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P39019 (RS19_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S19
Gene names
Name:RPS19
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length145 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for pre-rRNA processing and maturation of 40S ribosomal subunits. Ref.8

Subunit structure

Interacts with RPS19BP1 By similarity.

Subcellular location

Nucleus. Note: Located more specifically in the nucleoli. Ref.9 Ref.17

Tissue specificity

Higher level expression is seen in the colon carcinoma tissue than normal colon tissue.

Involvement in disease

Diamond-Blackfan anemia 1 (DBA1) [MIM:105650]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of developing leukemia. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.9 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20

Sequence similarities

Belongs to the ribosomal protein S19e family.

Ontologies

Keywords
   Cellular componentNucleus
   DiseaseDiamond-Blackfan anemia
Disease mutation
   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

erythrocyte differentiation

Inferred from mutant phenotype PubMed 16289379. Source: HGNC

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

maturation of SSU-rRNA

Inferred from mutant phenotype Ref.8PubMed 17053056. Source: UniProtKB

maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Inferred from mutant phenotype Ref.8PubMed 17053056. Source: UniProtKB

monocyte chemotaxis

Inferred from direct assay PubMed 11226885. Source: UniProtKB

negative regulation of respiratory burst involved in inflammatory response

Inferred from direct assay PubMed 15750715. Source: UniProtKB

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

nucleolus organization

Inferred from mutant phenotype PubMed 17053056. Source: UniProtKB

positive regulation of cellular component movement

Traceable author statement PubMed 16289379. Source: HGNC

positive regulation of respiratory burst involved in inflammatory response

Inferred from direct assay PubMed 15750715. Source: UniProtKB

protein tetramerization

Inferred from direct assay PubMed 11226885. Source: UniProtKB

rRNA processing

Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB

response to extracellular stimulus

Traceable author statement PubMed 16289379. Source: HGNC

ribosomal small subunit assembly

Inferred from mutant phenotype PubMed 17053056. Source: UniProtKB

ribosomal small subunit biogenesis

Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB

translation

Inferred by curator Ref.4. 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 Ref.9. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 11716516. Source: UniProtKB

cytosolic small ribosomal subunit

Inferred from direct assay PubMed 15883184Ref.4. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nucleolus

Inferred from direct assay Ref.17Ref.9. Source: UniProtKB

ribosome

Inferred from direct assay Ref.9. Source: UniProtKB

   Molecular_functionfibroblast growth factor binding

Inferred from physical interaction PubMed 11716516. Source: BHF-UCL

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 11226885. Source: UniProtKB

protein kinase binding

Inferred from physical interaction PubMed 16266891. Source: UniProtKB

structural constituent of ribosome

Inferred from direct assay PubMed 15883184. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PIM1P113097EBI-354451,EBI-696621

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4 Ref.5
Chain2 – 14514440S ribosomal protein S19
PRO_0000153810

Amino acid modifications

Modified residue231N6-acetyllysine Ref.11
Modified residue1111N6-acetyllysine Ref.11
Modified residue1151N6-acetyllysine By similarity
Modified residue1431N6-succinyllysine By similarity

Natural variations

Natural variant9 – 146Missing in DBA1.
VAR_055436
Natural variant151V → F in DBA1; affects protein stability; does not localize to the nucleolus. Ref.9 Ref.15 Ref.17
VAR_018438
Natural variant171A → P in DBA1. Ref.20
VAR_046145
Natural variant18 – 192LA → E in DBA1.
VAR_055437
Natural variant181L → P in DBA1; affects protein stability; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit. Ref.9 Ref.16
VAR_018439
Natural variant181L → R in DBA1. Ref.19
VAR_046146
Natural variant211F → S in DBA1.
VAR_055438
Natural variant471P → L in DBA1; affects assembly into a functional ribosomal subunit. Ref.9 Ref.16
VAR_018440
Natural variant521W → C in DBA1.
VAR_055439
Natural variant521W → R in DBA1; affects assembly into a functional ribosomal subunit. Ref.2 Ref.9
VAR_018441
Natural variant551T → M in DBA1. Ref.17
VAR_018442
Natural variant561R → Q in DBA1; affects assembly into a functional ribosomal subunit. Ref.9 Ref.15 Ref.19
VAR_018437
Natural variant571A → P in DBA1; affects protein stability; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit. Ref.9
VAR_055440
Natural variant58 – 603Missing in DBA1.
VAR_046147
Natural variant591S → F in DBA1. Ref.19
VAR_046148
Natural variant611A → E in DBA1; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit. Ref.9 Ref.15
VAR_018443
Natural variant621R → Q in DBA1; affects assembly into a functional ribosomal subunit. Ref.9 Ref.18 Ref.19
VAR_018444
Natural variant621R → W in DBA1; increased protein degradation; affects assembly into a functional ribosomal subunit. Ref.2 Ref.9 Ref.15 Ref.16
VAR_006924
Natural variant641L → P in DBA1.
VAR_055441
Natural variant761T → P in DBA1.
VAR_055442
Natural variant78 – 836IYGGRQ → R in DBA1.
VAR_055443
Natural variant1011R → H in DBA1; increased protein degradation; affects assembly into a functional ribosomal subunit. Ref.9 Ref.15 Ref.19
VAR_018445
Natural variant1201G → R in DBA1. Ref.9 Ref.15
VAR_018446
Natural variant1271G → E in DBA1; affects protein stability; does not localize to the nucleolus; affects assembly into a functional ribosomal subunit.
VAR_055444
Natural variant1311L → P in DBA1. Ref.18
VAR_018447
Natural variant1311L → R in DBA1. Ref.19
VAR_046149
Natural variant1351A → T in DBA1.
VAR_055445

Sequences

Sequence LengthMass (Da)Tools
P39019 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 181F2DB898E56E41

FASTA14516,060
        10         20         30         40         50         60 
MPGVTVKDVN QQEFVRALAA FLKKSGKLKV PEWVDTVKLA KHKELAPYDE NWFYTRAAST 

        70         80         90        100        110        120 
ARHLYLRGGA GVGSMTKIYG GRQRNGVMPS HFSRGSKSVA RRVLQALEGL KMVEKDQDGG 

       130        140 
RKLTPQGQRD LDRIAGQVAA ANKKH 

« Hide

References

« Hide 'large scale' references
[1]"Differential expression of S19 ribosomal protein, laminin-binding protein, and human lymphocyte antigen class I messenger RNAs associated with colon carcinoma progression and differentiation."
Kondoh N., Schweinfest C.W., Henderson K.W., Papas T.S.
Cancer Res. 52:791-796(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The gene encoding ribosomal protein S19 is mutated in Diamond-Blackfan anaemia."
Draptchinskaia N., Gustavsson P., Andersson B., Pettersson M., Willig T.-N.D., Dianzani I., Ball S., Tchernia G., Klar J., Matsson H., Tentler D., Mohandas N., Carlsson B., Dahl N.
Nat. Genet. 21:169-175(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS DBA1 ARG-52 AND TRP-62.
[3]"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: Colon, Eye and Placenta.
[4]"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 2-11.
Tissue: Placenta.
[5]Bienvenut W.V., Calvo F., Kolch W., Lourenco F., Olson M.F.
Submitted (DEC-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-24; 30-38; 83-94; 102-111 AND 134-145, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma and Mammary carcinoma.
[6]"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 120-137.
[7]"Molecular basis of Diamond-Blackfan anemia: new findings from the Italian registry and a review of the literature."
Campagnoli M.F., Garelli E., Quarello P., Carando A., Varotto S., Nobili B., Longoni D., Pecile V., Zecca M., Dufour C., Ramenghi U., Dianzan I.
Haematologica 89:480-489(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON DBA1 VARIANTS.
[8]"Human RPS19, the gene mutated in Diamond-Blackfan anemia, encodes a ribosomal protein required for the maturation of 40S ribosomal subunits."
Flygare J., Aspesi A., Bailey J.C., Miyake K., Caffrey J.M., Karlsson S., Ellis S.R.
Blood 109:980-986(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Missense mutations associated with Diamond-Blackfan anemia affect the assembly of ribosomal protein S19 into the ribosome."
Angelini M., Cannata S., Mercaldo V., Gibello L., Santoro C., Dianzani I., Loreni F.
Hum. Mol. Genet. 16:1720-1727(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS DBA1 PHE-15; PRO-18; LEU-47; ARG-52; GLN-56; PRO-57; GLU-61; GLN-62; TRP-62; HIS-101 AND ARG-120.
[10]"RPS19 mutations in patients with Diamond-Blackfan anemia."
Campagnoli M.F., Ramenghi U., Armiraglio M., Quarello P., Garelli E., Carando A., Avondo F., Pavesi E., Fribourg S., Gleizes P.E., Loreni F., Dianzani I.
Hum. Mutat. 29:911-920(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS DBA1.
[11]"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-23 AND LYS-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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].
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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) OF 80S RIBOSOME.
[15]"Mutations in ribosomal protein S19 gene and Diamond Blackfan anemia: wide variations in phenotypic expression."
Willig T.-N.D., Draptchinskaia N., Dianzani I., Ball S., Niemeyer C., Ramenghi U., Orfali K., Gustavsson P., Garelli E., Brusco A., Tiemann C., Perignon J.L., Bouchier C., Cicchiello L., Dahl N., Mohandas N., Tchernia G.
Blood 94:4294-4306(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DBA1 PHE-15; GLN-56; GLU-61; TRP-62; HIS-101 AND ARG-120.
[16]"Diamond-Blackfan anemia: report of seven further mutations in the RPS19 gene and evidence of mutation heterogeneity in the Italian population."
Ramenghi U., Campagnoli M.F., Garelli E., Carando A., Brusco A., Bagnara G.P., Strippoli P., Izzi G.C., Brandalise S., Riccardi R., Dianzani I.
Blood Cells Mol. Dis. 26:417-422(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DBA1 PRO-18; LEU-47 AND TRP-62.
[17]"Nucleolar localization of RPS19 protein in normal cells and mislocalization due to mutations in the nucleolar localization signals in 2 Diamond-Blackfan anemia patients: potential insights into pathophysiology."
Da Costa L., Tchernia G., Gascard P., Lo A., Meerpohl J., Niemeyer C., Chasis J.-A., Fixler J., Mohandas N.
Blood 101:5039-5045(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DBA1 PHE-15 AND MET-55, SUBCELLULAR LOCATION.
[18]"Ten novel Diamond-Blackfan anemia mutations and three polymorphisms within the rps19 gene."
Proust A., Da Costa L., Rince P., Landois A., Tamary H., Zaizov R., Tchernia G., Delaunay J.
Hematol. J. 4:132-136(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DBA1 GLN-62 AND PRO-131.
[19]"RNA and protein evidence for haplo-insufficiency in Diamond-Blackfan anaemia patients with RPS19 mutations."
Gazda H.T., Zhong R., Long L., Niewiadomska E., Lipton J.M., Ploszynska A., Zaucha J.M., Vlachos A., Atsidaftos E., Viskochil D.H., Niemeyer C.M., Meerpohl J.J., Rokicka-Milewska R., Pospisilova D., Wiktor-Jedrzejczak W., Nathan D.G., Beggs A.H., Sieff C.A.
Br. J. Haematol. 127:105-113(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DBA1 ARG-18; GLN-56; 58-ALA--THR-60 DEL; PHE-59; GLN-62; HIS-101 AND ARG-131.
[20]Erratum
Pereira J.C., Fiskerstrand T., Ribeiro M.L.
Hum. Genet. 115:349-349(2004)
Cited for: VARIANT DBA1 PRO-17.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M81757 mRNA. Translation: AAA89070.1.
AF092907, AF092906 Genomic DNA. Translation: AAD13668.1.
BC000023 mRNA. Translation: AAH00023.1.
BC007615 mRNA. Translation: AAH07615.1.
BC018616 mRNA. Translation: AAH18616.1.
AB007155 Genomic DNA. Translation: BAA28593.1.
PIRI52692.
RefSeqNP_001013.1. NM_001022.3.
UniGeneHs.438429.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00T1-145[»]
ProteinModelPortalP39019.
SMRP39019. Positions 4-144.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112137. 143 interactions.
IntActP39019. 16 interactions.
MINTMINT-189322.
STRING9606.ENSP00000221975.

PTM databases

PhosphoSiteP39019.

Polymorphism databases

DMDM730640.

Proteomic databases

PaxDbP39019.
PeptideAtlasP39019.
PRIDEP39019.

Protocols and materials databases

DNASU6223.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000593863; ENSP00000470004; ENSG00000105372.
ENST00000598742; ENSP00000470972; ENSG00000105372.
ENST00000608106; ENSP00000476258; ENSG00000272852.
ENST00000608215; ENSP00000476809; ENSG00000272852.
GeneID6223.
KEGGhsa:6223.
UCSCuc002ort.3. human.

Organism-specific databases

CTD6223.
GeneCardsGC19P042363.
HGNCHGNC:10402. RPS19.
MIM105650. phenotype.
603474. gene.
neXtProtNX_P39019.
Orphanet124. Blackfan-Diamond anemia.
PharmGKBPA34803.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2238.
HOVERGENHBG000240.
InParanoidP39019.
KOK02966.
OMACQSLEKI.
OrthoDBEOG74J99M.
PhylomeDBP39019.
TreeFamTF315008.

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

ArrayExpressP39019.
BgeeP39019.
CleanExHS_RPS19.
GenevestigatorP39019.

Family and domain databases

InterProIPR001266. Ribosomal_S19e.
IPR018277. Ribosomal_S19e_CS.
[Graphical view]
PANTHERPTHR11710. PTHR11710. 1 hit.
PfamPF01090. Ribosomal_S19e. 1 hit.
[Graphical view]
ProDomPD003854. Ribosomal_S19e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00628. RIBOSOMAL_S19E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPS19. human.
GeneWikiRibosomal_protein_S19.
GenomeRNAi6223.
NextBio24159.
PROP39019.
SOURCESearch...

Entry information

Entry nameRS19_HUMAN
AccessionPrimary (citable) accession number: P39019
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 140 of the entry and version 2 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