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Protein

40S ribosomal protein S7-A

Gene

RPS7A

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 (PubMed:22096102). eS7 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835).1 Publication1 Publication

Miscellaneous

Present with 41000 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eS7 in yeast.Curated

GO - Molecular functioni

  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • ribosome biogenesis Source: SGD
  • rRNA methylation Source: Reactome

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein
Biological processRibosome biogenesis, rRNA processing

Enzyme and pathway databases

BioCyciYEAST:G3O-33629-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-6790901. rRNA modification in the nucleus and cytosol.
R-SCE-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.
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 S7-A1 Publication
Alternative name(s):
RP30
RP40
Small ribosomal subunit protein eS7-A1 Publication
Gene namesi
Name:RPS7A1 Publication
Synonyms:RPS30
Ordered Locus Names:YOR096W
ORF Names:YOR3177W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR096W.
SGDiS000005622. RPS7A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: SGD
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • small-subunit processome Source: SGD

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001742122 – 19040S ribosomal protein S7-AAdd BLAST189

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine2 Publications1
Modified residuei10PhosphoserineBy similarity1
Modified residuei31PhosphoserineBy similarity1
Cross-linki124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP26786.
PRIDEiP26786.
TopDownProteomicsiP26786.

PTM databases

iPTMnetiP26786.

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). Interacts with snoRNA U3. uS11 interacts with MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3 (PubMed:15590835).1 Publication2 Publications

Protein-protein interaction databases

BioGridi34494. 123 interactors.
DIPiDIP-2592N.
IntActiP26786. 61 interactors.
MINTiMINT-427651.

Structurei

Secondary structure

1190
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 8Combined sources3
Beta strandi9 – 12Combined sources4
Helixi16 – 28Combined sources13
Helixi31 – 34Combined sources4
Beta strandi35 – 38Combined sources4
Beta strandi45 – 50Combined sources6
Beta strandi52 – 54Combined sources3
Beta strandi56 – 62Combined sources7
Beta strandi64 – 66Combined sources3
Helixi67 – 70Combined sources4
Beta strandi71 – 74Combined sources4
Helixi77 – 83Combined sources7
Beta strandi87 – 94Combined sources8
Beta strandi104 – 106Combined sources3
Helixi114 – 116Combined sources3
Helixi118 – 129Combined sources12
Beta strandi135 – 142Combined sources8
Beta strandi144 – 146Combined sources3
Beta strandi148 – 154Combined sources7
Beta strandi156 – 158Combined sources3
Helixi159 – 161Combined sources3
Turni162 – 165Combined sources4
Helixi166 – 177Combined sources12
Beta strandi178 – 180Combined sources3
Beta strandi181 – 184Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J6Xelectron microscopy6.10S71-190[»]
3J6Yelectron microscopy6.10S71-190[»]
3J77electron microscopy6.20S71-190[»]
3J78electron microscopy6.30S71-190[»]
3V88X-ray3.00H1-190[»]
4U3MX-ray3.00S7/s72-190[»]
4U3NX-ray3.20S7/s72-190[»]
4U3UX-ray2.90S7/s72-190[»]
4U4NX-ray3.10S7/s72-190[»]
4U4OX-ray3.60S7/s72-190[»]
4U4QX-ray3.00S7/s72-190[»]
4U4RX-ray2.80S7/s72-190[»]
4U4UX-ray3.00S7/s72-190[»]
4U4YX-ray3.20S7/s72-190[»]
4U4ZX-ray3.10S7/s72-190[»]
4U50X-ray3.20S7/s72-190[»]
4U51X-ray3.20S7/s72-190[»]
4U52X-ray3.00S7/s72-190[»]
4U53X-ray3.30S7/s72-190[»]
4U55X-ray3.20S7/s72-190[»]
4U56X-ray3.45S7/s72-190[»]
4U6FX-ray3.10S7/s72-190[»]
4V88X-ray3.00AH/CH1-190[»]
4V8Yelectron microscopy4.30AH1-190[»]
4V8Zelectron microscopy6.60AH1-190[»]
4V92electron microscopy3.70H4-187[»]
5DATX-ray3.15S7/s72-190[»]
5DC3X-ray3.25S7/s72-190[»]
5DGEX-ray3.45S7/s72-190[»]
5DGFX-ray3.30S7/s72-190[»]
5DGVX-ray3.10S7/s72-190[»]
5FCIX-ray3.40S7/s72-190[»]
5FCJX-ray3.10S7/s72-190[»]
5I4LX-ray3.10S7/s72-187[»]
5JUOelectron microscopy4.00EB1-190[»]
5JUPelectron microscopy3.50EB1-190[»]
5JUSelectron microscopy4.20EB1-190[»]
5JUTelectron microscopy4.00EB1-190[»]
5JUUelectron microscopy4.00EB1-190[»]
5LYBX-ray3.25S7/s72-187[»]
5M1Jelectron microscopy3.30H24-187[»]
5MC6electron microscopy3.80U1-190[»]
5TGAX-ray3.30S7/s72-187[»]
5TGMX-ray3.50S7/s72-187[»]
5TZSelectron microscopy5.1071-190[»]
5WYJelectron microscopy8.70SI1-190[»]
5WYKelectron microscopy4.50SI1-190[»]
ProteinModelPortaliP26786.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000014122.
HOGENOMiHOG000197237.
InParanoidiP26786.
KOiK02993.
OMAiKVQTRLT.
OrthoDBiEOG092C4XAM.

Family and domain databases

InterProiView protein in InterPro
IPR000554. Ribosomal_S7e.
PANTHERiPTHR11278. PTHR11278. 1 hit.
PfamiView protein in Pfam
PF01251. Ribosomal_S7e. 1 hit.
PROSITEiView protein in PROSITE
PS00948. RIBOSOMAL_S7E. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P26786-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAPQAKILS QAPTELELQV AQAFVELENS SPELKAELRP LQFKSIREID
60 70 80 90 100
VAGGKKALAI FVPVPSLAGF HKVQTKLTRE LEKKFQDRHV IFLAERRILP
110 120 130 140 150
KPSRTSRQVQ KRPRSRTLTA VHDKILEDLV FPTEIVGKRV RYLVGGNKIQ
160 170 180 190
KVLLDSKDVQ QIDYKLESFQ AVYNKLTGKQ IVFEIPSETH
Length:190
Mass (Da):21,622
Last modified:January 23, 2007 - v4
Checksum:i0096C3D7B6A196A3
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti24F → E AA sequence (PubMed:1544921).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94335 Genomic DNA. Translation: CAA64018.1. Sequence problems.
Z75004 Genomic DNA. Translation: CAA99293.1.
BK006948 Genomic DNA. Translation: DAA10873.1.
PIRiS66981.
RefSeqiNP_014739.1. NM_001183515.1.

Genome annotation databases

EnsemblFungiiYOR096W; YOR096W; YOR096W.
GeneIDi854263.
KEGGisce:YOR096W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X94335 Genomic DNA. Translation: CAA64018.1. Sequence problems.
Z75004 Genomic DNA. Translation: CAA99293.1.
BK006948 Genomic DNA. Translation: DAA10873.1.
PIRiS66981.
RefSeqiNP_014739.1. NM_001183515.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3J6Xelectron microscopy6.10S71-190[»]
3J6Yelectron microscopy6.10S71-190[»]
3J77electron microscopy6.20S71-190[»]
3J78electron microscopy6.30S71-190[»]
3V88X-ray3.00H1-190[»]
4U3MX-ray3.00S7/s72-190[»]
4U3NX-ray3.20S7/s72-190[»]
4U3UX-ray2.90S7/s72-190[»]
4U4NX-ray3.10S7/s72-190[»]
4U4OX-ray3.60S7/s72-190[»]
4U4QX-ray3.00S7/s72-190[»]
4U4RX-ray2.80S7/s72-190[»]
4U4UX-ray3.00S7/s72-190[»]
4U4YX-ray3.20S7/s72-190[»]
4U4ZX-ray3.10S7/s72-190[»]
4U50X-ray3.20S7/s72-190[»]
4U51X-ray3.20S7/s72-190[»]
4U52X-ray3.00S7/s72-190[»]
4U53X-ray3.30S7/s72-190[»]
4U55X-ray3.20S7/s72-190[»]
4U56X-ray3.45S7/s72-190[»]
4U6FX-ray3.10S7/s72-190[»]
4V88X-ray3.00AH/CH1-190[»]
4V8Yelectron microscopy4.30AH1-190[»]
4V8Zelectron microscopy6.60AH1-190[»]
4V92electron microscopy3.70H4-187[»]
5DATX-ray3.15S7/s72-190[»]
5DC3X-ray3.25S7/s72-190[»]
5DGEX-ray3.45S7/s72-190[»]
5DGFX-ray3.30S7/s72-190[»]
5DGVX-ray3.10S7/s72-190[»]
5FCIX-ray3.40S7/s72-190[»]
5FCJX-ray3.10S7/s72-190[»]
5I4LX-ray3.10S7/s72-187[»]
5JUOelectron microscopy4.00EB1-190[»]
5JUPelectron microscopy3.50EB1-190[»]
5JUSelectron microscopy4.20EB1-190[»]
5JUTelectron microscopy4.00EB1-190[»]
5JUUelectron microscopy4.00EB1-190[»]
5LYBX-ray3.25S7/s72-187[»]
5M1Jelectron microscopy3.30H24-187[»]
5MC6electron microscopy3.80U1-190[»]
5TGAX-ray3.30S7/s72-187[»]
5TGMX-ray3.50S7/s72-187[»]
5TZSelectron microscopy5.1071-190[»]
5WYJelectron microscopy8.70SI1-190[»]
5WYKelectron microscopy4.50SI1-190[»]
ProteinModelPortaliP26786.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34494. 123 interactors.
DIPiDIP-2592N.
IntActiP26786. 61 interactors.
MINTiMINT-427651.

PTM databases

iPTMnetiP26786.

Proteomic databases

MaxQBiP26786.
PRIDEiP26786.
TopDownProteomicsiP26786.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR096W; YOR096W; YOR096W.
GeneIDi854263.
KEGGisce:YOR096W.

Organism-specific databases

EuPathDBiFungiDB:YOR096W.
SGDiS000005622. RPS7A.

Phylogenomic databases

GeneTreeiENSGT00390000014122.
HOGENOMiHOG000197237.
InParanoidiP26786.
KOiK02993.
OMAiKVQTRLT.
OrthoDBiEOG092C4XAM.

Enzyme and pathway databases

BioCyciYEAST:G3O-33629-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-6790901. rRNA modification in the nucleus and cytosol.
R-SCE-6791226. Major pathway of rRNA processing in the nucleolus and cytosol.
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

PROiPR:P26786.

Family and domain databases

InterProiView protein in InterPro
IPR000554. Ribosomal_S7e.
PANTHERiPTHR11278. PTHR11278. 1 hit.
PfamiView protein in Pfam
PF01251. Ribosomal_S7e. 1 hit.
PROSITEiView protein in PROSITE
PS00948. RIBOSOMAL_S7E. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRS7A_YEAST
AccessioniPrimary (citable) accession number: P26786
Secondary accession number(s): D6W2F7, Q08502
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: May 10, 2017
This is version 150 of the entry and version 4 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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.