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Protein

40S ribosomal protein S15a-5

Gene

RPS15AE

Organism
Arabidopsis thaliana (Mouse-ear cress)
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

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 S15a-5
Gene namesi
Name:RPS15AE
Ordered Locus Names:At4g29430
ORF Names:F17A13.250
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G29430.

Subcellular locationi

GO - Cellular componenti

  • cytosolic ribosome Source: TAIR
  • cytosolic small ribosomal subunit Source: TAIR
  • mitochondrion Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12912940S ribosomal protein S15a-5PRO_0000250170Add
BLAST

Proteomic databases

PaxDbiQ9M0E0.
PRIDEiQ9M0E0.

Expressioni

Gene expression databases

GenevisibleiQ9M0E0. AT.

Interactioni

Protein-protein interaction databases

BioGridi14351. 1 interaction.
MINTiMINT-8070325.
STRINGi3702.AT4G29430.1.

Structurei

3D structure databases

ProteinModelPortaliQ9M0E0.
SMRiQ9M0E0. Positions 5-129.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S8P family.Curated

Phylogenomic databases

eggNOGiKOG1754. Eukaryota.
COG0096. LUCA.
HOGENOMiHOG000204097.
InParanoidiQ9M0E0.
KOiK02957.
OMAiRQDIKAK.
PhylomeDBiQ9M0E0.

Family and domain databases

InterProiIPR000630. Ribosomal_S8.
[Graphical view]
PANTHERiPTHR11758. PTHR11758. 1 hit.
PfamiPF00410. Ribosomal_S8. 1 hit.
[Graphical view]
SUPFAMiSSF56047. SSF56047. 1 hit.
PROSITEiPS00053. RIBOSOMAL_S8. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9M0E0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRRILNDAL RTIVNAERRG KASVELKPIS TVMSSFLRIM KEKGYIKNFQ
60 70 80 90 100
VYDPHRVGRI TVDLQGRVND CKALTYRQDV RAKEIEKYTE RTLPTRQWGY
110 120
VVITTPDGIL DHEEAIKRNV GGQVLGFFY
Length:129
Mass (Da):14,916
Last modified:October 1, 2000 - v1
Checksum:iFAFA0F2E921D1967
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL096692 Genomic DNA. No translation available.
AL161575 Genomic DNA. Translation: CAB79701.1.
CP002687 Genomic DNA. Translation: AEE85630.1.
AK228983 mRNA. Translation: BAF00871.1.
BT026503 mRNA. Translation: ABH04610.1.
AY085780 mRNA. Translation: AAM62997.1.
PIRiD85343.
RefSeqiNP_194672.1. NM_119088.3.
UniGeneiAt.31923.

Genome annotation databases

EnsemblPlantsiAT4G29430.1; AT4G29430.1; AT4G29430.
GeneIDi829064.
GrameneiAT4G29430.1; AT4G29430.1; AT4G29430.
KEGGiath:AT4G29430.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL096692 Genomic DNA. No translation available.
AL161575 Genomic DNA. Translation: CAB79701.1.
CP002687 Genomic DNA. Translation: AEE85630.1.
AK228983 mRNA. Translation: BAF00871.1.
BT026503 mRNA. Translation: ABH04610.1.
AY085780 mRNA. Translation: AAM62997.1.
PIRiD85343.
RefSeqiNP_194672.1. NM_119088.3.
UniGeneiAt.31923.

3D structure databases

ProteinModelPortaliQ9M0E0.
SMRiQ9M0E0. Positions 5-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi14351. 1 interaction.
MINTiMINT-8070325.
STRINGi3702.AT4G29430.1.

Proteomic databases

PaxDbiQ9M0E0.
PRIDEiQ9M0E0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G29430.1; AT4G29430.1; AT4G29430.
GeneIDi829064.
GrameneiAT4G29430.1; AT4G29430.1; AT4G29430.
KEGGiath:AT4G29430.

Organism-specific databases

TAIRiAT4G29430.

Phylogenomic databases

eggNOGiKOG1754. Eukaryota.
COG0096. LUCA.
HOGENOMiHOG000204097.
InParanoidiQ9M0E0.
KOiK02957.
OMAiRQDIKAK.
PhylomeDBiQ9M0E0.

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

PROiQ9M0E0.

Gene expression databases

GenevisibleiQ9M0E0. AT.

Family and domain databases

InterProiIPR000630. Ribosomal_S8.
[Graphical view]
PANTHERiPTHR11758. PTHR11758. 1 hit.
PfamiPF00410. Ribosomal_S8. 1 hit.
[Graphical view]
SUPFAMiSSF56047. SSF56047. 1 hit.
PROSITEiPS00053. RIBOSOMAL_S8. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [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. "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.
  4. "Arabidopsis ORF clones."
    Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  5. "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].
  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 nameiR15A5_ARATH
AccessioniPrimary (citable) accession number: Q9M0E0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: October 1, 2000
Last modified: February 17, 2016
This is version 82 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.