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Protein

40S ribosomal protein S13

Gene

Rps13

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S13
Gene namesi
Name:Rps13
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi621027. Rps13.

Subcellular locationi

GO - Cellular componenti

  • cytosolic small ribosomal subunit Source: RGD
  • nucleolus Source: GO_Central
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 15115040S ribosomal protein S13PRO_0000115664Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271N6-acetyllysine; alternateBy similarity
Modified residuei27 – 271N6-succinyllysine; alternateBy similarity
Modified residuei30 – 301PhosphoserineBy similarity
Modified residuei34 – 341N6-succinyllysineBy similarity
Modified residuei38 – 381PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP62278.
PRIDEiP62278.

PTM databases

iPTMnetiP62278.
PhosphoSiteiP62278.

Expressioni

Gene expression databases

GenevisibleiP62278. RN.

Interactioni

Protein-protein interaction databases

IntActiP62278. 1 interaction.
MINTiMINT-4577079.
STRINGi10116.ENSRNOP00000036690.

Structurei

3D structure databases

ProteinModelPortaliP62278.
SMRiP62278. Positions 2-150.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S15P family.Curated

Phylogenomic databases

eggNOGiKOG0400. Eukaryota.
COG0184. LUCA.
GeneTreeiENSGT00390000017491.
HOGENOMiHOG000180723.
HOVERGENiHBG000938.
InParanoidiP62278.
KOiK02953.
OMAiWHLVKKA.
OrthoDBiEOG7KH9MB.
PhylomeDBiP62278.
TreeFamiTF300190.

Family and domain databases

HAMAPiMF_01343_A. Ribosomal_S15_A.
InterProiIPR012606. Ribosomal_S13/S15_N.
IPR000589. Ribosomal_S15.
IPR023029. Ribosomal_S15P.
IPR009068. S15_NS1_RNA-bd.
[Graphical view]
PfamiPF08069. Ribosomal_S13_N. 1 hit.
PF00312. Ribosomal_S15. 1 hit.
[Graphical view]
SMARTiSM01386. Ribosomal_S13_N. 1 hit.
SM01387. Ribosomal_S15. 1 hit.
[Graphical view]
SUPFAMiSSF47060. SSF47060. 1 hit.
PROSITEiPS00362. RIBOSOMAL_S15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P62278-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRMHAPGKG LSQSALPYRR SVPTWLKLTS DDVKEQIYKL AKKGLTPSQI
60 70 80 90 100
GVILRDSHGV AQVRFVTGNK ILRILKSKGL APDLPEDLYH LIKKAVAVRK
110 120 130 140 150
HLERNRKDKD AKFRLILIES RIHRLARYYK TKRVLPPNWK YESSTASALV

A
Length:151
Mass (Da):17,222
Last modified:January 23, 2007 - v2
Checksum:i23F94D38F87B8D53
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53378 mRNA. Translation: CAA37458.1.
BC084724 mRNA. Translation: AAH84724.1.
L01123 mRNA. Translation: AAB59695.1.
PIRiA35889. R3RT13.
RefSeqiNP_569116.1. NM_130432.2.
XP_001053043.1. XM_001053043.4.
XP_003753737.1. XM_003753689.2.
UniGeneiRn.103229.
Rn.198625.

Genome annotation databases

EnsembliENSRNOT00000034694; ENSRNOP00000036690; ENSRNOG00000028021.
GeneIDi161477.
684988.
KEGGirno:161477.
rno:684988.
UCSCiRGD:621027. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53378 mRNA. Translation: CAA37458.1.
BC084724 mRNA. Translation: AAH84724.1.
L01123 mRNA. Translation: AAB59695.1.
PIRiA35889. R3RT13.
RefSeqiNP_569116.1. NM_130432.2.
XP_001053043.1. XM_001053043.4.
XP_003753737.1. XM_003753689.2.
UniGeneiRn.103229.
Rn.198625.

3D structure databases

ProteinModelPortaliP62278.
SMRiP62278. Positions 2-150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP62278. 1 interaction.
MINTiMINT-4577079.
STRINGi10116.ENSRNOP00000036690.

PTM databases

iPTMnetiP62278.
PhosphoSiteiP62278.

Proteomic databases

PaxDbiP62278.
PRIDEiP62278.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000034694; ENSRNOP00000036690; ENSRNOG00000028021.
GeneIDi161477.
684988.
KEGGirno:161477.
rno:684988.
UCSCiRGD:621027. rat.

Organism-specific databases

CTDi6207.
RGDi621027. Rps13.

Phylogenomic databases

eggNOGiKOG0400. Eukaryota.
COG0184. LUCA.
GeneTreeiENSGT00390000017491.
HOGENOMiHOG000180723.
HOVERGENiHBG000938.
InParanoidiP62278.
KOiK02953.
OMAiWHLVKKA.
OrthoDBiEOG7KH9MB.
PhylomeDBiP62278.
TreeFamiTF300190.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP62278.

Gene expression databases

GenevisibleiP62278. RN.

Family and domain databases

HAMAPiMF_01343_A. Ribosomal_S15_A.
InterProiIPR012606. Ribosomal_S13/S15_N.
IPR000589. Ribosomal_S15.
IPR023029. Ribosomal_S15P.
IPR009068. S15_NS1_RNA-bd.
[Graphical view]
PfamiPF08069. Ribosomal_S13_N. 1 hit.
PF00312. Ribosomal_S15. 1 hit.
[Graphical view]
SMARTiSM01386. Ribosomal_S13_N. 1 hit.
SM01387. Ribosomal_S15. 1 hit.
[Graphical view]
SUPFAMiSSF47060. SSF47060. 1 hit.
PROSITEiPS00362. RIBOSOMAL_S15. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structure of rat ribosomal protein S13."
    Suzuki K., Olvera J., Wool I.G.
    Biochem. Biophys. Res. Commun. 171:519-524(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "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: Brain.
  3. "Isolation of a cloned cDNA encoding the rat S13 ribosomal protein."
    Denis M.G.
    Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 123-151.

Entry informationi

Entry nameiRS13_RAT
AccessioniPrimary (citable) accession number: P62278
Secondary accession number(s): P19116, Q02546, Q29200
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.