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Q07020 (RL18_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S ribosomal protein L18
Gene names
Name:RPL18
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length188 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the ribosomal protein L18e family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMPhosphoprotein
   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

translation

Non-traceable author statement Ref.5. 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. Source: HPA

cytosol

Traceable author statement. Source: Reactome

cytosolic large ribosomal subunit

Inferred from direct assay Ref.5. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: ProtInc

structural constituent of ribosome

Non-traceable author statement Ref.5. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q07020-1)

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.
Isoform 2 (identifier: Q07020-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: MGVDIRHNKDRKVRRKEPKSQDIYLRLLVK → M
Note: No experimental confirmation available. Based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 18818760S ribosomal protein L18
PRO_0000132769

Amino acid modifications

Modified residue1301Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9 Ref.11
Modified residue1581Phosphothreonine Ref.8

Natural variations

Alternative sequence1 – 3030MGVDI…RLLVK → M in isoform 2.
VSP_055170

Experimental info

Sequence conflict621S → C in AAH21743. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: C4E416E7A5329B7C

FASTA18821,634
        10         20         30         40         50         60 
MGVDIRHNKD RKVRRKEPKS QDIYLRLLVK LYRFLARRTN STFNQVVLKR LFMSRTNRPP 

        70         80         90        100        110        120 
LSLSRMIRKM KLPGRENKTA VVVGTITDDV RVQEVPKLKV CALRVTSRAR SRILRAGGKI 

       130        140        150        160        170        180 
LTFDQLALDS PKGCGTVLLS GPRKGREVYR HFGKAPGTPH SHTKPYVRSK GRKFERARGR 


RASRGYKN 

« Hide

Isoform 2 [UniParc].

Checksum: 1F622F3CD8BABC8E
Show »

FASTA15918,091

References

« Hide 'large scale' references
[1]"Nucleotide and deduced amino acid sequence of human ribosomal protein L18."
Puder M., Barnard G.F., Staniunas R.J., Steele G.D. Jr., Chen L.B.
Biochim. Biophys. Acta 1216:134-136(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Colon.
[2]"The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORM 1).
Tissue: Brain and Lung.
[5]"Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing."
Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R., Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.
J. Protein Chem. 22:249-258(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-14, IDENTIFICATION BY MASS SPECTROMETRY.
[6]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 AND THR-158, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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].
[11]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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
L11566 mRNA. Translation: AAA16329.1.
AB061825 Genomic DNA. Translation: BAB79463.1.
AC022154 Genomic DNA. No translation available.
BC000374 mRNA. Translation: AAH00374.1.
BC009708 mRNA. Translation: AAH09708.1.
BC021743 mRNA. Translation: AAH21743.1.
CCDSCCDS12726.1.
PIRS38352.
RefSeqNP_000970.1. NM_000979.3.
UniGeneHs.515517.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00Q1-188[»]
ProteinModelPortalQ07020.
SMRQ07020. Positions 1-188.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112061. 137 interactions.
IntActQ07020. 20 interactions.
MINTMINT-5000047.
STRING9606.ENSP00000084795.

PTM databases

PhosphoSiteQ07020.

2D gel databases

SWISS-2DPAGEQ07020.

Proteomic databases

MaxQBQ07020.
PaxDbQ07020.
PeptideAtlasQ07020.
PRIDEQ07020.

Protocols and materials databases

DNASU6141.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000549920; ENSP00000447001; ENSG00000063177.
ENST00000552588; ENSP00000449204; ENSG00000063177.
GeneID6141.
KEGGhsa:6141.
UCSCuc002pjq.2. human.

Organism-specific databases

CTD6141.
GeneCardsGC19M049118.
H-InvDBHIX0018528.
HGNCHGNC:10310. RPL18.
HPAHPA046572.
MIM604179. gene.
neXtProtNX_Q07020.
PharmGKBPA34679.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1727.
HOGENOMHOG000213425.
HOVERGENHBG000875.
InParanoidQ07020.
KOK02883.
OrthoDBEOG7PS1GP.
PhylomeDBQ07020.
TreeFamTF300202.

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

ArrayExpressQ07020.
BgeeQ07020.
CleanExHS_RPL18.
GenevestigatorQ07020.

Family and domain databases

InterProIPR000039. Ribosomal_L18e.
IPR021131. Ribosomal_L18e/L15P.
IPR021132. Ribosomal_L18e_CS.
[Graphical view]
PANTHERPTHR10934. PTHR10934. 1 hit.
PfamPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMSSF52080. SSF52080. 1 hit.
PROSITEPS01106. RIBOSOMAL_L18E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPL18. human.
GeneWikiRPL18.
GenomeRNAi6141.
NextBio23857.
PROQ07020.
SOURCESearch...

Entry information

Entry nameRL18_HUMAN
AccessionPrimary (citable) accession number: Q07020
Secondary accession number(s): F8VWC5, Q8WTZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 134 of the entry and version 2 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 19

Human chromosome 19: entries, gene names and cross-references to MIM