Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

60S ribosomal protein L13

Gene

Rpl13

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-6791226. Major pathway of rRNA processing in the nucleolus.
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 L13
Alternative name(s):
A52
Gene namesi
Name:Rpl13
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:105922. Rpl13.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 21121160S ribosomal protein L13PRO_0000192920Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei16 – 161N6-acetyllysineBy similarity
Modified residuei52 – 521PhosphoserineBy similarity
Modified residuei77 – 771PhosphoserineBy similarity
Modified residuei106 – 1061PhosphoserineBy similarity
Cross-linki174 – 174Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei177 – 1771N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP47963.
MaxQBiP47963.
PaxDbiP47963.
PeptideAtlasiP47963.
PRIDEiP47963.

PTM databases

iPTMnetiP47963.
PhosphoSiteiP47963.
SwissPalmiP47963.

Expressioni

Gene expression databases

BgeeiP47963.
CleanExiMM_RPL13.
GenevisibleiP47963. MM.

Interactioni

Protein-protein interaction databases

BioGridi234761. 3 interactions.
IntActiP47963. 8 interactions.
MINTiMINT-1865813.
STRINGi10090.ENSMUSP00000000756.

Structurei

3D structure databases

ProteinModelPortaliP47963.
SMRiP47963. Positions 2-211.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L13e family.Curated

Phylogenomic databases

eggNOGiKOG3295. Eukaryota.
COG4352. LUCA.
GeneTreeiENSGT00390000007818.
HOGENOMiHOG000170452.
HOVERGENiHBG001156.
InParanoidiP47963.
KOiK02873.
OMAiHCPTFRY.
OrthoDBiEOG74TX1G.
PhylomeDBiP47963.
TreeFamiTF300073.

Family and domain databases

InterProiIPR001380. Ribosomal_L13e.
IPR018256. Ribosomal_L13e_CS.
[Graphical view]
PANTHERiPTHR11722. PTHR11722. 1 hit.
PfamiPF01294. Ribosomal_L13e. 1 hit.
[Graphical view]
PROSITEiPS01104. RIBOSOMAL_L13E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P47963-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPSRNGMIL KPHFHKDWQQ RVDTWFNQPA RKIRRRKARQ AKARRIAPRP
60 70 80 90 100
ASGPIRPIVR CPTVRYHTKV RAGRGFSLEE LRVAGIHKKV ARTIGISVDP
110 120 130 140 150
RRRNKSTESL QANVQRLKEY RSKLILFPRK PSAPKKGDSS AEELKLATQL
160 170 180 190 200
TGPVMPIRNV YKKEKARVIT EEEKNFKAFA SLRMARANAR LFGIRAKRAK
210
EAAEQDVEKK K
Length:211
Mass (Da):24,305
Last modified:January 23, 2007 - v3
Checksum:i27B1D4B97A9A1B74
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 401Q → L in AAA69923 (Ref. 1) Curated
Sequence conflicti190 – 1967RLFGIRA → PTLWQSEQ in AAA69923 (Ref. 1) Curated
Sequence conflicti203 – 2119AEQDVEKKK → SEQRCWKRKN in AAA69923 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28917 mRNA. Translation: AAA69923.1.
AK002787 mRNA. Translation: BAB22358.1.
AK010989 mRNA. Translation: BAB27309.1.
BC055358 mRNA. Translation: AAH55358.1.
CCDSiCCDS22747.1.
RefSeqiNP_058018.2. NM_016738.5.
UniGeneiMm.319719.
Mm.391834.

Genome annotation databases

EnsembliENSMUST00000000756; ENSMUSP00000000756; ENSMUSG00000000740.
GeneIDi270106.
KEGGimmu:270106.
UCSCiuc009nue.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28917 mRNA. Translation: AAA69923.1.
AK002787 mRNA. Translation: BAB22358.1.
AK010989 mRNA. Translation: BAB27309.1.
BC055358 mRNA. Translation: AAH55358.1.
CCDSiCCDS22747.1.
RefSeqiNP_058018.2. NM_016738.5.
UniGeneiMm.319719.
Mm.391834.

3D structure databases

ProteinModelPortaliP47963.
SMRiP47963. Positions 2-211.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi234761. 3 interactions.
IntActiP47963. 8 interactions.
MINTiMINT-1865813.
STRINGi10090.ENSMUSP00000000756.

PTM databases

iPTMnetiP47963.
PhosphoSiteiP47963.
SwissPalmiP47963.

Proteomic databases

EPDiP47963.
MaxQBiP47963.
PaxDbiP47963.
PeptideAtlasiP47963.
PRIDEiP47963.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000756; ENSMUSP00000000756; ENSMUSG00000000740.
GeneIDi270106.
KEGGimmu:270106.
UCSCiuc009nue.2. mouse.

Organism-specific databases

CTDi6137.
MGIiMGI:105922. Rpl13.

Phylogenomic databases

eggNOGiKOG3295. Eukaryota.
COG4352. LUCA.
GeneTreeiENSGT00390000007818.
HOGENOMiHOG000170452.
HOVERGENiHBG001156.
InParanoidiP47963.
KOiK02873.
OMAiHCPTFRY.
OrthoDBiEOG74TX1G.
PhylomeDBiP47963.
TreeFamiTF300073.

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-6791226. Major pathway of rRNA processing in the nucleolus.
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

PROiP47963.
SOURCEiSearch...

Gene expression databases

BgeeiP47963.
CleanExiMM_RPL13.
GenevisibleiP47963. MM.

Family and domain databases

InterProiIPR001380. Ribosomal_L13e.
IPR018256. Ribosomal_L13e_CS.
[Graphical view]
PANTHERiPTHR11722. PTHR11722. 1 hit.
PfamiPF01294. Ribosomal_L13e. 1 hit.
[Graphical view]
PROSITEiPS01104. RIBOSOMAL_L13E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Palacios R., Xie X.
    Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CBA/J.
  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: Embryonic liver 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: Mammary gland.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiRL13_MOUSE
AccessioniPrimary (citable) accession number: P47963
Secondary accession number(s): Q9CRZ9, Q9DCH1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 124 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.