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Protein

40S ribosomal protein S2-3

Gene

RPS2C

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 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-ATH-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-ATH-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-ATH-72689. Formation of a pool of free 40S subunits.
R-ATH-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-ATH-72702. Ribosomal scanning and start codon recognition.
R-ATH-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-ATH-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-ATH-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S2-3
Gene namesi
Name:RPS2C
Ordered Locus Names:At2g41840
ORF Names:T11A07.6
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G41840.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • cytosolic ribosome Source: TAIR
  • cytosolic small ribosomal subunit Source: TAIR
  • membrane Source: TAIR
  • nucleolus Source: TAIR
  • plasmodesma Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 28528540S ribosomal protein S2-3PRO_0000131682Add
BLAST

Proteomic databases

PaxDbiP49688.
PRIDEiP49688.

PTM databases

iPTMnetiP49688.

Expressioni

Gene expression databases

GenevisibleiP49688. AT.

Interactioni

Protein-protein interaction databases

BioGridi4121. 8 interactions.
IntActiP49688. 2 interactions.
STRINGi3702.AT2G41840.1.

Structurei

3D structure databases

ProteinModelPortaliP49688.
SMRiP49688. Positions 53-267.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini96 – 15964S5 DRBMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein S5P family.Curated
Contains 1 S5 DRBM domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0877. Eukaryota.
COG0098. LUCA.
HOGENOMiHOG000072596.
InParanoidiP49688.
KOiK02981.
OMAiIDFFIGP.
PhylomeDBiP49688.

Family and domain databases

Gene3Di3.30.160.20. 1 hit.
3.30.230.10. 1 hit.
InterProiIPR014720. dsRBD_dom.
IPR000851. Ribosomal_S5.
IPR005324. Ribosomal_S5_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005711. Ribosomal_S5_euk/arc.
IPR013810. Ribosomal_S5_N.
IPR018192. Ribosomal_S5_N_CS.
[Graphical view]
PANTHERiPTHR13718. PTHR13718. 1 hit.
PfamiPF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR01020. uS5_euk_arch. 1 hit.
PROSITEiPS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P49688-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAERGGERGV ERGGERGDFG RGFGGRGGRG DRGGRGRGGR GGRRGGRASE
60 70 80 90 100
EEKWVPVTKL GRLVAAGHIK QIEQIYLHSL PVKEYQIIDM LIGPTLKDEV
110 120 130 140 150
MKIMPVQKQT RAGQRTRFKA FVVVGDGNGH VGLGVKCSKE VATAIRGAII
160 170 180 190 200
LAKLSVVPVR RGYWGNKIGK PHTVPCKVTG KCGSVTVRMV PAPRGSGIVA
210 220 230 240 250
ARVPKKVLQF AGIDDVFTSS RGSTKTLGNF VKATFDCLQK TYGFLTPEFW
260 270 280
KETRFSRSPY QEHTDFLASK ALSTSKPDPV VEDQA
Length:285
Mass (Da):30,879
Last modified:December 15, 1998 - v2
Checksum:i68C8C98091D4995B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti268 – 2692AS → ST in CAA79017 (PubMed:8281187).Curated
Sequence conflicti272 – 28110LSTSKPDPVV → VSATKVITEG in CAA79017 (PubMed:8281187).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002339 Genomic DNA. Translation: AAC02764.1.
CP002685 Genomic DNA. Translation: AEC10039.1.
AY048250 mRNA. Translation: AAK82512.1.
AY133561 mRNA. Translation: AAM91391.1.
Z17622 mRNA. Translation: CAA79017.1.
PIRiG84846.
RefSeqiNP_181715.1. NM_129748.3.
UniGeneiAt.12251.
At.67324.

Genome annotation databases

EnsemblPlantsiAT2G41840.1; AT2G41840.1; AT2G41840.
GeneIDi818784.
GrameneiAT2G41840.1; AT2G41840.1; AT2G41840.
KEGGiath:AT2G41840.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002339 Genomic DNA. Translation: AAC02764.1.
CP002685 Genomic DNA. Translation: AEC10039.1.
AY048250 mRNA. Translation: AAK82512.1.
AY133561 mRNA. Translation: AAM91391.1.
Z17622 mRNA. Translation: CAA79017.1.
PIRiG84846.
RefSeqiNP_181715.1. NM_129748.3.
UniGeneiAt.12251.
At.67324.

3D structure databases

ProteinModelPortaliP49688.
SMRiP49688. Positions 53-267.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4121. 8 interactions.
IntActiP49688. 2 interactions.
STRINGi3702.AT2G41840.1.

PTM databases

iPTMnetiP49688.

Proteomic databases

PaxDbiP49688.
PRIDEiP49688.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G41840.1; AT2G41840.1; AT2G41840.
GeneIDi818784.
GrameneiAT2G41840.1; AT2G41840.1; AT2G41840.
KEGGiath:AT2G41840.

Organism-specific databases

TAIRiAT2G41840.

Phylogenomic databases

eggNOGiKOG0877. Eukaryota.
COG0098. LUCA.
HOGENOMiHOG000072596.
InParanoidiP49688.
KOiK02981.
OMAiIDFFIGP.
PhylomeDBiP49688.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP49688.

Gene expression databases

GenevisibleiP49688. AT.

Family and domain databases

Gene3Di3.30.160.20. 1 hit.
3.30.230.10. 1 hit.
InterProiIPR014720. dsRBD_dom.
IPR000851. Ribosomal_S5.
IPR005324. Ribosomal_S5_C.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR005711. Ribosomal_S5_euk/arc.
IPR013810. Ribosomal_S5_N.
IPR018192. Ribosomal_S5_N_CS.
[Graphical view]
PANTHERiPTHR13718. PTHR13718. 1 hit.
PfamiPF00333. Ribosomal_S5. 1 hit.
PF03719. Ribosomal_S5_C. 1 hit.
[Graphical view]
SUPFAMiSSF54211. SSF54211. 1 hit.
TIGRFAMsiTIGR01020. uS5_euk_arch. 1 hit.
PROSITEiPS00585. RIBOSOMAL_S5. 1 hit.
PS50881. S5_DSRBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 119-285.
    Strain: cv. Columbia.
    Tissue: Green siliques.
  5. "The organization of cytoplasmic ribosomal protein genes in the Arabidopsis genome."
    Barakat A., Szick-Miranda K., Chang I.-F., Guyot R., Blanc G., Cooke R., Delseny M., Bailey-Serres J.
    Plant Physiol. 127:398-415(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY ORGANIZATION, NOMENCLATURE.
  6. "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis thaliana."
    Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E., Rathjen J.P., Peck S.C.
    J. Proteomics 72:439-451(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: cv. Columbia.
  7. "Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
    Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
    Plant Physiol. 150:889-903(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRS23_ARATH
AccessioniPrimary (citable) accession number: P49688
Secondary accession number(s): O22936
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 15, 1998
Last modified: March 16, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. 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.