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P46781 (RS9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S9
Gene names
Name:RPS9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Ref.8

Subcellular location

Cytoplasm. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.8

Sequence similarities

Belongs to the ribosomal protein S4P family.

Contains 1 S4 RNA-binding domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   LigandRNA-binding
rRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
   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

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 18420587. Source: UniProtKB

regulation of translation

Inferred from mutant phenotype PubMed 18420587. Source: GOC

translation

Inferred from mutant phenotype PubMed 18420587. 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 PubMed 18420587. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

cytosolic small ribosomal subunit

Inferred from direct assay PubMed 15883184Ref.6. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nucleolus

Inferred from direct assay PubMed 18420587. Source: UniProtKB

ribonucleoprotein complex

Inferred from direct assay Ref.8. Source: UniProtKB

ribosome

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

rRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

translation regulator activity

Inferred from mutant phenotype PubMed 18420587. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

STAT3P407632EBI-351206,EBI-518675

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 19419340S ribosomal protein S9
PRO_0000132689

Regions

Domain108 – 18275S4 RNA-binding

Amino acid modifications

Modified residue661N6-acetyllysine By similarity
Modified residue1161N6-acetyllysine By similarity
Modified residue1551N6-acetyllysine Ref.10

Natural variations

Natural variant251L → F.
Corresponds to variant rs41423149 [ dbSNP | Ensembl ].
VAR_052069
Natural variant1371V → F in a breast cancer sample; somatic mutation. Ref.13
VAR_036543

Experimental info

Sequence conflict841I → L in AAA85659. Ref.1
Sequence conflict165 – 1673YGG → TGV in AAA85659. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P46781 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E9CE3CBD59524F81

FASTA19422,591
        10         20         30         40         50         60 
MPVARSWVCR KTYVTPRRPF EKSRLDQELK LIGEYGLRNK REVWRVKFTL AKIRKAAREL 

        70         80         90        100        110        120 
LTLDEKDPRR LFEGNALLRR LVRIGVLDEG KMKLDYILGL KIEDFLERRL QTQVFKLGLA 

       130        140        150        160        170        180 
KSIHHARVLI RQRHIRVRKQ VVNIPSFIVR LDSQKHIDFS LRSPYGGGRP GRVKRKNAKK 

       190 
GQGGAGAGDD EEED 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs."
Frigerio J.-M., Dagorn J.-C., Iovanna J.L.
Biochim. Biophys. Acta 1262:64-68(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
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].
[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]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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 Skin.
[6]"Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-19.
Tissue: Placenta.
[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 10-73.
[8]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[9]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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].
[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).
[13]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PHE-137.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U14971 mRNA. Translation: AAA85659.1.
AB061839 Genomic DNA. Translation: BAB79477.1.
CU457734 Genomic DNA. Translation: CAP19125.1.
CU151838 Genomic DNA. Translation: CAQ09597.1.
CH471135 Genomic DNA. Translation: EAW72209.1.
BC000802 mRNA. Translation: AAH00802.1.
BC007410 mRNA. Translation: AAH07410.1.
BC007434 mRNA. Translation: AAH07434.1.
BC007857 mRNA. Translation: AAH07857.1.
BC068055 mRNA. Translation: AAH68055.1.
BC071940 mRNA. Translation: AAH71940.1.
BC096756 mRNA. Translation: AAH96756.1.
AB007150 Genomic DNA. Translation: BAA25816.1.
PIRS55917.
RefSeqNP_001004.2. NM_001013.3.
XP_005259192.1. XM_005259135.1.
XP_005259193.1. XM_005259136.2.
XP_005277141.1. XM_005277084.2.
XP_005277142.1. XM_005277085.1.
XP_005277331.1. XM_005277274.1.
XP_005277372.1. XM_005277315.1.
XP_005277373.1. XM_005277316.2.
XP_005278344.1. XM_005278287.2.
XP_005278345.1. XM_005278288.1.
UniGeneHs.467284.
Hs.546288.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00J1-194[»]
ProteinModelPortalP46781.
SMRP46781. Positions 7-177.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112117. 110 interactions.
IntActP46781. 46 interactions.
MINTMINT-5001013.
STRING9606.ENSP00000302896.

PTM databases

PhosphoSiteP46781.

Polymorphism databases

DMDM20178311.

Proteomic databases

PaxDbP46781.
PeptideAtlasP46781.
PRIDEP46781.

Protocols and materials databases

DNASU6203.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302907; ENSP00000302896; ENSG00000170889.
ENST00000391752; ENSP00000375632; ENSG00000170889.
ENST00000391753; ENSP00000375633; ENSG00000170889.
ENST00000573353; ENSP00000461356; ENSG00000263332.
ENST00000573511; ENSP00000461393; ENSG00000263076.
ENST00000574910; ENSP00000458947; ENSG00000263332.
ENST00000575726; ENSP00000460241; ENSG00000263076.
ENST00000575746; ENSP00000461170; ENSG00000263332.
ENST00000576887; ENSP00000459239; ENSG00000263076.
ENST00000604018; ENSP00000474572; ENSG00000271572.
ENST00000604119; ENSP00000474184; ENSG00000271572.
ENST00000604611; ENSP00000473696; ENSG00000271572.
GeneID6203.
KEGGhsa:6203.
UCSCuc002qdx.3. human.

Organism-specific databases

CTD6203.
GeneCardsGC19P054851.
HGNCHGNC:10442. RPS9.
HPAHPA048746.
MIM603631. gene.
neXtProtNX_P46781.
PharmGKBPA34857.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0522.
HOGENOMHOG000194525.
HOVERGENHBG001135.
InParanoidP46781.
KOK02997.
OMAKHIDFAV.
PhylomeDBP46781.
TreeFamTF300795.

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

ArrayExpressP46781.
BgeeP46781.
CleanExHS_RPS9.
GenevestigatorP46781.

Family and domain databases

Gene3D3.10.290.10. 1 hit.
InterProIPR022801. Ribosomal_S4/S9.
IPR005710. Ribosomal_S4/S9_euk/arc.
IPR001912. Ribosomal_S4/S9_N.
IPR018079. Ribosomal_S4_CS.
IPR002942. S4_RNA-bd.
[Graphical view]
PANTHERPTHR11831. PTHR11831. 1 hit.
PfamPF00163. Ribosomal_S4. 1 hit.
PF01479. S4. 1 hit.
[Graphical view]
SMARTSM00363. S4. 1 hit.
[Graphical view]
TIGRFAMsTIGR01018. rpsD_arch. 1 hit.
PROSITEPS00632. RIBOSOMAL_S4. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPS9. human.
GeneWikiRPS9.
GenomeRNAi6203.
NextBio24091.
PROP46781.
SOURCESearch...

Entry information

Entry nameRS9_HUMAN
AccessionPrimary (citable) accession number: P46781
Secondary accession number(s): A9C4C1, Q4QRK7, Q9BVZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 144 of the entry and version 3 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

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