60S acidic ribosomal protein P1

RPLP1
Available structures
PDBHuman UniProt search: PDBe RCSB
Identifiers
Aliases RPLP1, LP1, P1, RPP1, ribosomal protein lateral stalk subunit P1
External IDs HomoloGene: 133573 GeneCards: RPLP1
Orthologs
Species Human Mouse
Entrez

6176

n/a

Ensembl

ENSG00000137818

n/a

UniProt

P05386

n/a

RefSeq (mRNA)

NM_213725
NM_001003

n/a

RefSeq (protein)

NP_000994.1
NP_998890.1
NP_000994.1

n/a

Location (UCSC) Chr 15: 69.45 – 69.46 Mb n/a
PubMed search [1] n/a
Wikidata
View/Edit Human

60S acidic ribosomal protein P1 is a protein that in humans is encoded by the RPLP1 gene.[2]

Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal phosphoprotein that is a component of the 60S subunit. The protein, which is a functional equivalent of the E. coli L7/L12 ribosomal protein, belongs to the L12P family of ribosomal proteins. It plays an important role in the elongation step of protein synthesis. Unlike most ribosomal proteins, which are basic, the encoded protein is acidic. Its C-terminal end is nearly identical to the C-terminal ends of the ribosomal phosphoproteins P0 and P2. The P1 protein can interact with P0 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. Two alternatively spliced transcript variants that encode different proteins have been observed. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.[2]

Interactions

RPLP1 has been shown to interact with RPLP2.[3]

References

  1. "Human PubMed Reference:".
  2. 1 2 "Entrez Gene: RPLP1 ribosomal protein, large, P1".
  3. Tchórzewski, M; Boldyreff B; Issinger O G; Grankowski N (July 2000). "Analysis of the protein-protein interactions between the human acidic ribosomal P-proteins: evaluation by the two hybrid system". Int. J. Biochem. Cell Biol. England. 32 (7): 737–46. doi:10.1016/S1357-2725(00)00017-0. PMID 10856704.

Further reading


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