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Protein

60S ribosomal protein L18a

Gene

Rpl18a

Organism
Mus musculus (Mouse)
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

ReactomeiR-MMU-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-MMU-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-MMU-72689. Formation of a pool of free 40S subunits.
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:
60S ribosomal protein L18a
Gene namesi
Name:Rpl18a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1924058. Rpl18a.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 17617660S ribosomal protein L18aPRO_0000213926Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei63 – 631PhosphotyrosineBy similarity
Modified residuei71 – 711PhosphoserineCombined sources
Modified residuei76 – 761N6-succinyllysineCombined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP62717.
MaxQBiP62717.
PaxDbiP62717.
PRIDEiP62717.

PTM databases

iPTMnetiP62717.
PhosphoSiteiP62717.

Expressioni

Gene expression databases

BgeeiP62717.
CleanExiMM_RPL18A.
GenevisibleiP62717. MM.

Interactioni

Subunit structurei

Binds IPO9 with high affinity.By similarity

Protein-protein interaction databases

BioGridi218328. 4 interactions.
IntActiP62717. 4 interactions.
MINTiMINT-1841289.
STRINGi10090.ENSMUSP00000058368.

Structurei

3D structure databases

ProteinModelPortaliP62717.
SMRiP62717. Positions 2-176.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L18Ae family.Curated

Phylogenomic databases

eggNOGiKOG0829. Eukaryota.
COG2157. LUCA.
GeneTreeiENSGT00390000015797.
HOGENOMiHOG000211377.
HOVERGENiHBG066281.
InParanoidiP62717.
KOiK02882.
OMAiCRRPAIK.
OrthoDBiEOG7TMZT2.
PhylomeDBiP62717.
TreeFamiTF300086.

Family and domain databases

HAMAPiMF_00273. Ribosomal_L18Ae.
InterProiIPR028877. 50S_L18Ae/Ribosomal_L18a/L20.
IPR023573. Ribosomal_L18a//L18Ae/LX.
IPR021138. Ribosomal_L18a/L20_eukaryotes.
[Graphical view]
PfamiPF01775. Ribosomal_L18A. 1 hit.
[Graphical view]
PIRSFiPIRSF002190. Ribosomal_L18a. 1 hit.

Sequencei

Sequence statusi: Complete.

P62717-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKASGTLREY KVVGRCLPTP KCHTPPLYRM RIFAPNHVVA KSRFWYFVSQ
60 70 80 90 100
LKKMKKSSGE IVYCGQVFEK SPLRVKNFGI WLRYDSRSGT HNMYREYRDL
110 120 130 140 150
TTAGAVTQCY RDMGARHRAR AHSIQIMKVE EIAAGKCRRP AVKQFHDSKI
160 170
KFPLPHRVLR RQHKPRFTTK RPNTFF
Length:176
Mass (Da):20,732
Last modified:July 19, 2004 - v1
Checksum:i5E404D28875BE580
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010983 mRNA. Translation: BAB27304.1.
AK146543 mRNA. Translation: BAE27248.1.
AK161942 mRNA. Translation: BAE36645.1.
AK162047 mRNA. Translation: BAE36696.1.
BC037146 mRNA. Translation: AAH37146.1.
CCDSiCCDS22386.1.
RefSeqiNP_084027.1. NM_029751.4.
UniGeneiMm.379251.
Mm.431334.

Genome annotation databases

EnsembliENSMUST00000054220; ENSMUSP00000058368; ENSMUSG00000045128.
GeneIDi76808.
KEGGimmu:76808.
UCSCiuc009mca.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK010983 mRNA. Translation: BAB27304.1.
AK146543 mRNA. Translation: BAE27248.1.
AK161942 mRNA. Translation: BAE36645.1.
AK162047 mRNA. Translation: BAE36696.1.
BC037146 mRNA. Translation: AAH37146.1.
CCDSiCCDS22386.1.
RefSeqiNP_084027.1. NM_029751.4.
UniGeneiMm.379251.
Mm.431334.

3D structure databases

ProteinModelPortaliP62717.
SMRiP62717. Positions 2-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi218328. 4 interactions.
IntActiP62717. 4 interactions.
MINTiMINT-1841289.
STRINGi10090.ENSMUSP00000058368.

PTM databases

iPTMnetiP62717.
PhosphoSiteiP62717.

Proteomic databases

EPDiP62717.
MaxQBiP62717.
PaxDbiP62717.
PRIDEiP62717.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000054220; ENSMUSP00000058368; ENSMUSG00000045128.
GeneIDi76808.
KEGGimmu:76808.
UCSCiuc009mca.2. mouse.

Organism-specific databases

CTDi6142.
MGIiMGI:1924058. Rpl18a.

Phylogenomic databases

eggNOGiKOG0829. Eukaryota.
COG2157. LUCA.
GeneTreeiENSGT00390000015797.
HOGENOMiHOG000211377.
HOVERGENiHBG066281.
InParanoidiP62717.
KOiK02882.
OMAiCRRPAIK.
OrthoDBiEOG7TMZT2.
PhylomeDBiP62717.
TreeFamiTF300086.

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-72689. Formation of a pool of free 40S subunits.
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

NextBioi345857.
PROiP62717.
SOURCEiSearch...

Gene expression databases

BgeeiP62717.
CleanExiMM_RPL18A.
GenevisibleiP62717. MM.

Family and domain databases

HAMAPiMF_00273. Ribosomal_L18Ae.
InterProiIPR028877. 50S_L18Ae/Ribosomal_L18a/L20.
IPR023573. Ribosomal_L18a//L18Ae/LX.
IPR021138. Ribosomal_L18a/L20_eukaryotes.
[Graphical view]
PfamiPF01775. Ribosomal_L18A. 1 hit.
[Graphical view]
PIRSFiPIRSF002190. Ribosomal_L18a. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "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: Kidney, Liver, Muellerian duct and Olfactory bulb.
  2. "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-3.
    Tissue: Mammary gland.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "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: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRL18A_MOUSE
AccessioniPrimary (citable) accession number: P62717
Secondary accession number(s): P11249, Q3TSN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: May 11, 2016
This is version 103 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

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.