60S ribosomal protein L4-A - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P10664 (RL4A_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 119. 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 L4-A

Alternative name(s):
L2
RP2
YL2

Gene names

Name:	RPL4A
Synonyms:	RPL2, RPL2A
Ordered Locus Names:	YBR031W
ORF Names:	YBR0315

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	362 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	Participates in the regulation of the accumulation of its own mRNA. Ref.5
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). Ref.7
Subcellular location	Cytoplasm Ref.8.
Post-translational modification	N-terminally acetylated by acetyltransferase NatA.
Miscellaneous	There are 2 genes for L4 in yeast.
Sequence similarities	Belongs to the ribosomal protein L4P family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	RNA-binding
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation 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
Cellular_component	cytosolic large ribosomal subunit Traceable author statement Ref.7. Source: SGD
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 362

361

60S ribosomal protein L4-A

PRO_0000129367

Amino acid modifications

Modified residue

N-acetylserine Ref.6

Modified residue

Phosphothreonine Ref.11

Modified residue

176

Phosphoserine Ref.11

Modified residue

200

Phosphothreonine Ref.9

Modified residue

278

Phosphoserine Ref.11

Modified residue

282

Phosphoserine Ref.10 Ref.11

Modified residue

283

Phosphothreonine Ref.11

Modified residue

284

Phosphoserine Ref.10 Ref.11

Modified residue

287

Phosphothreonine Ref.11

Modified residue

293

Phosphoserine Ref.10 Ref.11

Modified residue

297

Phosphoserine Ref.11

Experimental info

Sequence conflict

V → L in AAA34974. Ref.1

Sequence conflict

144

K → T in AAA34974. Ref.1

Sequence conflict

157

E → D in AAA34974. Ref.1

Sequence conflict

224

G → S in AAA34974. Ref.1

Sequence conflict

241

G → S in AAA34974. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P10664 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 37D0942A10AAE89F
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FASTA

362

39,092

        10         20         30         40         50         60 
MSRPQVTVHS LTGEATANAL PLPAVFSAPI RPDIVHTVFT SVNKNKRQAY AVSEKAGHQT 

        70         80         90        100        110        120 
SAESWGTGRA VARIPRVGGG GTGRSGQGAF GNMCRGGRMF APTKTWRKWN VKVNHNEKRY 

       130        140        150        160        170        180 
ATASAIAATA VASLVLARGH RVEKIPEIPL VVSTDLESIQ KTKEAVAALK AVGAHSDLLK 

       190        200        210        220        230        240 
VLKSKKLRAG KGKYRNRRWT QRRGPLVVYA EDNGIVKALR NVPGVETANV ASLNLLQLAP 

       250        260        270        280        290        300 
GAHLGRFVIW TEAAFTKLDQ VWGSETVASS KVGYTLPSHI ISTSDVTRII NSSEIQSAIR 

       310        320        330        340        350        360 
PAGQATQKRT HVLKKNPLKN KQVLLRLNPY AKVFAAEKLG SKKAEKTGTK PAAVFTETLK 


HD

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Ribosomal protein L2 in Saccharomyces cerevisiae is homologous to ribosomal protein L1 in Xenopus laevis. Isolation and characterization of the genes." Presutti C., Lucioli A., Bozzoni I. J. Biol. Chem. 263:6188-6192(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The complete sequence of a 33 kb fragment on the right arm of chromosome II from Saccharomyces cerevisiae reveals 16 open reading frames, including ten new open reading frames, five previously identified genes and a homologue of the SCO1 gene." Smits P.H.M., de Haan M., Maat C., Grivell L.A. Yeast 10:S75-S80(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Complete DNA sequence of yeast chromosome II." Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. Kleine K. EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"The ribosomal protein L2 in S. cerevisiae controls the level of accumulation of its own mRNA." Presutti C., Ciafre S.-A., Bozzoni I. EMBO J. 10:2215-2221(1991) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN L2 MRNA REGULATION.
[6]	"NH2-terminal acetylation of ribosomal proteins of Saccharomyces cerevisiae." Takakura H., Tsunasawa S., Miyagi M., Warner J.R. J. Biol. Chem. 267:5442-5445(1992) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21, ACETYLATION AT SER-2 BY NATA.
[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]	"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-200, MASS SPECTROMETRY.
[10]	"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 SER-282; SER-284 AND SER-293, MASS SPECTROMETRY.
[11]	"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 THR-60; SER-176; SER-278; SER-282; THR-283; SER-284; THR-287; SER-293 AND SER-297, MASS SPECTROMETRY.
[12]	"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 5-260, ELECTRON MICROSCOPY.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X76078 Genomic DNA. Translation: CAA53687.1.
J03195 Genomic DNA. Translation: AAA34974.1.
Z35900 Genomic DNA. Translation: CAA84973.1.
BK006936 Genomic DNA. Translation: DAA07152.1.

PIR

S45887.

RefSeq

NP_009587.1. NM_001178379.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K5Y	model	-	D	5-260	[»]
3IZS	electron microscopy	-	D	1-362	[»]
3O58	X-ray	4.00	D	1-362	[»]
3O5H	X-ray	4.00	D	1-362	[»]
3U5E	X-ray	3.00	C	1-362	[»]
3U5I	X-ray	3.00	C	1-362	[»]
4B6A	electron microscopy	8.10	C	1-362	[»]

ProteinModelPortal

P10664.

SMR

P10664. Positions 2-362.

ModBase

Search...

Protein-protein interaction databases

IntAct

P10664. 208 interactions.

MINT

MINT-1325639.

STRING

4932.YBR031W.

Proteomic databases

PeptideAtlas

P10664.

PRIDE

P10664.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YBR031W; YBR031W; YBR031W.

GeneID

852319.

KEGG

sce:YBR031W.

Organism-specific databases

SGD

S000000235. RPL4A.

Phylogenomic databases

GeneTree

ENSGT00390000018145.

HOGENOM

HOG000107331.

K02930.

OMA

HTNMRKN.

OrthoDB

EOG4GF6PS.

Gene expression databases

Genevestigator

P10664.

GermOnline

YBR031W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

3.40.1370.10. 1 hit.

InterPro

IPR025755. Ribos_L4_C_dom.
IPR002136. Ribosomal_L4/L1e.
IPR013000. Ribosomal_L4/L1e_euk/arc_CS.
IPR023574. Ribosomal_L4_dom.
[Graphical view]

Pfam

PF14374. Ribos_L4_asso_C. 1 hit.
PF00573. Ribosomal_L4. 1 hit.
[Graphical view]

SUPFAM

SSF52166. Ribosomal_L4/L1E. 1 hit.

PROSITE

PS00939. RIBOSOMAL_L1E. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

971014.

Entry information

Entry name

RL4A_YEAST

Accession

Primary (citable) accession number: P10664
Secondary accession number(s): D6VQ32

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 119 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 II

Yeast (Saccharomyces cerevisiae) chromosome II: 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