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P05388 (RLA0_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 162. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S acidic ribosomal protein P0
Alternative name(s):
60S ribosomal protein L10E
Gene names
Name:RPLP0
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length317 AA.
Sequence statusComplete.
Protein existenceEvidence 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 IGF2BP1-dependent mRNP granule complex containing 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 processHost-virus interaction
   Cellular componentCytoplasm
Nucleus
   Molecular functionRibonucleoprotein
Ribosomal protein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

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

translation

Non-traceable author statement PubMed 12962325. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.7. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

cytosolic large ribosomal subunit

Inferred from direct assay PubMed 12962325. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

nucleus

Inferred from direct assay Ref.7. Source: UniProtKB

ribonucleoprotein complex

Inferred from direct assay Ref.6. Source: UniProtKB

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7. Source: UniProtKB

structural constituent of ribosome

Non-traceable author statement PubMed 12962325. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

STAU1O957934EBI-354101,EBI-358174

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 31731760S acidic ribosomal protein P0
PRO_0000154758

Experimental info

Sequence conflict2461K → E in AAH01127. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P05388 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 255AD25571C51199

FASTA31734,274
        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 

« Hide

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] [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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY 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].
[9]"Structures of the human and Drosophila 80S ribosome."
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.
Nature 497:80-85(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
+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.
CCDSCCDS9193.1.
PIRR5HUP0. A27125.
RefSeqNP_000993.1. NM_001002.3.
NP_444505.1. NM_053275.3.
UniGeneHs.546285.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J39electron microscopy6.00q5-227[»]
3J3Belectron microscopy5.00q1-317[»]
ProteinModelPortalP05388.
SMRP05388. Positions 5-308.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112094. 128 interactions.
IntActP05388. 35 interactions.
MINTMINT-193149.
STRING9606.ENSP00000339027.

PTM databases

PhosphoSiteP05388.

Polymorphism databases

DMDM133041.

2D gel databases

REPRODUCTION-2DPAGEP05388.

Proteomic databases

MaxQBP05388.
PaxDbP05388.
PRIDEP05388.

Protocols and materials databases

DNASU6175.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228306; ENSP00000339027; ENSG00000089157.
ENST00000392514; ENSP00000376299; ENSG00000089157.
ENST00000551150; ENSP00000449328; ENSG00000089157.
GeneID6175.
KEGGhsa:6175.
UCSCuc001txp.3. human.

Organism-specific databases

CTD6175.
GeneCardsGC12M120634.
HGNCHGNC:10371. RPLP0.
HPAHPA003512.
MIM180510. gene.
neXtProtNX_P05388.
PharmGKBPA34772.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0244.
HOVERGENHBG000711.
InParanoidP05388.
KOK02941.
OMAGILATEM.
OrthoDBEOG71K63M.
PhylomeDBP05388.
TreeFamTF300849.

Enzyme and pathway databases

ReactomeREACT_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

BgeeP05388.
CleanExHS_RPLP0.
GenevestigatorP05388.

Family and domain databases

InterProIPR001790. Ribosomal_L10/acidic_P0.
IPR001813. Ribosomal_L10/L12.
[Graphical view]
PfamPF00428. Ribosomal_60s. 1 hit.
PF00466. Ribosomal_L10. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPLP0. human.
GeneWikiRPLP0.
GenomeRNAi6175.
NextBio23989.
PROP05388.
SOURCESearch...

Entry information

Entry nameRLA0_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 162 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM