P05388 (RLA0_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
60S acidic ribosomal protein P0

Alternative name(s):
60S ribosomal protein L10E

Gene names

Name:

RPLP0

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.6 Ref.7
Subcellular location	Nucleus. Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.6 Ref.7
Sequence similarities	Belongs to the ribosomal protein L10P family.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cytoplasm Nucleus
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	SRP-dependent cotranslational protein targeting to membrane Traceable author statement. Source: Reactome nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Traceable author statement. Source: Reactome ribosome biogenesis Inferred from electronic annotation. Source: InterPro translational elongation Traceable author statement. Source: Reactome translational initiation Traceable author statement. Source: Reactome translational termination Traceable author statement. Source: Reactome viral transcription Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosolic large ribosomal subunit Inferred from direct assay PubMed 12962325. Source: UniProtKB nucleus Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	RNA binding Traceable author statement Ref.1. Source: ProtInc structural constituent of ribosome Non-traceable author statement PubMed 12962325. Source: UniProtKB
Complete GO annotation...

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 By similarity
	Modified residue	304	1	Phosphoserine By similarity
	Modified residue	307	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	246	1	K → E in AAH01127. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P05388 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 218-310.
[6]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[7]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APEX1, MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[8]	"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] [Europe PMC] [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.
ModBase	Search...
Protein-protein interaction databases
IntAct	P05388. 25 interactions.
MINT	MINT-193149.
STRING	9606.ENSP00000339027.
PTM databases
PhosphoSite	P05388.
Polymorphism databases
DMDM	133041.
2D gel databases
REPRODUCTION-2DPAGE	P05388.
Proteomic databases
PaxDb	P05388.
PRIDE	P05388.
Protocols and materials databases
DNASU	6175.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000228306; ENSP00000339027; ENSG00000089157. ENST00000392514; ENSP00000376299; ENSG00000089157. ENST00000551150; ENSP00000449328; ENSG00000089157.
GeneID	6175.
KEGG	hsa:6175.
UCSC	uc001txp.3. human.
Organism-specific databases
CTD	6175.
GeneCards	GC12M120634.
HGNC	HGNC:10371. RPLP0.
HPA	HPA003512.
MIM	180510. gene.
neXtProt	NX_P05388.
PharmGKB	PA34772.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0244.
HOVERGEN	HBG000711.
InParanoid	P05388.
KO	K02941.
OMA	AYMHAFN.
OrthoDB	EOG4VDQ10.
PhylomeDB	P05388.
Enzyme and pathway databases
Reactome	REACT_116125. Disease. REACT_17015. Metabolism of proteins. REACT_1762. 3' -UTR-mediated translational regulation. REACT_21257. Metabolism of RNA. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P05388.
Bgee	P05388.
CleanEx	HS_RPLP0.
Genevestigator	P05388.
GermOnline	ENSG00000089157. Homo sapiens.
Family and domain databases
InterPro	IPR001790. Ribosomal_L10/acidic_P0. IPR001813. Ribosomal_L10/L12. [Graphical view]
Pfam	PF00428. Ribosomal_60s. 1 hit. PF00466. Ribosomal_L10. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RPLP0. human.
GenomeRNAi	6175.
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:	May 29, 2013
This is version 149 of the entry and version 1 of the sequence. [Complete history]

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.