60S acidic ribosomal protein P1

60S acidic ribosomal protein P1 is a protein that in humans is encoded by the RPLP1 gene.[3]

RPLP1
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 2LBF, 4BEH, 4V6X,%%s4V6X, 4BEH
Identifiers
Aliases	RPLP1, LP1, P1, RPP1, ribosomal protein lateral stalk subunit P1
External IDs	OMIM: 180520 HomoloGene: 133573 GeneCards: RPLP1
Gene location (Human) Chr. Chromosome 15 (human)[1] Band 15q23 Start 69,452,814 bp[1] End 69,456,205 bp[1]
Gene ontology Molecular function • structural constituent of ribosome • GO:0001948 protein binding • protein kinase activator activity • ribonucleoprotein complex binding Cellular component • cytosol • ribosome • focal adhesion • intracellular • cytosolic large ribosomal subunit • extracellular exosome Biological process • viral transcription • SRP-dependent cotranslational protein targeting to membrane • translational initiation • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay • translational elongation • activation of protein kinase activity • cytoplasmic translation • positive regulation of protein kinase activity • protein biosynthesis • rRNA processing Sources:Amigo / QuickGO
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 NP_998890 NP_000994.1	n/a
Location (UCSC)	Chr 15: 69.45 – 69.46 Mb	n/a
PubMed search	[2]	n/a
Wikidata
View/Edit Human

Function

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 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.[3]

Interactions

RPLP1 has been shown to interact with RPLP2.[4]

References

1. GRCh38: Ensembl release 89: ENSG00000137818 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Entrez Gene: RPLP1 ribosomal protein, large, P1".
4. Tchórzewski M, Boldyreff B, Issinger OG, Grankowski N (July 2000). "Analysis of the protein-protein interactions between the human acidic ribosomal P-proteins: evaluation by the two hybrid system". The International Journal of Biochemistry & Cell Biology. 32 (7): 737–46. 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". Biochemistry and Cell Biology. 73 (11–12): 933–47. doi:10.1139/o95-101. PMID 8722009.
• Rich BE, Steitz JA (November 1987). "Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly". Molecular and Cellular Biology. 7 (11): 4065–74. doi:10.1128/mcb.7.11.4065. PMC 368077. PMID 3323886.
• Kato S, Sekine S, Oh SW, Kim NS, Umezawa Y, Abe N, Yokoyama-Kobayashi M, Aoki T (December 1994). "Construction of a human full-length cDNA bank". Gene. 150 (2): 243–50. doi:10.1016/0378-1119(94)90433-2. PMID 7821789.
• Tchórzewski M, Boldyreff B, Issinger OG, Grankowski N (July 2000). "Analysis of the protein-protein interactions between the human acidic ribosomal P-proteins: evaluation by the two hybrid system". The International Journal of Biochemistry & Cell Biology. 32 (7): 737–46. doi:10.1016/S1357-2725(00)00017-0. PMID 10856704.
• Chan SH, Hung FS, Chan DS, Shaw PC (April 2001). "Trichosanthin interacts with acidic ribosomal proteins P0 and P1 and mitotic checkpoint protein MAD2B". European Journal of Biochemistry. 268 (7): 2107–12. doi:10.1046/j.1432-1327.2001.02091.x. PMID 11277934.
• Uechi T, Tanaka T, Kenmochi N (March 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): 223–30. doi:10.1006/geno.2000.6470. PMID 11401437.
• Yoshihama M, Uechi T, Asakawa S, Kawasaki K, Kato S, Higa S, Maeda N, Minoshima S, Tanaka T, Shimizu N, Kenmochi N (March 2002). "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes". Genome Research. 12 (3): 379–90. doi:10.1101/gr.214202. PMC 155282. PMID 11875025.
• Kang MJ, Ahn HS, Lee JY, Matsuhashi S, Park WY (April 2002). "Up-regulation of PDCD4 in senescent human diploid fibroblasts". Biochemical and Biophysical Research Communications. 293 (1): 617–21. doi:10.1016/S0006-291X(02)00264-4. PMID 12054647.
• Tchórzewski M, Krokowski D, Rzeski W, Issinger OG, Grankowski N (February 2003). "The subcellular distribution of the human ribosomal "stalk" components: P1, P2 and P0 proteins". The International Journal of Biochemistry & Cell Biology. 35 (2): 203–11. doi:10.1016/S1357-2725(02)00133-4. PMID 12479870.
• Shu H, Chen S, Bi Q, Mumby M, Brekken DL (March 2004). "Identification of phosphoproteins and their phosphorylation sites in the WEHI-231 B lymphoma cell line". Molecular & Cellular Proteomics. 3 (3): 279–86. doi:10.1074/mcp.D300003-MCP200. PMID 14729942.
• Giorgianni F, Beranova-Giorgianni S, Desiderio DM (March 2004). "Identification and characterization of phosphorylated proteins in the human pituitary". Proteomics. 4 (3): 587–98. doi:10.1002/pmic.200300584. PMID 14997482.
• Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R (August 2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry". Nature Methods. 2 (8): 591–8. doi:10.1038/nmeth776. PMID 16094384.
• Gevaert K, Staes A, Van Damme J, De Groot S, Hugelier K, Demol H, Martens L, Goethals M, Vandekerckhove J (September 2005). "Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC". Proteomics. 5 (14): 3589–99. doi:10.1002/pmic.200401217. PMID 16097034.
• Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (September 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl:11858/00-001M-0000-0010-8592-0. PMID 16169070.
• Nousiainen M, Silljé HH, Sauer G, Nigg EA, Körner R (April 2006). "Phosphoproteome analysis of the human mitotic spindle". Proceedings of the National Academy of Sciences of the United States of America. 103 (14): 5391–6. Bibcode:2006PNAS..103.5391N. doi:10.1073/pnas.0507066103. PMC 1459365. PMID 16565220.
• Beranova-Giorgianni S, Zhao Y, Desiderio DM, Giorgianni F (2006). "Phosphoproteomic analysis of the human pituitary". Pituitary. 9 (2): 109–20. doi:10.1007/s11102-006-8916-x. PMID 16807684.

External links

• Overview of all the structural information available in the PDB for UniProt: P05386 (60S acidic ribosomal protein P1) at the PDBe-KB.