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Protein

60S ribosomal protein L11

Gene

Rpl11

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Binds to 5S ribosomal RNA (By similarity). Required for rRNA maturation and formation of the 60S ribosomal subunits (By similarity). Promotes nucleolar location of PML.By similarity1 Publication

GO - Molecular functioni

  1. poly(A) RNA binding Source: Ensembl
  2. rRNA binding Source: UniProtKB-KW
  3. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. protein localization to nucleus Source: UniProtKB
  2. protein targeting Source: Ensembl
  3. ribosomal large subunit biogenesis Source: Ensembl
  4. rRNA processing Source: Ensembl
  5. translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L11
Gene namesi
Name:Rpl11
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1914275. Rpl11.

Subcellular locationi

Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. membrane Source: Ensembl
  4. nucleolus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 17817760S ribosomal protein L11PRO_0000125083Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei44 – 441PhosphothreonineBy similarity
Modified residuei52 – 521N6-acetyllysineBy similarity
Modified residuei85 – 851N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9CXW4.
PaxDbiQ9CXW4.
PRIDEiQ9CXW4.

PTM databases

PhosphoSiteiQ9CXW4.

Expressioni

Gene expression databases

BgeeiQ9CXW4.
CleanExiMM_RPL11.
ExpressionAtlasiQ9CXW4. baseline and differential.
GenevestigatoriQ9CXW4.

Interactioni

Subunit structurei

Interacts with PML and MDM2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Mdm2P238044EBI-1548890,EBI-641788

Protein-protein interaction databases

BioGridi211883. 13 interactions.
IntActiQ9CXW4. 6 interactions.
MINTiMINT-1859586.

Structurei

3D structure databases

ProteinModelPortaliQ9CXW4.
SMRiQ9CXW4. Positions 9-176.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L5P family.Curated

Phylogenomic databases

eggNOGiCOG0094.
GeneTreeiENSGT00390000013411.
HOGENOMiHOG000231312.
HOVERGENiHBG055214.
InParanoidiQ9CXW4.
KOiK02868.
OMAiFGMDVAI.
OrthoDBiEOG7ZPNMB.
PhylomeDBiQ9CXW4.
TreeFamiTF300017.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
[Graphical view]
PANTHERiPTHR11994. PTHR11994. 1 hit.
PfamiPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMiSSF55282. SSF55282. 1 hit.
PROSITEiPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9CXW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQDQGEKEN PMRELRIRKL CLNICVGESG DRLTRAAKVL EQLTGQTPVF
60 70 80 90 100
SKARYTVRSF GIRRNEKIAV HCTVRGAKAE EILEKGLKVR EYELRKNNFS
110 120 130 140 150
DTGNFGFGIQ EHIDLGIKYD PSIGIYGLDF YVVLGRPGFS IADKKRRTGC
160 170
IGAKHRISKE EAMRWFQQKY DGIILPGK
Length:178
Mass (Da):20,252
Last modified:January 23, 2007 - v4
Checksum:i26EC965C9239774E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481P → Q in BAB29059 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002998 mRNA. Translation: BAB22504.1.
AK008422 mRNA. Translation: BAB25660.1.
AK011211 mRNA. Translation: BAB27470.1.
AK011800 mRNA. Translation: BAB27850.1.
AK013923 mRNA. Translation: BAB29059.1.
AK088967 mRNA. Translation: BAC40676.1.
AK153486 mRNA. Translation: BAE32034.1.
AK164445 mRNA. Translation: BAE37793.1.
AK169053 mRNA. Translation: BAE40841.1.
BC025077 mRNA. Translation: AAH25077.1.
BC069896 mRNA. Translation: AAH69896.1.
CCDSiCCDS18799.1.
RefSeqiNP_080195.1. NM_025919.2.
UniGeneiMm.276856.

Genome annotation databases

EnsembliENSMUST00000102536; ENSMUSP00000099595; ENSMUSG00000059291.
GeneIDi67025.
KEGGimmu:67025.
UCSCiuc008vhr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK002998 mRNA. Translation: BAB22504.1.
AK008422 mRNA. Translation: BAB25660.1.
AK011211 mRNA. Translation: BAB27470.1.
AK011800 mRNA. Translation: BAB27850.1.
AK013923 mRNA. Translation: BAB29059.1.
AK088967 mRNA. Translation: BAC40676.1.
AK153486 mRNA. Translation: BAE32034.1.
AK164445 mRNA. Translation: BAE37793.1.
AK169053 mRNA. Translation: BAE40841.1.
BC025077 mRNA. Translation: AAH25077.1.
BC069896 mRNA. Translation: AAH69896.1.
CCDSiCCDS18799.1.
RefSeqiNP_080195.1. NM_025919.2.
UniGeneiMm.276856.

3D structure databases

ProteinModelPortaliQ9CXW4.
SMRiQ9CXW4. Positions 9-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211883. 13 interactions.
IntActiQ9CXW4. 6 interactions.
MINTiMINT-1859586.

PTM databases

PhosphoSiteiQ9CXW4.

Proteomic databases

MaxQBiQ9CXW4.
PaxDbiQ9CXW4.
PRIDEiQ9CXW4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102536; ENSMUSP00000099595; ENSMUSG00000059291.
GeneIDi67025.
KEGGimmu:67025.
UCSCiuc008vhr.1. mouse.

Organism-specific databases

CTDi6135.
MGIiMGI:1914275. Rpl11.

Phylogenomic databases

eggNOGiCOG0094.
GeneTreeiENSGT00390000013411.
HOGENOMiHOG000231312.
HOVERGENiHBG055214.
InParanoidiQ9CXW4.
KOiK02868.
OMAiFGMDVAI.
OrthoDBiEOG7ZPNMB.
PhylomeDBiQ9CXW4.
TreeFamiTF300017.

Enzyme and pathway databases

ReactomeiREACT_279505. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_292264. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_302277. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_308559. Formation of a pool of free 40S subunits.
REACT_311765. Peptide chain elongation.
REACT_319670. Eukaryotic Translation Termination.
REACT_331340. SRP-dependent cotranslational protein targeting to membrane.
REACT_340387. L13a-mediated translational silencing of Ceruloplasmin expression.

Miscellaneous databases

NextBioi323340.
PROiQ9CXW4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9CXW4.
CleanExiMM_RPL11.
ExpressionAtlasiQ9CXW4. baseline and differential.
GenevestigatoriQ9CXW4.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
[Graphical view]
PANTHERiPTHR11994. PTHR11994. 1 hit.
PfamiPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFiPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMiSSF55282. SSF55282. 1 hit.
PROSITEiPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Brain, Embryonic head, Eye, Small intestine and Thymus.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Colon and Mammary tumor.
  3. "PML regulates p53 stability by sequestering Mdm2 to the nucleolus."
    Bernardi R., Scaglioni P.P., Bergmann S., Horn H.F., Vousden K.H., Pandolfi P.P.
    Nat. Cell Biol. 6:665-672(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PML AND MDM2, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiRL11_MOUSE
AccessioniPrimary (citable) accession number: Q9CXW4
Secondary accession number(s): Q3TPE3, Q6ZWY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: January 23, 2007
Last modified: April 1, 2015
This is version 112 of the entry and version 4 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

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.