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Protein

40S ribosomal protein S16

Gene

RPS16

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

Functioni

GO - Molecular functioni

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

GO - Biological processi

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34796.

Polymorphism and mutation databases

BioMutaiRPS16.
DMDMi50403607.

PTM / Processingi

Molecule processing

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

Proteomic databases

MaxQBiP62249.
PaxDbiP62249.
PeptideAtlasiP62249.
PRIDEiP62249.

PTM databases

PhosphoSiteiP62249.

Expressioni

Gene expression databases

BgeeiP62249.
CleanExiHS_RPS16.
ExpressionAtlasiP62249. baseline and differential.
GenevestigatoriP62249.

Organism-specific databases

HPAiHPA064222.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112131. 155 interactions.
IntActiP62249. 25 interactions.
MINTiMINT-5001167.
STRINGi9606.ENSP00000251453.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AQ1-146[»]
ProteinModelPortaliP62249.
SMRiP62249. Positions 6-146.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S9P family.Curated

Phylogenomic databases

eggNOGiCOG0103.
GeneTreeiENSGT00390000013067.
HOGENOMiHOG000019803.
HOVERGENiHBG055171.
InParanoidiP62249.
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

        10         20         30         40         50
MPSKGPLQSV QVFGRKKTAT AVAHCKRGNG LIKVNGRPLE MIEPRTLQYK
60 70 80 90 100
LLEPVLLLGK ERFAGVDIRV RVKGGGHVAQ IYAIRQSISK ALVAYYQKYV
110 120 130 140
DEASKKEIKD ILIQYDRTLL VADPRRCESK KFGGPGARAR YQKSYR
Length:146
Mass (Da):16,445
Last modified:January 23, 2007 - v2
Checksum:i519BCFB91BB68A15
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 and mutation databases

BioMutaiRPS16.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AQ1-146[»]
ProteinModelPortaliP62249.
SMRiP62249. Positions 6-146.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112131. 155 interactions.
IntActiP62249. 25 interactions.
MINTiMINT-5001167.
STRINGi9606.ENSP00000251453.

PTM databases

PhosphoSiteiP62249.

Polymorphism and mutation databases

BioMutaiRPS16.
DMDMi50403607.

Proteomic databases

MaxQBiP62249.
PaxDbiP62249.
PeptideAtlasiP62249.
PRIDEiP62249.

Protocols and materials databases

DNASUi6217.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6217.
GeneCardsiGC19M039923.
H-InvDBHIX0212796.
HGNCiHGNC:10396. RPS16.
HPAiHPA064222.
MIMi603675. gene.
neXtProtiNX_P62249.
PharmGKBiPA34796.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0103.
GeneTreeiENSGT00390000013067.
HOGENOMiHOG000019803.
HOVERGENiHBG055171.
InParanoidiP62249.
KOiK02960.
OMAiNRRCEPK.
PhylomeDBiP62249.
TreeFamiTF300088.

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

ChiTaRSiRPS16. human.
GeneWikiiRPS16.
GenomeRNAii6217.
NextBioi24141.
PROiP62249.
SOURCEiSearch...

Gene expression databases

BgeeiP62249.
CleanExiHS_RPS16.
ExpressionAtlasiP62249. baseline and differential.
GenevestigatoriP62249.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. 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: April 29, 2015
This is version 108 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

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.