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Protein

60S ribosomal protein L9

Gene

RPL9

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

Functioni

GO - Molecular functioni

  1. RNA binding Source: ProtInc
  2. rRNA binding Source: InterPro
  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. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  5. translation Source: UniProtKB
  6. translational elongation Source: Reactome
  7. translational initiation Source: Reactome
  8. translational termination Source: Reactome
  9. viral life cycle Source: Reactome
  10. viral process Source: Reactome
  11. viral transcription Source: Reactome
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 L9
Gene namesi
Name:RPL9
ORF Names:OK/SW-cl.103
AND
Name:RPL9P7
AND
Name:RPL9P8
AND
Name:RPL9P9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componentsi: Chromosome 4, Unplaced

Organism-specific databases

HGNCiHGNC:10369. RPL9.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. cytosolic large ribosomal subunit Source: UniProtKB
  4. focal adhesion Source: UniProtKB
  5. membrane Source: UniProtKB
  6. nucleolus Source: HPA
  7. nucleus Source: UniProtKB
  8. ribosome Source: ProtInc
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34769.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19219260S ribosomal protein L9PRO_0000131097Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei121 – 1211N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP32969.
PeptideAtlasiP32969.
PRIDEiP32969.

2D gel databases

SWISS-2DPAGEP32969.

PTM databases

PhosphoSiteiP32969.

Expressioni

Gene expression databases

BgeeiP32969.
CleanExiHS_RPL9.
ExpressionAtlasiP32969. baseline.
GenevestigatoriP32969.

Organism-specific databases

HPAiHPA003372.

Interactioni

Protein-protein interaction databases

BioGridi112053. 122 interactions.
IntActiP32969. 18 interactions.
MINTiMINT-5000985.
STRINGi9606.ENSP00000346022.

Structurei

Secondary structure

1
192
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 103Combined sources
Beta strandi17 – 215Combined sources
Beta strandi24 – 296Combined sources
Beta strandi32 – 376Combined sources
Beta strandi44 – 485Combined sources
Beta strandi50 – 523Combined sources
Beta strandi54 – 585Combined sources
Beta strandi61 – 633Combined sources
Helixi65 – 8521Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQLNMR-A1-87[»]
4V6Xelectron microscopy5.00CH1-192[»]
ProteinModelPortaliP32969.
SMRiP32969. Positions 1-190.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32969.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L6P family.Curated

Phylogenomic databases

eggNOGiCOG0097.
HOGENOMiHOG000039905.
HOVERGENiHBG000942.
InParanoidiP32969.
KOiK02940.
OMAiLRVRKWF.
OrthoDBiEOG7353Z4.
PhylomeDBiP32969.
TreeFamiTF300033.

Family and domain databases

Gene3Di3.90.930.12. 2 hits.
InterProiIPR000702. Ribosomal_L6.
IPR020040. Ribosomal_L6_a/b-dom.
IPR002359. Ribosomal_L6_CS2.
[Graphical view]
PANTHERiPTHR11655. PTHR11655. 1 hit.
PfamiPF00347. Ribosomal_L6. 2 hits.
[Graphical view]
PIRSFiPIRSF002162. Ribosomal_L6. 1 hit.
SUPFAMiSSF56053. SSF56053. 2 hits.
PROSITEiPS00700. RIBOSOMAL_L6_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32969-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKTILSNQTV DIPENVDITL KGRTVIVKGP RGTLRRDFNH INVELSLLGK
60 70 80 90 100
KKKRLRVDKW WGNRKELATV RTICSHVQNM IKGVTLGFRY KMRSVYAHFP
110 120 130 140 150
INVVIQENGS LVEIRNFLGE KYIRRVRMRP GVACSVSQAQ KDELILEGND
160 170 180 190
IELVSNSAAL IQQATTVKNK DIRKFLDGIY VSEKGTVQQA DE
Length:192
Mass (Da):21,863
Last modified:October 1, 1993 - v1
Checksum:i0249E6CA12F77934
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111D → E in AAB01040 (PubMed:8597601).Curated
Sequence conflicti11 – 111D → E in AAB01041 (PubMed:8597601).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14531 mRNA. Translation: BAA03401.1.
U09953 mRNA. Translation: AAB01040.1.
U09954 Genomic DNA. Translation: AAB01041.1.
U21138 mRNA. Translation: AAA63752.1.
AB062431 mRNA. Translation: BAB93494.1.
BC000483 mRNA. Translation: AAH00483.1.
BC004156 mRNA. Translation: AAH04156.1.
BC004206 mRNA. Translation: AAH04206.1.
BC007967 mRNA. Translation: AAH07967.1.
BC012149 mRNA. Translation: AAH12149.1.
BC031906 mRNA. Translation: AAH31906.1.
BC066318 mRNA. Translation: AAH66318.1.
BC070214 mRNA. Translation: AAH70214.1.
AB007169 Genomic DNA. Translation: BAA25830.1.
CCDSiCCDS3452.1.
PIRiS65792.
RefSeqiNP_000652.2. NM_000661.4.
NP_001020092.1. NM_001024921.2.
XP_005262718.1. XM_005262661.1.
UniGeneiHs.412370.
Hs.513083.
Hs.730597.

Genome annotation databases

EnsembliENST00000295955; ENSP00000346022; ENSG00000163682.
ENST00000393394; ENSP00000480341; ENSG00000273673.
ENST00000449470; ENSP00000400467; ENSG00000163682.
GeneIDi6133.
KEGGihsa:6133.
UCSCiuc003gub.3. human.

Polymorphism databases

DMDMi417677.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D14531 mRNA. Translation: BAA03401.1.
U09953 mRNA. Translation: AAB01040.1.
U09954 Genomic DNA. Translation: AAB01041.1.
U21138 mRNA. Translation: AAA63752.1.
AB062431 mRNA. Translation: BAB93494.1.
BC000483 mRNA. Translation: AAH00483.1.
BC004156 mRNA. Translation: AAH04156.1.
BC004206 mRNA. Translation: AAH04206.1.
BC007967 mRNA. Translation: AAH07967.1.
BC012149 mRNA. Translation: AAH12149.1.
BC031906 mRNA. Translation: AAH31906.1.
BC066318 mRNA. Translation: AAH66318.1.
BC070214 mRNA. Translation: AAH70214.1.
AB007169 Genomic DNA. Translation: BAA25830.1.
CCDSiCCDS3452.1.
PIRiS65792.
RefSeqiNP_000652.2. NM_000661.4.
NP_001020092.1. NM_001024921.2.
XP_005262718.1. XM_005262661.1.
UniGeneiHs.412370.
Hs.513083.
Hs.730597.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQLNMR-A1-87[»]
4V6Xelectron microscopy5.00CH1-192[»]
ProteinModelPortaliP32969.
SMRiP32969. Positions 1-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112053. 122 interactions.
IntActiP32969. 18 interactions.
MINTiMINT-5000985.
STRINGi9606.ENSP00000346022.

PTM databases

PhosphoSiteiP32969.

Polymorphism databases

DMDMi417677.

2D gel databases

SWISS-2DPAGEP32969.

Proteomic databases

PaxDbiP32969.
PeptideAtlasiP32969.
PRIDEiP32969.

Protocols and materials databases

DNASUi6133.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295955; ENSP00000346022; ENSG00000163682.
ENST00000393394; ENSP00000480341; ENSG00000273673.
ENST00000449470; ENSP00000400467; ENSG00000163682.
GeneIDi6133.
KEGGihsa:6133.
UCSCiuc003gub.3. human.

Organism-specific databases

CTDi6133.
HGNCiHGNC:10369. RPL9.
HPAiHPA003372.
MIMi603686. gene.
neXtProtiNX_P32969.
PharmGKBiPA34769.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0097.
HOGENOMiHOG000039905.
HOVERGENiHBG000942.
InParanoidiP32969.
KOiK02940.
OMAiLRVRKWF.
OrthoDBiEOG7353Z4.
PhylomeDBiP32969.
TreeFamiTF300033.

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

ChiTaRSiRPL9. human.
EvolutionaryTraceiP32969.
GeneWikiiRPL9.
GenomeRNAii6133.
NextBioi23821.
PROiP32969.
SOURCEiSearch...

Gene expression databases

BgeeiP32969.
CleanExiHS_RPL9.
ExpressionAtlasiP32969. baseline.
GenevestigatoriP32969.

Family and domain databases

Gene3Di3.90.930.12. 2 hits.
InterProiIPR000702. Ribosomal_L6.
IPR020040. Ribosomal_L6_a/b-dom.
IPR002359. Ribosomal_L6_CS2.
[Graphical view]
PANTHERiPTHR11655. PTHR11655. 1 hit.
PfamiPF00347. Ribosomal_L6. 2 hits.
[Graphical view]
PIRSFiPIRSF002162. Ribosomal_L6. 1 hit.
SUPFAMiSSF56053. SSF56053. 2 hits.
PROSITEiPS00700. RIBOSOMAL_L6_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A new human ribosomal protein sequence, homologue of rat L9."
    Hori N., Murakawa K., Matoba R., Fukushima A., Okubo K., Matsubara K.
    Nucleic Acids Res. 21:4395-4395(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Structural organization and chromosomal localization of the human ribosomal protein L9 gene."
    Mazuruk K., Schoen T.J., Chader G.J., Iwata T., Rodriguez I.R.
    Biochim. Biophys. Acta 1305:151-162(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Retina.
  3. "Human homolog of rat ribosomal protein L9."
    Williams J.H., Pearse M.J., Power D.A.
    Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
    Shichijo S., Itoh K.
    Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon adenocarcinoma.
  5. "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].
    Tissue: Brain, Muscle, Placenta and Uterus.
  6. Bienvenut W.V., Bilsland A.E., Keith W.N.
    Submitted (DEC-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-21; 36-51; 94-115; 142-168 AND 174-184, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  7. "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 146-192.
  8. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Solution structure of the N-terminal domain of human ribosomal protein L9."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-87.
  13. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.

Entry informationi

Entry nameiRL9_HUMAN
AccessioniPrimary (citable) accession number: P32969
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: March 4, 2015
This is version 158 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 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  3. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. 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.