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Protein

40S ribosomal protein S11

Gene

RPS11

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

ReactomeiR-BTA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-BTA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-BTA-6791226. Major pathway of rRNA processing in the nucleolus.
R-BTA-72649. Translation initiation complex formation.
R-BTA-72689. Formation of a pool of free 40S subunits.
R-BTA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-BTA-72702. Ribosomal scanning and start codon recognition.
R-BTA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-BTA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-BTA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S11
Gene namesi
Name:RPS11
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 18

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 15815740S ribosomal protein S11PRO_0000240296Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei22 – 221CitrullineBy similarity
Modified residuei38 – 381N6-acetyllysineBy similarity
Modified residuei45 – 451N6-acetyllysineBy similarity
Modified residuei58 – 581N6-acetyllysineBy similarity
Lipidationi60 – 601S-palmitoyl cysteineBy similarity
Modified residuei67 – 671PhosphoserineBy similarity
Modified residuei110 – 1101PhosphoserineBy similarity

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiQ3T0V4.
PeptideAtlasiQ3T0V4.
PRIDEiQ3T0V4.

Expressioni

Gene expression databases

BgeeiENSBTAG00000013924.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000018491.

Structurei

3D structure databases

ProteinModelPortaliQ3T0V4.
SMRiQ3T0V4. Positions 2-152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S17P family.Curated

Phylogenomic databases

eggNOGiKOG1728. Eukaryota.
COG0186. LUCA.
GeneTreeiENSGT00390000002732.
HOGENOMiHOG000231341.
HOVERGENiHBG004670.
InParanoidiQ3T0V4.
KOiK02949.
OMAiVIIRREY.
OrthoDBiEOG091G0QVV.
TreeFamiTF300126.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_01345_B. Ribosomal_S17_B. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR032440. Ribosomal_S11_N.
IPR000266. Ribosomal_S17/S11.
IPR028333. Ribosomal_S17_arc-typ.
IPR019979. Ribosomal_S17_CS.
[Graphical view]
PANTHERiPTHR10744. PTHR10744. 1 hit.
PfamiPF00366. Ribosomal_S17. 1 hit.
PF16205. Ribosomal_S17_N. 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.

Q3T0V4-1 [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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti80 – 801M → V in AAW82130 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY911366 mRNA. Translation: AAW82130.1.
BC102249 mRNA. Translation: AAI02250.1.
RefSeqiNP_001019739.1. NM_001024568.2.
UniGeneiBt.3626.

Genome annotation databases

EnsembliENSBTAT00000018491; ENSBTAP00000018491; ENSBTAG00000013924.
GeneIDi539196.
KEGGibta:539196.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY911366 mRNA. Translation: AAW82130.1.
BC102249 mRNA. Translation: AAI02250.1.
RefSeqiNP_001019739.1. NM_001024568.2.
UniGeneiBt.3626.

3D structure databases

ProteinModelPortaliQ3T0V4.
SMRiQ3T0V4. Positions 2-152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000018491.

Proteomic databases

PaxDbiQ3T0V4.
PeptideAtlasiQ3T0V4.
PRIDEiQ3T0V4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000018491; ENSBTAP00000018491; ENSBTAG00000013924.
GeneIDi539196.
KEGGibta:539196.

Organism-specific databases

CTDi6205.

Phylogenomic databases

eggNOGiKOG1728. Eukaryota.
COG0186. LUCA.
GeneTreeiENSGT00390000002732.
HOGENOMiHOG000231341.
HOVERGENiHBG004670.
InParanoidiQ3T0V4.
KOiK02949.
OMAiVIIRREY.
OrthoDBiEOG091G0QVV.
TreeFamiTF300126.

Enzyme and pathway databases

ReactomeiR-BTA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-BTA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-BTA-6791226. Major pathway of rRNA processing in the nucleolus.
R-BTA-72649. Translation initiation complex formation.
R-BTA-72689. Formation of a pool of free 40S subunits.
R-BTA-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-BTA-72702. Ribosomal scanning and start codon recognition.
R-BTA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-BTA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-BTA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Gene expression databases

BgeeiENSBTAG00000013924.

Family and domain databases

Gene3Di2.40.50.140. 1 hit.
HAMAPiMF_01345_B. Ribosomal_S17_B. 1 hit.
InterProiIPR012340. NA-bd_OB-fold.
IPR032440. Ribosomal_S11_N.
IPR000266. Ribosomal_S17/S11.
IPR028333. Ribosomal_S17_arc-typ.
IPR019979. Ribosomal_S17_CS.
[Graphical view]
PANTHERiPTHR10744. PTHR10744. 1 hit.
PfamiPF00366. Ribosomal_S17. 1 hit.
PF16205. Ribosomal_S17_N. 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...

Entry informationi

Entry nameiRS11_BOVIN
AccessioniPrimary (citable) accession number: Q3T0V4
Secondary accession number(s): Q56JW5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 91 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Ribosomal proteins
    Ribosomal proteins families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.