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P08708 (RS17_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S17
Gene names
Name:RPS17
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length135 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Involvement in disease

Diamond-Blackfan anemia 4 (DBA4) [MIM:612527]: 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.8 Ref.9

Sequence similarities

Belongs to the ribosomal protein S17e family.

Ontologies

Keywords
   Coding sequence diversityPolymorphism
   DiseaseDiamond-Blackfan anemia
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMPhosphoprotein
   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 homeostasis

Inferred from mutant phenotype Ref.8. Source: UniProtKB

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

rRNA processing

Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB

ribosomal small subunit assembly

Inferred from Biological aspect of Ancestor. Source: RefGenome

ribosomal small subunit biogenesis

Inferred from mutant phenotype PubMed 18697920. Source: UniProtKB

translation

Inferred by curator Ref.7. Source: UniProtKB

translational elongation

Inferred from Biological aspect of Ancestor. Source: RefGenome

translational initiation

Non-traceable author statement Ref.8. Source: UniProtKB

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_componentcytosol

Traceable author statement. Source: Reactome

cytosolic small ribosomal subunit

Inferred from direct assay PubMed 15883184Ref.7. Source: UniProtKB

ribosome

Non-traceable author statement Ref.2. Source: UniProtKB

   Molecular_functionpoly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

structural constituent of ribosome

Non-traceable author statement Ref.8PubMed 18412286. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 13513440S ribosomal protein S17 HAMAP-Rule MF_00511
PRO_0000141525

Amino acid modifications

Modified residue191N6-succinyllysine By similarity
Modified residue1131Phosphoserine Ref.10 Ref.12 Ref.13 Ref.15
Modified residue1301Phosphothreonine Ref.10 Ref.13

Natural variations

Natural variant361E → K.
Corresponds to variant rs1043734 [ dbSNP | Ensembl ].
VAR_034478

Sequences

Sequence LengthMass (Da)Tools
P08708 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 299AD605C5401325

FASTA13515,550
        10         20         30         40         50         60 
MGRVRTKTVK KAARVIIEKY YTRLGNDFHT NKRVCEEIAI IPSKKLRNKI AGYVTHLMKR 

        70         80         90        100        110        120 
IQRGPVRGIS IKLQEEERER RDNYVPEVSA LDQEIIEVDP DTKEMLKLLD FGSLSNLQVT 

       130 
QPTVGMNFKT PRGPV 

« Hide

References

« Hide 'large scale' references
[1]"Homologous ribosomal proteins in bacteria, yeast, and humans."
Chen I.-T., Dixit A., Rhoads D.D., Roufa D.J.
Proc. Natl. Acad. Sci. U.S.A. 83:6907-6911(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptionally active human ribosomal protein S17 gene."
Chen I.-T., Roufa D.J.
Gene 70:107-116(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thymus.
[4]"Analysis of the DNA sequence and duplication history of human chromosome 15."
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A. expand/collapse author list , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.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].
[6]"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: B-cell, Kidney, Lung, Pancreas, Prostate and Salivary gland.
[7]"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 2-16.
Tissue: Placenta.
[8]"Ribosomal protein S17 gene (RPS17) is mutated in Diamond-Blackfan anemia."
Cmejla R., Cmejlova J., Handrkova H., Petrak J., Pospisilova D.
Hum. Mutat. 28:1178-1182(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN DBA4.
[9]"Ribosomal protein L5 and L11 mutations are associated with cleft palate and abnormal thumbs in Diamond-Blackfan anemia patients."
Gazda H.T., Sheen M.R., Vlachos A., Choesmel V., O'Donohue M.-F., Schneider H., Darras N., Hasman C., Sieff C.A., Newburger P.E., Ball S.E., Niewiadomska E., Matysiak M., Zaucha J.M., Glader B., Niemeyer C., Meerpohl J.J., Atsidaftos E. expand/collapse author list , Lipton J.M., Gleizes P.-E., Beggs A.H.
Am. J. Hum. Genet. 83:769-780(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN DBA4.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND THR-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND THR-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13932 mRNA. Translation: AAA60284.1.
M18000 Genomic DNA. Translation: AAA60285.1.
AK026570 mRNA. Translation: BAB15501.1.
AK311951 mRNA. Translation: BAG34891.1.
AC135995 Genomic DNA. No translation available.
CH471188 Genomic DNA. Translation: EAW62454.1.
BC009407 mRNA. Translation: AAH09407.1.
BC019899 mRNA. Translation: AAH19899.1.
BC022370 mRNA. Translation: AAH22370.1.
BC049824 mRNA. Translation: AAH49824.1.
BC070222 mRNA. Translation: AAH70222.1.
BC062715 mRNA. Translation: AAH62715.1.
BC071928 mRNA. Translation: AAH71928.1.
PIRR4HU17. JT0405.
RefSeqNP_001012.1. NM_001021.3.
NP_001185986.1. NM_001199057.1.
UniGeneHs.433427.
Hs.512525.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00R1-135[»]
ProteinModelPortalP08708.
SMRP08708. Positions 1-126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112132. 93 interactions.
1527840. 14 interactions.
IntActP08708. 17 interactions.
MINTMINT-5002404.
STRING9606.ENSP00000346045.

PTM databases

PhosphoSiteP08708.

Proteomic databases

PaxDbP08708.
PRIDEP08708.

Protocols and materials databases

DNASU6218.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330339; ENSP00000346045; ENSG00000184779.
GeneID100505503.
6218.
KEGGhsa:100505503.
hsa:6218.

Organism-specific databases

CTD100505503.
6218.
GeneCardsGC15M082821.
HGNCHGNC:10397. RPS17.
HPAHPA055060.
MIM180472. gene.
612527. phenotype.
neXtProtNX_P08708.
Orphanet124. Blackfan-Diamond anemia.
PharmGKBPA34797.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1383.
HOGENOMHOG000227166.
HOVERGENHBG001708.
InParanoidP08708.
KOK02962.
OrthoDBEOG72C52C.
PhylomeDBP08708.
TreeFamTF317992.

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

BgeeP08708.
CleanExHS_RPS17.
GenevestigatorP08708.

Family and domain databases

Gene3D1.10.60.20. 1 hit.
HAMAPMF_00511. Ribosomal_S17e.
InterProIPR001210. Ribosomal_S17e.
IPR018273. Ribosomal_S17e_CS.
[Graphical view]
PANTHERPTHR10732. PTHR10732. 1 hit.
PfamPF00833. Ribosomal_S17e. 1 hit.
[Graphical view]
SUPFAMSSF116820. SSF116820. 1 hit.
PROSITEPS00712. RIBOSOMAL_S17E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRPS17.
NextBio24145.
PROP08708.
SOURCESearch...

Entry information

Entry nameRS17_HUMAN
AccessionPrimary (citable) accession number: P08708
Secondary accession number(s): B2R4U4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 142 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 15

Human chromosome 15: entries, gene names and cross-references to MIM