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Protein

60S ribosomal protein L24-A

Gene

RPL24A

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.1 Publication

Miscellaneous

Present with 247000 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eL24 in yeast.Curated

GO - Molecular functioni

  • RNA binding Source: SGD
  • structural constituent of ribosome Source: GO_Central

GO - Biological processi

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-30547-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L24-A1 Publication
Alternative name(s):
L30
Large ribosomal subunit protein eL24-A1 Publication
RP29
YL21
Gene namesi
Name:RPL24A1 Publication
Synonyms:RP29, RPL30A
Ordered Locus Names:YGL031C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL031C.
SGDiS000002999. RPL24A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: SGD

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001368941 – 15560S ribosomal protein L24-AAdd BLAST155

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei7PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP04449.
PRIDEiP04449.

PTM databases

iPTMnetiP04449.

Interactioni

Subunit structurei

Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).1 Publication1 Publication

Protein-protein interaction databases

BioGridi33215. 242 interactors.
IntActiP04449. 23 interactors.
MINTiMINT-1325572.

Structurei

Secondary structure

1155
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni7 – 9Combined sources3
Beta strandi18 – 22Combined sources5
Beta strandi24 – 26Combined sources3
Beta strandi28 – 33Combined sources6
Helixi34 – 41Combined sources8
Helixi46 – 48Combined sources3
Helixi53 – 58Combined sources6
Turni59 – 62Combined sources4
Helixi64 – 66Combined sources3
Beta strandi83 – 85Combined sources3
Turni87 – 90Combined sources4
Beta strandi91 – 93Combined sources3
Helixi98 – 111Combined sources14
Helixi113 – 128Combined sources16
Turni130 – 132Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-S4-56[»]
2X7Nelectron microscopy11.80D1-56[»]
3J6Xelectron microscopy6.10641-155[»]
3J6Yelectron microscopy6.10641-155[»]
3J77electron microscopy6.20741-155[»]
3J78electron microscopy6.30741-155[»]
4U3MX-ray3.00N4/n41-155[»]
4U3NX-ray3.20N4/n41-155[»]
4U3UX-ray2.90N4/n41-155[»]
4U4NX-ray3.10N4/n41-155[»]
4U4OX-ray3.60N4/n41-155[»]
4U4QX-ray3.00N4/n41-155[»]
4U4RX-ray2.80N4/n41-155[»]
4U4UX-ray3.00N4/n41-155[»]
4U4YX-ray3.20N4/n41-155[»]
4U4ZX-ray3.10N4/n41-155[»]
4U50X-ray3.20N4/n41-155[»]
4U51X-ray3.20N4/n41-155[»]
4U52X-ray3.00N4/n41-155[»]
4U53X-ray3.30N4/n41-155[»]
4U55X-ray3.20N4/n41-155[»]
4U56X-ray3.45N4/n41-155[»]
4U6FX-ray3.10N4/n41-155[»]
4V4Belectron microscopy11.70BS1-56[»]
4V6Ielectron microscopy8.80BZ1-155[»]
4V7RX-ray4.00BV/DV1-155[»]
4V88X-ray3.00BW/DW1-155[»]
4V8Telectron microscopy8.10W1-155[»]
4V8Yelectron microscopy4.30BW1-155[»]
4V8Zelectron microscopy6.60BW1-155[»]
4V91electron microscopy3.70W1-155[»]
5APNelectron microscopy3.91W1-155[»]
5APOelectron microscopy3.41W1-155[»]
5DATX-ray3.15N4/n41-155[»]
5DC3X-ray3.25N4/n41-155[»]
5DGEX-ray3.45N4/n41-155[»]
5DGFX-ray3.30N4/n41-155[»]
5DGVX-ray3.10N4/n41-155[»]
5FCIX-ray3.40N4/n41-155[»]
5FCJX-ray3.10N4/n41-155[»]
5GAKelectron microscopy3.88Y1-155[»]
5H4Pelectron microscopy3.07W1-155[»]
5I4LX-ray3.10N41-98[»]
n41-135[»]
5JUOelectron microscopy4.00BA1-155[»]
5JUPelectron microscopy3.50BA1-155[»]
5JUSelectron microscopy4.20BA1-155[»]
5JUTelectron microscopy4.00BA1-155[»]
5JUUelectron microscopy4.00BA1-155[»]
5LYBX-ray3.25N41-98[»]
n41-135[»]
5M1Jelectron microscopy3.30W51-98[»]
5MC6electron microscopy3.80AE1-155[»]
5T62electron microscopy3.30j1-155[»]
5T6Relectron microscopy4.50j1-155[»]
5TGAX-ray3.30N4/n41-135[»]
5TGMX-ray3.50N41-98[»]
n41-135[»]
ProteinModelPortaliP04449.
SMRiP04449.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04449.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000074809.
HOGENOMiHOG000184343.
InParanoidiP04449.
KOiK02896.
OMAiAKLRWTQ.
OrthoDBiEOG092C5LTS.

Family and domain databases

CDDicd00472. Ribosomal_L24e_L24. 1 hit.
InterProiView protein in InterPro
IPR000988. Ribosomal_L24e-rel.
IPR023442. Ribosomal_L24e_CS.
PANTHERiPTHR10792. PTHR10792. 1 hit.
PfamiView protein in Pfam
PF01246. Ribosomal_L24e. 1 hit.
PROSITEiView protein in PROSITE
PS01073. RIBOSOMAL_L24E. 1 hit.

Sequencei

Sequence statusi: Complete.

P04449-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVEIDSFSG AKIYPGRGTL FVRGDSKIFR FQNSKSASLF KQRKNPRRIA
60 70 80 90 100
WTVLFRKHHK KGITEEVAKK RSRKTVKAQR PITGASLDLI KERRSLKPEV
110 120 130 140 150
RKANREEKLK ANKEKKKAEK AARKAEKAKS AGTQSSKFSK QQAKGAFQKV

AATSR
Length:155
Mass (Da):17,614
Last modified:August 13, 1987 - v1
Checksum:i9A79C4E409515716
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02650 Genomic DNA. Translation: AAA35004.1.
Z72553 Genomic DNA. Translation: CAA96732.1.
EF123140 mRNA. Translation: ABM97484.1.
BK006941 Genomic DNA. Translation: DAA08068.1.
PIRiA02783. R6BYT9.
RefSeqiNP_011484.1. NM_001180896.1.

Genome annotation databases

EnsemblFungiiYGL031C; YGL031C; YGL031C.
GeneIDi852852.
KEGGisce:YGL031C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
K02650 Genomic DNA. Translation: AAA35004.1.
Z72553 Genomic DNA. Translation: CAA96732.1.
EF123140 mRNA. Translation: ABM97484.1.
BK006941 Genomic DNA. Translation: DAA08068.1.
PIRiA02783. R6BYT9.
RefSeqiNP_011484.1. NM_001180896.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-S4-56[»]
2X7Nelectron microscopy11.80D1-56[»]
3J6Xelectron microscopy6.10641-155[»]
3J6Yelectron microscopy6.10641-155[»]
3J77electron microscopy6.20741-155[»]
3J78electron microscopy6.30741-155[»]
4U3MX-ray3.00N4/n41-155[»]
4U3NX-ray3.20N4/n41-155[»]
4U3UX-ray2.90N4/n41-155[»]
4U4NX-ray3.10N4/n41-155[»]
4U4OX-ray3.60N4/n41-155[»]
4U4QX-ray3.00N4/n41-155[»]
4U4RX-ray2.80N4/n41-155[»]
4U4UX-ray3.00N4/n41-155[»]
4U4YX-ray3.20N4/n41-155[»]
4U4ZX-ray3.10N4/n41-155[»]
4U50X-ray3.20N4/n41-155[»]
4U51X-ray3.20N4/n41-155[»]
4U52X-ray3.00N4/n41-155[»]
4U53X-ray3.30N4/n41-155[»]
4U55X-ray3.20N4/n41-155[»]
4U56X-ray3.45N4/n41-155[»]
4U6FX-ray3.10N4/n41-155[»]
4V4Belectron microscopy11.70BS1-56[»]
4V6Ielectron microscopy8.80BZ1-155[»]
4V7RX-ray4.00BV/DV1-155[»]
4V88X-ray3.00BW/DW1-155[»]
4V8Telectron microscopy8.10W1-155[»]
4V8Yelectron microscopy4.30BW1-155[»]
4V8Zelectron microscopy6.60BW1-155[»]
4V91electron microscopy3.70W1-155[»]
5APNelectron microscopy3.91W1-155[»]
5APOelectron microscopy3.41W1-155[»]
5DATX-ray3.15N4/n41-155[»]
5DC3X-ray3.25N4/n41-155[»]
5DGEX-ray3.45N4/n41-155[»]
5DGFX-ray3.30N4/n41-155[»]
5DGVX-ray3.10N4/n41-155[»]
5FCIX-ray3.40N4/n41-155[»]
5FCJX-ray3.10N4/n41-155[»]
5GAKelectron microscopy3.88Y1-155[»]
5H4Pelectron microscopy3.07W1-155[»]
5I4LX-ray3.10N41-98[»]
n41-135[»]
5JUOelectron microscopy4.00BA1-155[»]
5JUPelectron microscopy3.50BA1-155[»]
5JUSelectron microscopy4.20BA1-155[»]
5JUTelectron microscopy4.00BA1-155[»]
5JUUelectron microscopy4.00BA1-155[»]
5LYBX-ray3.25N41-98[»]
n41-135[»]
5M1Jelectron microscopy3.30W51-98[»]
5MC6electron microscopy3.80AE1-155[»]
5T62electron microscopy3.30j1-155[»]
5T6Relectron microscopy4.50j1-155[»]
5TGAX-ray3.30N4/n41-135[»]
5TGMX-ray3.50N41-98[»]
n41-135[»]
ProteinModelPortaliP04449.
SMRiP04449.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33215. 242 interactors.
IntActiP04449. 23 interactors.
MINTiMINT-1325572.

PTM databases

iPTMnetiP04449.

Proteomic databases

MaxQBiP04449.
PRIDEiP04449.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL031C; YGL031C; YGL031C.
GeneIDi852852.
KEGGisce:YGL031C.

Organism-specific databases

EuPathDBiFungiDB:YGL031C.
SGDiS000002999. RPL24A.

Phylogenomic databases

GeneTreeiENSGT00550000074809.
HOGENOMiHOG000184343.
InParanoidiP04449.
KOiK02896.
OMAiAKLRWTQ.
OrthoDBiEOG092C5LTS.

Enzyme and pathway databases

BioCyciYEAST:G3O-30547-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP04449.
PROiPR:P04449.

Family and domain databases

CDDicd00472. Ribosomal_L24e_L24. 1 hit.
InterProiView protein in InterPro
IPR000988. Ribosomal_L24e-rel.
IPR023442. Ribosomal_L24e_CS.
PANTHERiPTHR10792. PTHR10792. 1 hit.
PfamiView protein in Pfam
PF01246. Ribosomal_L24e. 1 hit.
PROSITEiView protein in PROSITE
PS01073. RIBOSOMAL_L24E. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL24A_YEAST
AccessioniPrimary (citable) accession number: P04449
Secondary accession number(s): A2TBN7, D6VUA7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: June 7, 2017
This is version 158 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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 VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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.