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ECOLI:RS1

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Species (Taxon ID) Escherichia coli (strain K12). (83333)
Gene Name(s) rpsA (synonyms: ssyF)
Protein Name(s) 30S ribosomal protein S1
External Links
UniProt P0AG67
EMBL V00342
V00352
U00096
AP009048
X00785
X04864
PIR F64830
RefSeq NP_415431.1
YP_489183.1
PDB 2BH8
2KHI
2KHJ
4Q7J
PDBsum 2BH8
2KHI
2KHJ
4Q7J
ProteinModelPortal P0AG67
SMR P0AG67
BioGrid 849910
DIP DIP-35884N
IntAct P0AG67
MINT MINT-1315122
STRING 511145.b0911
ChEMBL CHEMBL2363135
PhosSite P010447
SWISS-2DPAGE P0AG67
PaxDb P0AG67
PRIDE P0AG67
EnsemblBacteria AAC73997
BAA35655
GeneID 12934066
945536
KEGG ecj:Y75_p0883
eco:b0911
PATRIC 32117035
EchoBASE EB0893
EcoGene EG10900
eggNOG COG0539
HOGENOM HOG000044052
InParanoid P0AG67
KO K02945
OMA IIVHVSE
OrthoDB EOG6WT8CC
PhylomeDB P0AG67
BioCyc EcoCyc:EG10900-MONOMER
ECOL316407:JW0894-MONOMER
EvolutionaryTrace P0AG67
PRO PR:P0AG67
Proteomes UP000000318
UP000000625
Genevestigator P0AG67
GO GO:0005737
GO:0022627
GO:0016020
GO:0003729
GO:0003723
GO:0003735
GO:2000766
GO:0006412
Gene3D 2.40.50.140
InterPro IPR012340
IPR003029
IPR000110
IPR022967
Pfam PF00575
PIRSF PIRSF002111
PRINTS PR00681
SMART SM00316
SUPFAM SSF50249
TIGRFAMs TIGR00717
PROSITE PS50126

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0003735

structural constituent of ribosome

PMID:3297162[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0000028

ribosomal small subunit assembly

PMID:3297162[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0022627

cytosolic small ribosomal subunit

PMID:3297162[1]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0016020

membrane

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

PMID:16858726[2]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0022627

cytosolic small ribosomal subunit

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10900
PANTHER:PTN000076734

C

Seeded From UniProt

complete

involved_in

GO:0006412

translation

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10900
PANTHER:PTN000076677

P

Seeded From UniProt

complete

enables

GO:0003735

structural constituent of ribosome

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10900
PANTHER:PTN000076677

F

Seeded From UniProt

complete

enables

GO:0003729

mRNA binding

PMID:21873635[3]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

EcoGene:EG10900
PANTHER:PTN000076677
TAIR:locus:2145860

F

Seeded From UniProt

complete

involved_in

GO:2000766

negative regulation of cytoplasmic translation

PMID:2120211[4]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:2000766

negative regulation of cytoplasmic translation

PMID:2120211[4]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0022627

cytosolic small ribosomal subunit

PMID:4942549[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0022627

cytosolic small ribosomal subunit

PMID:342903[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006412

translation

PMID:9677288[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003735

structural constituent of ribosome

PMID:22412910[8]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003729

mRNA binding

PMID:16890206[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

PMID:15494393[10]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003676

nucleic acid binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003029

F

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000110

F

Seeded From UniProt

complete

enables

GO:0003735

structural constituent of ribosome

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000110

F

Seeded From UniProt

complete

part_of

GO:0005840

ribosome

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000110

C

Seeded From UniProt

complete

involved_in

GO:0006412

translation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR000110

P

Seeded From UniProt

complete

part_of

GO:0005840

ribosome

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0689

C

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0694

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 1.2 Littlechild, J et al. (1987) The tertiary structure of salt-extracted ribosomal proteins from Escherichia coli as studied by proton magnetic resonance spectroscopy and limited proteolysis experiments. Biochim. Biophys. Acta 913 245-55 PubMed GONUTS page
  2. ↑ 2.0 2.1 Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 3.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  4. ↑ 4.0 4.1 Skouv, J et al. (1990) Ribosomal protein S1 of Escherichia coli is the effector for the regulation of its own synthesis. J. Biol. Chem. 265 17044-9 PubMed GONUTS page
  5. ↑ Hindennach, I et al. (1971) Ribosomal proteins. Isolation of the proteins from 30S ribosomal subunits of Escherichia coli. Eur. J. Biochem. 23 7-11 PubMed GONUTS page
  6. ↑ Subramanian, AR & van Duin, J (1977) Exchange of individual ribosomal proteins between ribosomes as studied by heavy isotope-transfer experiments. Mol. Gen. Genet. 158 1-9 PubMed GONUTS page
  7. ↑ Sørensen, MA et al. (1998) Ribosomal protein S1 is required for translation of most, if not all, natural mRNAs in Escherichia coli in vivo. J. Mol. Biol. 280 561-9 PubMed GONUTS page
  8. ↑ Byrgazov, K et al. (2012) Direct interaction of the N-terminal domain of ribosomal protein S1 with protein S2 in Escherichia coli. PLoS ONE 7 e32702 PubMed GONUTS page
  9. ↑ Koleva, RI et al. (2006) Interactions of ribosomal protein S1 with DsrA and rpoS mRNA. Biochem. Biophys. Res. Commun. 348 662-8 PubMed GONUTS page
  10. ↑ Wower, IK et al. (2004) Contributions of pseudoknots and protein SmpB to the structure and function of tmRNA in trans-translation. J. Biol. Chem. 279 54202-9 PubMed GONUTS page
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