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Q9CXW4 (RL11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S ribosomal protein L11
Gene names
Name:Rpl11
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3

Subunit structure

Interacts with PML and MDM2. Ref.3

Subcellular location

Nucleus › nucleolus Ref.3.

Sequence similarities

Belongs to the ribosomal protein L5P family.

Ontologies

Keywords
   Cellular componentNucleus
   LigandRNA-binding
rRNA-binding
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein localization to nucleus

Inferred from mutant phenotype Ref.3. Source: UniProtKB

translation

Inferred from electronic annotation. Source: InterPro

   Cellular_componentnucleolus

Inferred from direct assay Ref.3. Source: UniProtKB

ribosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionrRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

structural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Mdm2P238044EBI-1548890,EBI-641788

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 17817760S ribosomal protein L11
PRO_0000125083

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue441Phosphothreonine By similarity
Modified residue521N6-acetyllysine By similarity
Modified residue851N6-acetyllysine By similarity

Experimental info

Sequence conflict481P → Q in BAB29059. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CXW4 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 26EC965C9239774E

FASTA17820,252
        10         20         30         40         50         60 
MAQDQGEKEN PMRELRIRKL CLNICVGESG DRLTRAAKVL EQLTGQTPVF SKARYTVRSF 

        70         80         90        100        110        120 
GIRRNEKIAV HCTVRGAKAE EILEKGLKVR EYELRKNNFS DTGNFGFGIQ EHIDLGIKYD 

       130        140        150        160        170 
PSIGIYGLDF YVVLGRPGFS IADKKRRTGC IGAKHRISKE EAMRWFQQKY DGIILPGK

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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 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(2004) [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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PML AND MDM2, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00331461.
RefSeqNP_080195.1. NM_025919.2.
UniGeneMm.276856.

3D structure databases

ProteinModelPortalQ9CXW4.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9CXW4. 2 interactions.

PTM databases

PhosphoSiteQ9CXW4.

Proteomic databases

PaxDbQ9CXW4.
PRIDEQ9CXW4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102536; ENSMUSP00000099595; ENSMUSG00000059291.
GeneID67025.
KEGGmmu:67025.

Organism-specific databases

CTD6135.
MGIMGI:1914275. Rpl11.

Phylogenomic databases

eggNOGCOG0094.
GeneTreeENSGT00390000013411.
HOGENOMHOG000231312.
HOVERGENHBG055214.
KOK02868.
OMAHMGVGES.
OrthoDBEOG4BG8X4.

Gene expression databases

ArrayExpressQ9CXW4.
BgeeQ9CXW4.
CleanExMM_RPL11.
GenevestigatorQ9CXW4.
GermOnlineENSMUSG00000070343. Mus musculus.

Family and domain databases

Gene3D3.30.1440.10. 1 hit.
InterProIPR002132. Ribosomal_L5.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
[Graphical view]
PANTHERPTHR11994. PTHR11994. 1 hit.
PfamPF00281. Ribosomal_L5. 1 hit.
PF00673. Ribosomal_L5_C. 1 hit.
[Graphical view]
PIRSFPIRSF002161. Ribosomal_L5. 1 hit.
SUPFAMSSF55282. Ribosomal_L5. 1 hit.
PROSITEPS00358. RIBOSOMAL_L5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio323340.
SOURCESearch...

Entry information

Entry nameRL11_MOUSE
AccessionPrimary (citable) accession number: Q9CXW4
Secondary accession number(s): Q3TPE3, Q6ZWY0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 94 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Ribosomal proteins

Ribosomal proteins families and list of entries

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents