Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

60S acidic ribosomal protein P0

Gene

RPLP0

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Ribosomal protein P0 is the functional equivalent of E.coli protein L10.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. RNA binding Source: ProtInc
  3. structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  4. ribosome biogenesis Source: InterPro
  5. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  6. translation Source: UniProtKB
  7. translational elongation Source: Reactome
  8. translational initiation Source: Reactome
  9. translational termination Source: Reactome
  10. viral life cycle Source: Reactome
  11. viral process Source: Reactome
  12. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
60S acidic ribosomal protein P0
Alternative name(s):
60S ribosomal protein L10E
Gene namesi
Name:RPLP0
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:10371. RPLP0.

Subcellular locationi

Nucleus. Cytoplasm
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  3. cytosol Source: Reactome
  4. cytosolic large ribosomal subunit Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProtKB
  6. focal adhesion Source: UniProtKB
  7. membrane Source: UniProtKB
  8. nucleus Source: UniProtKB
  9. ribonucleoprotein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34772.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 31731760S acidic ribosomal protein P0PRO_0000154758Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei304 – 3041Phosphoserine1 Publication
Modified residuei307 – 3071Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP05388.
PaxDbiP05388.
PRIDEiP05388.

2D gel databases

REPRODUCTION-2DPAGEP05388.

PTM databases

PhosphoSiteiP05388.

Expressioni

Gene expression databases

BgeeiP05388.
CleanExiHS_RPLP0.
ExpressionAtlasiP05388. baseline and differential.
GenevestigatoriP05388.

Organism-specific databases

HPAiHPA003512.

Interactioni

Subunit structurei

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 APEX1.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
STAU1O957934EBI-354101,EBI-358174

Protein-protein interaction databases

BioGridi112094. 141 interactions.
IntActiP05388. 37 interactions.
MINTiMINT-193149.
STRINGi9606.ENSP00000339027.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00q5-227[»]
4V6Xelectron microscopy5.00Cq1-317[»]
ProteinModelPortaliP05388.
SMRiP05388. Positions 5-308.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L10P family.Curated

Phylogenomic databases

eggNOGiCOG0244.
GeneTreeiENSGT00390000017839.
HOGENOMiHOG000210987.
HOVERGENiHBG000711.
InParanoidiP05388.
KOiK02941.
OMAiNYVERGA.
OrthoDBiEOG71K63M.
PhylomeDBiP05388.
TreeFamiTF300849.

Family and domain databases

InterProiIPR030670. L10E_eukaryotes.
IPR001790. Ribosomal_L10P.
[Graphical view]
PfamiPF00466. Ribosomal_L10. 1 hit.
[Graphical view]
PIRSFiPIRSF039087. L10E. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P05388-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPREDRATWK SNYFLKIIQL LDDYPKCFIV GADNVGSKQM QQIRMSLRGK
60 70 80 90 100
AVVLMGKNTM MRKAIRGHLE NNPALEKLLP HIRGNVGFVF TKEDLTEIRD
110 120 130 140 150
MLLANKVPAA ARAGAIAPCE VTVPAQNTGL GPEKTSFFQA LGITTKISRG
160 170 180 190 200
TIEILSDVQL IKTGDKVGAS EATLLNMLNI SPFSFGLVIQ QVFDNGSIYN
210 220 230 240 250
PEVLDITEET LHSRFLEGVR NVASVCLQIG YPTVASVPHS IINGYKRVLA
260 270 280 290 300
LSVETDYTFP LAEKVKAFLA DPSAFVAAAP VAAATTAAPA AAAAPAKVEA
310
KEESEESDED MGFGLFD
Length:317
Mass (Da):34,274
Last modified:October 31, 1988 - v1
Checksum:i255AD25571C51199
GO
Isoform 2 (identifier: P05388-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     156-217: Missing.

Note: No experimental confirmation available.

Show »
Length:255
Mass (Da):27,436
Checksum:iB10D4073AAA5990A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti246 – 2461K → E in AAH01127 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei156 – 21762Missing in isoform 2. 1 PublicationVSP_055867Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BC107717 mRNA. Translation: AAI07718.1.
AB007187 Genomic DNA. Translation: BAA25845.1.
CCDSiCCDS9193.1. [P05388-1]
PIRiA27125. R5HUP0.
RefSeqiNP_000993.1. NM_001002.3. [P05388-1]
NP_444505.1. NM_053275.3. [P05388-1]
UniGeneiHs.546285.

Genome annotation databases

EnsembliENST00000228306; ENSP00000339027; ENSG00000089157. [P05388-1]
ENST00000313104; ENSP00000366471; ENSG00000089157. [P05388-2]
ENST00000392514; ENSP00000376299; ENSG00000089157. [P05388-1]
ENST00000551150; ENSP00000449328; ENSG00000089157. [P05388-1]
GeneIDi6175.
KEGGihsa:6175.
UCSCiuc001txp.3. human. [P05388-1]
uc001txr.3. human.

Polymorphism databases

DMDMi133041.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BC107717 mRNA. Translation: AAI07718.1.
AB007187 Genomic DNA. Translation: BAA25845.1.
CCDSiCCDS9193.1. [P05388-1]
PIRiA27125. R5HUP0.
RefSeqiNP_000993.1. NM_001002.3. [P05388-1]
NP_444505.1. NM_053275.3. [P05388-1]
UniGeneiHs.546285.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Welectron microscopy6.00q5-227[»]
4V6Xelectron microscopy5.00Cq1-317[»]
ProteinModelPortaliP05388.
SMRiP05388. Positions 5-308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112094. 141 interactions.
IntActiP05388. 37 interactions.
MINTiMINT-193149.
STRINGi9606.ENSP00000339027.

PTM databases

PhosphoSiteiP05388.

Polymorphism databases

DMDMi133041.

2D gel databases

REPRODUCTION-2DPAGEP05388.

Proteomic databases

MaxQBiP05388.
PaxDbiP05388.
PRIDEiP05388.

Protocols and materials databases

DNASUi6175.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000228306; ENSP00000339027; ENSG00000089157. [P05388-1]
ENST00000313104; ENSP00000366471; ENSG00000089157. [P05388-2]
ENST00000392514; ENSP00000376299; ENSG00000089157. [P05388-1]
ENST00000551150; ENSP00000449328; ENSG00000089157. [P05388-1]
GeneIDi6175.
KEGGihsa:6175.
UCSCiuc001txp.3. human. [P05388-1]
uc001txr.3. human.

Organism-specific databases

CTDi6175.
GeneCardsiGC12M120634.
HGNCiHGNC:10371. RPLP0.
HPAiHPA003512.
MIMi180510. gene.
neXtProtiNX_P05388.
PharmGKBiPA34772.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0244.
GeneTreeiENSGT00390000017839.
HOGENOMiHOG000210987.
HOVERGENiHBG000711.
InParanoidiP05388.
KOiK02941.
OMAiNYVERGA.
OrthoDBiEOG71K63M.
PhylomeDBiP05388.
TreeFamiTF300849.

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSiRPLP0. human.
GeneWikiiRPLP0.
GenomeRNAii6175.
NextBioi23989.
PROiP05388.
SOURCEiSearch...

Gene expression databases

BgeeiP05388.
CleanExiHS_RPLP0.
ExpressionAtlasiP05388. baseline and differential.
GenevestigatoriP05388.

Family and domain databases

InterProiIPR030670. L10E_eukaryotes.
IPR001790. Ribosomal_L10P.
[Graphical view]
PfamiPF00466. Ribosomal_L10. 1 hit.
[Graphical view]
PIRSFiPIRSF039087. L10E. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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(2005) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain, Cervix, Colon, Lung, Lymph, Muscle and Pancreas.
  4. Lubec G., Chen W.-Q., Sun Y.
    Submitted (NOV-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(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 218-310.
  6. 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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APEX1, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304 AND SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRLA0_HUMAN
AccessioniPrimary (citable) accession number: P05388
Secondary accession number(s): Q3B7A4, Q9BVK4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1988
Last sequence update: October 31, 1988
Last modified: March 31, 2015
This is version 169 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.