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Protein

40S ribosomal protein S20

Gene

RPS20

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

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. cytoplasmic translation Source: GO_Central
  3. gene expression Source: Reactome
  4. mRNA metabolic process Source: Reactome
  5. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  6. RNA metabolic process Source: Reactome
  7. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  8. translation Source: UniProtKB
  9. translational elongation Source: Reactome
  10. translational initiation Source: Reactome
  11. translational termination Source: Reactome
  12. viral life cycle Source: Reactome
  13. viral process Source: Reactome
  14. 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 S20
Gene namesi
Name:RPS20
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:10405. RPS20.

Subcellular locationi

Cytoplasm By similarity

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. membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34807.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 11911840S ribosomal protein S20PRO_0000146683Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei8 – 81N6-succinyllysine; alternateBy similarity
Cross-linki8 – 8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residuei9 – 91Phosphothreonine1 Publication
Modified residuei34 – 341N6-acetyllysineBy similarity
Modified residuei75 – 751N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP60866.
PaxDbiP60866.
PRIDEiP60866.

PTM databases

PhosphoSiteiP60866.

Expressioni

Gene expression databases

BgeeiP60866.
CleanExiHS_RPS20.
ExpressionAtlasiP60866. baseline and differential.
GenevestigatoriP60866.

Organism-specific databases

HPAiHPA003570.

Interactioni

Subunit structurei

Component of the 40S small ribosomal subunit.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0072EBI-353105,EBI-5323863
NEDD8Q158432EBI-353105,EBI-716247

Protein-protein interaction databases

BioGridi112138. 129 interactions.
IntActiP60866. 25 interactions.
MINTiMINT-5000180.
STRINGi9606.ENSP00000009589.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00U1-119[»]
ProteinModelPortaliP60866.
SMRiP60866. Positions 16-119.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S10P family.Curated

Phylogenomic databases

eggNOGiCOG0051.
GeneTreeiENSGT00390000003248.
HOGENOMiHOG000270245.
HOVERGENiHBG004448.
InParanoidiP60866.
KOiK02969.
OMAiYELKIHK.
OrthoDBiEOG7KH9MQ.
PhylomeDBiP60866.
TreeFamiTF300222.

Family and domain databases

Gene3Di3.30.70.600. 1 hit.
HAMAPiMF_00508. Ribosomal_S10.
InterProiIPR001848. Ribosomal_S10.
IPR018268. Ribosomal_S10_CS.
IPR027486. Ribosomal_S10_dom.
IPR005729. Ribosomal_S10_euk/arc.
[Graphical view]
PANTHERiPTHR11700. PTHR11700. 1 hit.
PfamiPF00338. Ribosomal_S10. 1 hit.
[Graphical view]
PRINTSiPR00971. RIBOSOMALS10.
SUPFAMiSSF54999. SSF54999. 1 hit.
TIGRFAMsiTIGR01046. S10_Arc_S20_Euk. 1 hit.
PROSITEiPS00361. RIBOSOMAL_S10. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P60866-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAFKDTGKTP VEPEVAIHRI RITLTSRNVK SLEKVCADLI RGAKEKNLKV
60 70 80 90 100
KGPVRMPTKT LRITTRKTPC GEGSKTWDRF QMRIHKRLID LHSPSEIVKQ
110
ITSISIEPGV EVEVTIADA
Length:119
Mass (Da):13,373
Last modified:April 13, 2004 - v1
Checksum:i8802DF7894ADDF94
GO
Isoform 2 (identifier: P60866-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     112-119: VEVTIADA → LIESTDAEPMDTEGQQYTLRSVFESPGTCPF

Note: No experimental confirmation available.

Show »
Length:142
Mass (Da):16,006
Checksum:i9EB2D51538E812A9
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei112 – 1198VEVTIADA → LIESTDAEPMDTEGQQYTLR SVFESPGTCPF in isoform 2. 1 PublicationVSP_042724

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06498 mRNA. Translation: AAA60286.1.
AB061842 Genomic DNA. Translation: BAB79480.1.
AK301342 mRNA. Translation: BAG62890.1.
AK311808 mRNA. Translation: BAG34751.1.
AC107376 Genomic DNA. No translation available.
CH471068 Genomic DNA. Translation: EAW86771.1.
CH471068 Genomic DNA. Translation: EAW86772.1.
BC007507 mRNA. Translation: AAH07507.1.
BC087850 mRNA. Translation: AAH87850.1.
AB007156 Genomic DNA. Translation: BAA25820.1.
CCDSiCCDS55231.1. [P60866-2]
CCDS6163.1. [P60866-1]
PIRiS33710.
RefSeqiNP_001014.1. NM_001023.3. [P60866-1]
NP_001139699.1. NM_001146227.1. [P60866-2]
UniGeneiHs.8102.

Genome annotation databases

EnsembliENST00000009589; ENSP00000009589; ENSG00000008988. [P60866-1]
ENST00000519807; ENSP00000429374; ENSG00000008988. [P60866-2]
ENST00000521262; ENSP00000427788; ENSG00000008988. [P60866-1]
ENST00000618656; ENSP00000478703; ENSG00000008988. [P60866-2]
GeneIDi6224.
KEGGihsa:6224.
UCSCiuc003xsm.2. human. [P60866-2]
uc003xsn.2. human. [P60866-1]

Polymorphism databases

DMDMi46397703.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L06498 mRNA. Translation: AAA60286.1.
AB061842 Genomic DNA. Translation: BAB79480.1.
AK301342 mRNA. Translation: BAG62890.1.
AK311808 mRNA. Translation: BAG34751.1.
AC107376 Genomic DNA. No translation available.
CH471068 Genomic DNA. Translation: EAW86771.1.
CH471068 Genomic DNA. Translation: EAW86772.1.
BC007507 mRNA. Translation: AAH07507.1.
BC087850 mRNA. Translation: AAH87850.1.
AB007156 Genomic DNA. Translation: BAA25820.1.
CCDSiCCDS55231.1. [P60866-2]
CCDS6163.1. [P60866-1]
PIRiS33710.
RefSeqiNP_001014.1. NM_001023.3. [P60866-1]
NP_001139699.1. NM_001146227.1. [P60866-2]
UniGeneiHs.8102.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00U1-119[»]
ProteinModelPortaliP60866.
SMRiP60866. Positions 16-119.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112138. 129 interactions.
IntActiP60866. 25 interactions.
MINTiMINT-5000180.
STRINGi9606.ENSP00000009589.

PTM databases

PhosphoSiteiP60866.

Polymorphism databases

DMDMi46397703.

Proteomic databases

MaxQBiP60866.
PaxDbiP60866.
PRIDEiP60866.

Protocols and materials databases

DNASUi6224.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000009589; ENSP00000009589; ENSG00000008988. [P60866-1]
ENST00000519807; ENSP00000429374; ENSG00000008988. [P60866-2]
ENST00000521262; ENSP00000427788; ENSG00000008988. [P60866-1]
ENST00000618656; ENSP00000478703; ENSG00000008988. [P60866-2]
GeneIDi6224.
KEGGihsa:6224.
UCSCiuc003xsm.2. human. [P60866-2]
uc003xsn.2. human. [P60866-1]

Organism-specific databases

CTDi6224.
GeneCardsiGC08M056982.
HGNCiHGNC:10405. RPS20.
HPAiHPA003570.
MIMi603682. gene.
neXtProtiNX_P60866.
PharmGKBiPA34807.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0051.
GeneTreeiENSGT00390000003248.
HOGENOMiHOG000270245.
HOVERGENiHBG004448.
InParanoidiP60866.
KOiK02969.
OMAiYELKIHK.
OrthoDBiEOG7KH9MQ.
PhylomeDBiP60866.
TreeFamiTF300222.

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

ChiTaRSiRPS20. human.
GeneWikiiRPS20.
GenomeRNAii6224.
NextBioi24163.
PROiP60866.
SOURCEiSearch...

Gene expression databases

BgeeiP60866.
CleanExiHS_RPS20.
ExpressionAtlasiP60866. baseline and differential.
GenevestigatoriP60866.

Family and domain databases

Gene3Di3.30.70.600. 1 hit.
HAMAPiMF_00508. Ribosomal_S10.
InterProiIPR001848. Ribosomal_S10.
IPR018268. Ribosomal_S10_CS.
IPR027486. Ribosomal_S10_dom.
IPR005729. Ribosomal_S10_euk/arc.
[Graphical view]
PANTHERiPTHR11700. PTHR11700. 1 hit.
PfamiPF00338. Ribosomal_S10. 1 hit.
[Graphical view]
PRINTSiPR00971. RIBOSOMALS10.
SUPFAMiSSF54999. SSF54999. 1 hit.
TIGRFAMsiTIGR01046. S10_Arc_S20_Euk. 1 hit.
PROSITEiPS00361. RIBOSOMAL_S10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  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] (ISOFORMS 1 AND 2).
    Tissue: Synovium and Thymus.
  4. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1).
    Tissue: Ovary and Testis.
  7. Bienvenut W.V., Murray L., Brunton V.G., Frame M.C.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-19; 35-41 AND 88-99, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon adenocarcinoma.
  8. "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 9-24.
    Tissue: Placenta.
  9. "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 51-110.
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRS20_HUMAN
AccessioniPrimary (citable) accession number: P60866
Secondary accession number(s): B2R4F4
, B4DW28, P17075, Q5M8S9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: February 4, 2015
This is version 110 of the entry and version 1 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 8
    Human chromosome 8: 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.