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Protein

40S ribosomal protein S13

Gene

RPS13

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 binding Source: UniProtKB
  2. poly(A) RNA binding Source: UniProtKB
  3. small ribosomal subunit rRNA binding Source: GO_Central
  4. structural constituent of ribosome Source: GO_Central

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. negative regulation of RNA splicing Source: UniProtKB
  4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  5. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  6. translation Source: UniProtKB
  7. translational elongation Source: Reactome
  8. translational initiation Source: Reactome
  9. translational termination Source: Reactome
  10. viral life cycle Source: Reactome
  11. viral process Source: Reactome
  12. 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 S13
Gene namesi
Name:RPS13
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:10386. RPS13.

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. nucleolus Source: UniProtKB
  7. nucleus Source: UniProtKB
  8. ribosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34785.

Polymorphism and mutation databases

BioMutaiRPS13.
DMDMi50403608.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 15115040S ribosomal protein S13PRO_0000115661Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271N6-acetyllysine; alternate1 Publication
Modified residuei27 – 271N6-succinyllysine; alternateBy similarity
Modified residuei34 – 341N6-succinyllysineBy similarity
Modified residuei38 – 381Phosphotyrosine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP62277.
PaxDbiP62277.
PeptideAtlasiP62277.
PRIDEiP62277.

PTM databases

PhosphoSiteiP62277.

Expressioni

Gene expression databases

BgeeiP62277.
CleanExiHS_RPS13.
ExpressionAtlasiP62277. baseline.
GenevestigatoriP62277.

Organism-specific databases

HPAiHPA005985.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
PDCD4Q53EL62EBI-351850,EBI-935824

Protein-protein interaction databases

BioGridi112121. 150 interactions.
IntActiP62277. 27 interactions.
MINTiMINT-4999984.
STRINGi9606.ENSP00000228140.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AN1-151[»]
ProteinModelPortaliP62277.
SMRiP62277. Positions 2-151.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S15P family.Curated

Phylogenomic databases

eggNOGiCOG0184.
GeneTreeiENSGT00390000017491.
HOGENOMiHOG000180723.
HOVERGENiHBG000938.
InParanoidiP62277.
KOiK02953.
OMAiWHLVKKA.
PhylomeDBiP62277.
TreeFamiTF300190.

Family and domain databases

HAMAPiMF_01343_A. Ribosomal_S15_A.
InterProiIPR012606. Ribosomal_S13/S15_N.
IPR000589. Ribosomal_S15.
IPR023029. Ribosomal_S15P.
IPR009068. S15_NS1_RNA-bd.
[Graphical view]
PfamiPF08069. Ribosomal_S13_N. 1 hit.
PF00312. Ribosomal_S15. 1 hit.
[Graphical view]
SUPFAMiSSF47060. SSF47060. 1 hit.
PROSITEiPS00362. RIBOSOMAL_S15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62277-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRMHAPGKG LSQSALPYRR SVPTWLKLTS DDVKEQIYKL AKKGLTPSQI
60 70 80 90 100
GVILRDSHGV AQVRFVTGNK ILRILKSKGL APDLPEDLYH LIKKAVAVRK
110 120 130 140 150
HLERNRKDKD AKFRLILIES RIHRLARYYK TKRVLPPNWK YESSTASALV

A
Length:151
Mass (Da):17,222
Last modified:January 23, 2007 - v2
Checksum:i23F94D38F87B8D53
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821P → S in AAC15854 (Ref. 8) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7823.1.
PIRiS34109.
RefSeqiNP_001008.1. NM_001017.2.
UniGeneiHs.446588.

Genome annotation databases

EnsembliENST00000525634; ENSP00000435777; ENSG00000110700.
GeneIDi6207.
KEGGihsa:6207.
UCSCiuc001mmp.3. human.

Polymorphism and mutation databases

BioMutaiRPS13.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7823.1.
PIRiS34109.
RefSeqiNP_001008.1. NM_001017.2.
UniGeneiHs.446588.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AN1-151[»]
ProteinModelPortaliP62277.
SMRiP62277. Positions 2-151.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112121. 150 interactions.
IntActiP62277. 27 interactions.
MINTiMINT-4999984.
STRINGi9606.ENSP00000228140.

PTM databases

PhosphoSiteiP62277.

Polymorphism and mutation databases

BioMutaiRPS13.
DMDMi50403608.

Proteomic databases

MaxQBiP62277.
PaxDbiP62277.
PeptideAtlasiP62277.
PRIDEiP62277.

Protocols and materials databases

DNASUi6207.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000525634; ENSP00000435777; ENSG00000110700.
GeneIDi6207.
KEGGihsa:6207.
UCSCiuc001mmp.3. human.

Organism-specific databases

CTDi6207.
GeneCardsiGC11M017095.
HGNCiHGNC:10386. RPS13.
HPAiHPA005985.
MIMi180476. gene.
neXtProtiNX_P62277.
PharmGKBiPA34785.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0184.
GeneTreeiENSGT00390000017491.
HOGENOMiHOG000180723.
HOVERGENiHBG000938.
InParanoidiP62277.
KOiK02953.
OMAiWHLVKKA.
PhylomeDBiP62277.
TreeFamiTF300190.

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

ChiTaRSiRPS13. human.
GeneWikiiRPS13.
GenomeRNAii6207.
NextBioi24107.
PROiP62277.
SOURCEiSearch...

Gene expression databases

BgeeiP62277.
CleanExiHS_RPS13.
ExpressionAtlasiP62277. baseline.
GenevestigatoriP62277.

Family and domain databases

HAMAPiMF_01343_A. Ribosomal_S15_A.
InterProiIPR012606. Ribosomal_S13/S15_N.
IPR000589. Ribosomal_S15.
IPR023029. Ribosomal_S15P.
IPR009068. S15_NS1_RNA-bd.
[Graphical view]
PfamiPF08069. Ribosomal_S13_N. 1 hit.
PF00312. Ribosomal_S15. 1 hit.
[Graphical view]
SUPFAMiSSF47060. SSF47060. 1 hit.
PROSITEiPS00362. RIBOSOMAL_S15. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRS13_HUMAN
AccessioniPrimary (citable) accession number: P62277
Secondary accession number(s): B2R549
, P19116, Q02546, Q29200, Q498Y0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: April 29, 2015
This is version 121 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 11
    Human chromosome 11: 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.