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Protein

40S ribosomal protein S5

Gene

RPS5

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

Functioni

GO - Molecular functioni

  • mRNA binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  • cellular protein metabolic process Source: Reactome
  • gene expression Source: Reactome
  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  • regulation of translational fidelity Source: UniProtKB
  • SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  • translation Source: UniProtKB
  • translational elongation Source: Reactome
  • translational initiation Source: UniProtKB
  • translational termination Source: Reactome
  • viral life cycle Source: Reactome
  • viral process Source: Reactome
  • 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 S5
Cleaved into the following chain:
Gene namesi
Name:RPS5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:10426. RPS5.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • cytosolic small ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • ribonucleoprotein complex Source: MGI
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34841.

Polymorphism and mutation databases

BioMutaiRPS5.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20420440S ribosomal protein S5PRO_0000370369Add
BLAST
Initiator methioninei1 – 11Removed; alternate4 Publications
Chaini2 – 20420340S ribosomal protein S5, N-terminally processedPRO_0000124526Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine; in 40S ribosomal protein S5; alternate3 Publications
Modified residuei2 – 21N-acetylthreonine; in 40S ribosomal protein S5, N-terminally processed4 Publications
Modified residuei14 – 141Phosphothreonine1 Publication
Modified residuei47 – 471N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP46782.
PaxDbiP46782.
PeptideAtlasiP46782.
PRIDEiP46782.

2D gel databases

SWISS-2DPAGEP46782.

PTM databases

PhosphoSiteiP46782.

Expressioni

Gene expression databases

BgeeiP46782.
CleanExiHS_RPS5.
ExpressionAtlasiP46782. baseline and differential.
GenevisibleiP46782. HS.

Organism-specific databases

HPAiHPA055878.

Interactioni

Protein-protein interaction databases

BioGridi112107. 129 interactions.
IntActiP46782. 17 interactions.
MINTiMINT-1142463.
STRINGi9606.ENSP00000196551.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AF1-204[»]
ProteinModelPortaliP46782.
SMRiP46782. Positions 14-204.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S7P family.Curated

Phylogenomic databases

eggNOGiCOG0049.
GeneTreeiENSGT00390000010806.
HOGENOMiHOG000039066.
HOVERGENiHBG028547.
InParanoidiP46782.
KOiK02989.
OrthoDBiEOG7PZRZS.
PhylomeDBiP46782.
TreeFamiTF300872.

Family and domain databases

Gene3Di1.10.455.10. 1 hit.
InterProiIPR000235. Ribosomal_S5/S7.
IPR005716. Ribosomal_S5/S7_euk/arc.
IPR020606. Ribosomal_S7_CS.
IPR023798. Ribosomal_S7_dom.
[Graphical view]
PANTHERiPTHR11205. PTHR11205. 1 hit.
PfamiPF00177. Ribosomal_S7. 1 hit.
[Graphical view]
PIRSFiPIRSF002122. RPS7p_RPS7a_RPS5e_RPS7o. 1 hit.
SUPFAMiSSF47973. SSF47973. 1 hit.
TIGRFAMsiTIGR01028. uS7_euk_arch. 1 hit.
PROSITEiPS00052. RIBOSOMAL_S7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P46782-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTEWETAAPA VAETPDIKLF GKWSTDDVQI NDISLQDYIA VKEKYAKYLP
60 70 80 90 100
HSAGRYAAKR FRKAQCPIVE RLTNSMMMHG RNNGKKLMTV RIVKHAFEII
110 120 130 140 150
HLLTGENPLQ VLVNAIINSG PREDSTRIGR AGTVRRQAVD VSPLRRVNQA
160 170 180 190 200
IWLLCTGARE AAFRNIKTIA ECLADELINA AKGSSNSYAI KKKDELERVA

KSNR
Length:204
Mass (Da):22,876
Last modified:January 23, 2007 - v4
Checksum:iDFE2FD5AAFCFD894
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti59 – 602KR → NA in AAA85658 (PubMed:7772601).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14970 mRNA. Translation: AAA85658.1.
AB061853 Genomic DNA. Translation: BAB79493.1.
AK311938 mRNA. Translation: BAG34879.1.
CH471135 Genomic DNA. Translation: EAW72581.1.
BC015405 mRNA. Translation: AAH15405.1.
BC018151 mRNA. Translation: AAH18151.1.
AB007149 Genomic DNA. Translation: BAA25815.1.
CCDSiCCDS12978.1.
PIRiS55916.
RefSeqiNP_001000.2. NM_001009.3.
UniGeneiHs.378103.

Genome annotation databases

EnsembliENST00000196551; ENSP00000196551; ENSG00000083845.
ENST00000596046; ENSP00000472985; ENSG00000083845.
ENST00000601521; ENSP00000470114; ENSG00000083845.
GeneIDi6193.
KEGGihsa:6193.
UCSCiuc002qsn.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U14970 mRNA. Translation: AAA85658.1.
AB061853 Genomic DNA. Translation: BAB79493.1.
AK311938 mRNA. Translation: BAG34879.1.
CH471135 Genomic DNA. Translation: EAW72581.1.
BC015405 mRNA. Translation: AAH15405.1.
BC018151 mRNA. Translation: AAH18151.1.
AB007149 Genomic DNA. Translation: BAA25815.1.
CCDSiCCDS12978.1.
PIRiS55916.
RefSeqiNP_001000.2. NM_001009.3.
UniGeneiHs.378103.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AF1-204[»]
ProteinModelPortaliP46782.
SMRiP46782. Positions 14-204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112107. 129 interactions.
IntActiP46782. 17 interactions.
MINTiMINT-1142463.
STRINGi9606.ENSP00000196551.

PTM databases

PhosphoSiteiP46782.

Polymorphism and mutation databases

BioMutaiRPS5.

2D gel databases

SWISS-2DPAGEP46782.

Proteomic databases

MaxQBiP46782.
PaxDbiP46782.
PeptideAtlasiP46782.
PRIDEiP46782.

Protocols and materials databases

DNASUi6193.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000196551; ENSP00000196551; ENSG00000083845.
ENST00000596046; ENSP00000472985; ENSG00000083845.
ENST00000601521; ENSP00000470114; ENSG00000083845.
GeneIDi6193.
KEGGihsa:6193.
UCSCiuc002qsn.3. human.

Organism-specific databases

CTDi6193.
GeneCardsiGC19P059295.
H-InvDBHIX0020415.
HGNCiHGNC:10426. RPS5.
HPAiHPA055878.
MIMi603630. gene.
neXtProtiNX_P46782.
PharmGKBiPA34841.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0049.
GeneTreeiENSGT00390000010806.
HOGENOMiHOG000039066.
HOVERGENiHBG028547.
InParanoidiP46782.
KOiK02989.
OrthoDBiEOG7PZRZS.
PhylomeDBiP46782.
TreeFamiTF300872.

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

ChiTaRSiRPS5. human.
GeneWikiiRPS5.
GenomeRNAii6193.
NextBioi24049.
PROiP46782.
SOURCEiSearch...

Gene expression databases

BgeeiP46782.
CleanExiHS_RPS5.
ExpressionAtlasiP46782. baseline and differential.
GenevisibleiP46782. HS.

Family and domain databases

Gene3Di1.10.455.10. 1 hit.
InterProiIPR000235. Ribosomal_S5/S7.
IPR005716. Ribosomal_S5/S7_euk/arc.
IPR020606. Ribosomal_S7_CS.
IPR023798. Ribosomal_S7_dom.
[Graphical view]
PANTHERiPTHR11205. PTHR11205. 1 hit.
PfamiPF00177. Ribosomal_S7. 1 hit.
[Graphical view]
PIRSFiPIRSF002122. RPS7p_RPS7a_RPS5e_RPS7o. 1 hit.
SUPFAMiSSF47973. SSF47973. 1 hit.
TIGRFAMsiTIGR01028. uS7_euk_arch. 1 hit.
PROSITEiPS00052. RIBOSOMAL_S7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs."
    Frigerio J.-M., Dagorn J.-C., Iovanna J.L.
    Biochim. Biophys. Acta 1262:64-68(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Colon.
  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: Bone and Ovary.
  6. Bienvenut W.V.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-18; 23-42; 48-55; 137-145 AND 168-182, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  7. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-18; 23-42; 137-159 AND 168-182, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma.
  8. "A map of 75 human ribosomal protein genes."
    Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.
    Genome Res. 8:509-523(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 150-204.
  9. "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 192-197.
    Tissue: Placenta.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  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-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "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 THR-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRS5_HUMAN
AccessioniPrimary (citable) accession number: P46782
Secondary accession number(s): B2R4T2, Q96BN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 151 of the entry and version 4 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.