Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

40S ribosomal protein S9

Gene

Rps9

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_283953. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_292503. Translation initiation complex formation.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_305839. Ribosomal scanning and start codon recognition.
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S9
Gene namesi
Name:Rps9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1924096. Rps9.

Subcellular locationi

  • Cytoplasm By similarity

  • Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 19419340S ribosomal protein S9PRO_0000132690Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661N6-acetyllysine1 Publication
Modified residuei116 – 1161N6-acetyllysine1 Publication
Modified residuei155 – 1551N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ6ZWN5.
PaxDbiQ6ZWN5.
PRIDEiQ6ZWN5.

PTM databases

PhosphoSiteiQ6ZWN5.

Expressioni

Gene expression databases

BgeeiQ6ZWN5.
CleanExiMM_RPS9.
ExpressionAtlasiQ6ZWN5. baseline and differential.
GenevisibleiQ6ZWN5. MM.

Interactioni

Subunit structurei

Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs.By similarity

Protein-protein interaction databases

BioGridi218346. 9 interactions.
STRINGi10090.ENSMUSP00000006496.

Structurei

3D structure databases

ProteinModelPortaliQ6ZWN5.
SMRiQ6ZWN5. Positions 7-177.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini108 – 18275S4 RNA-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein S4P family.Curated
Contains 1 S4 RNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0522.
GeneTreeiENSGT00550000074829.
HOGENOMiHOG000194525.
HOVERGENiHBG001135.
InParanoidiQ6ZWN5.
KOiK02997.
OMAiTIVYRKG.
OrthoDBiEOG7KH9KZ.
PhylomeDBiQ6ZWN5.
TreeFamiTF300795.

Family and domain databases

Gene3Di3.10.290.10. 1 hit.
InterProiIPR022801. Ribosomal_S4/S9.
IPR005710. Ribosomal_S4/S9_euk/arc.
IPR001912. Ribosomal_S4/S9_N.
IPR018079. Ribosomal_S4_CS.
IPR002942. S4_RNA-bd.
[Graphical view]
PANTHERiPTHR11831. PTHR11831. 1 hit.
PfamiPF00163. Ribosomal_S4. 1 hit.
PF01479. S4. 1 hit.
[Graphical view]
SMARTiSM00363. S4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01018. uS4_arch. 1 hit.
PROSITEiPS00632. RIBOSOMAL_S4. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q6ZWN5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPVARSWVCR KTYVTPRRPF EKSRLDQELK LIGEYGLRNK REVWRVKFTL
60 70 80 90 100
AKIRKAAREL LTLDEKDPRR LFEGNALLRR LVRIGVLDEG KMKLDYILGL
110 120 130 140 150
KIEDFLERRL QTQVFKLGLA KSIHHARVLI RQRHIRVRKQ VVNIPSFIVR
160 170 180 190
LDSQKHIDFS LRSPYGGGRP GRVKRKNAKK GQGGAGAGDD EEED
Length:194
Mass (Da):22,591
Last modified:January 23, 2007 - v3
Checksum:iE9CE3CBD59524F81
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti156 – 1561H → P in AAH31746 (PubMed:15489334).Curated
Sequence conflicti163 – 1631S → F in AAH31746 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK050591 mRNA. Translation: BAC34330.1.
AK081889 mRNA. Translation: BAC38361.1.
AK150800 mRNA. Translation: BAE29863.1.
AK150988 mRNA. Translation: BAE30013.1.
AK151029 mRNA. Translation: BAE30046.1.
AK151621 mRNA. Translation: BAE30558.1.
BC031746 mRNA. Translation: AAH31746.1.
CCDSiCCDS20726.1.
RefSeqiNP_084043.1. NM_029767.2.
UniGeneiMm.13944.

Genome annotation databases

EnsembliENSMUST00000006496; ENSMUSP00000006496; ENSMUSG00000006333.
ENSMUST00000108625; ENSMUSP00000104265; ENSMUSG00000006333.
GeneIDi76846.
KEGGimmu:76846.
UCSCiuc009ewa.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK050591 mRNA. Translation: BAC34330.1.
AK081889 mRNA. Translation: BAC38361.1.
AK150800 mRNA. Translation: BAE29863.1.
AK150988 mRNA. Translation: BAE30013.1.
AK151029 mRNA. Translation: BAE30046.1.
AK151621 mRNA. Translation: BAE30558.1.
BC031746 mRNA. Translation: AAH31746.1.
CCDSiCCDS20726.1.
RefSeqiNP_084043.1. NM_029767.2.
UniGeneiMm.13944.

3D structure databases

ProteinModelPortaliQ6ZWN5.
SMRiQ6ZWN5. Positions 7-177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi218346. 9 interactions.
STRINGi10090.ENSMUSP00000006496.

PTM databases

PhosphoSiteiQ6ZWN5.

Proteomic databases

MaxQBiQ6ZWN5.
PaxDbiQ6ZWN5.
PRIDEiQ6ZWN5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000006496; ENSMUSP00000006496; ENSMUSG00000006333.
ENSMUST00000108625; ENSMUSP00000104265; ENSMUSG00000006333.
GeneIDi76846.
KEGGimmu:76846.
UCSCiuc009ewa.1. mouse.

Organism-specific databases

CTDi6203.
MGIiMGI:1924096. Rps9.

Phylogenomic databases

eggNOGiCOG0522.
GeneTreeiENSGT00550000074829.
HOGENOMiHOG000194525.
HOVERGENiHBG001135.
InParanoidiQ6ZWN5.
KOiK02997.
OMAiTIVYRKG.
OrthoDBiEOG7KH9KZ.
PhylomeDBiQ6ZWN5.
TreeFamiTF300795.

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_283953. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_292503. Translation initiation complex formation.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_305839. Ribosomal scanning and start codon recognition.
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Miscellaneous databases

ChiTaRSiRps9. mouse.
NextBioi345919.
PROiQ6ZWN5.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZWN5.
CleanExiMM_RPS9.
ExpressionAtlasiQ6ZWN5. baseline and differential.
GenevisibleiQ6ZWN5. MM.

Family and domain databases

Gene3Di3.10.290.10. 1 hit.
InterProiIPR022801. Ribosomal_S4/S9.
IPR005710. Ribosomal_S4/S9_euk/arc.
IPR001912. Ribosomal_S4/S9_N.
IPR018079. Ribosomal_S4_CS.
IPR002942. S4_RNA-bd.
[Graphical view]
PANTHERiPTHR11831. PTHR11831. 1 hit.
PfamiPF00163. Ribosomal_S4. 1 hit.
PF01479. S4. 1 hit.
[Graphical view]
SMARTiSM00363. S4. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01018. uS4_arch. 1 hit.
PROSITEiPS00632. RIBOSOMAL_S4. 1 hit.
PS50889. S4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow, Head and Thymus.
  2. "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].
    Strain: Czech II.
    Tissue: Mammary tumor.
  3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66 AND LYS-116, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRS9_MOUSE
AccessioniPrimary (citable) accession number: Q6ZWN5
Secondary accession number(s): Q3UBF1, Q8K2D1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 98 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. 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.