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Protein

60S ribosomal protein L19-3

Gene

RPL19C

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-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:
60S ribosomal protein L19-3
Gene namesi
Name:RPL19C
Ordered Locus Names:At4g02230
ORF Names:T2H3.3
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G02230.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: TAIR
  • cytosolic large ribosomal subunit Source: TAIR
  • cytosolic ribosome Source: TAIR
  • plasma membrane Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 20820860S ribosomal protein L19-3PRO_0000131181Add
BLAST

Proteomic databases

PaxDbiP49693.
PRIDEiP49693.

PTM databases

iPTMnetiP49693.

Expressioni

Gene expression databases

GenevisibleiP49693. AT.

Interactioni

Protein-protein interaction databases

BioGridi13389. 1 interaction.
STRINGi3702.AT4G02230.1.

Structurei

3D structure databases

ProteinModelPortaliP49693.
SMRiP49693. Positions 1-132.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L19e family.Curated

Phylogenomic databases

eggNOGiKOG1696. Eukaryota.
COG2147. LUCA.
HOGENOMiHOG000231277.
InParanoidiP49693.
KOiK02885.
OMAiDIAMANS.
PhylomeDBiP49693.

Family and domain databases

Gene3Di1.10.1200.60. 1 hit.
1.10.1650.10. 1 hit.
HAMAPiMF_01475. Ribosomal_L19e.
InterProiIPR027547. Ribosomal_L19/L19e.
IPR023638. Ribosomal_L19/L19e_CS.
IPR000196. Ribosomal_L19/L19e_dom.
IPR015972. Ribosomal_L19/L19e_dom1.
IPR015974. Ribosomal_L19/L19e_dom3.
[Graphical view]
PfamiPF01280. Ribosomal_L19e. 1 hit.
[Graphical view]
SMARTiSM01416. Ribosomal_L19e. 1 hit.
[Graphical view]
SUPFAMiSSF48140. SSF48140. 1 hit.
PROSITEiPS00526. RIBOSOMAL_L19E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P49693-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVSLKLQKRL ASSVLKCGKR KVWLDPNEGS DISMANSRQN IRKLVKDGFI
60 70 80 90 100
IRKPTKIHSR SRARQLNIAK RKGRHSGYGK RKGTREARLP TKVLWMRRMR
110 120 130 140 150
VLRRLLKKYR ETKKIDRHMY HDMYMKVKGN VFKNKRVLME SIHKSKAEKA
160 170 180 190 200
REKTLSDQFE AKRAKNKASR ERKHARREER LAKGPGGDIP AAAPPAQTAE

VPAKKSKK
Length:208
Mass (Da):24,202
Last modified:December 13, 2001 - v3
Checksum:iFF0D3C023117E5F6
GO

Sequence cautioni

The sequence AAC28170.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111A → R in CAA79080 (PubMed:8281187).Curated
Sequence conflicti82 – 854KGTR → NGYP (PubMed:8281187).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF075597 Genomic DNA. Translation: AAC28170.1. Sequence problems.
AL161494 Genomic DNA. Translation: CAB80716.1.
CP002687 Genomic DNA. Translation: AEE82143.1.
AF386993 mRNA. Translation: AAK62438.1.
AY072494 mRNA. Translation: AAL66909.1.
Z17981 mRNA. Translation: CAA79080.1.
PIRiE85028.
T01426.
RefSeqiNP_192132.1. NM_116456.3.
UniGeneiAt.23066.

Genome annotation databases

EnsemblPlantsiAT4G02230.1; AT4G02230.1; AT4G02230.
GeneIDi828099.
GrameneiAT4G02230.1; AT4G02230.1; AT4G02230.
KEGGiath:AT4G02230.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF075597 Genomic DNA. Translation: AAC28170.1. Sequence problems.
AL161494 Genomic DNA. Translation: CAB80716.1.
CP002687 Genomic DNA. Translation: AEE82143.1.
AF386993 mRNA. Translation: AAK62438.1.
AY072494 mRNA. Translation: AAL66909.1.
Z17981 mRNA. Translation: CAA79080.1.
PIRiE85028.
T01426.
RefSeqiNP_192132.1. NM_116456.3.
UniGeneiAt.23066.

3D structure databases

ProteinModelPortaliP49693.
SMRiP49693. Positions 1-132.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi13389. 1 interaction.
STRINGi3702.AT4G02230.1.

PTM databases

iPTMnetiP49693.

Proteomic databases

PaxDbiP49693.
PRIDEiP49693.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G02230.1; AT4G02230.1; AT4G02230.
GeneIDi828099.
GrameneiAT4G02230.1; AT4G02230.1; AT4G02230.
KEGGiath:AT4G02230.

Organism-specific databases

TAIRiAT4G02230.

Phylogenomic databases

eggNOGiKOG1696. Eukaryota.
COG2147. LUCA.
HOGENOMiHOG000231277.
InParanoidiP49693.
KOiK02885.
OMAiDIAMANS.
PhylomeDBiP49693.

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-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

PROiP49693.

Gene expression databases

GenevisibleiP49693. AT.

Family and domain databases

Gene3Di1.10.1200.60. 1 hit.
1.10.1650.10. 1 hit.
HAMAPiMF_01475. Ribosomal_L19e.
InterProiIPR027547. Ribosomal_L19/L19e.
IPR023638. Ribosomal_L19/L19e_CS.
IPR000196. Ribosomal_L19/L19e_dom.
IPR015972. Ribosomal_L19/L19e_dom1.
IPR015974. Ribosomal_L19/L19e_dom3.
[Graphical view]
PfamiPF01280. Ribosomal_L19e. 1 hit.
[Graphical view]
SMARTiSM01416. Ribosomal_L19e. 1 hit.
[Graphical view]
SUPFAMiSSF48140. SSF48140. 1 hit.
PROSITEiPS00526. RIBOSOMAL_L19E. 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. "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 4-85.
    Strain: cv. Columbia.
  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.

Entry informationi

Entry nameiRL193_ARATH
AccessioniPrimary (citable) accession number: P49693
Secondary accession number(s): O81422, Q9M114
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 13, 2001
Last modified: June 8, 2016
This is version 132 of the entry and version 3 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.