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P32969

- RL9_HUMAN

UniProt

P32969 - RL9_HUMAN

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Protein

60S ribosomal protein L9

Gene
RPL9, OK/SW-cl.103
RPL9P7
RPL9P8
RPL9P9
Organism
Homo sapiens (Human)
Status
Reviewed - 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. mRNA metabolic process Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  5. RNA metabolic process Source: Reactome
  6. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  7. translation Source: UniProtKB
  8. translational elongation Source: Reactome
  9. translational initiation Source: Reactome
  10. translational termination Source: Reactome
  11. viral life cycle Source: Reactome
  12. viral process Source: Reactome
  13. 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

Organism-specific databases

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: Chromosome 4
HGNCiHGNC:10369. RPL9.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. cytosolic large ribosomal subunit Source: UniProtKB
  4. nucleolus Source: HPA
  5. nucleus Source: UniProt
  6. ribosome Source: ProtInc

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

MaxQBiP32969.
PaxDbiP32969.
PeptideAtlasiP32969.
PRIDEiP32969.

2D gel databases

SWISS-2DPAGEP32969.

PTM databases

PhosphoSiteiP32969.

Expressioni

Gene expression databases

BgeeiP32969.
CleanExiHS_RPL9.
GenevestigatoriP32969.

Organism-specific databases

HPAiHPA003372.

Interactioni

Protein-protein interaction databases

BioGridi112053. 102 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 – 103
Beta strandi17 – 215
Beta strandi24 – 296
Beta strandi32 – 376
Beta strandi44 – 485
Beta strandi50 – 523
Beta strandi54 – 585
Beta strandi61 – 633
Helixi65 – 8521

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQLNMR-A1-87[»]
3J3Belectron microscopy5.00H1-192[»]
ProteinModelPortaliP32969.
SMRiP32969. Positions 1-191.

Miscellaneous databases

EvolutionaryTraceiP32969.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0097.
HOGENOMiHOG000039905.
HOVERGENiHBG000942.
InParanoidiP32969.
KOiK02940.
OMAiEFVGQTA.
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

MKTILSNQTV DIPENVDITL KGRTVIVKGP RGTLRRDFNH INVELSLLGK    50
KKKRLRVDKW WGNRKELATV RTICSHVQNM IKGVTLGFRY KMRSVYAHFP 100
INVVIQENGS LVEIRNFLGE KYIRRVRMRP GVACSVSQAQ KDELILEGND 150
IELVSNSAAL IQQATTVKNK DIRKFLDGIY VSEKGTVQQA DE 192
Length:192
Mass (Da):21,863
Last modified:October 1, 1993 - v1
Checksum:i0249E6CA12F77934
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111D → E in AAB01040. 1 Publication
Sequence conflicti11 – 111D → E in AAB01041. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENST00000449470; ENSP00000400467; ENSG00000163682.
GeneIDi6133.
KEGGihsa:6133.
UCSCiuc003gub.3. human.

Polymorphism databases

DMDMi417677.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS3452.1.
PIRi S65792.
RefSeqi NP_000652.2. NM_000661.4.
NP_001020092.1. NM_001024921.2.
XP_005262718.1. XM_005262661.1.
UniGenei Hs.412370.
Hs.513083.
Hs.730597.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2CQL NMR - A 1-87 [» ]
3J3B electron microscopy 5.00 H 1-192 [» ]
ProteinModelPortali P32969.
SMRi P32969. Positions 1-191.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112053. 102 interactions.
IntActi P32969. 18 interactions.
MINTi MINT-5000985.
STRINGi 9606.ENSP00000346022.

PTM databases

PhosphoSitei P32969.

Polymorphism databases

DMDMi 417677.

2D gel databases

SWISS-2DPAGE P32969.

Proteomic databases

MaxQBi P32969.
PaxDbi P32969.
PeptideAtlasi P32969.
PRIDEi P32969.

Protocols and materials databases

DNASUi 6133.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000295955 ; ENSP00000346022 ; ENSG00000163682 .
ENST00000449470 ; ENSP00000400467 ; ENSG00000163682 .
GeneIDi 6133.
KEGGi hsa:6133.
UCSCi uc003gub.3. human.

Organism-specific databases

CTDi 6133.
HGNCi HGNC:10369. RPL9.
HPAi HPA003372.
MIMi 603686. gene.
neXtProti NX_P32969.
PharmGKBi PA34769.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0097.
HOGENOMi HOG000039905.
HOVERGENi HBG000942.
InParanoidi P32969.
KOi K02940.
OMAi EFVGQTA.
OrthoDBi EOG7353Z4.
PhylomeDBi P32969.
TreeFami TF300033.

Enzyme and pathway databases

Reactomei REACT_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

EvolutionaryTracei P32969.
GeneWikii RPL9.
GenomeRNAii 6133.
NextBioi 23821.
PROi P32969.
SOURCEi Search...

Gene expression databases

Bgeei P32969.
CleanExi HS_RPL9.
Genevestigatori P32969.

Family and domain databases

Gene3Di 3.90.930.12. 2 hits.
InterProi IPR000702. Ribosomal_L6.
IPR020040. Ribosomal_L6_a/b-dom.
IPR002359. Ribosomal_L6_CS2.
[Graphical view ]
PANTHERi PTHR11655. PTHR11655. 1 hit.
Pfami PF00347. Ribosomal_L6. 2 hits.
[Graphical view ]
PIRSFi PIRSF002162. Ribosomal_L6. 1 hit.
SUPFAMi SSF56053. SSF56053. 2 hits.
PROSITEi PS00700. RIBOSOMAL_L6_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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(1993) [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(1996) [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 (FEB-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 (MAY-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(2004) [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 (JAN-2010) 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(1998) [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(2009) [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. "Solution structure of the N-terminal domain of human ribosomal protein L9."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 1-87.
  12. 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: September 3, 2014
This is version 152 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

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