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Protein

60S ribosomal protein L4-A

Gene

RPL4A

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Participates in the regulation of the accumulation of its own mRNA.1 Publication

GO - Molecular functioni

  • RNA binding Source: UniProtKB-KW
  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29009-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L4-A
Alternative name(s):
L2
RP2
YL2
Gene namesi
Name:RPL4A
Synonyms:RPL2, RPL2A
Ordered Locus Names:YBR031W
ORF Names:YBR0315
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBR031W.
SGDiS000000235. RPL4A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: SGD
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi95R → E: Leads to a slower growth at higher temperatures but allows RPL4 assembly into the 60S subunit; when associated with E-98. 1 Publication1
Mutagenesisi98R → E: Leads to a slower growth at higher temperatures but allows RPL4 assembly into the 60S subunit; when associated with E-95. 1 Publication1
Mutagenesisi289I → A: Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit; when associated with A-290 and A-295. 1 Publication1
Mutagenesisi290I → A: Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit; when associated with A-289 and A-295. 1 Publication1
Mutagenesisi295I → A: Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit; when associated with A-289 and A-290. 1 Publication1
Mutagenesisi314K → A: Significantly diminished nuclear localization; when associated with A-315 and A-319. 1 Publication1
Mutagenesisi315K → A: Significantly diminished nuclear localization; when associated with A-314 and A-319. 1 Publication1
Mutagenesisi319K → A: Significantly diminished nuclear localization; when associated with A-314 and A-315. 1 Publication1
Mutagenesisi332K → E: Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit; when associated with A-334. 1 Publication1
Mutagenesisi334F → A: Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit; when associated with e-332. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001293672 – 36260S ribosomal protein L4-AAdd BLAST361

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP10664.
PRIDEiP10664.
TopDownProteomicsiP10664.

PTM databases

iPTMnetiP10664.

Interactioni

Subunit structurei

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). Interacts with its chaperone ACL4 and the nuclear import receptor KAP104 (PubMed:25936803).4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EGD2P388792EBI-15390,EBI-6379

Protein-protein interaction databases

BioGridi32733. 133 interactors.
DIPiDIP-8314N.
IntActiP10664. 219 interactors.
MINTiMINT-1325639.

Structurei

Secondary structure

1362
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 10Combined sources5
Beta strandi11 – 13Combined sources3
Beta strandi15 – 20Combined sources6
Helixi25 – 27Combined sources3
Helixi32 – 42Combined sources11
Turni43 – 46Combined sources4
Turni54 – 57Combined sources4
Beta strandi62 – 64Combined sources3
Beta strandi67 – 71Combined sources5
Beta strandi74 – 76Combined sources3
Beta strandi81 – 84Combined sources4
Beta strandi94 – 97Combined sources4
Helixi115 – 129Combined sources15
Helixi132 – 137Combined sources6
Beta strandi143 – 146Combined sources4
Beta strandi148 – 152Combined sources5
Helixi154 – 158Combined sources5
Helixi162 – 172Combined sources11
Helixi175 – 183Combined sources9
Beta strandi189 – 191Combined sources3
Helixi192 – 194Combined sources3
Beta strandi206 – 211Combined sources6
Helixi215 – 218Combined sources4
Turni219 – 221Combined sources3
Beta strandi222 – 224Combined sources3
Beta strandi226 – 232Combined sources7
Helixi235 – 238Combined sources4
Helixi240 – 242Combined sources3
Beta strandi248 – 251Combined sources4
Helixi252 – 262Combined sources11
Beta strandi265 – 267Combined sources3
Beta strandi280 – 282Combined sources3
Helixi286 – 291Combined sources6
Turni292 – 298Combined sources7
Beta strandi317 – 319Combined sources3
Helixi321 – 326Combined sources6
Helixi331 – 336Combined sources6
Helixi339 – 341Combined sources3
Helixi353 – 360Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-D5-260[»]
3J6Xelectron microscopy6.10L41-362[»]
3J6Yelectron microscopy6.10L41-362[»]
3J77electron microscopy6.20L41-362[»]
3J78electron microscopy6.30L41-362[»]
3JCTelectron microscopy3.08C1-362[»]
4U3MX-ray3.00L4/l42-362[»]
4U3NX-ray3.20L4/l42-362[»]
4U3UX-ray2.90L4/l42-362[»]
4U4NX-ray3.10L4/l42-362[»]
4U4OX-ray3.60L4/l42-362[»]
4U4QX-ray3.00L4/l42-362[»]
4U4RX-ray2.80L4/l42-362[»]
4U4UX-ray3.00L4/l42-362[»]
4U4YX-ray3.20L4/l42-362[»]
4U4ZX-ray3.10L4/l42-362[»]
4U50X-ray3.20L4/l42-362[»]
4U51X-ray3.20L4/l42-362[»]
4U52X-ray3.00L4/l42-362[»]
4U53X-ray3.30L4/l42-362[»]
4U55X-ray3.20L4/l42-362[»]
4U56X-ray3.45L4/l42-362[»]
4U6FX-ray3.10L4/l42-362[»]
4V6Ielectron microscopy8.80BD1-362[»]
4V7Felectron microscopy8.70D1-362[»]
4V7RX-ray4.00BD/DD1-362[»]
4V88X-ray3.00BC/DC1-362[»]
4V8Telectron microscopy8.10C1-362[»]
4V8Yelectron microscopy4.30BC2-362[»]
4V8Zelectron microscopy6.60BC2-362[»]
4V91electron microscopy3.70C1-362[»]
5APNelectron microscopy3.91C1-362[»]
5APOelectron microscopy3.41C1-362[»]
5DATX-ray3.15L4/l42-362[»]
5DC3X-ray3.25L4/l42-362[»]
5FCIX-ray3.40L4/l42-362[»]
5FCJX-ray3.10L4/l42-362[»]
5FL8electron microscopy9.50C1-362[»]
5GAKelectron microscopy3.88G1-362[»]
5I4LX-ray3.10L4/l42-362[»]
5JUOelectron microscopy4.00H1-362[»]
5JUPelectron microscopy3.50H1-362[»]
5JUSelectron microscopy4.20H1-362[»]
5JUTelectron microscopy4.00H1-362[»]
5JUUelectron microscopy4.00H1-362[»]
ProteinModelPortaliP10664.
SMRiP10664.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni277 – 362C-terminal-extended nuclear localization signal1 PublicationAdd BLAST86

Domaini

The eukaryote-specific C-terminal extension harbors a nuclear import signal and delivers the ACL4-RPL4 complex to the pre-ribosome, triggering RPL4 release from ACL4 and incorporation into the 60S ribosomal subunit.1 Publication

Sequence similaritiesi

Belongs to the ribosomal protein L4P family.Curated

Phylogenomic databases

HOGENOMiHOG000107331.
InParanoidiP10664.
KOiK02930.
OMAiKGRKAHP.
OrthoDBiEOG092C37AK.

Family and domain databases

Gene3Di3.40.1370.10. 1 hit.
InterProiIPR025755. Ribos_L4_C_dom.
IPR002136. Ribosomal_L4/L1e.
IPR013000. Ribosomal_L4/L1e_euk/arc_CS.
IPR023574. Ribosomal_L4_dom.
[Graphical view]
PfamiPF14374. Ribos_L4_asso_C. 1 hit.
PF00573. Ribosomal_L4. 1 hit.
[Graphical view]
SUPFAMiSSF52166. SSF52166. 1 hit.
PROSITEiPS00939. RIBOSOMAL_L1E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10664-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRPQVTVHS LTGEATANAL PLPAVFSAPI RPDIVHTVFT SVNKNKRQAY
60 70 80 90 100
AVSEKAGHQT SAESWGTGRA VARIPRVGGG GTGRSGQGAF GNMCRGGRMF
110 120 130 140 150
APTKTWRKWN VKVNHNEKRY ATASAIAATA VASLVLARGH RVEKIPEIPL
160 170 180 190 200
VVSTDLESIQ KTKEAVAALK AVGAHSDLLK VLKSKKLRAG KGKYRNRRWT
210 220 230 240 250
QRRGPLVVYA EDNGIVKALR NVPGVETANV ASLNLLQLAP GAHLGRFVIW
260 270 280 290 300
TEAAFTKLDQ VWGSETVASS KVGYTLPSHI ISTSDVTRII NSSEIQSAIR
310 320 330 340 350
PAGQATQKRT HVLKKNPLKN KQVLLRLNPY AKVFAAEKLG SKKAEKTGTK
360
PAAVFTETLK HD
Length:362
Mass (Da):39,092
Last modified:January 23, 2007 - v4
Checksum:i37D0942A10AAE89F
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti38V → L in AAA34974 (PubMed:2834365).Curated1
Sequence conflicti144K → T in AAA34974 (PubMed:2834365).Curated1
Sequence conflicti157E → D in AAA34974 (PubMed:2834365).Curated1
Sequence conflicti224G → S in AAA34974 (PubMed:2834365).Curated1
Sequence conflicti241G → S in AAA34974 (PubMed:2834365).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76078 Genomic DNA. Translation: CAA53687.1.
J03195 Genomic DNA. Translation: AAA34974.1.
Z35900 Genomic DNA. Translation: CAA84973.1.
BK006936 Genomic DNA. Translation: DAA07152.1.
PIRiS45887.
RefSeqiNP_009587.1. NM_001178379.1.

Genome annotation databases

EnsemblFungiiYBR031W; YBR031W; YBR031W.
GeneIDi852319.
KEGGisce:YBR031W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76078 Genomic DNA. Translation: CAA53687.1.
J03195 Genomic DNA. Translation: AAA34974.1.
Z35900 Genomic DNA. Translation: CAA84973.1.
BK006936 Genomic DNA. Translation: DAA07152.1.
PIRiS45887.
RefSeqiNP_009587.1. NM_001178379.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-D5-260[»]
3J6Xelectron microscopy6.10L41-362[»]
3J6Yelectron microscopy6.10L41-362[»]
3J77electron microscopy6.20L41-362[»]
3J78electron microscopy6.30L41-362[»]
3JCTelectron microscopy3.08C1-362[»]
4U3MX-ray3.00L4/l42-362[»]
4U3NX-ray3.20L4/l42-362[»]
4U3UX-ray2.90L4/l42-362[»]
4U4NX-ray3.10L4/l42-362[»]
4U4OX-ray3.60L4/l42-362[»]
4U4QX-ray3.00L4/l42-362[»]
4U4RX-ray2.80L4/l42-362[»]
4U4UX-ray3.00L4/l42-362[»]
4U4YX-ray3.20L4/l42-362[»]
4U4ZX-ray3.10L4/l42-362[»]
4U50X-ray3.20L4/l42-362[»]
4U51X-ray3.20L4/l42-362[»]
4U52X-ray3.00L4/l42-362[»]
4U53X-ray3.30L4/l42-362[»]
4U55X-ray3.20L4/l42-362[»]
4U56X-ray3.45L4/l42-362[»]
4U6FX-ray3.10L4/l42-362[»]
4V6Ielectron microscopy8.80BD1-362[»]
4V7Felectron microscopy8.70D1-362[»]
4V7RX-ray4.00BD/DD1-362[»]
4V88X-ray3.00BC/DC1-362[»]
4V8Telectron microscopy8.10C1-362[»]
4V8Yelectron microscopy4.30BC2-362[»]
4V8Zelectron microscopy6.60BC2-362[»]
4V91electron microscopy3.70C1-362[»]
5APNelectron microscopy3.91C1-362[»]
5APOelectron microscopy3.41C1-362[»]
5DATX-ray3.15L4/l42-362[»]
5DC3X-ray3.25L4/l42-362[»]
5FCIX-ray3.40L4/l42-362[»]
5FCJX-ray3.10L4/l42-362[»]
5FL8electron microscopy9.50C1-362[»]
5GAKelectron microscopy3.88G1-362[»]
5I4LX-ray3.10L4/l42-362[»]
5JUOelectron microscopy4.00H1-362[»]
5JUPelectron microscopy3.50H1-362[»]
5JUSelectron microscopy4.20H1-362[»]
5JUTelectron microscopy4.00H1-362[»]
5JUUelectron microscopy4.00H1-362[»]
ProteinModelPortaliP10664.
SMRiP10664.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32733. 133 interactors.
DIPiDIP-8314N.
IntActiP10664. 219 interactors.
MINTiMINT-1325639.

PTM databases

iPTMnetiP10664.

Proteomic databases

MaxQBiP10664.
PRIDEiP10664.
TopDownProteomicsiP10664.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR031W; YBR031W; YBR031W.
GeneIDi852319.
KEGGisce:YBR031W.

Organism-specific databases

EuPathDBiFungiDB:YBR031W.
SGDiS000000235. RPL4A.

Phylogenomic databases

HOGENOMiHOG000107331.
InParanoidiP10664.
KOiK02930.
OMAiKGRKAHP.
OrthoDBiEOG092C37AK.

Enzyme and pathway databases

BioCyciYEAST:G3O-29009-MONOMER.

Miscellaneous databases

PROiP10664.

Family and domain databases

Gene3Di3.40.1370.10. 1 hit.
InterProiIPR025755. Ribos_L4_C_dom.
IPR002136. Ribosomal_L4/L1e.
IPR013000. Ribosomal_L4/L1e_euk/arc_CS.
IPR023574. Ribosomal_L4_dom.
[Graphical view]
PfamiPF14374. Ribos_L4_asso_C. 1 hit.
PF00573. Ribosomal_L4. 1 hit.
[Graphical view]
SUPFAMiSSF52166. SSF52166. 1 hit.
PROSITEiPS00939. RIBOSOMAL_L1E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL4A_YEAST
AccessioniPrimary (citable) accession number: P10664
Secondary accession number(s): D6VQ32
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 154 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

There are 2 genes for L4 in yeast.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.