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Protein

40S ribosomal protein S17

Gene

RPS17

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  • cellular protein metabolic process Source: Reactome
  • erythrocyte homeostasis Source: UniProtKB
  • gene expression Source: Reactome
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  • ribosomal small subunit assembly Source: GO_Central
  • ribosomal small subunit biogenesis Source: UniProtKB
  • rRNA processing Source: UniProtKB
  • SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  • translation Source: UniProtKB
  • translational elongation Source: Reactome
  • translational initiation Source: UniProtKB
  • translational termination Source: Reactome
  • viral life cycle Source: Reactome
  • viral process Source: Reactome
  • viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S17
Gene namesi
Name:RPS17
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:10397. RPS17.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • cytosolic small ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • ribosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Diamond-Blackfan anemia 4 (DBA4)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:612527

Keywords - Diseasei

Diamond-Blackfan anemia

Organism-specific databases

MIMi612527. phenotype.
Orphaneti124. Blackfan-Diamond anemia.
PharmGKBiPA34797.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 13513440S ribosomal protein S17PRO_0000141525Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191N6-succinyllysineBy similarity
Modified residuei113 – 1131Phosphoserine4 Publications
Modified residuei130 – 1301Phosphothreonine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP08708.
PRIDEiP08708.

PTM databases

PhosphoSiteiP08708.

Expressioni

Gene expression databases

BgeeiP08708.
CleanExiHS_RPS17.
ExpressionAtlasiP08708. baseline.
GenevisibleiP08708. HS.

Organism-specific databases

HPAiHPA055060.

Interactioni

Protein-protein interaction databases

BioGridi112132. 81 interactions.
IntActiP08708. 17 interactions.
MINTiMINT-5002404.
STRINGi9606.ENSP00000346046.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AR1-135[»]
5AJ0electron microscopy3.50BR1-135[»]
ProteinModelPortaliP08708.
SMRiP08708. Positions 1-126.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S17e family.Curated

Phylogenomic databases

eggNOGiCOG1383.
HOGENOMiHOG000227166.
HOVERGENiHBG001708.
InParanoidiP08708.
KOiK02962.
OrthoDBiEOG72C52C.
PhylomeDBiP08708.
TreeFamiTF317992.

Family and domain databases

Gene3Di1.10.60.20. 1 hit.
HAMAPiMF_00511. Ribosomal_S17e.
InterProiIPR001210. Ribosomal_S17e.
IPR018273. Ribosomal_S17e_CS.
[Graphical view]
PANTHERiPTHR10732. PTHR10732. 1 hit.
PfamiPF00833. Ribosomal_S17e. 1 hit.
[Graphical view]
SUPFAMiSSF116820. SSF116820. 1 hit.
PROSITEiPS00712. RIBOSOMAL_S17E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08708-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRVRTKTVK KAARVIIEKY YTRLGNDFHT NKRVCEEIAI IPSKKLRNKI
60 70 80 90 100
AGYVTHLMKR IQRGPVRGIS IKLQEEERER RDNYVPEVSA LDQEIIEVDP
110 120 130
DTKEMLKLLD FGSLSNLQVT QPTVGMNFKT PRGPV
Length:135
Mass (Da):15,550
Last modified:January 23, 2007 - v2
Checksum:i299AD605C5401325
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361E → K.
Corresponds to variant rs1043734 [ dbSNP | Ensembl ].
VAR_034478

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10320.1.
PIRiJT0405. R4HU17.
RefSeqiNP_001012.1. NM_001021.4.
UniGeneiHs.433427.
Hs.512525.

Genome annotation databases

EnsembliENST00000330244; ENSP00000346046; ENSG00000182774.
GeneIDi6218.
KEGGihsa:6218.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Diamond-Blackfan Anemia mutation database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10320.1.
PIRiJT0405. R4HU17.
RefSeqiNP_001012.1. NM_001021.4.
UniGeneiHs.433427.
Hs.512525.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AR1-135[»]
5AJ0electron microscopy3.50BR1-135[»]
ProteinModelPortaliP08708.
SMRiP08708. Positions 1-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112132. 81 interactions.
IntActiP08708. 17 interactions.
MINTiMINT-5002404.
STRINGi9606.ENSP00000346046.

PTM databases

PhosphoSiteiP08708.

Proteomic databases

PaxDbiP08708.
PRIDEiP08708.

Protocols and materials databases

DNASUi6218.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330244; ENSP00000346046; ENSG00000182774.
GeneIDi6218.
KEGGihsa:6218.

Organism-specific databases

CTDi6218.
GeneCardsiGC15M082821.
GeneReviewsiRPS17.
HGNCiHGNC:10397. RPS17.
HPAiHPA055060.
MIMi180472. gene.
612527. phenotype.
neXtProtiNX_P08708.
Orphaneti124. Blackfan-Diamond anemia.
PharmGKBiPA34797.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1383.
HOGENOMiHOG000227166.
HOVERGENiHBG001708.
InParanoidiP08708.
KOiK02962.
OrthoDBiEOG72C52C.
PhylomeDBiP08708.
TreeFamiTF317992.

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1979. Translation initiation complex formation.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

GeneWikiiRPS17.
GenomeRNAii6218.
NextBioi24145.
PROiP08708.
SOURCEiSearch...

Gene expression databases

BgeeiP08708.
CleanExiHS_RPS17.
ExpressionAtlasiP08708. baseline.
GenevisibleiP08708. HS.

Family and domain databases

Gene3Di1.10.60.20. 1 hit.
HAMAPiMF_00511. Ribosomal_S17e.
InterProiIPR001210. Ribosomal_S17e.
IPR018273. Ribosomal_S17e_CS.
[Graphical view]
PANTHERiPTHR10732. PTHR10732. 1 hit.
PfamiPF00833. Ribosomal_S17e. 1 hit.
[Graphical view]
SUPFAMiSSF116820. SSF116820. 1 hit.
PROSITEiPS00712. RIBOSOMAL_S17E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. Cited for: INVOLVEMENT IN DBA4.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND THR-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. 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. 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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRS17_HUMAN
AccessioniPrimary (citable) accession number: P08708
Secondary accession number(s): B2R4U4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. 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.