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Protein

60S ribosomal protein L19

Gene

RPL19

Organism
Canis familiaris (Dog) (Canis lupus familiaris)
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

ReactomeiREACT_280121. Eukaryotic Translation Termination.
REACT_280392. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_298388. SRP-dependent cotranslational protein targeting to membrane.
REACT_306007. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_329635. Formation of a pool of free 40S subunits.
REACT_330632. Peptide chain elongation.
REACT_346841. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_353757. L13a-mediated translational silencing of Ceruloplasmin expression.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L19
Gene namesi
Name:RPL19
OrganismiCanis familiaris (Dog) (Canis lupus familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
ProteomesiUP000002254 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19619660S ribosomal protein L19PRO_0000405590Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51CitrullineBy similarity
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei16 – 161CitrullineBy similarity
Modified residuei38 – 381CitrullineBy similarity
Modified residuei187 – 1871PhosphothreonineBy similarity

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Citrullination, Phosphoprotein

Proteomic databases

PaxDbiD0VWQ5.
PRIDEiD0VWQ5.

Interactioni

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000024264.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V5Zelectron microscopy8.70798-110[»]
p1-196[»]
ProteinModelPortaliD0VWQ5.
SMRiD0VWQ5. Positions 1-142.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiD0VWQ5.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L19e family.Curated

Phylogenomic databases

eggNOGiCOG2147.
InParanoidiD0VWQ5.
KOiK02885.

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]
SUPFAMiSSF48140. SSF48140. 1 hit.
PROSITEiPS00526. RIBOSOMAL_L19E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

D0VWQ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMLRLQKRL ASSVLRCGKK KVWLDPNETN EIANANSRQQ IRKLIKDGLI
60 70 80 90 100
IRKPVTVHSR ARCRKNTLAR RKGRHMGIGK RKGTANARMP EKVTWMRRMR
110 120 130 140 150
ILRRLLRRYR ESKKIDRHMY HSLYLKVKGN VFKNKRILME HIHKLKADKA
160 170 180 190
RKKLLADQAE ARRSKTKEAR KRREERLQAK KEEIIKTLSK EEETKK
Length:196
Mass (Da):23,466
Last modified:December 15, 2009 - v1
Checksum:i4AF506393E526216
GO

Sequence databases

RefSeqiXP_005624628.1. XM_005624571.1.
UniGeneiCfa.47841.

Genome annotation databases

GeneIDi403682.
KEGGicfa:403682.

Cross-referencesi

Sequence databases

RefSeqiXP_005624628.1. XM_005624571.1.
UniGeneiCfa.47841.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V5Zelectron microscopy8.70798-110[»]
p1-196[»]
ProteinModelPortaliD0VWQ5.
SMRiD0VWQ5. Positions 1-142.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9615.ENSCAFP00000024264.

Proteomic databases

PaxDbiD0VWQ5.
PRIDEiD0VWQ5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi403682.
KEGGicfa:403682.

Organism-specific databases

CTDi6143.

Phylogenomic databases

eggNOGiCOG2147.
InParanoidiD0VWQ5.
KOiK02885.

Enzyme and pathway databases

ReactomeiREACT_280121. Eukaryotic Translation Termination.
REACT_280392. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_298388. SRP-dependent cotranslational protein targeting to membrane.
REACT_306007. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_329635. Formation of a pool of free 40S subunits.
REACT_330632. Peptide chain elongation.
REACT_346841. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_353757. L13a-mediated translational silencing of Ceruloplasmin expression.

Miscellaneous databases

EvolutionaryTraceiD0VWQ5.
NextBioi20817186.

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]
SUPFAMiSSF48140. SSF48140. 1 hit.
PROSITEiPS00526. RIBOSOMAL_L19E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence, comparative analysis and haplotype structure of the domestic dog."
    Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B., Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E., Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F., Smith D.R.
    , deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W., Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S., Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A., Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P., Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A., Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P., Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P., Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B., Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A., Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M., Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S., Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L., Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S., Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C., Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G., Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N., Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A., Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A., Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M., Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L., LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A., Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S., Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T., Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A., Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N., Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S., Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M., Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F., Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T., Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C., Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C., Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D., Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H., Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J., Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J., Zembek L., Zimmer A., Lander E.S.
    Nature 438:803-819(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Boxer.
  2. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (8.70 ANGSTROMS).

Entry informationi

Entry nameiRL19_CANFA
AccessioniPrimary (citable) accession number: D0VWQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 8, 2011
Last sequence update: December 15, 2009
Last modified: June 24, 2015
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.