Reviewed, UniProtKB/Swiss-Prot P05388 (RLA0_HUMAN)

Names and origin

Protein names

Recommended name:
    60S acidic ribosomal protein P0
Alternative name(s):
    L10E

Gene names

Name:

RPLP0

Organism

Homo sapiens (Human) [Complete proteome]

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.
Sequence processing	The displayed sequence is not processed.
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.
Subcellular location	Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.13
Sequence similarities	Belongs to the ribosomal protein L10P family.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW ribosome biogenesis Inferred from electronic annotation. Source: InterPro translational elongation Inferred from Experiment. Source: Reactome
Cellular component	cytosolic large ribosomal subunit Ref.1 Traceable author statement. Source: ProtInc
Molecular function	RNA binding Ref.1 Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct structural constituent of ribosome Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
STAU1	O95793	1	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.20
	Modified residue	77	1	N6-acetyllysine Ref.22
	Modified residue	304	1	Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17
	Modified residue	307	1	Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.6 Ref.18
Experimental info
	Sequence conflict	246	1	K → E in AAH01127. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P05388-1 [UniParc]. Last modified November 1, 1988. Version 1. Checksum: 255AD25571C51199	FASTA	317	34,274
	10 20 30 40 50 60 MPREDRATWK SNYFLKIIQL LDDYPKCFIV GADNVGSKQM QQIRMSLRGK AVVLMGKNTM 70 80 90 100 110 120 MRKAIRGHLE NNPALEKLLP HIRGNVGFVF TKEDLTEIRD MLLANKVPAA ARAGAIAPCE 130 140 150 160 170 180 VTVPAQNTGL GPEKTSFFQA LGITTKISRG TIEILSDVQL IKTGDKVGAS EATLLNMLNI 190 200 210 220 230 240 SPFSFGLVIQ QVFDNGSIYN PEVLDITEET LHSRFLEGVR NVASVCLQIG YPTVASVPHS 250 260 270 280 290 300 IINGYKRVLA LSVETDYTFP LAEKVKAFLA DPSAFVAAAP VAAATTAAPA AAAAPAKVEA 310 KEESEESDED MGFGLFD

References

	« Hide 'large scale' referencesShow '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. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., 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: Epithelium.
[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: Epithelium.
[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: Epithelium.
[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. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24, MASS SPECTROMETRY.
[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.
[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.
[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.
[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.
[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]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"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.
[21]	"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: T-cell.
[22]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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. NP_444505.1.
UniGene	Hs.546285 Hs.709403
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P05388. 9 interactions.
STRING	P05388.
PTM databases
PhosphoSite	P05388.
2-D gel databases
REPRODUCTION-2DPAGE	P05388.
Proteomic databases
PRIDE	P05388.
Genome annotation databases
Ensembl	ENST00000228306; ENSP00000339027; ENSG00000089157; Homo sapiens. [Genome view] ENST00000392514; ENSP00000376299; ENSG00000089157; Homo sapiens. [Genome view]
GeneID	6175.
KEGG	hsa:6175.
UCSC	uc001txp.1. human.
Organism-specific databases
CTD	6175.
GeneCards	GC12M119097.
H-InvDB	HIX0011057. HIX0057540.
HGNC	HGNC:10371. RPLP0.
HPA	HPA003512.
MIM	180510. gene.
PharmGKB	PA34772.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P05388.
HOVERGEN	P05388.
OMA	GKNTMIR
OrthoDB	EOG9Z91FR
Enzyme and pathway databases
Reactome	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. [Graphical view]
Pfam	PF00428. Ribosomal_60s. 1 hit. PF00466. Ribosomal_L10. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	23989.
SOURCE	Search...

Entry information

Entry name

RLA0_HUMAN

Accession

Primary (citable) accession number: P05388
Secondary accession number(s): Q9BVK4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	November 1, 1988
Last modified:	November 24, 2009
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.