Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

60S ribosomal protein L16-A

Gene

RPL16A

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -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 43300 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for uL13 in yeast.Curated

GO - Molecular functioni

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

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • translation Source: GO_Central

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-31384-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 L16-A1 Publication
Alternative name(s):
L13a
L21
Large ribosomal subunit protein uL13-A1 Publication
RP22
YL15
Gene namesi
Name:RPL16A1 Publication
Synonyms:RPL13, RPL21A
Ordered Locus Names:YIL133C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IX

Organism-specific databases

EuPathDBiFungiDB:YIL133C
SGDiS000001395 RPL16A

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001337912 – 19960S ribosomal protein L16-AAdd BLAST198

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine1 Publication1
Cross-linki177Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP26784
PaxDbiP26784
PRIDEiP26784

PTM databases

CarbonylDBiP26784
iPTMnetiP26784

Interactioni

Subunit structurei

Component of the large ribosomal subunit (LSU). 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

BioGridi34858, 350 interactors
IntActiP26784, 42 interactors
MINTiP26784
STRINGi4932.YIL133C

Structurei

Secondary structure

1199
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi12 – 14Combined sources3
Helixi16 – 28Combined sources13
Beta strandi35 – 37Combined sources3
Helixi38 – 40Combined sources3
Helixi47 – 59Combined sources13
Helixi66 – 68Combined sources3
Helixi76 – 85Combined sources10
Helixi93 – 96Combined sources4
Helixi99 – 101Combined sources3
Turni110 – 114Combined sources5
Beta strandi121 – 124Combined sources4
Turni125 – 128Combined sources4
Helixi139 – 144Combined sources6
Helixi150 – 185Combined sources36
Helixi191 – 197Combined sources7

3D structure databases

ProteinModelPortaliP26784
SMRiP26784
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26784

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000010799
HOGENOMiHOG000225289
InParanoidiP26784
KOiK02872
OMAiCCQGINI
OrthoDBiEOG092C5KDG

Family and domain databases

CDDicd00392 Ribosomal_L13, 1 hit
Gene3Di3.90.1180.10, 1 hit
HAMAPiMF_01366 Ribosomal_L13, 1 hit
InterProiView protein in InterPro
IPR005822 Ribosomal_L13
IPR023563 Ribosomal_L13_CS
IPR005755 Ribosomal_L13_euk/arc
IPR036899 Ribosomal_L13_sf
PANTHERiPTHR11545 PTHR11545, 1 hit
PTHR11545:SF3 PTHR11545:SF3, 1 hit
PfamiView protein in Pfam
PF00572 Ribosomal_L13, 1 hit
PIRSFiPIRSF002181 Ribosomal_L13, 1 hit
SUPFAMiSSF52161 SSF52161, 1 hit
TIGRFAMsiTIGR01077 L13_A_E, 1 hit
PROSITEiView protein in PROSITE
PS00783 RIBOSOMAL_L13, 1 hit

Sequencei

Sequence statusi: Complete.

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

P26784-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVEPVVVID GKGHLVGRLA SVVAKQLLNG QKIVVVRAEE LNISGEFFRN
60 70 80 90 100
KLKYHDFLRK ATAFNKTRGP FHFRAPSRIF YKALRGMVSH KTARGKAALE
110 120 130 140 150
RLKVFEGIPP PYDKKKRVVV PQALRVLRLK PGRKYTTLGK LSTSVGWKYE
160 170 180 190
DVVAKLEAKR KVSSAEYYAK KRAFTKKVAS ANATAAESDV AKQLAALGY
Length:199
Mass (Da):22,201
Last modified:January 23, 2007 - v3
Checksum:iDAB11B0D4A91EF0B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14H → L AA sequence (PubMed:1544921).Curated1
Sequence conflicti21S → E AA sequence (PubMed:1544921).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z38059 Genomic DNA Translation: CAA86145.1
BK006942 Genomic DNA Translation: DAA08420.1
PIRiS48401
RefSeqiNP_012133.1, NM_001179481.1

Genome annotation databases

EnsemblFungiiYIL133C; YIL133C; YIL133C
GeneIDi854673
KEGGisce:YIL133C

Similar proteinsi

Entry informationi

Entry nameiRL16A_YEAST
AccessioniPrimary (citable) accession number: P26784
Secondary accession number(s): D6VVF4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: July 18, 2018
This is version 167 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 IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health