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Protein

40S ribosomal protein S14

Gene

RPS14

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

Functioni

GO - Molecular functioni

  1. mRNA 5'-UTR binding Source: UniProtKB
  2. poly(A) RNA binding Source: UniProtKB
  3. RNA binding Source: UniProtKB
  4. structural constituent of ribosome Source: InterPro
  5. translation regulator activity Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. erythrocyte differentiation Source: UniProtKB
  3. gene expression Source: Reactome
  4. maturation of SSU-rRNA Source: UniProtKB
  5. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  6. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  7. regulation of translation Source: GOC
  8. ribosomal small subunit assembly Source: UniProtKB
  9. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  10. translation Source: UniProtKB
  11. translational elongation Source: Reactome
  12. translational initiation Source: Reactome
  13. translational termination Source: Reactome
  14. viral life cycle Source: Reactome
  15. viral process Source: Reactome
  16. 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.

Protein family/group databases

MoonProtiP62263.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S14
Gene namesi
Name:RPS14
ORF Names:PRO2640
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:10387. RPS14.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. cytosolic small ribosomal subunit Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. focal adhesion Source: UniProtKB
  6. membrane Source: UniProtKB
  7. mitochondrion Source: Ensembl
  8. nucleolus Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

Orphaneti86841. Myelodysplastic syndrome associated with isolated del(5q) chromosome abnormality.
PharmGKBiPA34786.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 15115040S ribosomal protein S14PRO_0000123337Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161Phosphoserine1 Publication
Modified residuei133 – 1331Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP62263.
PaxDbiP62263.
PeptideAtlasiP62263.
PRIDEiP62263.

2D gel databases

SWISS-2DPAGEP62263.

PTM databases

PhosphoSiteiP62263.

Expressioni

Gene expression databases

BgeeiP62263.
CleanExiHS_RPS14.
ExpressionAtlasiP62263. baseline and differential.
GenevestigatoriP62263.

Organism-specific databases

HPAiHPA018504.

Interactioni

Protein-protein interaction databases

BioGridi112122. 129 interactions.
IntActiP62263. 26 interactions.
MINTiMINT-4999998.
STRINGi9606.ENSP00000311028.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AO1-151[»]
ProteinModelPortaliP62263.
SMRiP62263. Positions 16-140.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S11P family.Curated

Phylogenomic databases

eggNOGiCOG0100.
GeneTreeiENSGT00390000000703.
HOGENOMiHOG000111598.
HOVERGENiHBG053098.
InParanoidiP62263.
KOiK02955.
OMAiPYAAMIA.
OrthoDBiEOG77DJ81.
PhylomeDBiP62263.
TreeFamiTF300125.

Family and domain databases

Gene3Di3.30.420.80. 1 hit.
HAMAPiMF_01310. Ribosomal_S11.
InterProiIPR001971. Ribosomal_S11.
IPR018102. Ribosomal_S11_CS.
[Graphical view]
PANTHERiPTHR11759. PTHR11759. 1 hit.
PfamiPF00411. Ribosomal_S11. 1 hit.
[Graphical view]
PIRSFiPIRSF002131. Ribosomal_S11. 1 hit.
PROSITEiPS00054. RIBOSOMAL_S11. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62263-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPRKGKEKK EEQVISLGPQ VAEGENVFGV CHIFASFNDT FVHVTDLSGK
60 70 80 90 100
ETICRVTGGM KVKADRDESS PYAAMLAAQD VAQRCKELGI TALHIKLRAT
110 120 130 140 150
GGNRTKTPGP GAQSALRALA RSGMKIGRIE DVTPIPSDST RRKGGRRGRR

L
Length:151
Mass (Da):16,273
Last modified:January 23, 2007 - v3
Checksum:i4F4387F9FADAC278
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13934 Genomic DNA. Translation: AAB59505.1.
AF116710 mRNA. Translation: AAF71130.1.
AK312179 mRNA. Translation: BAG35112.1.
CH471062 Genomic DNA. Translation: EAW61723.1.
CH471062 Genomic DNA. Translation: EAW61724.1.
CH471062 Genomic DNA. Translation: EAW61725.1.
CH471062 Genomic DNA. Translation: EAW61726.1.
BC001126 mRNA. Translation: AAH01126.1.
BC003401 mRNA. Translation: AAH03401.1.
BC006784 mRNA. Translation: AAH06784.1.
BC020515 mRNA. Translation: AAH20515.1.
BC091474 mRNA. Translation: AAH91474.1.
CCDSiCCDS4307.1.
PIRiA25220.
RefSeqiNP_001020241.1. NM_001025070.1.
NP_001020242.1. NM_001025071.1.
NP_005608.1. NM_005617.3.
UniGeneiHs.744846.

Genome annotation databases

EnsembliENST00000312037; ENSP00000311028; ENSG00000164587.
ENST00000401695; ENSP00000385958; ENSG00000164587.
ENST00000407193; ENSP00000385425; ENSG00000164587.
ENST00000521466; ENSP00000428509; ENSG00000164587.
GeneIDi6208.
KEGGihsa:6208.
UCSCiuc003lsh.3. human.

Polymorphism databases

DMDMi50403752.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13934 Genomic DNA. Translation: AAB59505.1.
AF116710 mRNA. Translation: AAF71130.1.
AK312179 mRNA. Translation: BAG35112.1.
CH471062 Genomic DNA. Translation: EAW61723.1.
CH471062 Genomic DNA. Translation: EAW61724.1.
CH471062 Genomic DNA. Translation: EAW61725.1.
CH471062 Genomic DNA. Translation: EAW61726.1.
BC001126 mRNA. Translation: AAH01126.1.
BC003401 mRNA. Translation: AAH03401.1.
BC006784 mRNA. Translation: AAH06784.1.
BC020515 mRNA. Translation: AAH20515.1.
BC091474 mRNA. Translation: AAH91474.1.
CCDSiCCDS4307.1.
PIRiA25220.
RefSeqiNP_001020241.1. NM_001025070.1.
NP_001020242.1. NM_001025071.1.
NP_005608.1. NM_005617.3.
UniGeneiHs.744846.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AO1-151[»]
ProteinModelPortaliP62263.
SMRiP62263. Positions 16-140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112122. 129 interactions.
IntActiP62263. 26 interactions.
MINTiMINT-4999998.
STRINGi9606.ENSP00000311028.

Protein family/group databases

MoonProtiP62263.

PTM databases

PhosphoSiteiP62263.

Polymorphism databases

DMDMi50403752.

2D gel databases

SWISS-2DPAGEP62263.

Proteomic databases

MaxQBiP62263.
PaxDbiP62263.
PeptideAtlasiP62263.
PRIDEiP62263.

Protocols and materials databases

DNASUi6208.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000312037; ENSP00000311028; ENSG00000164587.
ENST00000401695; ENSP00000385958; ENSG00000164587.
ENST00000407193; ENSP00000385425; ENSG00000164587.
ENST00000521466; ENSP00000428509; ENSG00000164587.
GeneIDi6208.
KEGGihsa:6208.
UCSCiuc003lsh.3. human.

Organism-specific databases

CTDi6208.
GeneCardsiGC05M149803.
HGNCiHGNC:10387. RPS14.
HPAiHPA018504.
MIMi130620. gene.
neXtProtiNX_P62263.
Orphaneti86841. Myelodysplastic syndrome associated with isolated del(5q) chromosome abnormality.
PharmGKBiPA34786.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0100.
GeneTreeiENSGT00390000000703.
HOGENOMiHOG000111598.
HOVERGENiHBG053098.
InParanoidiP62263.
KOiK02955.
OMAiPYAAMIA.
OrthoDBiEOG77DJ81.
PhylomeDBiP62263.
TreeFamiTF300125.

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

ChiTaRSiRPS14. human.
GeneWikiiRPS14.
GenomeRNAii6208.
NextBioi24111.
PROiP62263.
SOURCEiSearch...

Gene expression databases

BgeeiP62263.
CleanExiHS_RPS14.
ExpressionAtlasiP62263. baseline and differential.
GenevestigatoriP62263.

Family and domain databases

Gene3Di3.30.420.80. 1 hit.
HAMAPiMF_01310. Ribosomal_S11.
InterProiIPR001971. Ribosomal_S11.
IPR018102. Ribosomal_S11_CS.
[Graphical view]
PANTHERiPTHR11759. PTHR11759. 1 hit.
PfamiPF00411. Ribosomal_S11. 1 hit.
[Graphical view]
PIRSFiPIRSF002131. Ribosomal_S11. 1 hit.
PROSITEiPS00054. RIBOSOMAL_S11. 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 [GENOMIC DNA].
  2. "Primary structure of human ribosomal protein S14 and the gene that encodes it."
    Rhoads D.D., Dixit A., Roufa D.J.
    Mol. Cell. Biol. 6:2774-2783(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Functional prediction of the coding sequences of 121 new genes deduced by analysis of cDNA clones from human fetal liver."
    Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J., Liu M., He F.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal liver.
  4. "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].
  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: Ovary, Placenta and Skin.
  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 2-15.
    Tissue: Placenta.
  8. "Fine-structure map of the human ribosomal protein gene RPS14."
    Diaz J.-J., Roufa D.J.
    Mol. Cell. Biol. 12:1680-1686(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRS14_HUMAN
AccessioniPrimary (citable) accession number: P62263
Secondary accession number(s): B2R5G5
, D3DQG5, P06366, Q5BJI0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: March 4, 2015
This is version 116 of the entry and version 3 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 5
    Human chromosome 5: 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.