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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

Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.1 Publication

GO - Molecular functioni

  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • ribosomal small subunit biogenesis Source: GO_Central
  • ribosome biogenesis Source: SGD
  • rRNA methylation Source: Reactome
  • rRNA processing Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Ribosome 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.
R-SCE-6791226. Major pathway of rRNA processing in the nucleolus.
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-A
Alternative name(s):
RP30
RP40
Gene namesi
Name:RPS7A
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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 19018940S ribosomal protein S7-APRO_0000174212Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei10 – 101PhosphoserineBy similarity
Modified residuei31 – 311PhosphoserineBy similarity
Cross-linki124 – 124Glycyl 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. 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). Interacts with snoRNA U3. Interacts with MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.2 Publications

Protein-protein interaction databases

BioGridi34494. 72 interactions.
DIPiDIP-2592N.
IntActiP26786. 60 interactions.
MINTiMINT-427651.

Structurei

Secondary structure

1
190
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 83Combined sources
Beta strandi9 – 124Combined sources
Helixi16 – 2813Combined sources
Helixi31 – 344Combined sources
Beta strandi35 – 384Combined sources
Beta strandi45 – 506Combined sources
Beta strandi52 – 543Combined sources
Beta strandi56 – 627Combined sources
Beta strandi64 – 663Combined sources
Helixi67 – 704Combined sources
Beta strandi71 – 744Combined sources
Helixi77 – 837Combined sources
Beta strandi87 – 948Combined sources
Beta strandi104 – 1063Combined sources
Helixi114 – 1163Combined sources
Helixi118 – 12912Combined sources
Beta strandi135 – 1428Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi148 – 1547Combined sources
Beta strandi156 – 1583Combined sources
Helixi159 – 1613Combined sources
Turni162 – 1654Combined sources
Helixi166 – 17712Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi181 – 1844Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
5FCIX-ray3.40S7/s72-190[»]
5FCJX-ray3.10S7/s72-190[»]
ProteinModelPortaliP26786.
SMRiP26786. Positions 4-187.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S7e family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000014122.
HOGENOMiHOG000197237.
InParanoidiP26786.
KOiK02993.
OMAiVFEFPIT.
OrthoDBiEOG7P02W9.

Family and domain databases

InterProiIPR000554. Ribosomal_S7e.
[Graphical view]
PANTHERiPTHR11278. PTHR11278. 1 hit.
PfamiPF01251. Ribosomal_S7e. 1 hit.
[Graphical view]
PROSITEiPS00948. RIBOSOMAL_S7E. 1 hit.
[Graphical view]

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241F → E AA sequence (PubMed:1544921).Curated

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
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[»]
5FCIX-ray3.40S7/s72-190[»]
5FCJX-ray3.10S7/s72-190[»]
ProteinModelPortaliP26786.
SMRiP26786. Positions 4-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34494. 72 interactions.
DIPiDIP-2592N.
IntActiP26786. 60 interactions.
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.
OMAiVFEFPIT.
OrthoDBiEOG7P02W9.

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.
R-SCE-6791226. Major pathway of rRNA processing in the nucleolus.
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

PROiP26786.

Family and domain databases

InterProiIPR000554. Ribosomal_S7e.
[Graphical view]
PANTHERiPTHR11278. PTHR11278. 1 hit.
PfamiPF01251. Ribosomal_S7e. 1 hit.
[Graphical view]
PROSITEiPS00948. RIBOSOMAL_S7E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
    Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
    , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
    Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "NH2-terminal acetylation of ribosomal proteins of Saccharomyces cerevisiae."
    Takakura H., Tsunasawa S., Miyagi M., Warner J.R.
    J. Biol. Chem. 267:5442-5445(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-26, ACETYLATION AT SER-2 BY NATA.
  5. "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae."
    Planta R.J., Mager W.H.
    Yeast 14:471-477(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE, SUBUNIT.
  6. "The action of N-terminal acetyltransferases on yeast ribosomal proteins."
    Arnold R.J., Polevoda B., Reilly J.P., Sherman F.
    J. Biol. Chem. 274:37035-37040(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2 BY NATA.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "The small-subunit processome is a ribosome assembly intermediate."
    Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S., Baserga S.J.
    Eukaryot. Cell 3:1619-1626(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU PROCESSOME, SUBCELLULAR LOCATION.
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRS7A_YEAST
AccessioniPrimary (citable) accession number: P26786
Secondary accession number(s): D6W2F7, Q08502
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 142 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 41000 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for S7 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 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.