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Protein

60S ribosomal protein L19

Gene

Rpl19

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: MGI
  2. structural constituent of ribosome Source: MGI

GO - Biological processi

  1. translation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_196445. SRP-dependent cotranslational protein targeting to membrane.
REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_231519. Eukaryotic Translation Termination.
REACT_249044. Formation of a pool of free 40S subunits.
REACT_253640. Peptide chain elongation.
REACT_259469. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_262078. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L19
Gene namesi
Name:Rpl19
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:98020. Rpl19.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosolic large ribosomal subunit Source: MGI
  3. focal adhesion Source: MGI
  4. membrane Source: MGI
  5. nucleolus Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19619660S ribosomal protein L19PRO_0000131171Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei5 – 51Citrulline1 Publication
Modified residuei13 – 131PhosphoserineBy similarity
Modified residuei16 – 161Citrulline1 Publication
Modified residuei38 – 381Citrulline1 Publication
Modified residuei187 – 1871PhosphothreonineBy similarity

Post-translational modificationi

Citrullinated by PADI4.1 Publication

Keywords - PTMi

Citrullination, Phosphoprotein

Proteomic databases

MaxQBiP84099.
PaxDbiP84099.
PRIDEiP84099.

PTM databases

PhosphoSiteiP84099.

Expressioni

Gene expression databases

BgeeiP84099.
CleanExiMM_RPL19.
ExpressionAtlasiP84099. baseline and differential.
GenevestigatoriP84099.

Interactioni

Protein-protein interaction databases

BioGridi202969. 9 interactions.
IntActiP84099. 6 interactions.
MINTiMINT-1864295.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K8DX-ray2.30P137-145[»]
ProteinModelPortaliP84099.
SMRiP84099. Positions 2-181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP84099.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L19e family.Curated

Phylogenomic databases

eggNOGiCOG2147.
HOGENOMiHOG000231277.
HOVERGENiHBG056059.
InParanoidiP84099.
KOiK02885.
OMAiILSDQME.
PhylomeDBiP84099.
TreeFamiTF313598.

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.

P84099-1 [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:August 16, 2004 - v1
Checksum:i4AF506393E526216
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti179 – 1791A → S in AAB48630 (PubMed:1702292).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62952 mRNA. Translation: AAB48630.1.
AK010440 mRNA. Translation: BAB26941.1.
BC010710 mRNA. Translation: AAH10710.1.
BC083131 mRNA. Translation: AAH83131.1.
CCDSiCCDS25337.1.
PIRiA36554.
RefSeqiNP_033104.2. NM_009078.2.
UniGeneiMm.10247.

Genome annotation databases

EnsembliENSMUST00000017548; ENSMUSP00000017548; ENSMUSG00000017404.
GeneIDi19921.
KEGGimmu:19921.
UCSCiuc007lfj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62952 mRNA. Translation: AAB48630.1.
AK010440 mRNA. Translation: BAB26941.1.
BC010710 mRNA. Translation: AAH10710.1.
BC083131 mRNA. Translation: AAH83131.1.
CCDSiCCDS25337.1.
PIRiA36554.
RefSeqiNP_033104.2. NM_009078.2.
UniGeneiMm.10247.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K8DX-ray2.30P137-145[»]
ProteinModelPortaliP84099.
SMRiP84099. Positions 2-181.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202969. 9 interactions.
IntActiP84099. 6 interactions.
MINTiMINT-1864295.

PTM databases

PhosphoSiteiP84099.

Proteomic databases

MaxQBiP84099.
PaxDbiP84099.
PRIDEiP84099.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000017548; ENSMUSP00000017548; ENSMUSG00000017404.
GeneIDi19921.
KEGGimmu:19921.
UCSCiuc007lfj.2. mouse.

Organism-specific databases

CTDi6143.
MGIiMGI:98020. Rpl19.

Phylogenomic databases

eggNOGiCOG2147.
HOGENOMiHOG000231277.
HOVERGENiHBG056059.
InParanoidiP84099.
KOiK02885.
OMAiILSDQME.
PhylomeDBiP84099.
TreeFamiTF313598.

Enzyme and pathway databases

ReactomeiREACT_196445. SRP-dependent cotranslational protein targeting to membrane.
REACT_198524. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_198528. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_231519. Eukaryotic Translation Termination.
REACT_249044. Formation of a pool of free 40S subunits.
REACT_253640. Peptide chain elongation.
REACT_259469. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_262078. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

ChiTaRSiRpl19. mouse.
EvolutionaryTraceiP84099.
NextBioi23865.
PROiP84099.
SOURCEiSearch...

Gene expression databases

BgeeiP84099.
CleanExiMM_RPL19.
ExpressionAtlasiP84099. baseline and differential.
GenevestigatoriP84099.

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. "Nucleotide sequence of mouse L19 ribosomal protein cDNA isolated in screening with tre oncogene probes."
    Nakamura T., Onno M., Mariage-Samson R., Hillova J., Hill M.
    DNA Cell Biol. 9:697-703(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 187-195, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. Cited for: CITRULLINATION AT ARG-5; ARG-16 AND ARG-38.
  6. "Promiscuous antigen presentation by the nonclassical MHC Ib Qa-2 is enabled by a shallow, hydrophobic groove and self-stabilized peptide conformation."
    He X., Tabaczewski P., Ho J., Stroynowski I., Garcia K.C.
    Structure 9:1213-1224(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 137-145 IN COMPLEX WITH MHC.

Entry informationi

Entry nameiRL19_MOUSE
AccessioniPrimary (citable) accession number: P84099
Secondary accession number(s): P14118, P22908
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: March 4, 2015
This is version 98 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, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. 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.