P05388 (RLA0_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 136.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: 60S acidic ribosomal protein P0 Alternative name(s): 60S ribosomal protein L10E | ||
| Gene names |
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| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 317 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Ribosomal protein P0 is the functional equivalent of E.coli protein L10. |
| Subunit structure | P0 forms a pentameric complex by interaction with dimers of P1 and P2. Identified in a mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Interacts with Lassa virus Z protein. Interacts with APEX1. Ref.20 |
| Subcellular location | Nucleus. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.13 Ref.20 |
| Sequence similarities | Belongs to the ribosomal protein L10P family. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| STAU1 | O95793 | 4 | EBI-354101,EBI-358174 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 317 | 317 | 60S acidic ribosomal protein P0 | PRO_0000154758 | |||||
Amino acid modifications | |||||||||
| Modified residue | 24 | 1 | Phosphotyrosine Ref.7 Ref.11 Ref.19 Ref.22 | ||||||
| Modified residue | 77 | 1 | N6-acetyllysine Ref.23 | ||||||
| Modified residue | 304 | 1 | Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.21 Ref.22 | ||||||
| Modified residue | 307 | 1 | Phosphoserine Ref.6 Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.21 Ref.22 | ||||||
Experimental info | |||||||||
| Sequence conflict | 246 | 1 | K → E in AAH01127. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Human acidic ribosomal phosphoproteins P0, P1, and P2: analysis of cDNA clones, in vitro synthesis, and assembly." Rich B.E., Steitz J.A. Mol. Cell. Biol. 7:4065-4074(1987) [PubMed: 3323886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [2] | "The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. Gibbs R.A.Nature 440:346-351(2006) [PubMed: 16541075] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Cervix, Colon, Lung, Lymph, Muscle and Pancreas. |
| [4] | Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 17-38; 84-92; 135-146; 150-162; 248-264 AND 267-297, MASS SPECTROMETRY. Tissue: Fetal brain cortex. |
| [5] | "A map of 75 human ribosomal protein genes." Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C. Genome Res. 8:509-523(1998) [PubMed: 9582194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 218-310. |
| [6] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [7] | "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24, MASS SPECTROMETRY. |
| [8] | "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [9] | "Phosphoproteomic analysis of the human pituitary." Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F. Pituitary 9:109-120(2006) [PubMed: 16807684] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, MASS SPECTROMETRY. Tissue: Pituitary. |
| [10] | "Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, MASS SPECTROMETRY. Tissue: Cervix adenocarcinoma. |
| [11] | "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J.Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24, MASS SPECTROMETRY. Tissue: Lung carcinoma. |
| [12] | "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed: 17487921] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, MASS SPECTROMETRY. Tissue: Prostate cancer. |
| [13] | "Molecular composition of IMP1 ribonucleoprotein granules." Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C. Mol. Cell. Proteomics 6:798-811(2007) [PubMed: 17289661] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION. |
| [14] | "Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [15] | "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, MASS SPECTROMETRY. Tissue: T-cell. |
| [16] | "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [17] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [18] | "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed: 18318008] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, MASS SPECTROMETRY. Tissue: Liver. |
| [19] | "An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24, MASS SPECTROMETRY. Tissue: Mammary epithelium. |
| [20] | "APE1/Ref-1 interacts with NPM1 within nucleoli and plays a role in the rRNA quality control process." Vascotto C., Fantini D., Romanello M., Cesaratto L., Deganuto M., Leonardi A., Radicella J.P., Kelley M.R., D'Ambrosio C., Scaloni A., Quadrifoglio F., Tell G. Mol. Cell. Biol. 29:1834-1854(2009) [PubMed: 19188445] [Abstract] Cited for: INTERACTION WITH APEX1, MASS SPECTROMETRY, SUBCELLULAR LOCATION. |
| [21] | "Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, MASS SPECTROMETRY. |
| [22] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24; SER-304 AND SER-307, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [23] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-77, MASS SPECTROMETRY. |
| [24] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M17885 mRNA. Translation: AAA36470.1. AC004263 Genomic DNA. Translation: AAC05176.1. BC000087 mRNA. Translation: AAH00087.1. BC000345 mRNA. Translation: AAH00345.1. BC000752 mRNA. Translation: AAH00752.1. BC001127 mRNA. Translation: AAH01127.1. BC001834 mRNA. Translation: AAH01834.1. BC003655 mRNA. Translation: AAH03655.1. BC005863 mRNA. Translation: AAH05863.1. BC008092 mRNA. Translation: AAH08092.1. BC008594 mRNA. Translation: AAH08594.1. BC009867 mRNA. Translation: AAH09867.1. BC015173 mRNA. Translation: AAH15173.1. BC015690 mRNA. Translation: AAH15690.1. AB007187 Genomic DNA. Translation: BAA25845.1. |
| IPI | IPI00008530. |
| PIR | R5HUP0. A27125. |
| RefSeq | NP_000993.1. NM_001002.3. NP_444505.1. NM_053275.3. |
| UniGene | Hs.546285. |
3D structure databases | |
| ProteinModelPortal | P05388. |
| SMR | P05388. Positions 1-259, 261-308. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P05388. 18 interactions. |
| MINT | MINT-193149. |
| STRING | P05388. |
PTM databases | |
| PhosphoSite | P05388. |
Polymorphism databases | |
| DMDM | 133041. |
2D gel databases | |
| REPRODUCTION-2DPAGE | P05388. |
Proteomic databases | |
| PRIDE | P05388. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000228306; ENSP00000339027; ENSG00000089157. ENST00000392514; ENSP00000376299; ENSG00000089157. |
| GeneID | 6175. |
| KEGG | hsa:6175. |
| UCSC | uc001txp.1. human. |
Organism-specific databases | |
| CTD | 6175. |
| GeneCards | GC12M120634. |
| H-InvDB | HIX0011057. HIX0026908. |
| HGNC | HGNC:10371. RPLP0. |
| HPA | HPA003512. |
| MIM | 180510. gene. |
| neXtProt | NX_P05388. |
| PharmGKB | PA34772. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG05739. |
| HOVERGEN | HBG000711. |
| InParanoid | P05388. |
| OMA | GSTGMPP. |
| OrthoDB | EOG4VDQ10. |
| PhylomeDB | P05388. |
Enzyme and pathway databases | |
| Reactome | REACT_111045. Developmental Biology. REACT_111217. Metabolism. REACT_15380. Diabetes pathways. REACT_17015. Metabolism of proteins. REACT_1762. 3' -UTR-mediated translational regulation. REACT_6167. Influenza Infection. REACT_71. Gene Expression. |
Gene expression databases | |
| CleanEx | HS_RPLP0. |
| Genevestigator | P05388. |
| GermOnline | ENSG00000089157. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR001813. Ribosomal_60S. IPR001790. Ribosomal_L10/acidic_P0. [Graphical view] |
| KO | K02941. |
| Pfam | PF00428. Ribosomal_60s. 1 hit. PF00466. Ribosomal_L10. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 23989. |
| SOURCE | Search... |
Entry information
| Entry name | RLA0_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P05388 Secondary accession number(s): Q9BVK4 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Ribosomal proteins Ribosomal proteins families and list of entries |
| Human chromosome 12 Human chromosome 12: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with