60S acidic ribosomal protein P2

RPLP2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1S4J, 2JDL, 2LBF, 2W1O, 4BEH, 4V6X
Identifiers
Aliases	RPLP2 , D11S2243E, LP2, P2, RPP2, ribosomal protein lateral stalk subunit P2
External IDs	OMIM: 180530 MGI: 1914436 HomoloGene: 133574 GeneCards: RPLP2
Gene location (Human) Chr. Chromosome 11 (human) [1] Band 11p15.5 Start 809,965 bp [1] End 812,880 bp [1]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in nipple abdominal fat lower lobe of lung superficial temporal artery peritoneum pericardium urethra thymus pylorus human penis n/a More reference expression data BioGPS More reference expression data
Gene ontology Molecular function structural constituent of ribosome protein binding Cellular component cytosol ribosome membrane focal adhesion intracellular anatomical structure cytosolic large ribosomal subunit extracellular exosome synapse Biological process viral transcription SRP-dependent cotranslational protein targeting to membrane translational initiation nuclear-transcribed mRNA catabolic process, nonsense-mediated decay cytoplasmic translation translational elongation protein biosynthesis rRNA processing Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6181 67186 Ensembl ENSG00000177600 ENSMUSG00000025508 UniProt P05387 P99027 RefSeq (mRNA) NM_001004 NM_026020 NM_001360657 NM_001360658 RefSeq (protein) NP_000995 NP_080296 NP_001347586 NP_001347587 Location (UCSC) Chr 11: 0.81 – 0.81 Mb n/a PubMed search [2] [3]
Wikidata
View/Edit Human View/Edit Mouse

60S acidic ribosomal protein P2 is a protein that in humans is encoded by the RPLP2 gene. ^{[4] [5]}

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 Escherichia 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 P1. The P2 protein can interact with P0 and P1 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome. ^[5]

Interactions

RPLP2 has been shown to interact with RPLP1. ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000177600 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. Rich BE, Steitz JA (March 1988). "Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly". Mol Cell Biol. 7 (11): 4065–74. doi:10.1128/mcb.7.11.4065. PMC   368077 . PMID   3323886.
5. "Entrez Gene: RPLP2 ribosomal protein, large, P2".
6. 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): 737–746. doi:10.1016/S1357-2725(00)00017-0. PMID   10856704.

Further reading

• Wool IG; Chan YL; Glück A (1996). "Structure and evolution of mammalian ribosomal proteins". Biochem. Cell Biol. 73 (11–12): 933–947. doi:10.1139/o95-101. PMID   8722009.
• Hochstrasser DF, Frutiger S, Paquet N, et al. (1993). "Human liver protein map: a reference database established by microsequencing and gel comparison". Electrophoresis. 13 (12): 992–1001. doi:10.1002/elps.11501301201. PMID   1286669. S2CID   23518983.
• Sharp MG, Adams SM, Elvin P, et al. (1990). "A sequence previously identified as metastasis-related encodes an acidic ribosomal phosphoprotein, P2". Br. J. Cancer. 61 (1): 83–8. doi:10.1038/bjc.1990.19. PMC   1971331 . PMID   2153399.
• Kato S, Sekine S, Oh SW, et al. (1995). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–250. doi:10.1016/0378-1119(94)90433-2. PMID   7821789.
• Matoba R, Okubo K, Hori N, et al. (1994). "The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression". Gene. 146 (2): 199–207. doi:10.1016/0378-1119(94)90293-3. PMID   8076819.
• Scanlan MJ, Gordan JD, Williamson B, et al. (1999). "Antigens recognized by autologous antibody in patients with renal-cell carcinoma". Int. J. Cancer. 83 (4): 456–464. doi: 10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5 . PMID   10508479.
• Tchórzewski M, Boldyreff B, Issinger O, Grankowski N (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. 32 (7): 737–746. doi:10.1016/S1357-2725(00)00017-0. PMID   10856704.
• Uechi T, Tanaka T, Kenmochi N (2001). "A complete map of the human ribosomal protein genes: assignment of 80 genes to the cytogenetic map and implications for human disorders". Genomics. 72 (3): 223–230. doi:10.1006/geno.2000.6470. PMID   11401437.
• Yoshihama M, Uechi T, Asakawa S, et al. (2002). "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes". Genome Res. 12 (3): 379–390. doi:10.1101/gr.214202. PMC   155282 . PMID   11875025.
• Freeman JL, Gonzalo P, Pitcher JA, et al. (2002). "Beta 2-adrenergic receptor stimulated, G protein-coupled receptor kinase 2 mediated, phosphorylation of ribosomal protein P2". Biochemistry. 41 (42): 12850–12857. doi:10.1021/bi020145d. PMID   12379128.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Tchórzewski M, Krokowski D, Rzeski W, et al. (2003). "The subcellular distribution of the human ribosomal "stalk" components: P1, P2 and P0 proteins". Int. J. Biochem. Cell Biol. 35 (2): 203–211. doi:10.1016/S1357-2725(02)00133-4. PMID   12479870.
• Shu H, Chen S, Bi Q, et al. (2004). "Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line". Mol. Cell. Proteomics. 3 (3): 279–286. doi: 10.1074/mcp.D300003-MCP200 . PMID   14729942.
• Gardner-Thorpe J, Ito H, Ashley SW, Whang EE (2004). "Ribosomal protein P2: a potential molecular target for antisense therapy of human malignancies". Anticancer Res. 23 (6C): 4549–60. PMID   14981896.
• Giorgianni F, Beranova-Giorgianni S, Desiderio DM (2004). "Identification and characterization of phosphorylated proteins in the human pituitary". Proteomics. 4 (3): 587–598. doi:10.1002/pmic.200300584. PMID   14997482. S2CID   25355914.
• Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–716. doi:10.1038/nbt971. PMID   15146197. S2CID   27764390.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–2127. doi:10.1101/gr.2596504. PMC   528928 . PMID   15489334.
• Andersen JS, Lam YW, Leung AK, et al. (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID   15635413. S2CID   4344740.