Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Rpsa. (This text reflects annotations as of Wednesday, January 23, 2013.) MGI curation of this mouse gene is considered complete, including annotations derived from the biomedical literature as of August 29, 2008. If you know of any additional information regarding this mouse gene please let us know. Please supply mouse gene symbol and a PubMed ID.

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Many of the effects of laminin are mediated through interactions with cell surface receptors. These receptors include members of the integrin family, as well as non-integrin laminin-binding proteins. This gene encodes a high-affinity, non-integrin family, laminin receptor 1. This receptor has been variously called 67 kD laminin receptor, 37 kD laminin receptor precursor (37LRP) and p40 ribosome-associated protein. The amino acid sequence of laminin receptor 1 is highly conserved through evolution, suggesting a key biological function. It has been observed that the level of the laminin receptor transcript is higher in colon carcinoma tissue and lung cancer cell line than their normal counterparts. Also, there is a correlation between the upregulation of this polypeptide in cancer cells and their invasive and metastatic phenotype. Multiple copies of this gene exist, however, most of them are pseudogenes thought to have arisen from retropositional events. Two alternatively spliced transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Rpsa
  • performs the following molecular functions:
    • laminin binding ^[1]
  • is located in the following cellular components:
    • cytoplasm ^[2]
    • nucleus ^[2]
    • small ribosomal subunit ^[2]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Rpsa:
  • participates in the following biological processes:
    • cell-cell adhesion
    • endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
    • endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA)
    • ribosomal small subunit assembly
    • rRNA export from nucleus
    • translation
  • performs the following molecular functions:
    • ribosome binding
    • structural constituent of ribosome
  • is located in the following cellular components:
    • 90S preribosome
    • basement membrane
    • cytoplasm
    • cytosol
    • cytosolic small ribosomal subunit
    • extracellular matrix
    • membrane
    • neuronal cell body
    • plasma membrane

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Summary text based on GO annotations supported by structural data

• Rpsa encodes a protein or proteins that contain the following InterPro domains: Ribosomal protein S2, Ribosomal protein S2, conserved site, Ribosomal protein S2, eukaryotic/archaeal, Ribosomal protein S2, flavodoxin-like domain, indicating that the gene product:
  • is located in the following cellular components:
    • intracellular
    • ribosome

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Rpsa indicates that it:
  • is located in the following cellular components:
    • ribonucleoprotein complex
    • ribosome

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References

1. Fulcher KD et al. (1993) Characterization of laminin receptor messenger ribonucleic acid and protein expression in mouse spermatogenic cells. Biol Reprod, 48:674-82. (PubMed:8452943)
2. McCaffery P et al. (1990) A dorso-ventral asymmetry in the embryonic retina defined by protein conformation. Proc Natl Acad Sci U S A, 87:8570-4. (PubMed:2146686)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

ISS Inferred from sequence or structural similarity

ISO Inferred from sequence orthology

ISA Inferred from sequence alignment

ISM Inferred from sequence model

NAS Non-traceable author statement

ND No biological data available

RCA Reviewed computational analysis

TAS Traceable author statement

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