Ribosome biogenesis protein RLP7 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Contribute

Send feedback

Read comments (?) or add your own

P40693 (RLP7_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Ribosome biogenesis protein RLP7

Alternative name(s):
Ribosomal protein L7-like

Gene names

Name:	RLP7
Synonyms:	RPL7
Ordered Locus Names:	YNL002C
ORF Names:	N2014

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	322 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the biogenesis of the 60S ribosomal subunit. May act as a specificity factor that binds precursor rRNAs and tethers the enzymes that carry out the early 5' to 3' exonucleolytic reactions that generate the mature rRNAs. Ref.8
Subcellular location	Nucleus › nucleolus Ref.8.
Miscellaneous	Present with 7720 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the ribosomal protein L30P family.

Ontologies

Keywords
Biological process	Ribosome biogenesis
Cellular component	Nucleus
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	exonucleolytic trimming to generate mature 5'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Inferred from mutant phenotype Ref.8. Source: SGD maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Inferred from mutant phenotype Ref.8. Source: SGD
Cellular_component	nucleolus Inferred from direct assay Ref.8. Source: SGD preribosome, large subunit precursor Inferred from direct assay PubMed 11583614 PubMed 17443350. Source: SGD
Molecular_function	rRNA binding Inferred from sequence or structural similarity Ref.8. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
CIC1	P38779	1	EBI-15415,EBI-24538
EBP2	P36049	1	EBI-15415,EBI-6289
PWP1	P21304	1	EBI-15415,EBI-14328
RRP5	Q05022	1	EBI-15415,EBI-16011
UBP10	P53874	1	EBI-15415,EBI-19873

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 322

322

Ribosome biogenesis protein RLP7

PRO_0000104658

Amino acid modifications

Modified residue

Phosphoserine Ref.12

Modified residue

120

Phosphothreonine Ref.10 Ref.12

Modified residue

278

Phosphoserine Ref.11 Ref.12

Sequences

Sequence

Length

Mass (Da)

Tools

P40693 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 64714DDFAFB90B5D
Show »

FASTA

322

36,559

        10         20         30         40         50         60 
MSSTQDSKAQ TLNSNPEILL RKRRNADRTR IERQELAKKK REEQIKKKRS NKNKFVRAES 

        70         80         90        100        110        120 
IVAKTLATSR EKERIKRVSI LEDKKAKNET QHIASGKDFI LKITEKANGA EENSVDLEET 

       130        140        150        160        170        180 
EEEEDDGLIR EKTTYDGKPA LLFIVRVRGP LAVNIPNKAF KILSLLRLVE TNTGVFVKLT 

       190        200        210        220        230        240 
KNVYPLLKVI APYVVIGKPS LSSIRSLIQK RGRIIYKGEN EAEPHEIVLN DNNIVEEQLG 

       250        260        270        280        290        300 
DHGIICVEDI IHEIATMGES FSVCNFFLQP FKLNREVSGF GSLNRLRKIK QREAESRTRQ 

       310        320 
FSNAATAPVI EVDIDSLLAK LN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two yeast chromosomes are related by a fossil duplication of their centromeric regions." Lalo D., Stettler S., Mariotte S., Slonimski P.P., Thuriaux P. C. R. Acad. Sci. III, Sci. Vie 316:367-373(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / GRF88.
[2]	"Two distinct yeast proteins are related to the mammalian ribosomal polypeptide L7." Lalo D., Mariotte S., Thuriaux P. Yeast 9:1085-1091(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / GRF88.
[3]	"Organization of the centromeric region of chromosome XIV in Saccharomyces cerevisiae." Lalo D., Stettler S., Mariotte S., Gendreau E., Thuriaux P. Yeast 10:523-533(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: S288c / GRF88.
[4]	"Nucleotide sequence analysis of an 8887 bp region of the left arm of yeast chromosome XIV, encompassing the centromere sequence." Verhasselt P., Aert R., Voet M., Volckaert G. Yeast 10:945-951(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[6]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[7]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[8]	"A nucleolar protein related to ribosomal protein L7 is required for an early step in large ribosomal subunit biogenesis." Dunbar D.A., Dragon F., Lee S.J., Baserga S.J. Proc. Natl. Acad. Sci. U.S.A. 97:13027-13032(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[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]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-120, MASS SPECTROMETRY. Strain: ADR376.
[11]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, MASS SPECTROMETRY.
[12]	"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-14; THR-120 AND SER-278, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L19167 Genomic DNA. Translation: AAA34982.1. X77114 Genomic DNA. Translation: CAA54376.1. Z71278 Genomic DNA. Translation: CAA95861.1. AY693031 Genomic DNA. Translation: AAT93050.1. BK006947 Genomic DNA. Translation: DAA10541.1.
PIR	S38194.
RefSeq	NP_014396.3. NM_001182841.3.
3D structure databases
ProteinModelPortal	P40693.
SMR	P40693. Positions 84-321.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6476N.
IntAct	P40693. 31 interactions.
MINT	MINT-616491.
STRING	4932.YNL002C.
Proteomic databases
PaxDb	P40693.
PeptideAtlas	P40693.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YNL002C; YNL002C; YNL002C.
GeneID	855730.
KEGG	sce:YNL002C. sce:YNR007C.
Organism-specific databases
CYGD	YNL002c.
SGD	S000004947. RLP7.
Phylogenomic databases
eggNOG	COG1841.
HOGENOM	HOG000170917.
KO	K02937. K08343.
OMA	PFKLNRE.
OrthoDB	EOG48PQVC.
Gene expression databases
Genevestigator	P40693.
GermOnline	YNL002C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.30.1390.20. 2 hits.
InterPro	IPR018038. Ribosomal_L30_CS. IPR016082. Ribosomal_L30_ferredoxin-like. [Graphical view]
Pfam	PF00327. Ribosomal_L30. 1 hit. [Graphical view]
SUPFAM	SSF55129. Ribosomal_L30. 1 hit.
PROSITE	PS00634. RIBOSOMAL_L30. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	980111.

Entry information

Entry name

RLP7_YEAST

Accession

Primary (citable) accession number: P40693
Secondary accession number(s): D6W1H5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

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

Ribosomal proteins

Ribosomal proteins families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents