60S ribosomal protein L5 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P26321 (RL5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 124. History...

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

Documents (5) |

Third-party data

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

Names and origin

Protein names

Recommended name:
60S ribosomal protein L5

Alternative name(s):
L1
L1a
Ribosomal 5S RNA-binding protein
YL3

Gene names

Name:	RPL5
Synonyms:	RPL1, RPL1A
Ordered Locus Names:	YPL131W
ORF Names:	LPI14W

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	297 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds 5S RNA and is required for 60S subunit assembly.
Subunit structure	Component of the large ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains 32 different proteins (encoded by 56 genes) and 1 molecule of RNA (18S). The 60S subunit contains 46 different proteins (encoded by 81 genes) and 3 molecules of RNA (25S, 5.8S and 5S). Forms a heterotrimeric complex with SYO1 and RPL11A or RPL11B. Interaction of this complex with KAP104 allows the nuclear import of the heterotrimer. Ref.7
Subcellular location	Cytoplasm. Nucleus. Note: The SYO1/RPL11/RPL5 complex is transported into the nucleus by KAP104. Ref.8 Ref.10
Sequence similarities	Belongs to the ribosomal protein L18P family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Ligand	RNA-binding rRNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cytoplasmic translation Traceable author statement Ref.7. Source: SGD ribosomal large subunit assembly Inferred from mutant phenotype Ref.3. Source: SGD
Cellular_component	cytosolic large ribosomal subunit Traceable author statement Ref.7. Source: SGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	5S rRNA binding Inferred from electronic annotation. Source: InterPro RNA binding Inferred from direct assay Ref.3. Source: SGD structural constituent of ribosome Traceable author statement Ref.7. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 297

296

60S ribosomal protein L5

PRO_0000131454

Amino acid modifications

Modified residue

153

Phosphothreonine Ref.11

Modified residue

154

Phosphothreonine Ref.11

Modified residue

155

Phosphothreonine Ref.11 Ref.12

Modified residue

235

Phosphoserine Ref.9 Ref.12

Modified residue

242

Phosphoserine Ref.11

Experimental info

Sequence conflict

T → Y AA sequence Ref.6

Sequence conflict

112

K → R in AAA35234. Ref.1

Sequence conflict

112

K → R in AAA35236. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P26321 [UniParc].

Last modified October 5, 2010. Version 4.
Checksum: 14E3B2931C3CAE2B
Show »

FASTA

297

33,715

        10         20         30         40         50         60 
MAFQKDAKSS AYSSRFQTPF RRRREGKTDY YQRKRLVTQH KAKYNTPKYR LVVRFTNKDI 

        70         80         90        100        110        120 
ICQIISSTIT GDVVLAAAYS HELPRYGITH GLTNWAAAYA TGLLIARRTL QKLGLDETYK 

       130        140        150        160        170        180 
GVEEVEGEYE LTEAVEDGPR PFKVFLDIGL QRTTTGARVF GALKGASDGG LYVPHSENRF 

       190        200        210        220        230        240 
PGWDFETEEI DPELLRSYIF GGHVSQYMEE LADDDEERFS ELFKGYLADD IDADSLEDIY 

       250        260        270        280        290 
TSAHEAIRAD PAFKPTEKKF TKEQYAAESK KYRQTKLSKE ERAARVAAKI AALAGQQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structure of the yeast ribosomal 5 S RNA-binding protein YL3." Tang B., Nazar R.N. J. Biol. Chem. 266:6120-6123(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"Unbalanced regulation of the ribosomal 5 S RNA-binding protein in Saccharomyces cerevisiae expressing mutant 5 S rRNAs." Tang B., Nazar R.N. J. Biol. Chem. 267:17738-17742(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Yeast ribosomal protein L1 is required for the stability of newly synthesized 5S rRNA and the assembly of 60S ribosomal subunits." Deshmukh M.P., Tsay Y.F., Paulovich A.G., Woolford J.L. Jr. Mol. Cell. Biol. 13:2835-2845(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI." Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M. Hani J. Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[6]	"The 5-S RNA binding protein from yeast (Saccharomyces cerevisiae) ribosomes. Evolution of the eukaryotic 5-S RNA binding protein." Nazar R.N., Yaguchi M., Willick G.E., Rollin C.F., Roy C. Eur. J. Biochem. 102:573-582(1979) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-31 AND 219-253.
[7]	"The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae." Planta R.J., Mager W.H. Yeast 14:471-477(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NOMENCLATURE, SUBUNIT.
[8]	"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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[9]	"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 SER-235, MASS SPECTROMETRY. Strain: ADR376.
[10]	"Synchronizing nuclear import of ribosomal proteins with ribosome assembly." Kressler D., Bange G., Ogawa Y., Stjepanovic G., Bradatsch B., Pratte D., Amlacher S., Strauss D., Yoneda Y., Katahira J., Sinning I., Hurt E. Science 338:666-671(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RPL11A; RPL11B AND SYO1, SUBCELLULAR LOCATION.
[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 THR-153; THR-154; THR-155 AND SER-242, MASS SPECTROMETRY.
[12]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-155 AND SER-235, MASS SPECTROMETRY.
[13]	"Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-ribosome and subunit-subunit interactions." Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G., Frank J. Cell 107:373-386(2001) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 11-232, ELECTRON MICROSCOPY.
[14]	"Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation." Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R., Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J. EMBO J. 23:1008-1019(2004) [PubMed] [Europe PMC] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 11-232, ELECTRON MICROSCOPY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M65056 Genomic DNA. Translation: AAA35234.1.
M94864 Genomic DNA. Translation: AAA35236.1.
L01796 Genomic DNA. Translation: AAA34979.1.
U43703 Genomic DNA. Translation: AAB68228.1.
BK006949 Genomic DNA. Translation: DAA11302.1.

PIR

S42144.

RefSeq

NP_015194.1. NM_001183945.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K5Y	model	-	E	11-232	[»]
1S1I	electron microscopy	11.70	E	11-232	[»]
3IZS	electron microscopy	-	Q	1-297	[»]
3O58	X-ray	4.00	E	1-297	[»]
3O5H	X-ray	4.00	E	1-297	[»]
3U5E	X-ray	3.00	D	1-297	[»]
3U5I	X-ray	3.00	D	1-297	[»]
4B6A	electron microscopy	8.10	D	1-297	[»]

ProteinModelPortal

P26321.

SMR

P26321. Positions 2-297.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-1790N.

IntAct

P26321. 159 interactions.

MINT

MINT-412082.

STRING

4932.YPL131W.

Proteomic databases

PaxDb

P26321.

PeptideAtlas

P26321.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YPL131W; YPL131W; YPL131W.

GeneID

855972.

KEGG

sce:YPL131W.

Organism-specific databases

SGD

S000006052. RPL5.

Phylogenomic databases

eggNOG

COG0256.

GeneTree

ENSGT00390000008456.

HOGENOM

HOG000105947.

K02932.

OMA

RQFSQYI.

OrthoDB

EOG4VT966.

Gene expression databases

Genevestigator

P26321.

GermOnline

YPL131W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR005485. Rbsml_L5_euk/L18_arc.
IPR025607. Rbsml_L5e/L18P_C.
IPR005484. Ribosomal_L18/L5.
[Graphical view]

PANTHER

PTHR23410. PTHR23410. 1 hit.

Pfam

PF14204. Ribosomal_L18_c. 1 hit.
PF00861. Ribosomal_L18p. 1 hit.
[Graphical view]

PRINTS

PR00058. RIBOSOMALL5.

ProtoNet

Search...

Other

EvolutionaryTrace

P26321.

NextBio

980789.

Entry information

Entry name

RL5_YEAST

Accession

Primary (citable) accession number: P26321
Secondary accession number(s): D6W3N6

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	October 5, 2010
Last modified:	April 3, 2013
This is version 124 of the entry and version 4 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 XVI

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

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

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