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Protein

40S ribosomal protein S2-4

Gene

RPS2D

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript 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 S2-4
Gene namesi
Name:RPS2D
Ordered Locus Names:At3g57490
ORF Names:T8H10.90
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G57490.

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 27627640S ribosomal protein S2-4PRO_0000250176Add
BLAST

Proteomic databases

PaxDbiQ9SCM3.
PRIDEiQ9SCM3.

PTM databases

iPTMnetiQ9SCM3.

Expressioni

Gene expression databases

GenevisibleiQ9SCM3. AT.

Interactioni

Protein-protein interaction databases

BioGridi10232. 2 interactions.
IntActiQ9SCM3. 1 interaction.
STRINGi3702.AT3G57490.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SCM3.
SMRiQ9SCM3. Positions 42-259.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini87 – 15064S5 DRBMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi5 – 3733Gly-richAdd
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.
InParanoidiQ9SCM3.
KOiK02981.
OMAiGIKDVWT.
PhylomeDBiQ9SCM3.

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.

Q9SCM3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAERGVERGG DRGDFGRGFG GRGGGRGGPR GRGRRAGRAP EEEKWVPVTK
60 70 80 90 100
LGRLVKEGKI TKIEQIYLHS LPVKEYQIID LLVGPSLKDE VMKIMPVQKQ
110 120 130 140 150
TRAGQRTRFK AFIVVGDSNG HVGLGVKCSK EVATAIRGAI ILAKLSVVPI
160 170 180 190 200
RRGYWGNKIG KPHTVPCKVT GKCGSVTVRM VPAPRGSGIV AARVPKKVLQ
210 220 230 240 250
FAGIDDVFTS SRGSTKTLGN FVKATFDCLQ KTYGFLTPEF WKETRFSKSP
260 270
YQEHTDFLLI PPGVKISEVV VDKSVE
Length:276
Mass (Da):30,116
Last modified:May 1, 2000 - v1
Checksum:i6BFF69F96D15922D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL133248 Genomic DNA. Translation: CAB66106.1.
CP002686 Genomic DNA. Translation: AEE79662.1.
BT006200 mRNA. Translation: AAP12849.1.
AY084252 mRNA. Translation: AAM60846.1.
AK228054 mRNA. Translation: BAF00015.1.
PIRiT46185.
RefSeqiNP_191308.1. NM_115609.2.
UniGeneiAt.34827.

Genome annotation databases

EnsemblPlantsiAT3G57490.1; AT3G57490.1; AT3G57490.
GeneIDi824916.
GrameneiAT3G57490.1; AT3G57490.1; AT3G57490.
KEGGiath:AT3G57490.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL133248 Genomic DNA. Translation: CAB66106.1.
CP002686 Genomic DNA. Translation: AEE79662.1.
BT006200 mRNA. Translation: AAP12849.1.
AY084252 mRNA. Translation: AAM60846.1.
AK228054 mRNA. Translation: BAF00015.1.
PIRiT46185.
RefSeqiNP_191308.1. NM_115609.2.
UniGeneiAt.34827.

3D structure databases

ProteinModelPortaliQ9SCM3.
SMRiQ9SCM3. Positions 42-259.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi10232. 2 interactions.
IntActiQ9SCM3. 1 interaction.
STRINGi3702.AT3G57490.1.

PTM databases

iPTMnetiQ9SCM3.

Proteomic databases

PaxDbiQ9SCM3.
PRIDEiQ9SCM3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G57490.1; AT3G57490.1; AT3G57490.
GeneIDi824916.
GrameneiAT3G57490.1; AT3G57490.1; AT3G57490.
KEGGiath:AT3G57490.

Organism-specific databases

TAIRiAT3G57490.

Phylogenomic databases

eggNOGiKOG0877. Eukaryota.
COG0098. LUCA.
HOGENOMiHOG000072596.
InParanoidiQ9SCM3.
KOiK02981.
OMAiGIKDVWT.
PhylomeDBiQ9SCM3.

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

PROiQ9SCM3.

Gene expression databases

GenevisibleiQ9SCM3. 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. "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [PubMed] [Europe PMC] [Abstract]
    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. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  6. "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.

Entry informationi

Entry nameiRS24_ARATH
AccessioniPrimary (citable) accession number: Q9SCM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: May 1, 2000
Last modified: February 17, 2016
This is version 102 of the entry and version 1 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.