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P62277 (RS13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 113. 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 S13
Gene names
Name:RPS13
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 S15P family.

Ontologies

Keywords
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
Phosphoprotein
   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

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

negative regulation of RNA splicing

Inferred from direct assay PubMed 17881366. Source: UniProtKB

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

translation

Inferred by curator PubMed 15883184Ref.7. 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.7. Source: UniProtKB

extracellular vesicular exosome

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

nucleolus

Inferred from direct assay PubMed 17881366. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 17881366. Source: UniProtKB

ribosome

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_functionmRNA binding

Inferred from direct assay PubMed 17881366. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12054647. Source: UniProtKB

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PDCD4Q53EL62EBI-351850,EBI-935824

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 15115040S ribosomal protein S13 HAMAP-Rule MF_01343_A
PRO_0000115661

Amino acid modifications

Modified residue271N6-acetyllysine; alternate Ref.11
Modified residue271N6-succinyllysine; alternate By similarity
Modified residue341N6-succinyllysine By similarity
Modified residue381Phosphotyrosine Ref.9

Experimental info

Sequence conflict821P → S in AAC15854. Ref.8

Sequences

Sequence LengthMass (Da)Tools
P62277 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 23F94D38F87B8D53

FASTA15117,222
        10         20         30         40         50         60 
MGRMHAPGKG LSQSALPYRR SVPTWLKLTS DDVKEQIYKL AKKGLTPSQI GVILRDSHGV 

        70         80         90        100        110        120 
AQVRFVTGNK ILRILKSKGL APDLPEDLYH LIKKAVAVRK HLERNRKDKD AKFRLILIES 

       130        140        150 
RIHRLARYYK TKRVLPPNWK YESSTASALV A 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and analysis of the human S13 ribosomal protein cDNA."
Chadeneau C., Lemoullac B., Denis M.G.
Nucleic Acids Res. 21:2945-2945(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Filipenko M.L.
Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[3]"U14 snoRNAs are encoded in introns of human ribosomal protein S13 gene."
Kenmochi N., Higa S., Yoshihama M., Tanaka T.
Biochem. Biophys. Res. Commun. 228:371-374(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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].
Tissue: Uterus.
[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: Bone, Brain, Muscle, Pancreas and Placenta.
[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 2-8, CLEAVAGE OF INITIATOR METHIONINE.
Tissue: Placenta.
[8]Bhat K.S.
Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-127.
[9]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-38, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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].
[13]"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
L01124 mRNA. Translation: AAA60283.1.
X79239 mRNA. Translation: CAA55821.1.
D88010 Genomic DNA. Translation: BAA13528.1.
AK312060 mRNA. Translation: BAG34996.1.
CH471064 Genomic DNA. Translation: EAW68448.1.
BC000475 mRNA. Translation: AAH00475.1.
BC006772 mRNA. Translation: AAH06772.1.
BC029732 mRNA. Translation: AAH29732.1.
BC066322 mRNA. Translation: AAH66322.1.
BC100032 mRNA. Translation: AAI00033.1.
L05090 mRNA. Translation: AAC15854.1.
CCDSCCDS7823.1.
PIRS34109.
RefSeqNP_001008.1. NM_001017.2.
UniGeneHs.446588.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00N1-151[»]
ProteinModelPortalP62277.
SMRP62277. Positions 2-151.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112121. 158 interactions.
IntActP62277. 25 interactions.
MINTMINT-4999984.
STRING9606.ENSP00000228140.

PTM databases

PhosphoSiteP62277.

Polymorphism databases

DMDM50403608.

Proteomic databases

MaxQBP62277.
PaxDbP62277.
PeptideAtlasP62277.
PRIDEP62277.

Protocols and materials databases

DNASU6207.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000525634; ENSP00000435777; ENSG00000110700.
GeneID6207.
KEGGhsa:6207.
UCSCuc001mmp.3. human.

Organism-specific databases

CTD6207.
GeneCardsGC11M017055.
HGNCHGNC:10386. RPS13.
HPAHPA005985.
MIM180476. gene.
neXtProtNX_P62277.
PharmGKBPA34785.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0184.
HOGENOMHOG000180723.
HOVERGENHBG000938.
InParanoidP62277.
KOK02953.
OMANWKYESA.
PhylomeDBP62277.
TreeFamTF300190.

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

ArrayExpressP62277.
BgeeP62277.
CleanExHS_RPS13.
GenevestigatorP62277.

Family and domain databases

HAMAPMF_01343_A. Ribosomal_S15_A.
InterProIPR012606. Ribosomal_S13/S15_N.
IPR000589. Ribosomal_S15.
IPR023029. Ribosomal_S15P.
IPR009068. S15_NS1_RNA-bd.
[Graphical view]
PfamPF08069. Ribosomal_S13_N. 1 hit.
PF00312. Ribosomal_S15. 1 hit.
[Graphical view]
SUPFAMSSF47060. SSF47060. 1 hit.
PROSITEPS00362. RIBOSOMAL_S15. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPS13. human.
GeneWikiRPS13.
GenomeRNAi6207.
NextBio24107.
PROP62277.
SOURCESearch...

Entry information

Entry nameRS13_HUMAN
AccessionPrimary (citable) accession number: P62277
Secondary accession number(s): B2R549 expand/collapse secondary AC list , P19116, Q02546, Q29200, Q498Y0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 113 of the entry and version 2 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 11

Human chromosome 11: entries, gene names and cross-references to MIM