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P62263 (RS14_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S14
Gene names
Name:RPS14
ORF Names:PRO2640
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length151 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the ribosomal protein S11P family.

Ontologies

Keywords
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

erythrocyte differentiation

Inferred from mutant phenotype PubMed 18202658. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

maturation of SSU-rRNA

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 7867928. Source: UniProtKB

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

regulation of translation

Inferred from mutant phenotype PubMed 3683397. Source: GOC

ribosomal small subunit assembly

Inferred from mutant phenotype PubMed 9152021. Source: UniProtKB

translation

Inferred from mutant phenotype PubMed 3683397. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

cytosolic small ribosomal subunit

Inferred from direct assay PubMed 15883184Ref.7PubMed 9152021. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from direct assay PubMed 9152021. Source: UniProtKB

   Molecular_functionRNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

mRNA 5'-UTR binding

Inferred from direct assay PubMed 7867928. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

translation regulator activity

Inferred from mutant phenotype PubMed 3683397. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 15115040S ribosomal protein S14 HAMAP-Rule MF_01310
PRO_0000123337

Amino acid modifications

Modified residue1331Phosphothreonine Ref.10

Sequences

Sequence LengthMass (Da)Tools
P62263 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 4F4387F9FADAC278

FASTA15116,273
        10         20         30         40         50         60 
MAPRKGKEKK EEQVISLGPQ VAEGENVFGV CHIFASFNDT FVHVTDLSGK ETICRVTGGM 

        70         80         90        100        110        120 
KVKADRDESS PYAAMLAAQD VAQRCKELGI TALHIKLRAT GGNRTKTPGP GAQSALRALA 

       130        140        150 
RSGMKIGRIE DVTPIPSDST RRKGGRRGRR L 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"Structures of the human and Drosophila 80S ribosome."
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.
Nature 497:80-85(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS4307.1.
PIRA25220.
RefSeqNP_001020241.1. NM_001025070.1.
NP_001020242.1. NM_001025071.1.
NP_005608.1. NM_005617.3.
UniGeneHs.744846.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00O1-151[»]
ProteinModelPortalP62263.
SMRP62263. Positions 16-140.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112122. 145 interactions.
IntActP62263. 25 interactions.
MINTMINT-4999998.
STRING9606.ENSP00000311028.

PTM databases

PhosphoSiteP62263.

Polymorphism databases

DMDM50403752.

2D gel databases

SWISS-2DPAGEP62263.

Proteomic databases

MaxQBP62263.
PaxDbP62263.
PeptideAtlasP62263.
PRIDEP62263.

Protocols and materials databases

DNASU6208.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000312037; ENSP00000311028; ENSG00000164587.
ENST00000401695; ENSP00000385958; ENSG00000164587.
ENST00000407193; ENSP00000385425; ENSG00000164587.
ENST00000521466; ENSP00000428509; ENSG00000164587.
GeneID6208.
KEGGhsa:6208.
UCSCuc003lsh.3. human.

Organism-specific databases

CTD6208.
GeneCardsGC05M149803.
HGNCHGNC:10387. RPS14.
HPAHPA018504.
MIM130620. gene.
neXtProtNX_P62263.
Orphanet86841. Myelodysplastic syndrome associated with isolated del(5q) chromosome abnormality.
PharmGKBPA34786.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0100.
HOGENOMHOG000111598.
HOVERGENHBG053098.
InParanoidP62263.
KOK02955.
OMALHVKIRA.
OrthoDBEOG77DJ81.
PhylomeDBP62263.
TreeFamTF300125.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP62263.
BgeeP62263.
CleanExHS_RPS14.
GenevestigatorP62263.

Family and domain databases

Gene3D3.30.420.80. 1 hit.
HAMAPMF_01310. Ribosomal_S11.
InterProIPR001971. Ribosomal_S11.
IPR018102. Ribosomal_S11_CS.
[Graphical view]
PANTHERPTHR11759. PTHR11759. 1 hit.
PfamPF00411. Ribosomal_S11. 1 hit.
[Graphical view]
PIRSFPIRSF002131. Ribosomal_S11. 1 hit.
PROSITEPS00054. RIBOSOMAL_S11. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPS14. human.
GeneWikiRPS14.
GenomeRNAi6208.
NextBio24111.
PROP62263.
SOURCESearch...

Entry information

Entry nameRS14_HUMAN
AccessionPrimary (citable) accession number: P62263
Secondary accession number(s): B2R5G5 expand/collapse secondary AC list , D3DQG5, P06366, Q5BJI0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM