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P08708

- RS17_HUMAN

UniProt

P08708 - RS17_HUMAN

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Protein

40S ribosomal protein S17

Gene

RPS17

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

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. erythrocyte homeostasis Source: UniProtKB
  3. gene expression Source: Reactome
  4. mRNA metabolic process Source: Reactome
  5. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  6. ribosomal small subunit assembly Source: RefGenome
  7. ribosomal small subunit biogenesis Source: UniProtKB
  8. RNA metabolic process Source: Reactome
  9. rRNA processing Source: UniProtKB
  10. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  11. translation Source: UniProtKB
  12. translational elongation Source: RefGenome
  13. translational initiation Source: UniProtKB
  14. translational termination Source: Reactome
  15. viral life cycle Source: Reactome
  16. viral process Source: Reactome
  17. 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: Chromosome 15

Organism-specific databases

HGNCiHGNC:10397. RPS17.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. cytosolic small ribosomal subunit Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. focal adhesion Source: UniProtKB
  5. membrane Source: UniProtKB
  6. ribosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.

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.
GenevestigatoriP08708.

Organism-specific databases

HPAiHPA055060.

Interactioni

Protein-protein interaction databases

BioGridi112132. 74 interactions.
1527840. 16 interactions.
IntActiP08708. 17 interactions.
MINTiMINT-5002404.
STRINGi9606.ENSP00000346045.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00R1-135[»]
ProteinModelPortaliP08708.
SMRiP08708. Positions 1-129.
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:
EMBL
GenBank
DDBJ
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

GeneIDi6218.
KEGGihsa:6218.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Diamond-Blackfan Anemia mutation database

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS10320.1.
PIRi JT0405. R4HU17.
RefSeqi NP_001012.1. NM_001021.4.
UniGenei Hs.433427.
Hs.512525.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3J3A electron microscopy 5.00 R 1-135 [» ]
ProteinModelPortali P08708.
SMRi P08708. Positions 1-129.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112132. 74 interactions.
1527840. 16 interactions.
IntActi P08708. 17 interactions.
MINTi MINT-5002404.
STRINGi 9606.ENSP00000346045.

PTM databases

PhosphoSitei P08708.

Proteomic databases

PaxDbi P08708.
PRIDEi P08708.

Protocols and materials databases

DNASUi 6218.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 6218.
KEGGi hsa:6218.

Organism-specific databases

CTDi 6218.
GeneCardsi GC15M082821.
GeneReviewsi RPS17.
HGNCi HGNC:10397. RPS17.
HPAi HPA055060.
MIMi 180472. gene.
612527. phenotype.
neXtProti NX_P08708.
Orphaneti 124. Blackfan-Diamond anemia.
PharmGKBi PA34797.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1383.
HOGENOMi HOG000227166.
HOVERGENi HBG001708.
InParanoidi P08708.
KOi K02962.
OrthoDBi EOG72C52C.
PhylomeDBi P08708.
TreeFami TF317992.

Enzyme and pathway databases

Reactomei REACT_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

GeneWikii RPS17.
NextBioi 24145.
PROi P08708.
SOURCEi Search...

Gene expression databases

Bgeei P08708.
CleanExi HS_RPS17.
ExpressionAtlasi P08708. baseline.
Genevestigatori P08708.

Family and domain databases

Gene3Di 1.10.60.20. 1 hit.
HAMAPi MF_00511. Ribosomal_S17e.
InterProi IPR001210. Ribosomal_S17e.
IPR018273. Ribosomal_S17e_CS.
[Graphical view ]
PANTHERi PTHR10732. PTHR10732. 1 hit.
Pfami PF00833. Ribosomal_S17e. 1 hit.
[Graphical view ]
SUPFAMi SSF116820. SSF116820. 1 hit.
PROSITEi PS00712. RIBOSOMAL_S17E. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. 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: October 29, 2014
This is version 148 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