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Protein

60S ribosomal protein L26-A

Gene

RPL26A

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

There are 2 genes for uL24 in yeast.Curated

GO - Molecular functioni

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

GO - Biological processi

  • cytoplasmic translation Source: SGD

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-32420-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L26-A1 Publication
Alternative name(s):
L33
Large ribosomal subunit protein uL24-A1 Publication
YL33
Gene namesi
Name:RPL26A1 Publication
Synonyms:RPL26, RPL33A
Ordered Locus Names:YLR344W
ORF Names:L8300.4
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR344W.
SGDiS000004336. RPL26A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: SGD

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001308012 – 12760S ribosomal protein L26-AAdd BLAST126

Proteomic databases

MaxQBiP05743.
PRIDEiP05743.
TopDownProteomicsiP05743.

PTM databases

iPTMnetiP05743.

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

BioGridi31607. 89 interactors.
DIPiDIP-5584N.
IntActiP05743. 8 interactors.
MINTiMINT-8285368.

Structurei

Secondary structure

1127
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 8Combined sources3
Helixi12 – 20Combined sources9
Helixi24 – 30Combined sources7
Beta strandi32 – 35Combined sources4
Helixi37 – 43Combined sources7
Beta strandi47 – 49Combined sources3
Beta strandi55 – 58Combined sources4
Turni62 – 65Combined sources4
Beta strandi67 – 74Combined sources8
Helixi75 – 77Combined sources3
Beta strandi79 – 83Combined sources5
Beta strandi86 – 88Combined sources3
Beta strandi90 – 92Combined sources3
Beta strandi94 – 96Combined sources3
Helixi101 – 103Combined sources3
Beta strandi104 – 108Combined sources5
Helixi113 – 121Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-U9-123[»]
2WW9electron microscopy8.60L1-127[»]
2WWAelectron microscopy8.90L1-127[»]
2WWBelectron microscopy6.48L1-127[»]
3J6Xelectron microscopy6.10661-127[»]
3J6Yelectron microscopy6.10661-127[»]
3J77electron microscopy6.20761-127[»]
3J78electron microscopy6.30761-127[»]
3JCTelectron microscopy3.08Y1-127[»]
4U3MX-ray3.00N6/n62-127[»]
4U3NX-ray3.20N6/n62-127[»]
4U3UX-ray2.90N6/n62-127[»]
4U4NX-ray3.10N6/n62-127[»]
4U4OX-ray3.60N6/n62-127[»]
4U4QX-ray3.00N6/n62-127[»]
4U4RX-ray2.80N6/n62-127[»]
4U4UX-ray3.00N6/n62-127[»]
4U4YX-ray3.20N6/n62-127[»]
4U4ZX-ray3.10N6/n62-127[»]
4U50X-ray3.20N6/n62-127[»]
4U51X-ray3.20N6/n62-127[»]
4U52X-ray3.00N6/n62-127[»]
4U53X-ray3.30N6/n62-127[»]
4U55X-ray3.20N6/n62-127[»]
4U56X-ray3.45N6/n62-127[»]
4U6FX-ray3.10N6/n62-127[»]
4V4Belectron microscopy11.70BU2-127[»]
4V6Ielectron microscopy8.80BY1-123[»]
4V7Felectron microscopy8.70X1-127[»]
4V7RX-ray4.00BX/DX1-127[»]
4V88X-ray3.00BY/DY1-127[»]
4V8Telectron microscopy8.10Y1-127[»]
4V8Yelectron microscopy4.30BY2-127[»]
4V8Zelectron microscopy6.60BY2-127[»]
4V91electron microscopy3.70Y1-127[»]
5APNelectron microscopy3.91Y1-127[»]
5APOelectron microscopy3.41Y1-127[»]
5DATX-ray3.15N6/n62-127[»]
5DC3X-ray3.25N6/n62-127[»]
5DGEX-ray3.45N6/n62-127[»]
5DGFX-ray3.30N6/n62-127[»]
5DGVX-ray3.10N6/n62-127[»]
5FCIX-ray3.40N6/n62-127[»]
5FCJX-ray3.10N6/n62-127[»]
5FL8electron microscopy9.50Y1-127[»]
5GAKelectron microscopy3.88a1-127[»]
5H4Pelectron microscopy3.07Y1-127[»]
5I4LX-ray3.10N6/n62-127[»]
5JCSelectron microscopy9.50Y1-127[»]
5JUOelectron microscopy4.00DA1-127[»]
5JUPelectron microscopy3.50DA1-127[»]
5JUSelectron microscopy4.20DA1-127[»]
5JUTelectron microscopy4.00DA1-127[»]
5JUUelectron microscopy4.00DA1-127[»]
5LYBX-ray3.25N6/n62-127[»]
5M1Jelectron microscopy3.30Y52-127[»]
5MC6electron microscopy3.80AK1-127[»]
5T62electron microscopy3.30l1-127[»]
5T6Relectron microscopy4.50l1-127[»]
5TGAX-ray3.30N6/n62-127[»]
5TGMX-ray3.50N6/n62-127[»]
ProteinModelPortaliP05743.
SMRiP05743.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05743.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000014165.
HOGENOMiHOG000216571.
InParanoidiP05743.
KOiK02898.
OMAiANIGIHP.
OrthoDBiEOG092C5U93.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
InterProiView protein in InterPro
IPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR005825. Ribosomal_L24/26_CS.
IPR005756. Ribosomal_L26/L24P_euk/arc.
IPR008991. Translation_prot_SH3-like.
PANTHERiPTHR11143. PTHR11143. 1 hit.
PfamiView protein in Pfam
PF00467. KOW. 1 hit.
PF16906. Ribosomal_L26. 1 hit.
SUPFAMiSSF50104. SSF50104. 1 hit.
TIGRFAMsiTIGR01080. rplX_A_E. 1 hit.
PROSITEiView protein in PROSITE
PS01108. RIBOSOMAL_L24. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P05743-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKQSLDVSS DRRKARKAYF TAPSSQRRVL LSAPLSKELR AQYGIKALPI
60 70 80 90 100
RRDDEVLVVR GSKKGQEGKI SSVYRLKFAV QVDKVTKEKV NGASVPINLH
110 120
PSKLVITKLH LDKDRKALIQ RKGGKLE
Length:127
Mass (Da):14,234
Last modified:January 23, 2007 - v3
Checksum:i3888654AC1587E8E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19028 Genomic DNA. Translation: AAB67254.1.
BK006945 Genomic DNA. Translation: DAA09649.1.
PIRiS51347.
RefSeqiNP_013448.1. NM_001182233.1.

Genome annotation databases

EnsemblFungiiYLR344W; YLR344W; YLR344W.
GeneIDi851058.
KEGGisce:YLR344W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U19028 Genomic DNA. Translation: AAB67254.1.
BK006945 Genomic DNA. Translation: DAA09649.1.
PIRiS51347.
RefSeqiNP_013448.1. NM_001182233.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-U9-123[»]
2WW9electron microscopy8.60L1-127[»]
2WWAelectron microscopy8.90L1-127[»]
2WWBelectron microscopy6.48L1-127[»]
3J6Xelectron microscopy6.10661-127[»]
3J6Yelectron microscopy6.10661-127[»]
3J77electron microscopy6.20761-127[»]
3J78electron microscopy6.30761-127[»]
3JCTelectron microscopy3.08Y1-127[»]
4U3MX-ray3.00N6/n62-127[»]
4U3NX-ray3.20N6/n62-127[»]
4U3UX-ray2.90N6/n62-127[»]
4U4NX-ray3.10N6/n62-127[»]
4U4OX-ray3.60N6/n62-127[»]
4U4QX-ray3.00N6/n62-127[»]
4U4RX-ray2.80N6/n62-127[»]
4U4UX-ray3.00N6/n62-127[»]
4U4YX-ray3.20N6/n62-127[»]
4U4ZX-ray3.10N6/n62-127[»]
4U50X-ray3.20N6/n62-127[»]
4U51X-ray3.20N6/n62-127[»]
4U52X-ray3.00N6/n62-127[»]
4U53X-ray3.30N6/n62-127[»]
4U55X-ray3.20N6/n62-127[»]
4U56X-ray3.45N6/n62-127[»]
4U6FX-ray3.10N6/n62-127[»]
4V4Belectron microscopy11.70BU2-127[»]
4V6Ielectron microscopy8.80BY1-123[»]
4V7Felectron microscopy8.70X1-127[»]
4V7RX-ray4.00BX/DX1-127[»]
4V88X-ray3.00BY/DY1-127[»]
4V8Telectron microscopy8.10Y1-127[»]
4V8Yelectron microscopy4.30BY2-127[»]
4V8Zelectron microscopy6.60BY2-127[»]
4V91electron microscopy3.70Y1-127[»]
5APNelectron microscopy3.91Y1-127[»]
5APOelectron microscopy3.41Y1-127[»]
5DATX-ray3.15N6/n62-127[»]
5DC3X-ray3.25N6/n62-127[»]
5DGEX-ray3.45N6/n62-127[»]
5DGFX-ray3.30N6/n62-127[»]
5DGVX-ray3.10N6/n62-127[»]
5FCIX-ray3.40N6/n62-127[»]
5FCJX-ray3.10N6/n62-127[»]
5FL8electron microscopy9.50Y1-127[»]
5GAKelectron microscopy3.88a1-127[»]
5H4Pelectron microscopy3.07Y1-127[»]
5I4LX-ray3.10N6/n62-127[»]
5JCSelectron microscopy9.50Y1-127[»]
5JUOelectron microscopy4.00DA1-127[»]
5JUPelectron microscopy3.50DA1-127[»]
5JUSelectron microscopy4.20DA1-127[»]
5JUTelectron microscopy4.00DA1-127[»]
5JUUelectron microscopy4.00DA1-127[»]
5LYBX-ray3.25N6/n62-127[»]
5M1Jelectron microscopy3.30Y52-127[»]
5MC6electron microscopy3.80AK1-127[»]
5T62electron microscopy3.30l1-127[»]
5T6Relectron microscopy4.50l1-127[»]
5TGAX-ray3.30N6/n62-127[»]
5TGMX-ray3.50N6/n62-127[»]
ProteinModelPortaliP05743.
SMRiP05743.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31607. 89 interactors.
DIPiDIP-5584N.
IntActiP05743. 8 interactors.
MINTiMINT-8285368.

PTM databases

iPTMnetiP05743.

Proteomic databases

MaxQBiP05743.
PRIDEiP05743.
TopDownProteomicsiP05743.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR344W; YLR344W; YLR344W.
GeneIDi851058.
KEGGisce:YLR344W.

Organism-specific databases

EuPathDBiFungiDB:YLR344W.
SGDiS000004336. RPL26A.

Phylogenomic databases

GeneTreeiENSGT00390000014165.
HOGENOMiHOG000216571.
InParanoidiP05743.
KOiK02898.
OMAiANIGIHP.
OrthoDBiEOG092C5U93.

Enzyme and pathway databases

BioCyciYEAST:G3O-32420-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

EvolutionaryTraceiP05743.
PROiPR:P05743.

Family and domain databases

Gene3Di2.30.30.30. 1 hit.
InterProiView protein in InterPro
IPR005824. KOW.
IPR014722. Rib_L2_dom2.
IPR005825. Ribosomal_L24/26_CS.
IPR005756. Ribosomal_L26/L24P_euk/arc.
IPR008991. Translation_prot_SH3-like.
PANTHERiPTHR11143. PTHR11143. 1 hit.
PfamiView protein in Pfam
PF00467. KOW. 1 hit.
PF16906. Ribosomal_L26. 1 hit.
SUPFAMiSSF50104. SSF50104. 1 hit.
TIGRFAMsiTIGR01080. rplX_A_E. 1 hit.
PROSITEiView protein in PROSITE
PS01108. RIBOSOMAL_L24. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL26A_YEAST
AccessioniPrimary (citable) accession number: P05743
Secondary accession number(s): D6VYY3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: April 12, 2017
This is version 159 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.