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Protein

40S ribosomal protein S16-A

Gene

RPS16A

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

GO - Molecular functioni

  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • translation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-32835-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-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.
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:
40S ribosomal protein S16-A
Alternative name(s):
RP61R
Gene namesi
Name:RPS16A
Synonyms:RP61R
Ordered Locus Names:YMR143W
ORF Names:YM9375.12
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIII

Organism-specific databases

SGDiS000004751. RPS16A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 14314240S ribosomal protein S16-APRO_0000111503Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Cross-linki30 – 30Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei34 – 341PhosphoserineCombined sources
Cross-linki47 – 47Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki59 – 59Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei61 – 611PhosphoserineCombined sources
Modified residuei70 – 701PhosphothreonineCombined sources
Modified residuei76 – 761PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP0CX51.
TopDownProteomicsiP0CX51.

PTM databases

iPTMnetiP0CX51.

Expressioni

Gene expression databases

ExpressionAtlasiP0CX51. differential.

Interactioni

Subunit structurei

Component of the small ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains 32 different proteins (encoded by 56 genes) and 1 molecule of RNA (18S). The 60S subunit contains 46 different proteins (encoded by 81 genes) and 3 molecules of RNA (25S, 5.8S and 5S).1 Publication

Protein-protein interaction databases

BioGridi31978. 80 interactions.
35319. 90 interactions.
IntActiP0CX51. 2 interactions.
MINTiMINT-8285666.

Structurei

Secondary structure

1
143
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 139Combined sources
Beta strandi16 – 2611Combined sources
Beta strandi29 – 313Combined sources
Turni36 – 383Combined sources
Beta strandi40 – 423Combined sources
Turni43 – 453Combined sources
Helixi46 – 549Combined sources
Helixi57 – 593Combined sources
Beta strandi63 – 7210Combined sources
Helixi76 – 9520Combined sources
Helixi99 – 11214Combined sources
Beta strandi114 – 1185Combined sources
Beta strandi129 – 1357Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-I5-143[»]
3J6Xelectron microscopy6.10161-143[»]
3J6Yelectron microscopy6.10161-143[»]
3J77electron microscopy6.20161-143[»]
3J78electron microscopy6.30161-143[»]
3V88X-ray3.00Q1-143[»]
4U3MX-ray3.00C6/c62-143[»]
4U3NX-ray3.20C6/c62-143[»]
4U3UX-ray2.90C6/c62-143[»]
4U4NX-ray3.10C6/c62-143[»]
4U4OX-ray3.60C6/c62-143[»]
4U4QX-ray3.00C6/c62-143[»]
4U4RX-ray2.80C6/c62-143[»]
4U4UX-ray3.00C6/c62-143[»]
4U4YX-ray3.20C6/c62-143[»]
4U4ZX-ray3.10C6/c62-143[»]
4U50X-ray3.20C6/c62-143[»]
4U51X-ray3.20C6/c62-143[»]
4U52X-ray3.00C6/c62-143[»]
4U53X-ray3.30C6/c62-143[»]
4U55X-ray3.20C6/c62-143[»]
4U56X-ray3.45C6/c62-143[»]
4U6FX-ray3.10C6/c62-143[»]
4V4Belectron microscopy11.70AI2-143[»]
4V6Ielectron microscopy8.80AI1-143[»]
4V7RX-ray4.00AJ/CJ1-143[»]
4V88X-ray3.00AQ/CQ1-143[»]
4V8Yelectron microscopy4.30AQ1-143[»]
4V8Zelectron microscopy6.60AQ1-143[»]
4V92electron microscopy3.70Q3-142[»]
5DC3X-ray3.25C6/c62-143[»]
5FCIX-ray3.40C6/c62-143[»]
5FCJX-ray3.10C6/c62-143[»]
5I4LX-ray3.10C6/c62-143[»]
ProteinModelPortaliP0CX51.
SMRiP0CX51. Positions 3-143.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0CX51.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S9P family.Curated

Phylogenomic databases

InParanoidiP0CX51.
KOiK02960.
OrthoDBiEOG092C5DBH.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000754. Ribosomal_S9.
IPR020574. Ribosomal_S9_CS.
[Graphical view]
PANTHERiPTHR21569. PTHR21569. 1 hit.
PfamiPF00380. Ribosomal_S9. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
PROSITEiPS00360. RIBOSOMAL_S9. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0CX51-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAVPSVQTF GKKKSATAVA HVKAGKGLIK VNGSPITLVE PEILRFKVYE
60 70 80 90 100
PLLLVGLDKF SNIDIRVRVT GGGHVSQVYA IRQAIAKGLV AYHQKYVDEQ
110 120 130 140
SKNELKKAFT SYDRTLLIAD SRRPEPKKFG GKGARSRFQK SYR
Length:143
Mass (Da):15,847
Last modified:June 28, 2011 - v1
Checksum:i46360374CD9730CC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47071 Genomic DNA. Translation: CAA87357.1.
BK006946 Genomic DNA. Translation: DAA10039.1.
PIRiS67619.
RefSeqiNP_010200.1. NM_001180142.1.
NP_013863.2. NM_001182645.1.

Genome annotation databases

EnsemblFungiiYDL083C; YDL083C; YDL083C.
YMR143W; YMR143W; YMR143W.
GeneIDi851476.
855174.
KEGGisce:YDL083C.
sce:YMR143W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z47071 Genomic DNA. Translation: CAA87357.1.
BK006946 Genomic DNA. Translation: DAA10039.1.
PIRiS67619.
RefSeqiNP_010200.1. NM_001180142.1.
NP_013863.2. NM_001182645.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Xmodel-I5-143[»]
3J6Xelectron microscopy6.10161-143[»]
3J6Yelectron microscopy6.10161-143[»]
3J77electron microscopy6.20161-143[»]
3J78electron microscopy6.30161-143[»]
3V88X-ray3.00Q1-143[»]
4U3MX-ray3.00C6/c62-143[»]
4U3NX-ray3.20C6/c62-143[»]
4U3UX-ray2.90C6/c62-143[»]
4U4NX-ray3.10C6/c62-143[»]
4U4OX-ray3.60C6/c62-143[»]
4U4QX-ray3.00C6/c62-143[»]
4U4RX-ray2.80C6/c62-143[»]
4U4UX-ray3.00C6/c62-143[»]
4U4YX-ray3.20C6/c62-143[»]
4U4ZX-ray3.10C6/c62-143[»]
4U50X-ray3.20C6/c62-143[»]
4U51X-ray3.20C6/c62-143[»]
4U52X-ray3.00C6/c62-143[»]
4U53X-ray3.30C6/c62-143[»]
4U55X-ray3.20C6/c62-143[»]
4U56X-ray3.45C6/c62-143[»]
4U6FX-ray3.10C6/c62-143[»]
4V4Belectron microscopy11.70AI2-143[»]
4V6Ielectron microscopy8.80AI1-143[»]
4V7RX-ray4.00AJ/CJ1-143[»]
4V88X-ray3.00AQ/CQ1-143[»]
4V8Yelectron microscopy4.30AQ1-143[»]
4V8Zelectron microscopy6.60AQ1-143[»]
4V92electron microscopy3.70Q3-142[»]
5DC3X-ray3.25C6/c62-143[»]
5FCIX-ray3.40C6/c62-143[»]
5FCJX-ray3.10C6/c62-143[»]
5I4LX-ray3.10C6/c62-143[»]
ProteinModelPortaliP0CX51.
SMRiP0CX51. Positions 3-143.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31978. 80 interactions.
35319. 90 interactions.
IntActiP0CX51. 2 interactions.
MINTiMINT-8285666.

PTM databases

iPTMnetiP0CX51.

Proteomic databases

MaxQBiP0CX51.
TopDownProteomicsiP0CX51.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL083C; YDL083C; YDL083C.
YMR143W; YMR143W; YMR143W.
GeneIDi851476.
855174.
KEGGisce:YDL083C.
sce:YMR143W.

Organism-specific databases

SGDiS000004751. RPS16A.

Phylogenomic databases

InParanoidiP0CX51.
KOiK02960.
OrthoDBiEOG092C5DBH.

Enzyme and pathway databases

BioCyciYEAST:G3O-32835-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-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SCE-72702. Ribosomal scanning and start codon recognition.
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

EvolutionaryTraceiP0CX51.
PROiP0CX51.

Gene expression databases

ExpressionAtlasiP0CX51. differential.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR000754. Ribosomal_S9.
IPR020574. Ribosomal_S9_CS.
[Graphical view]
PANTHERiPTHR21569. PTHR21569. 1 hit.
PfamiPF00380. Ribosomal_S9. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
PROSITEiPS00360. RIBOSOMAL_S9. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRS16A_YEAST
AccessioniPrimary (citable) accession number: P0CX51
Secondary accession number(s): D6VRR6, P26787, P40213
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: September 7, 2016
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 33800 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for S16 in yeast.

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 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.