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P08708

- RS17_HUMAN

UniProt

P08708 - RS17_HUMAN

Protein

40S ribosomal protein S17

Gene

RPS17

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    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. membrane Source: UniProtKB
    5. ribosome Source: UniProtKB

    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

    MaxQBiP08708.
    PaxDbiP08708.
    PRIDEiP08708.

    PTM databases

    PhosphoSiteiP08708.

    Expressioni

    Gene expression databases

    BgeeiP08708.
    CleanExiHS_RPS17.
    GenevestigatoriP08708.

    Organism-specific databases

    HPAiHPA055060.

    Interactioni

    Protein-protein interaction databases

    BioGridi112132. 68 interactions.
    1527840. 14 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 1-126.
    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

    MGRVRTKTVK KAARVIIEKY YTRLGNDFHT NKRVCEEIAI IPSKKLRNKI    50
    AGYVTHLMKR IQRGPVRGIS IKLQEEERER RDNYVPEVSA LDQEIIEVDP 100
    DTKEMLKLLD FGSLSNLQVT QPTVGMNFKT PRGPV 135
    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:100505503.
    hsa: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 1-126.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112132. 68 interactions.
    1527840. 14 interactions.
    IntActi P08708. 17 interactions.
    MINTi MINT-5002404.
    STRINGi 9606.ENSP00000346045.

    PTM databases

    PhosphoSitei P08708.

    Proteomic databases

    MaxQBi P08708.
    PaxDbi P08708.
    PRIDEi P08708.

    Protocols and materials databases

    DNASUi 6218.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 6218.
    KEGGi hsa:100505503.
    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.
    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

    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 1, 2014
    This is version 147 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