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Protein

40S ribosomal protein S19

Gene

Rps19

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

Functioni

Required for pre-rRNA processing and maturation of 40S ribosomal subunits.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-MMU-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S19
Gene namesi
Name:Rps19
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1333780. Rps19.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 14514440S ribosomal protein S19PRO_0000153811Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei23 – 231N6-acetyllysineBy similarity
Modified residuei111 – 1111N6-acetyllysineBy similarity
Modified residuei115 – 1151N6-acetyllysineCombined sources
Modified residuei143 – 1431N6-succinyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ9CZX8.
MaxQBiQ9CZX8.
PaxDbiQ9CZX8.
PeptideAtlasiQ9CZX8.
PRIDEiQ9CZX8.
TopDownProteomicsiQ9CZX8.

PTM databases

iPTMnetiQ9CZX8.
PhosphoSiteiQ9CZX8.
SwissPalmiQ9CZX8.

Expressioni

Gene expression databases

BgeeiQ9CZX8.
CleanExiMM_RPS19.
ExpressionAtlasiQ9CZX8. baseline and differential.
GenevisibleiQ9CZX8. MM.

Interactioni

Subunit structurei

Interacts with RPS19BP1.1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi203007. 4 interactions.
IntActiQ9CZX8. 6 interactions.
MINTiMINT-1870161.
STRINGi10090.ENSMUSP00000104067.

Structurei

3D structure databases

ProteinModelPortaliQ9CZX8.
SMRiQ9CZX8. Positions 2-145.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S19e family.Curated

Phylogenomic databases

eggNOGiKOG3411. Eukaryota.
COG2238. LUCA.
GeneTreeiENSGT00390000013102.
HOGENOMiHOG000230649.
HOVERGENiHBG000240.
InParanoidiQ9CZX8.
KOiK02966.
OrthoDBiEOG74J99M.
PhylomeDBiQ9CZX8.
TreeFamiTF315008.

Family and domain databases

InterProiIPR001266. Ribosomal_S19e.
IPR018277. Ribosomal_S19e_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR11710. PTHR11710. 1 hit.
PfamiPF01090. Ribosomal_S19e. 1 hit.
[Graphical view]
ProDomiPD003854. Ribosomal_S19e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM01413. Ribosomal_S19e. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS00628. RIBOSOMAL_S19E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9CZX8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGVTVKDVN QQEFVRALAA FLKKSGKLKV PEWVDTVKLA KHKELAPYDE
60 70 80 90 100
NWFYTRAAST ARHLYLRGGA GVGSMTKIYG GRQRNGVRPS HFSRGSKSVA
110 120 130 140
RRVLQALEGL KMVEKDQDGG RKLTPQGQRD LDRIAGQVAA ANKKH
Length:145
Mass (Da):16,085
Last modified:January 23, 2007 - v3
Checksum:i180032B887FA6E41
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF216207 Genomic DNA. Translation: AAF65683.1.
AK013524 mRNA. Translation: BAB28898.1.
AK018725 mRNA. Translation: BAB31370.1.
AK028244 mRNA. Translation: BAC25836.1.
BC034506 mRNA. Translation: AAH34506.1.
BC086938 mRNA. Translation: AAH86938.1.
CCDSiCCDS20966.1.
RefSeqiNP_075622.1. NM_023133.1.
XP_006539743.1. XM_006539680.2.
XP_006539744.1. XM_006539681.2.
UniGeneiMm.300281.
Mm.445088.

Genome annotation databases

EnsembliENSMUST00000108429; ENSMUSP00000104067; ENSMUSG00000040952.
ENSMUST00000108430; ENSMUSP00000104068; ENSMUSG00000040952.
GeneIDi20085.
KEGGimmu:20085.
UCSCiuc009fqq.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF216207 Genomic DNA. Translation: AAF65683.1.
AK013524 mRNA. Translation: BAB28898.1.
AK018725 mRNA. Translation: BAB31370.1.
AK028244 mRNA. Translation: BAC25836.1.
BC034506 mRNA. Translation: AAH34506.1.
BC086938 mRNA. Translation: AAH86938.1.
CCDSiCCDS20966.1.
RefSeqiNP_075622.1. NM_023133.1.
XP_006539743.1. XM_006539680.2.
XP_006539744.1. XM_006539681.2.
UniGeneiMm.300281.
Mm.445088.

3D structure databases

ProteinModelPortaliQ9CZX8.
SMRiQ9CZX8. Positions 2-145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203007. 4 interactions.
IntActiQ9CZX8. 6 interactions.
MINTiMINT-1870161.
STRINGi10090.ENSMUSP00000104067.

PTM databases

iPTMnetiQ9CZX8.
PhosphoSiteiQ9CZX8.
SwissPalmiQ9CZX8.

Proteomic databases

EPDiQ9CZX8.
MaxQBiQ9CZX8.
PaxDbiQ9CZX8.
PeptideAtlasiQ9CZX8.
PRIDEiQ9CZX8.
TopDownProteomicsiQ9CZX8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108429; ENSMUSP00000104067; ENSMUSG00000040952.
ENSMUST00000108430; ENSMUSP00000104068; ENSMUSG00000040952.
GeneIDi20085.
KEGGimmu:20085.
UCSCiuc009fqq.1. mouse.

Organism-specific databases

CTDi6223.
MGIiMGI:1333780. Rps19.

Phylogenomic databases

eggNOGiKOG3411. Eukaryota.
COG2238. LUCA.
GeneTreeiENSGT00390000013102.
HOGENOMiHOG000230649.
HOVERGENiHBG000240.
InParanoidiQ9CZX8.
KOiK02966.
OrthoDBiEOG74J99M.
PhylomeDBiQ9CZX8.
TreeFamiTF315008.

Enzyme and pathway databases

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-MMU-72649. Translation initiation complex formation.
R-MMU-72689. Formation of a pool of free 40S subunits.
R-MMU-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-MMU-72702. Ribosomal scanning and start codon recognition.
R-MMU-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-MMU-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-MMU-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

PROiQ9CZX8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CZX8.
CleanExiMM_RPS19.
ExpressionAtlasiQ9CZX8. baseline and differential.
GenevisibleiQ9CZX8. MM.

Family and domain databases

InterProiIPR001266. Ribosomal_S19e.
IPR018277. Ribosomal_S19e_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR11710. PTHR11710. 1 hit.
PfamiPF01090. Ribosomal_S19e. 1 hit.
[Graphical view]
ProDomiPD003854. Ribosomal_S19e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM01413. Ribosomal_S19e. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS00628. RIBOSOMAL_S19E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "RPS19 gene in Mus musculus and Drosophila melanogaster, and conserved features among 40 different species."
    Willig T.-N.D., Peters L.L., Parra M.K., Tchernia G., Mohandas N.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  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.
    Tissue: Hippocampus and Kidney.
  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].
    Strain: FVB/N.
    Tissue: Kidney and Mammary gland.
  4. "A novel nucleolar protein interacts with ribosomal protein S19."
    Maeda N., Toku S., Kenmochi N., Tanaka T.
    Biochem. Biophys. Res. Commun. 339:41-46(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RPS19BP1.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-115, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRS19_MOUSE
AccessioniPrimary (citable) accession number: Q9CZX8
Secondary accession number(s): Q5M9J4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 115 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.