANDLAA GNDDSSGKGY 

       130        140        150        160        170        180 
GSQVAQQFEI GGYVKVFGAL KEFGGKKNIQ YAVIKPIDSF NEVLTHHLEV IKCHSIASGM 

       190        200        210        220        230        240 
MKQPLESASN NNGQSLFVKD DNDTSSGSSP LQRILEFCKK QCEGKDANSF AVPIPLISQS 

       250        260        270 
LNLDETTVRN CCTTLTDQGF IYPTFDDNNF FAL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Replication factor-A from Saccharomyces cerevisiae is encoded by three essential genes coordinately expressed at S phase." Brill S.J., Stillman B. Genes Dev. 5:1589-1600(1991) [PubMed: 1885001] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 100-118; 150-172 AND 184-196. Strain: ATCC 208353 / W303-1A.
[2]	"Saccharomyces cerevisiae BUF protein binds to sequences participating in DNA replication in addition to those mediating transcriptional repression (URS1) and activation." Luche R.M., Smart W.C., Marion T., Tillman M., Sumrada R.A., Cooper T.G. Mol. Cell. Biol. 13:5749-5761(1993) [PubMed: 8355713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 5-16.
[3]	"Sequencing analysis of a 24.7 kb fragment of yeast chromosome XIV identifies six known genes, a new member of the hexose transporter family and ten new open reading frames." Maftahi M., Nicaud J.-M., Levesque H., Gaillardin C. Yeast 11:1077-1085(1995) [PubMed: 7502583] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / FY1676.
[4]	"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. Hani J. Nature 387:93-98(1997) [PubMed: 9169873] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[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]	"Mcm10 regulates the stability and chromatin association of DNA polymerase-alpha." Ricke R.M., Bielinsky A.-K. Mol. Cell 16:173-185(2004) [PubMed: 15494305] [Abstract] Cited for: INTERACTION WITH MCM10.
[7]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, MASS SPECTROMETRY.
[8]	"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-122, MASS SPECTROMETRY.
[9]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-189, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; TYR-120; SER-122 AND SER-189, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	X59749 Genomic DNA. Translation: CAA42421.1. S64861 Genomic DNA. Translation: AAB27888.1. Z46259 Genomic DNA. No translation available. Z71588 Genomic DNA. Translation: CAA96241.1.
PIR	B37281.
RefSeq	NP_014087.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2518N.
IntAct	P26754. 15 interactions.
STRING	P26754.
Proteomic databases
PeptideAtlas	P26754.
PRIDE	P26754.
Genome annotation databases
Ensembl	YNL312W; YNL312W; YNL312W; Saccharomyces cerevisiae. [Genome view]
GeneID	855404.
KEGG	sce:YNL312W.
NMPDR	fig\|4932.3.peg.5149.
Organism-specific databases
CYGD	YNL312w.
SGD	S000005256. RFA2.
Phylogenomic databases
HOGENOM	P26754.
OMA	LTPVTIK
OrthoDB	EOG9X3JHM
Gene expression databases
ArrayExpress	P26754.
Genevestigator	P26754.
GermOnline	YNL312W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR012340. NA-bd_OB-fold. IPR016027. NA-bd_OB-fold-like. IPR004365. NA_bd_OB_tRNA-helicase. IPR014646. RPA32. IPR014892. RPA_C. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
Pfam	PF08784. RPA_C. 1 hit. PF01336. tRNA_anti. 1 hit. [Graphical view]
PIRSF	PIRSF036949. RPA32. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	979235.

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Entry information

Entry name

RFA2_YEAST

Accession

Primary (citable) accession number: P26754
Secondary accession number(s): P38905

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	November 24, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

Yeast

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

Yeast chromosome XIV

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

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents