RpS9

Functionⁱ

GO - Molecular functionⁱ

rRNA binding Source: GO_Central
structural constituent of ribosome
Source: FlyBase
Inferred from high throughput direct assayⁱ
- 16889426

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cytoplasmic translation
Source: FlyBase
Traceable author statementⁱ
- 17927810
positive regulation of translational fidelity Source: GO_Central

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding

Molecular function

Ribonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding

Enzyme and pathway databases

Reactomeⁱ	R-DME-156827 L13a-mediated translational silencing of Ceruloplasmin expression R-DME-1799339 SRP-dependent cotranslational protein targeting to membrane R-DME-6791226 Major pathway of rRNA processing in the nucleolus and cytosol R-DME-72649 Translation initiation complex formation R-DME-72689 Formation of a pool of free 40S subunits R-DME-72695 Formation of the ternary complex, and subsequently, the 43S complex R-DME-72702 Ribosomal scanning and start codon recognition R-DME-72706 GTP hydrolysis and joining of the 60S ribosomal subunit R-DME-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) R-DME-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Reactomeⁱ

R-DME-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-DME-1799339 SRP-dependent cotranslational protein targeting to membrane
R-DME-6791226 Major pathway of rRNA processing in the nucleolus and cytosol
R-DME-72649 Translation initiation complex formation
R-DME-72689 Formation of a pool of free 40S subunits
R-DME-72695 Formation of the ternary complex, and subsequently, the 43S complex
R-DME-72702 Ribosomal scanning and start codon recognition
R-DME-72706 GTP hydrolysis and joining of the 60S ribosomal subunit
R-DME-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-DME-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: 40S ribosomal protein S9
Gene namesⁱ	Name:RpS9Imported ORF Names:CG3395Imported
Organismⁱ	Drosophila melanogaster (Fruit fly)
Taxonomic identifierⁱ	7227 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Holometabola › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophila › Sophophora › melanogaster group › melanogaster subgroup
Proteomesⁱ	UP000000803 Componentⁱ: Chromosome 3L

Organism-specific databases

Drosophila genome database More...FlyBaseⁱ	FBgn0010408 RpS9

FlyBaseⁱ

FBgn0010408 RpS9

Subcellular locationⁱ

GO - Cellular component

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000132695	1 – 195	40S ribosomal protein S9Add BLAST		195

Proteomic databases

PaxDbⁱ	P55935
PRIDEⁱ	P55935

Expressionⁱ

Developmental stageⁱ

Expressed both maternally and zygotically throughout development.1 Publication

Gene expression databases

Bgeeⁱ	FBgn0010408
ExpressionAtlasⁱ	P55935 baseline and differential
Genevisibleⁱ	P55935 DM

Interactionⁱ

Protein-protein interaction databases

BioGridⁱ	64500, 26 interactors
IntActⁱ	P55935, 4 interactors
Molecular INTeraction database More...MINTⁱ	P55935
STRINGⁱ	7227.FBpp0076152

Structureⁱ

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4V6W	electron microscopy	6.00	AJ	1-195	[»]
ProteinModelPortalⁱ	P55935
SMRⁱ	P55935
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	109 – 183	S4 RNA-bindingPROSITE-ProRule annotationAdd BLAST		75

Sequence similaritiesⁱ

Belongs to the universal ribosomal protein uS4 family.Curated

Phylogenomic databases

eggNOGⁱ	KOG3301 Eukaryota COG0522 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00550000074829
InParanoidⁱ	P55935
KEGG Orthology (KO) More...KOⁱ	K02997
OMAⁱ	THGHIAI
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0S57
PhylomeDBⁱ	P55935

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00165 S4, 1 hit
Gene3Dⁱ	3.10.290.10, 1 hit
InterProⁱ	View protein in InterPro IPR022801 Ribosomal_S4/S9 IPR005710 Ribosomal_S4/S9_euk/arc IPR001912 Ribosomal_S4/S9_N IPR018079 Ribosomal_S4_CS IPR002942 S4_RNA-bd IPR036986 S4_RNA-bd_sf
PANTHERⁱ	PTHR11831 PTHR11831, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00163 Ribosomal_S4, 1 hit PF01479 S4, 1 hit
SMARTⁱ	View protein in SMART SM01390 Ribosomal_S4, 1 hit SM00363 S4, 1 hit
TIGRFAMsⁱ	TIGR01018 uS4_arch, 1 hit
PROSITEⁱ	View protein in PROSITE PS00632 RIBOSOMAL_S4, 1 hit PS50889 S4, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P55935-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MVNGRIPSVF SKTYVTPRRP YEKARLDQEL KIIGEYGLRN KREVWRVKYA 
        60         70         80         90        100
LAKIRKAARE LLTLDEKDEK RLFQGNALLR RLVRIGVLDE SRMKLDYVLG 
       110        120        130        140        150
LKIEDFLERR LQTQVFKLGL AKSIHHARVL IRQRHIRVRK QVVNIPSFVV 
       160        170        180        190 
RLDSQKHIDF SLKSPFGGGR PGRVKRKNLK KNQGGGGGAA EEEED

Length:195

Mass (Da):22,623

Last modified:March 1, 2005 - v2

Checksum:ⁱ7619DFAEF8B4157F

GO

Sequence cautionⁱ

The sequence CAB41492 differs from that shown. Reason: Frameshift at positions 39, 47, 90, 91, 119, 135, 145, 151, 157, 159, 165 and 180.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	57	A → V in CAB41492 (PubMed:8400363).Curated	1
Sequence conflictⁱ	69	E → A in CAB41492 (PubMed:8400363).Curated	1
Sequence conflictⁱ	76 – 79	NALL → KSLV in CAB41492 (PubMed:8400363).Curated	4
Sequence conflictⁱ	104	E → Q in CAB41492 (PubMed:8400363).Curated	1
Sequence conflictⁱ	138	V → A in CAB41492 (PubMed:8400363).Curated	1
Sequence conflictⁱ	164	S → M in CAB41492 (PubMed:8400363).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X69677 mRNA Translation: CAB41492.1 Frameshift. AE014296 Genomic DNA Translation: AAF50249.1 AE014296 Genomic DNA Translation: AAN11946.1
NCBI Reference Sequences More...RefSeqⁱ	NP_001287008.1, NM_001300079.1 NP_524004.2, NM_079280.4 NP_729506.1, NM_168350.2
UniGeneⁱ	Dm.6943

Genome annotation databases

EnsemblMetazoaⁱ	FBtr0076423; FBpp0076152; FBgn0010408 FBtr0076425; FBpp0076154; FBgn0010408 FBtr0342577; FBpp0309532; FBgn0010408
GeneIDⁱ	39108
KEGGⁱ	dme:Dmel_CG3395

Protein	Similar proteins		Species	Score	Length
P55935	40S ribosomal protein S9		DROYA		195
LD13662p		DROME		195
GD12912		DROSI		195
Uncharacterized protein		DROER		195
GM24860		DROSE		195
+161

Protein	Similar proteins		Species	Score	Length
P55935	40S ribosomal protein S9		DROYA		195
LD13662p		DROME		195
GD12912		DROSI		195
Uncharacterized protein		DROER		195
GM24860		DROSE		195
+213

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	X69677 mRNA Translation: CAB41492.1 Frameshift. AE014296 Genomic DNA Translation: AAF50249.1 AE014296 Genomic DNA Translation: AAN11946.1
NCBI Reference Sequences More...RefSeqⁱ	NP_001287008.1, NM_001300079.1 NP_524004.2, NM_079280.4 NP_729506.1, NM_168350.2
UniGeneⁱ	Dm.6943

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4V6W	electron microscopy	6.00	AJ	1-195	[»]
ProteinModelPortalⁱ	P55935
SMRⁱ	P55935
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	64500, 26 interactors
IntActⁱ	P55935, 4 interactors
Molecular INTeraction database More...MINTⁱ	P55935
STRINGⁱ	7227.FBpp0076152

Proteomic databases

PaxDbⁱ	P55935
PRIDEⁱ	P55935

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblMetazoaⁱ	FBtr0076423; FBpp0076152; FBgn0010408 FBtr0076425; FBpp0076154; FBgn0010408 FBtr0342577; FBpp0309532; FBgn0010408
GeneIDⁱ	39108
KEGGⁱ	dme:Dmel_CG3395

Organism-specific databases

CTDⁱ	6203
Drosophila genome database More...FlyBaseⁱ	FBgn0010408 RpS9

Phylogenomic databases

eggNOGⁱ	KOG3301 Eukaryota COG0522 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00550000074829
InParanoidⁱ	P55935
KEGG Orthology (KO) More...KOⁱ	K02997
OMAⁱ	THGHIAI
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0S57
PhylomeDBⁱ	P55935

Enzyme and pathway databases

Reactomeⁱ	R-DME-156827 L13a-mediated translational silencing of Ceruloplasmin expression R-DME-1799339 SRP-dependent cotranslational protein targeting to membrane R-DME-6791226 Major pathway of rRNA processing in the nucleolus and cytosol R-DME-72649 Translation initiation complex formation R-DME-72689 Formation of a pool of free 40S subunits R-DME-72695 Formation of the ternary complex, and subsequently, the 43S complex R-DME-72702 Ribosomal scanning and start codon recognition R-DME-72706 GTP hydrolysis and joining of the 60S ribosomal subunit R-DME-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) R-DME-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Reactomeⁱ

R-DME-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-DME-1799339 SRP-dependent cotranslational protein targeting to membrane
R-DME-6791226 Major pathway of rRNA processing in the nucleolus and cytosol
R-DME-72649 Translation initiation complex formation
R-DME-72689 Formation of a pool of free 40S subunits
R-DME-72695 Formation of the ternary complex, and subsequently, the 43S complex
R-DME-72702 Ribosomal scanning and start codon recognition
R-DME-72706 GTP hydrolysis and joining of the 60S ribosomal subunit
R-DME-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-DME-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Miscellaneous databases

ChiTaRSⁱ	RpS9 fly
GenomeRNAiⁱ	39108
Protein Ontology More...PROⁱ	PR:P55935

Gene expression databases

Bgeeⁱ	FBgn0010408
ExpressionAtlasⁱ	P55935 baseline and differential
Genevisibleⁱ	P55935 DM

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00165 S4, 1 hit
Gene3Dⁱ	3.10.290.10, 1 hit
InterProⁱ	View protein in InterPro IPR022801 Ribosomal_S4/S9 IPR005710 Ribosomal_S4/S9_euk/arc IPR001912 Ribosomal_S4/S9_N IPR018079 Ribosomal_S4_CS IPR002942 S4_RNA-bd IPR036986 S4_RNA-bd_sf
PANTHERⁱ	PTHR11831 PTHR11831, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00163 Ribosomal_S4, 1 hit PF01479 S4, 1 hit
SMARTⁱ	View protein in SMART SM01390 Ribosomal_S4, 1 hit SM00363 S4, 1 hit
TIGRFAMsⁱ	TIGR01018 uS4_arch, 1 hit
PROSITEⁱ	View protein in PROSITE PS00632 RIBOSOMAL_S4, 1 hit PS50889 S4, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	RS9_DROME
Accessionⁱ	P55935Primary (citable) accession number: P55935 Secondary accession number(s): A4V1R4 , Q6XIN2, Q9VT06, Q9VT07, Q9XZU5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
	Last sequence update:	March 1, 2005
	Last modified:	May 23, 2018
	This is version 132 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Drosophila annotation project

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UniProtKB - P55935 (RS9_DROME)

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40S ribosomal protein S9

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytosol

Nucleus

Other locations

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ