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Protein

60S ribosomal protein L16-A

Gene

RPL16A

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 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
Modified residuei44PhosphoserineBy similarity1
Cross-linki177Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei188PhosphoserineBy similarity1

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP26784.
PRIDEiP26784.

PTM databases

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. 340 interactors.
IntActiP26784. 38 interactors.
MINTiMINT-2981627.
STRINGi4932.YIL133C.

Structurei

Secondary structure

1199
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 10Combined sources6
Helixi16 – 28Combined sources13
Beta strandi32 – 36Combined sources5
Helixi38 – 40Combined sources3
Beta strandi42 – 45Combined sources4
Helixi47 – 58Combined sources12
Helixi66 – 68Combined sources3
Helixi76 – 85Combined sources10
Turni86 – 91Combined sources6
Helixi93 – 100Combined sources8
Beta strandi102 – 104Combined sources3
Helixi112 – 114Combined sources3
Beta strandi117 – 119Combined sources3
Helixi121 – 123Combined sources3
Helixi125 – 128Combined sources4
Beta strandi135 – 137Combined sources3
Helixi138 – 144Combined sources7
Helixi150 – 184Combined sources35
Turni185 – 187Combined sources3
Helixi189 – 196Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-M2-147[»]
3J6Xelectron microscopy6.10561-199[»]
3J6Yelectron microscopy6.10561-199[»]
3J77electron microscopy6.20661-199[»]
3J78electron microscopy6.30661-199[»]
3JCTelectron microscopy3.08O1-199[»]
4U3MX-ray3.00M6/m62-199[»]
4U3NX-ray3.20M6/m62-199[»]
4U3UX-ray2.90M6/m62-199[»]
4U4NX-ray3.10M6/m62-199[»]
4U4OX-ray3.60M6/m62-199[»]
4U4QX-ray3.00M6/m62-199[»]
4U4RX-ray2.80M6/m62-199[»]
4U4UX-ray3.00M6/m62-199[»]
4U4YX-ray3.20M6/m62-199[»]
4U4ZX-ray3.10M6/m62-199[»]
4U50X-ray3.20M6/m62-199[»]
4U51X-ray3.20M6/m62-199[»]
4U52X-ray3.00M6/m62-199[»]
4U53X-ray3.30M6/m62-199[»]
4U55X-ray3.20M6/m62-199[»]
4U56X-ray3.45M6/m62-199[»]
4U6FX-ray3.10M6/m62-199[»]
4V4Belectron microscopy11.70BM2-147[»]
4V6Ielectron microscopy8.80BK1-199[»]
4V7Felectron microscopy8.70J1-199[»]
4V7RX-ray4.00BP/DP1-199[»]
4V88X-ray3.00BO/DO1-199[»]
4V8Telectron microscopy8.10O1-199[»]
4V8Yelectron microscopy4.30BO2-199[»]
4V8Zelectron microscopy6.60BO2-199[»]
4V91electron microscopy3.70O1-199[»]
5APNelectron microscopy3.91O1-199[»]
5APOelectron microscopy3.41O1-199[»]
5DATX-ray3.15M6/m62-199[»]
5DC3X-ray3.25M6/m62-199[»]
5DGEX-ray3.45M6/m62-199[»]
5DGFX-ray3.30M6/m62-199[»]
5DGVX-ray3.10M6/m62-199[»]
5FCIX-ray3.40M6/m62-199[»]
5FCJX-ray3.10M6/m62-199[»]
5FL8electron microscopy9.50O1-199[»]
5GAKelectron microscopy3.88Q1-199[»]
5H4Pelectron microscopy3.07O1-199[»]
5I4LX-ray3.10M6/m63-199[»]
5JCSelectron microscopy9.50O1-199[»]
5JUOelectron microscopy4.00T1-199[»]
5JUPelectron microscopy3.50T1-199[»]
5JUSelectron microscopy4.20T1-199[»]
5JUTelectron microscopy4.00T1-199[»]
5JUUelectron microscopy4.00T1-199[»]
5LYBX-ray3.25M6/m63-199[»]
5M1Jelectron microscopy3.30K53-199[»]
5MC6electron microscopy3.80AU1-199[»]
5MEIX-ray3.50CQ/w3-199[»]
5T62electron microscopy3.30b1-199[»]
5T6Relectron microscopy4.50b1-199[»]
5TBWX-ray3.00CQ/w3-199[»]
5TGAX-ray3.30M6/m63-199[»]
5TGMX-ray3.50M6/m63-199[»]
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: October 25, 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 IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names