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P62280

- RS11_HUMAN

UniProt

P62280 - RS11_HUMAN

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Protein

40S ribosomal protein S11

Gene

RPS11

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

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. rRNA binding Source: UniProtKB-KW
  3. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. mRNA metabolic process Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  5. RNA metabolic process Source: Reactome
  6. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  7. translation Source: UniProtKB
  8. translational elongation Source: Reactome
  9. translational initiation Source: Reactome
  10. translational termination Source: Reactome
  11. viral life cycle Source: Reactome
  12. viral process Source: Reactome
  13. viral transcription Source: Reactome
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: Chromosome 19

Organism-specific databases

HGNCiHGNC:10384. RPS11.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. cytosolic small ribosomal subunit Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. focal adhesion Source: UniProtKB
  5. membrane Source: UniProtKB
  6. 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.

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. 122 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
3J3Aelectron microscopy5.00L1-158[»]
ProteinModelPortaliP62280.
SMRiP62280. Positions 2-153.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S17P family.Curated

Phylogenomic databases

eggNOGiCOG0186.
GeneTreeiENSGT00390000002732.
HOGENOMiHOG000231341.
HOVERGENiHBG004670.
InParanoidiP62280.
KOiK02949.
OMAiGAKKQFQ.
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. arch_S17P. 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.

Polymorphism databases

DMDMi50403609.

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 .
CCDSi CCDS12769.1.
PIRi S02133. R3HU11.
RefSeqi NP_001006.1. NM_001015.4.
UniGenei Hs.433529.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3J3A electron microscopy 5.00 L 1-158 [» ]
ProteinModelPortali P62280.
SMRi P62280. Positions 2-153.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112119. 122 interactions.
IntActi P62280. 34 interactions.
MINTi MINT-1154341.
STRINGi 9606.ENSP00000270625.

PTM databases

PhosphoSitei P62280.

Polymorphism databases

DMDMi 50403609.

2D gel databases

SWISS-2DPAGE P62280.

Proteomic databases

MaxQBi P62280.
PaxDbi P62280.
PeptideAtlasi P62280.
PRIDEi P62280.

Protocols and materials databases

DNASUi 6205.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000270625 ; ENSP00000270625 ; ENSG00000142534 .
GeneIDi 6205.
KEGGi hsa:6205.
UCSCi uc002pob.2. human.

Organism-specific databases

CTDi 6205.
GeneCardsi GC19P049999.
H-InvDB HIX0037158.
HGNCi HGNC:10384. RPS11.
HPAi HPA049719.
MIMi 180471. gene.
neXtProti NX_P62280.
PharmGKBi PA34782.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0186.
GeneTreei ENSGT00390000002732.
HOGENOMi HOG000231341.
HOVERGENi HBG004670.
InParanoidi P62280.
KOi K02949.
OMAi GAKKQFQ.
OrthoDBi EOG78H3VQ.
PhylomeDBi P62280.
TreeFami TF300126.

Enzyme and pathway databases

Reactomei REACT_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

ChiTaRSi RPS11. human.
GeneWikii RPS11.
GenomeRNAii 6205.
NextBioi 24099.
PMAP-CutDB P62280.
PROi P62280.
SOURCEi Search...

Gene expression databases

Bgeei P62280.
CleanExi HS_RPS11.
ExpressionAtlasi P62280. baseline and differential.
Genevestigatori P62280.

Family and domain databases

Gene3Di 2.40.50.140. 1 hit.
HAMAPi MF_01345_B. Ribosomal_S17_B.
InterProi IPR012340. NA-bd_OB-fold.
IPR000266. Ribosomal_S17.
IPR028333. Ribosomal_S17_arc-typ.
IPR019979. Ribosomal_S17_CS.
[Graphical view ]
PANTHERi PTHR10744. PTHR10744. 1 hit.
Pfami PF00366. Ribosomal_S17. 1 hit.
[Graphical view ]
PRINTSi PR00973. RIBOSOMALS17.
ProDomi PD001295. Ribosomal_S17. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SUPFAMi SSF50249. SSF50249. 1 hit.
TIGRFAMsi TIGR03630. arch_S17P. 1 hit.
PROSITEi PS00056. RIBOSOMAL_S17. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].
  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].
  14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. 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: November 26, 2014
This is version 121 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