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Q6ZWN5

- RS9_MOUSE

UniProt

Q6ZWN5 - RS9_MOUSE

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Protein

40S ribosomal protein S9

Gene

Rps9

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: Ensembl
  2. rRNA binding Source: UniProtKB-KW
  3. structural constituent of ribosome Source: InterPro
  4. translation regulator activity Source: Ensembl

GO - Biological processi

  1. positive regulation of cell proliferation Source: Ensembl
  2. translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

ReactomeiREACT_196445. SRP-dependent cotranslational protein targeting to membrane.
REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

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

  1. cytosolic small ribosomal subunit Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. nucleolus Source: Ensembl
  4. ribonucleoprotein complex Source: UniProtKB
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.
GenevestigatoriQ6ZWN5.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi218346. 9 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ6ZWN5.
SMRiQ6ZWN5. Positions 2-186.
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.
OMAiMAPRSYS.
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. rpsD_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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS20726.1.
RefSeqi NP_084043.1. NM_029767.2.
UniGenei Mm.13944.

3D structure databases

ProteinModelPortali Q6ZWN5.
SMRi Q6ZWN5. Positions 2-186.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 218346. 9 interactions.

PTM databases

PhosphoSitei Q6ZWN5.

Proteomic databases

MaxQBi Q6ZWN5.
PaxDbi Q6ZWN5.
PRIDEi Q6ZWN5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000006496 ; ENSMUSP00000006496 ; ENSMUSG00000006333 .
ENSMUST00000108625 ; ENSMUSP00000104265 ; ENSMUSG00000006333 .
GeneIDi 76846.
KEGGi mmu:76846.
UCSCi uc009ewa.1. mouse.

Organism-specific databases

CTDi 6203.
MGIi MGI:1924096. Rps9.

Phylogenomic databases

eggNOGi COG0522.
GeneTreei ENSGT00550000074829.
HOGENOMi HOG000194525.
HOVERGENi HBG001135.
InParanoidi Q6ZWN5.
KOi K02997.
OMAi MAPRSYS.
OrthoDBi EOG7KH9KZ.
PhylomeDBi Q6ZWN5.
TreeFami TF300795.

Enzyme and pathway databases

Reactomei REACT_196445. SRP-dependent cotranslational protein targeting to membrane.
REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

ChiTaRSi RPS9. mouse.
NextBioi 345919.
PROi Q6ZWN5.
SOURCEi Search...

Gene expression databases

Bgeei Q6ZWN5.
CleanExi MM_RPS9.
ExpressionAtlasi Q6ZWN5. baseline and differential.
Genevestigatori Q6ZWN5.

Family and domain databases

Gene3Di 3.10.290.10. 1 hit.
InterProi IPR022801. Ribosomal_S4/S9.
IPR005710. Ribosomal_S4/S9_euk/arc.
IPR001912. Ribosomal_S4/S9_N.
IPR018079. Ribosomal_S4_CS.
IPR002942. S4_RNA-bd.
[Graphical view ]
PANTHERi PTHR11831. PTHR11831. 1 hit.
Pfami PF00163. Ribosomal_S4. 1 hit.
PF01479. S4. 1 hit.
[Graphical view ]
SMARTi SM00363. S4. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01018. rpsD_arch. 1 hit.
PROSITEi PS00632. RIBOSOMAL_S4. 1 hit.
PS50889. S4. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 90 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