Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

40S ribosomal protein S11

Gene

RPS11

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

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • rRNA binding Source: UniProtKB-KW
  • structural constituent of ribosome Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

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 S11
Gene namesi
Name:RPS11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:10384. RPS11.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • cytosolic small ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleolus Source: UniProtKB
  • ribosome Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi60 – 601C → S: Abolishes S-acylation. 1 Publication

Organism-specific databases

PharmGKBiPA34782.

Polymorphism and mutation databases

BioMutaiRPS11.
DMDMi50403609.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 15815740S ribosomal protein S11PRO_0000128509Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei22 – 221CitrullineBy similarity
Modified residuei38 – 381N6-acetyllysine1 Publication
Modified residuei45 – 451N6-acetyllysine1 Publication
Modified residuei58 – 581N6-acetyllysineBy similarity
Lipidationi60 – 601S-palmitoyl cysteine1 Publication

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Lipoprotein, Palmitate

Proteomic databases

MaxQBiP62280.
PaxDbiP62280.
PeptideAtlasiP62280.
PRIDEiP62280.

2D gel databases

SWISS-2DPAGEP62280.

PTM databases

PhosphoSiteiP62280.

Miscellaneous databases

PMAP-CutDBP62280.

Expressioni

Gene expression databases

BgeeiP62280.
CleanExiHS_RPS11.
ExpressionAtlasiP62280. baseline and differential.
GenevestigatoriP62280.

Organism-specific databases

HPAiHPA049719.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
LRRK2Q5S0073EBI-1047710,EBI-5323863

Protein-protein interaction databases

BioGridi112119. 123 interactions.
IntActiP62280. 34 interactions.
MINTiMINT-1154341.
STRINGi9606.ENSP00000270625.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AL1-158[»]
ProteinModelPortaliP62280.
SMRiP62280. Positions 1-158.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S17P family.Curated

Phylogenomic databases

eggNOGiCOG0186.
GeneTreeiENSGT00390000002732.
HOGENOMiHOG000231341.
HOVERGENiHBG004670.
InParanoidiP62280.
KOiK02949.
OMAiKCPFTSD.
OrthoDBiEOG78H3VQ.
PhylomeDBiP62280.
TreeFamiTF300126.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_01345_B. Ribosomal_S17_B.
InterProiIPR012340. NA-bd_OB-fold.
IPR000266. Ribosomal_S17.
IPR028333. Ribosomal_S17_arc-typ.
IPR019979. Ribosomal_S17_CS.
[Graphical view]
PANTHERiPTHR10744. PTHR10744. 1 hit.
PfamiPF00366. Ribosomal_S17. 1 hit.
[Graphical view]
PRINTSiPR00973. RIBOSOMALS17.
ProDomiPD001295. Ribosomal_S17. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR03630. uS17_arch. 1 hit.
PROSITEiPS00056. RIBOSOMAL_S17. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62280-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADIQTERAY QKQPTIFQNK KRVLLGETGK EKLPRYYKNI GLGFKTPKEA
60 70 80 90 100
IEGTYIDKKC PFTGNVSIRG RILSGVVTKM KMQRTIVIRR DYLHYIRKYN
110 120 130 140 150
RFEKRHKNMS VHLSPCFRDV QIGDIVTVGE CRPLSKTVRF NVLKVTKAAG

TKKQFQKF
Length:158
Mass (Da):18,431
Last modified:January 23, 2007 - v3
Checksum:i9FB75DC1D99614B0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06617 mRNA. Translation: CAA29834.1.
AB028893 Genomic DNA. Translation: BAA88215.1.
AK311809 mRNA. Translation: BAG34752.1.
CH471177 Genomic DNA. Translation: EAW52497.1.
BC007283 mRNA. Translation: AAH07283.1.
BC007603 mRNA. Translation: AAH07603.1.
BC007945 mRNA. Translation: AAH07945.1.
BC010028 mRNA. Translation: AAH10028.1.
BC016378 mRNA. Translation: AAH16378.1.
BC070224 mRNA. Translation: AAH70224.1.
BC100025 mRNA. Translation: AAI00026.1.
AB007152 Genomic DNA. Translation: BAA25818.1.
CCDSiCCDS12769.1.
PIRiS02133. R3HU11.
RefSeqiNP_001006.1. NM_001015.4.
UniGeneiHs.433529.

Genome annotation databases

EnsembliENST00000270625; ENSP00000270625; ENSG00000142534.
GeneIDi6205.
KEGGihsa:6205.
UCSCiuc002pob.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06617 mRNA. Translation: CAA29834.1.
AB028893 Genomic DNA. Translation: BAA88215.1.
AK311809 mRNA. Translation: BAG34752.1.
CH471177 Genomic DNA. Translation: EAW52497.1.
BC007283 mRNA. Translation: AAH07283.1.
BC007603 mRNA. Translation: AAH07603.1.
BC007945 mRNA. Translation: AAH07945.1.
BC010028 mRNA. Translation: AAH10028.1.
BC016378 mRNA. Translation: AAH16378.1.
BC070224 mRNA. Translation: AAH70224.1.
BC100025 mRNA. Translation: AAI00026.1.
AB007152 Genomic DNA. Translation: BAA25818.1.
CCDSiCCDS12769.1.
PIRiS02133. R3HU11.
RefSeqiNP_001006.1. NM_001015.4.
UniGeneiHs.433529.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AL1-158[»]
ProteinModelPortaliP62280.
SMRiP62280. Positions 1-158.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112119. 123 interactions.
IntActiP62280. 34 interactions.
MINTiMINT-1154341.
STRINGi9606.ENSP00000270625.

PTM databases

PhosphoSiteiP62280.

Polymorphism and mutation databases

BioMutaiRPS11.
DMDMi50403609.

2D gel databases

SWISS-2DPAGEP62280.

Proteomic databases

MaxQBiP62280.
PaxDbiP62280.
PeptideAtlasiP62280.
PRIDEiP62280.

Protocols and materials databases

DNASUi6205.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000270625; ENSP00000270625; ENSG00000142534.
GeneIDi6205.
KEGGihsa:6205.
UCSCiuc002pob.2. human.

Organism-specific databases

CTDi6205.
GeneCardsiGC19P049999.
H-InvDBHIX0037158.
HGNCiHGNC:10384. RPS11.
HPAiHPA049719.
MIMi180471. gene.
neXtProtiNX_P62280.
PharmGKBiPA34782.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0186.
GeneTreeiENSGT00390000002732.
HOGENOMiHOG000231341.
HOVERGENiHBG004670.
InParanoidiP62280.
KOiK02949.
OMAiKCPFTSD.
OrthoDBiEOG78H3VQ.
PhylomeDBiP62280.
TreeFamiTF300126.

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

ChiTaRSiRPS11. human.
GeneWikiiRPS11.
GenomeRNAii6205.
NextBioi24099.
PMAP-CutDBP62280.
PROiP62280.
SOURCEiSearch...

Gene expression databases

BgeeiP62280.
CleanExiHS_RPS11.
ExpressionAtlasiP62280. baseline and differential.
GenevestigatoriP62280.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_01345_B. Ribosomal_S17_B.
InterProiIPR012340. NA-bd_OB-fold.
IPR000266. Ribosomal_S17.
IPR028333. Ribosomal_S17_arc-typ.
IPR019979. Ribosomal_S17_CS.
[Graphical view]
PANTHERiPTHR10744. PTHR10744. 1 hit.
PfamiPF00366. Ribosomal_S17. 1 hit.
[Graphical view]
PRINTSiPR00973. RIBOSOMALS17.
ProDomiPD001295. Ribosomal_S17. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF50249. SSF50249. 1 hit.
TIGRFAMsiTIGR03630. uS17_arch. 1 hit.
PROSITEiPS00056. RIBOSOMAL_S17. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of a cloned cDNA encoding human ribosomal protein S11."
    Lott J.B., Mackie G.A.
    Nucleic Acids Res. 16:1205-1205(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Gene organization and sequence of the region containing the ribosomal protein genes RPL13A and RPS11 in the human genome and conserved features in the mouse genome."
    Higa S., Yoshihama M., Tanaka T., Kenmochi N.
    Gene 240:371-377(1999) [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: Thymus.
  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: B-cell, Eye, Lung and Prostate.
  6. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
    Submitted (MAY-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-11, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: T-cell.
  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 39-45 AND 137-143.
    Tissue: Placenta.
  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 76-158.
  9. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  10. "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-38 AND LYS-45, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Site-specific analysis of protein S-acylation by resin-assisted capture."
    Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A., Stamler J.S., Casey P.J.
    J. Lipid Res. 52:393-398(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-60, PALMITOYLATION AT CYS-60.
  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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  15. "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.
  16. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRS11_HUMAN
AccessioniPrimary (citable) accession number: P62280
Secondary accession number(s): B2R4F5
, P04643, Q498Y6, Q6IRY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 23, 2007
Last modified: May 27, 2015
This is version 127 of the entry and version 3 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.