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Protein

60S ribosomal protein L36-A

Gene

RPL36A

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

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 31600 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eL36 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-32881-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 L36-A1 Publication
Alternative name(s):
L39
Large ribosomal subunit protein eL36-A1 Publication
YL39
Gene namesi
Name:RPL36A1 Publication
Synonyms:RPL39A
Ordered Locus Names:YMR194W
ORF Names:YM9646.06
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

EuPathDBiFungiDB:YMR194W.
SGDiS000004807. RPL36A.

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_00001950202 – 10060S ribosomal protein L36-AAdd BLAST99

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonine1 Publication1

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP05745.
PRIDEiP05745.
TopDownProteomicsiP05745.

PTM databases

iPTMnetiP05745.

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

BioGridi35372. 150 interactors.
IntActiP05745. 14 interactors.
MINTiMINT-1898050.

Structurei

Secondary structure

1100
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 10Combined sources5
Helixi26 – 29Combined sources4
Helixi35 – 48Combined sources14
Helixi52 – 64Combined sources13
Helixi66 – 76Combined sources11
Beta strandi77 – 79Combined sources3
Helixi80 – 96Combined sources17
Turni97 – 99Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J6Xelectron microscopy6.10761-100[»]
3J6Yelectron microscopy6.10761-100[»]
3J77electron microscopy6.20861-100[»]
3J78electron microscopy6.30861-100[»]
3JCTelectron microscopy3.08i1-100[»]
4U3MX-ray3.00O6/o62-100[»]
4U3NX-ray3.20O6/o62-100[»]
4U3UX-ray2.90O6/o62-100[»]
4U4NX-ray3.10O6/o62-100[»]
4U4OX-ray3.60O6/o62-100[»]
4U4QX-ray3.00O6/o62-100[»]
4U4RX-ray2.80O6/o62-100[»]
4U4UX-ray3.00O6/o62-100[»]
4U4YX-ray3.20O6/o62-100[»]
4U4ZX-ray3.10O6/o62-100[»]
4U50X-ray3.20O6/o62-100[»]
4U51X-ray3.20O6/o62-100[»]
4U52X-ray3.00O6/o62-100[»]
4U53X-ray3.30O6/o62-100[»]
4U55X-ray3.20O6/o62-100[»]
4U56X-ray3.45O6/o62-100[»]
4U6FX-ray3.10O6/o62-100[»]
4V6Ielectron microscopy8.80Bk1-100[»]
4V7Felectron microscopy8.70g1-100[»]
4V88X-ray3.00Bi/Di1-100[»]
4V8Telectron microscopy8.10i1-100[»]
4V8Yelectron microscopy4.30Bi2-100[»]
4V8Zelectron microscopy6.60Bi2-100[»]
4V91electron microscopy3.70i1-100[»]
5APNelectron microscopy3.91i1-100[»]
5APOelectron microscopy3.41i1-100[»]
5DATX-ray3.15O6/o62-100[»]
5DC3X-ray3.25O6/o62-100[»]
5DGEX-ray3.45O6/o62-100[»]
5DGFX-ray3.30O6/o62-100[»]
5DGVX-ray3.10O6/o62-100[»]
5FCIX-ray3.40O6/o62-100[»]
5FCJX-ray3.10O6/o62-100[»]
5FL8electron microscopy9.50i1-100[»]
5GAKelectron microscopy3.88k1-100[»]
5H4Pelectron microscopy3.07i1-100[»]
5I4LX-ray3.10O6/o62-100[»]
5JCSelectron microscopy9.50i1-100[»]
5JUOelectron microscopy4.00NA1-100[»]
5JUPelectron microscopy3.50NA1-100[»]
5JUSelectron microscopy4.20NA1-100[»]
5JUTelectron microscopy4.00NA1-100[»]
5JUUelectron microscopy4.00NA1-100[»]
5LYBX-ray3.25O6/o62-100[»]
5M1Jelectron microscopy3.30i52-100[»]
5MC6electron microscopy3.80AC1-100[»]
5T62electron microscopy3.30v1-100[»]
5T6Relectron microscopy4.50v1-100[»]
5TGAX-ray3.30O6/o62-100[»]
5TGMX-ray3.50O6/o62-100[»]
ProteinModelPortaliP05745.
SMRiP05745.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000011943.
HOGENOMiHOG000155312.
InParanoidiP05745.
KOiK02920.
OMAiNICAKRR.
OrthoDBiEOG092C5H47.

Family and domain databases

InterProiView protein in InterPro
IPR000509. Ribosomal_L36e.
PANTHERiPTHR10114. PTHR10114. 1 hit.
PfamiView protein in Pfam
PF01158. Ribosomal_L36e. 1 hit.
PROSITEiView protein in PROSITE
PS01190. RIBOSOMAL_L36E. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P05745-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTVKTGIAIG LNKGKKVTSM TPAPKISYKK GAASNRTKFV RSLVREIAGL
60 70 80 90 100
SPYERRLIDL IRNSGEKRAR KVAKKRLGSF TRAKAKVEEM NNIIAASRRH
Length:100
Mass (Da):11,124
Last modified:January 23, 2007 - v3
Checksum:i9CAA7BFFF33D0C25
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47815 Genomic DNA. Translation: CAA87815.1.
BK006946 Genomic DNA. Translation: DAA10092.1.
PIRiS11263. S50922.
RefSeqiNP_013920.1. NM_001182701.1.

Genome annotation databases

EnsemblFungiiYMR194W; YMR194W; YMR194W.
GeneIDi855232.
KEGGisce:YMR194W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47815 Genomic DNA. Translation: CAA87815.1.
BK006946 Genomic DNA. Translation: DAA10092.1.
PIRiS11263. S50922.
RefSeqiNP_013920.1. NM_001182701.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J6Xelectron microscopy6.10761-100[»]
3J6Yelectron microscopy6.10761-100[»]
3J77electron microscopy6.20861-100[»]
3J78electron microscopy6.30861-100[»]
3JCTelectron microscopy3.08i1-100[»]
4U3MX-ray3.00O6/o62-100[»]
4U3NX-ray3.20O6/o62-100[»]
4U3UX-ray2.90O6/o62-100[»]
4U4NX-ray3.10O6/o62-100[»]
4U4OX-ray3.60O6/o62-100[»]
4U4QX-ray3.00O6/o62-100[»]
4U4RX-ray2.80O6/o62-100[»]
4U4UX-ray3.00O6/o62-100[»]
4U4YX-ray3.20O6/o62-100[»]
4U4ZX-ray3.10O6/o62-100[»]
4U50X-ray3.20O6/o62-100[»]
4U51X-ray3.20O6/o62-100[»]
4U52X-ray3.00O6/o62-100[»]
4U53X-ray3.30O6/o62-100[»]
4U55X-ray3.20O6/o62-100[»]
4U56X-ray3.45O6/o62-100[»]
4U6FX-ray3.10O6/o62-100[»]
4V6Ielectron microscopy8.80Bk1-100[»]
4V7Felectron microscopy8.70g1-100[»]
4V88X-ray3.00Bi/Di1-100[»]
4V8Telectron microscopy8.10i1-100[»]
4V8Yelectron microscopy4.30Bi2-100[»]
4V8Zelectron microscopy6.60Bi2-100[»]
4V91electron microscopy3.70i1-100[»]
5APNelectron microscopy3.91i1-100[»]
5APOelectron microscopy3.41i1-100[»]
5DATX-ray3.15O6/o62-100[»]
5DC3X-ray3.25O6/o62-100[»]
5DGEX-ray3.45O6/o62-100[»]
5DGFX-ray3.30O6/o62-100[»]
5DGVX-ray3.10O6/o62-100[»]
5FCIX-ray3.40O6/o62-100[»]
5FCJX-ray3.10O6/o62-100[»]
5FL8electron microscopy9.50i1-100[»]
5GAKelectron microscopy3.88k1-100[»]
5H4Pelectron microscopy3.07i1-100[»]
5I4LX-ray3.10O6/o62-100[»]
5JCSelectron microscopy9.50i1-100[»]
5JUOelectron microscopy4.00NA1-100[»]
5JUPelectron microscopy3.50NA1-100[»]
5JUSelectron microscopy4.20NA1-100[»]
5JUTelectron microscopy4.00NA1-100[»]
5JUUelectron microscopy4.00NA1-100[»]
5LYBX-ray3.25O6/o62-100[»]
5M1Jelectron microscopy3.30i52-100[»]
5MC6electron microscopy3.80AC1-100[»]
5T62electron microscopy3.30v1-100[»]
5T6Relectron microscopy4.50v1-100[»]
5TGAX-ray3.30O6/o62-100[»]
5TGMX-ray3.50O6/o62-100[»]
ProteinModelPortaliP05745.
SMRiP05745.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35372. 150 interactors.
IntActiP05745. 14 interactors.
MINTiMINT-1898050.

PTM databases

iPTMnetiP05745.

Proteomic databases

MaxQBiP05745.
PRIDEiP05745.
TopDownProteomicsiP05745.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYMR194W; YMR194W; YMR194W.
GeneIDi855232.
KEGGisce:YMR194W.

Organism-specific databases

EuPathDBiFungiDB:YMR194W.
SGDiS000004807. RPL36A.

Phylogenomic databases

GeneTreeiENSGT00390000011943.
HOGENOMiHOG000155312.
InParanoidiP05745.
KOiK02920.
OMAiNICAKRR.
OrthoDBiEOG092C5H47.

Enzyme and pathway databases

BioCyciYEAST:G3O-32881-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

PROiPR:P05745.

Family and domain databases

InterProiView protein in InterPro
IPR000509. Ribosomal_L36e.
PANTHERiPTHR10114. PTHR10114. 1 hit.
PfamiView protein in Pfam
PF01158. Ribosomal_L36e. 1 hit.
PROSITEiView protein in PROSITE
PS01190. RIBOSOMAL_L36E. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL36A_YEAST
AccessioniPrimary (citable) accession number: P05745
Secondary accession number(s): D6W018
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: June 7, 2017
This is version 144 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, 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 XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: 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.