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P62249

- RS16_HUMAN

UniProt

P62249 - RS16_HUMAN

Protein

40S ribosomal protein S16

Gene

RPS16

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. protein binding Source: IntAct
    3. RNA binding Source: UniProtKB
    4. structural constituent of ribosome Source: InterPro

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. gene expression Source: Reactome
    3. mRNA metabolic process Source: Reactome
    4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
    5. ribosomal small subunit biogenesis Source: UniProtKB
    6. RNA metabolic process Source: Reactome
    7. rRNA processing Source: UniProtKB
    8. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
    9. translation Source: UniProtKB
    10. translational elongation Source: Reactome
    11. translational initiation Source: Reactome
    12. translational termination Source: Reactome
    13. viral life cycle Source: Reactome
    14. viral process Source: Reactome
    15. 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 S16
    Gene namesi
    Name:RPS16
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:10396. RPS16.

    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. small ribosomal subunit Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34796.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 14614540S ribosomal protein S16PRO_0000111479Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei60 – 601N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP62249.
    PaxDbiP62249.
    PeptideAtlasiP62249.
    PRIDEiP62249.

    PTM databases

    PhosphoSiteiP62249.

    Expressioni

    Gene expression databases

    ArrayExpressiP62249.
    BgeeiP62249.
    CleanExiHS_RPS16.
    GenevestigatoriP62249.

    Organism-specific databases

    HPAiHPA064222.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    LRRK2Q5S0072EBI-352480,EBI-5323863

    Protein-protein interaction databases

    BioGridi112131. 144 interactions.
    IntActiP62249. 25 interactions.
    MINTiMINT-5001167.
    STRINGi9606.ENSP00000251453.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3J3Aelectron microscopy5.00Q1-146[»]
    ProteinModelPortaliP62249.
    SMRiP62249. Positions 6-146.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ribosomal protein S9P family.Curated

    Phylogenomic databases

    eggNOGiCOG0103.
    HOGENOMiHOG000019803.
    HOVERGENiHBG055171.
    KOiK02960.
    OMAiNRRCEPK.
    PhylomeDBiP62249.
    TreeFamiTF300088.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    InterProiIPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR000754. Ribosomal_S9.
    IPR020574. Ribosomal_S9_CS.
    [Graphical view]
    PANTHERiPTHR21569. PTHR21569. 1 hit.
    PfamiPF00380. Ribosomal_S9. 1 hit.
    [Graphical view]
    SUPFAMiSSF54211. SSF54211. 1 hit.
    PROSITEiPS00360. RIBOSOMAL_S9. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P62249-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSKGPLQSV QVFGRKKTAT AVAHCKRGNG LIKVNGRPLE MIEPRTLQYK    50
    LLEPVLLLGK ERFAGVDIRV RVKGGGHVAQ IYAIRQSISK ALVAYYQKYV 100
    DEASKKEIKD ILIQYDRTLL VADPRRCESK KFGGPGARAR YQKSYR 146
    Length:146
    Mass (Da):16,445
    Last modified:January 23, 2007 - v2
    Checksum:i519BCFB91BB68A15
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60854 mRNA. Translation: AAA60583.1.
    AB061841 Genomic DNA. Translation: BAB79479.1.
    AK315498 mRNA. Translation: BAG37882.1.
    CH471126 Genomic DNA. Translation: EAW56894.1.
    BC004324 mRNA. Translation: AAH04324.1.
    BC007977 mRNA. Translation: AAH07977.1.
    CCDSiCCDS12535.1.
    PIRiA39760. R3HU16.
    RefSeqiNP_001011.1. NM_001020.4.
    UniGeneiHs.397609.

    Genome annotation databases

    EnsembliENST00000251453; ENSP00000251453; ENSG00000105193.
    GeneIDi6217.
    KEGGihsa:6217.
    UCSCiuc002olk.3. human.

    Polymorphism databases

    DMDMi50403607.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M60854 mRNA. Translation: AAA60583.1 .
    AB061841 Genomic DNA. Translation: BAB79479.1 .
    AK315498 mRNA. Translation: BAG37882.1 .
    CH471126 Genomic DNA. Translation: EAW56894.1 .
    BC004324 mRNA. Translation: AAH04324.1 .
    BC007977 mRNA. Translation: AAH07977.1 .
    CCDSi CCDS12535.1.
    PIRi A39760. R3HU16.
    RefSeqi NP_001011.1. NM_001020.4.
    UniGenei Hs.397609.

    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 Q 1-146 [» ]
    ProteinModelPortali P62249.
    SMRi P62249. Positions 6-146.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112131. 144 interactions.
    IntActi P62249. 25 interactions.
    MINTi MINT-5001167.
    STRINGi 9606.ENSP00000251453.

    PTM databases

    PhosphoSitei P62249.

    Polymorphism databases

    DMDMi 50403607.

    Proteomic databases

    MaxQBi P62249.
    PaxDbi P62249.
    PeptideAtlasi P62249.
    PRIDEi P62249.

    Protocols and materials databases

    DNASUi 6217.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000251453 ; ENSP00000251453 ; ENSG00000105193 .
    GeneIDi 6217.
    KEGGi hsa:6217.
    UCSCi uc002olk.3. human.

    Organism-specific databases

    CTDi 6217.
    GeneCardsi GC19M039923.
    H-InvDB HIX0212796.
    HGNCi HGNC:10396. RPS16.
    HPAi HPA064222.
    MIMi 603675. gene.
    neXtProti NX_P62249.
    PharmGKBi PA34796.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0103.
    HOGENOMi HOG000019803.
    HOVERGENi HBG055171.
    KOi K02960.
    OMAi NRRCEPK.
    PhylomeDBi P62249.
    TreeFami TF300088.

    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

    ChiTaRSi RPS16. human.
    GeneWikii RPS16.
    GenomeRNAii 6217.
    NextBioi 24141.
    PROi P62249.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P62249.
    Bgeei P62249.
    CleanExi HS_RPS16.
    Genevestigatori P62249.

    Family and domain databases

    Gene3Di 3.30.230.10. 1 hit.
    InterProi IPR020568. Ribosomal_S5_D2-typ_fold.
    IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
    IPR000754. Ribosomal_S9.
    IPR020574. Ribosomal_S9_CS.
    [Graphical view ]
    PANTHERi PTHR21569. PTHR21569. 1 hit.
    Pfami PF00380. Ribosomal_S9. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54211. SSF54211. 1 hit.
    PROSITEi PS00360. RIBOSOMAL_S9. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and sequence analysis of the human ribosomal protein S16."
      Batra S.K., Metzgar R.S., Hollingsworth M.A.
      J. Biol. Chem. 266:6830-6833(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
      Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
      Genome Res. 12:379-390(2002) [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: Tongue.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Brain and Kidney.
    6. "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.
    7. Bienvenut W.V., Lourenco F., Olson M.F.
      Submitted (DEC-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-15 AND 51-62, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Mammary carcinoma.
    8. "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-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

    Entry informationi

    Entry nameiRS16_HUMAN
    AccessioniPrimary (citable) accession number: P62249
    Secondary accession number(s): B2RDD5, P17008
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 101 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 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Ribosomal proteins
      Ribosomal proteins families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3