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Protein

60S ribosomal protein L18

Gene

RPL18

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

Functioni

GO - Molecular functioni

  • RNA binding Source: ProtInc
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

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 ribosomal protein L18
Gene namesi
Name:RPL18
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:10310. RPL18.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • cytosolic large ribosomal subunit Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleolus Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34679.

Polymorphism and mutation databases

BioMutaiRPL18.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 18818760S ribosomal protein L18PRO_0000132769Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei130 – 1301Phosphoserine5 Publications
Modified residuei158 – 1581Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ07020.
PaxDbiQ07020.
PeptideAtlasiQ07020.
PRIDEiQ07020.

2D gel databases

SWISS-2DPAGEQ07020.

PTM databases

PhosphoSiteiQ07020.

Expressioni

Gene expression databases

BgeeiQ07020.
CleanExiHS_RPL18.
ExpressionAtlasiQ07020. baseline and differential.
GenevisibleiQ07020. HS.

Organism-specific databases

HPAiHPA046572.

Interactioni

Protein-protein interaction databases

BioGridi112061. 144 interactions.
IntActiQ07020. 21 interactions.
MINTiMINT-5000047.
STRINGi9606.ENSP00000447001.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CQ1-188[»]
ProteinModelPortaliQ07020.
SMRiQ07020. Positions 54-121.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L18e family.Curated

Phylogenomic databases

eggNOGiCOG1727.
GeneTreeiENSGT00390000012976.
HOGENOMiHOG000213425.
HOVERGENiHBG000875.
InParanoidiQ07020.
KOiK02883.
OrthoDBiEOG7PS1GP.
PhylomeDBiQ07020.
TreeFamiTF300202.

Family and domain databases

InterProiIPR000039. Ribosomal_L18e.
IPR021131. Ribosomal_L18e/L15P.
IPR021132. Ribosomal_L18e_CS.
[Graphical view]
PANTHERiPTHR10934. PTHR10934. 1 hit.
PfamiPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
PROSITEiPS01106. RIBOSOMAL_L18E. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

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

Isoform 1 (identifier: Q07020-1) [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
MGVDIRHNKD RKVRRKEPKS QDIYLRLLVK LYRFLARRTN STFNQVVLKR
60 70 80 90 100
LFMSRTNRPP LSLSRMIRKM KLPGRENKTA VVVGTITDDV RVQEVPKLKV
110 120 130 140 150
CALRVTSRAR SRILRAGGKI LTFDQLALDS PKGCGTVLLS GPRKGREVYR
160 170 180
HFGKAPGTPH SHTKPYVRSK GRKFERARGR RASRGYKN
Length:188
Mass (Da):21,634
Last modified:January 23, 2007 - v2
Checksum:iC4E416E7A5329B7C
GO
Isoform 2 (identifier: Q07020-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:159
Mass (Da):18,091
Checksum:i1F622F3CD8BABC8E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621S → C in AAH21743 (PubMed:15489334).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3030MGVDI…RLLVK → M in isoform 2. CuratedVSP_055170Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12726.1. [Q07020-1]
CCDS58669.1. [Q07020-2]
PIRiS38352.
RefSeqiNP_000970.1. NM_000979.3. [Q07020-1]
NP_001257419.1. NM_001270490.1. [Q07020-2]
UniGeneiHs.515517.

Genome annotation databases

EnsembliENST00000549920; ENSP00000447001; ENSG00000063177. [Q07020-1]
ENST00000552588; ENSP00000449204; ENSG00000063177. [Q07020-2]
GeneIDi6141.
KEGGihsa:6141.
UCSCiuc002pjq.2. human. [Q07020-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS12726.1. [Q07020-1]
CCDS58669.1. [Q07020-2]
PIRiS38352.
RefSeqiNP_000970.1. NM_000979.3. [Q07020-1]
NP_001257419.1. NM_001270490.1. [Q07020-2]
UniGeneiHs.515517.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CQ1-188[»]
ProteinModelPortaliQ07020.
SMRiQ07020. Positions 54-121.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112061. 144 interactions.
IntActiQ07020. 21 interactions.
MINTiMINT-5000047.
STRINGi9606.ENSP00000447001.

PTM databases

PhosphoSiteiQ07020.

Polymorphism and mutation databases

BioMutaiRPL18.

2D gel databases

SWISS-2DPAGEQ07020.

Proteomic databases

MaxQBiQ07020.
PaxDbiQ07020.
PeptideAtlasiQ07020.
PRIDEiQ07020.

Protocols and materials databases

DNASUi6141.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000549920; ENSP00000447001; ENSG00000063177. [Q07020-1]
ENST00000552588; ENSP00000449204; ENSG00000063177. [Q07020-2]
GeneIDi6141.
KEGGihsa:6141.
UCSCiuc002pjq.2. human. [Q07020-1]

Organism-specific databases

CTDi6141.
GeneCardsiGC19M049118.
H-InvDBHIX0018528.
HGNCiHGNC:10310. RPL18.
HPAiHPA046572.
MIMi604179. gene.
neXtProtiNX_Q07020.
PharmGKBiPA34679.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1727.
GeneTreeiENSGT00390000012976.
HOGENOMiHOG000213425.
HOVERGENiHBG000875.
InParanoidiQ07020.
KOiK02883.
OrthoDBiEOG7PS1GP.
PhylomeDBiQ07020.
TreeFamiTF300202.

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

ChiTaRSiRPL18. human.
GeneWikiiRPL18.
GenomeRNAii6141.
NextBioi23857.
PROiQ07020.
SOURCEiSearch...

Gene expression databases

BgeeiQ07020.
CleanExiHS_RPL18.
ExpressionAtlasiQ07020. baseline and differential.
GenevisibleiQ07020. HS.

Family and domain databases

InterProiIPR000039. Ribosomal_L18e.
IPR021131. Ribosomal_L18e/L15P.
IPR021132. Ribosomal_L18e_CS.
[Graphical view]
PANTHERiPTHR10934. PTHR10934. 1 hit.
PfamiPF00828. Ribosomal_L18e. 1 hit.
[Graphical view]
SUPFAMiSSF52080. SSF52080. 1 hit.
PROSITEiPS01106. RIBOSOMAL_L18E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL18_HUMAN
AccessioniPrimary (citable) accession number: Q07020
Secondary accession number(s): F8VWC5, Q8WTZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 143 of the entry and version 2 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 19
    Human chromosome 19: 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.