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Protein

60S ribosomal protein L11

Gene

Rpl11

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L11
Gene namesi
Name:Rpl11
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi1308681. Rpl11.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: RGD
  • cytosolic ribosome Source: RGD
  • nucleolus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 17817760S ribosomal protein L11PRO_0000125085Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei44 – 441PhosphothreonineBy similarity
Modified residuei47 – 471PhosphothreonineBy similarity
Modified residuei52 – 521N6-acetyllysineBy similarity
Modified residuei85 – 851N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP62914.
PRIDEiP62914.

PTM databases

iPTMnetiP62914.

Expressioni

Gene expression databases

ExpressionAtlasiP62914. baseline and differential.
GenevisibleiP62914. RN.

Interactioni

Subunit structurei

Interacts with PML and MDM2.By similarity

GO - Molecular functioni

  • peroxisome proliferator activated receptor binding Source: RGD

Protein-protein interaction databases

BioGridi263597. 2 interactions.
IntActiP62914. 2 interactions.
MINTiMINT-4579402.
STRINGi10116.ENSRNOP00000037110.

Structurei

3D structure databases

ProteinModelPortaliP62914.
SMRiP62914. Positions 10-172.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L5P family.Curated

Phylogenomic databases

eggNOGiKOG0397. Eukaryota.
COG0094. LUCA.
GeneTreeiENSGT00390000013411.
HOGENOMiHOG000231312.
HOVERGENiHBG055214.
InParanoidiP62914.
OMAiEDTMAWF.
OrthoDBiEOG7ZPNMB.
PhylomeDBiP62914.
TreeFamiTF300017.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR031309. Ribosomal_L5_C.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
IPR031310. Ribosomal_L5_N.
[Graphical view]
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.

P62914-1 [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 - v2
Checksum:i26EC965C9239774E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62146 mRNA. Translation: CAA44072.1.
PIRiJT0606. R5RT11.
RefSeqiXP_006239286.1. XM_006239224.2.
UniGeneiRn.14687.

Genome annotation databases

EnsembliENSRNOT00000030043; ENSRNOP00000037110; ENSRNOG00000026260.
GeneIDi362631.
UCSCiRGD:1308681. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62146 mRNA. Translation: CAA44072.1.
PIRiJT0606. R5RT11.
RefSeqiXP_006239286.1. XM_006239224.2.
UniGeneiRn.14687.

3D structure databases

ProteinModelPortaliP62914.
SMRiP62914. Positions 10-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi263597. 2 interactions.
IntActiP62914. 2 interactions.
MINTiMINT-4579402.
STRINGi10116.ENSRNOP00000037110.

PTM databases

iPTMnetiP62914.

Proteomic databases

PaxDbiP62914.
PRIDEiP62914.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000030043; ENSRNOP00000037110; ENSRNOG00000026260.
GeneIDi362631.
UCSCiRGD:1308681. rat.

Organism-specific databases

CTDi6135.
RGDi1308681. Rpl11.

Phylogenomic databases

eggNOGiKOG0397. Eukaryota.
COG0094. LUCA.
GeneTreeiENSGT00390000013411.
HOGENOMiHOG000231312.
HOVERGENiHBG055214.
InParanoidiP62914.
OMAiEDTMAWF.
OrthoDBiEOG7ZPNMB.
PhylomeDBiP62914.
TreeFamiTF300017.

Miscellaneous databases

PROiP62914.

Gene expression databases

ExpressionAtlasiP62914. baseline and differential.
GenevisibleiP62914. RN.

Family and domain databases

Gene3Di3.30.1440.10. 1 hit.
InterProiIPR002132. Ribosomal_L5.
IPR031309. Ribosomal_L5_C.
IPR020929. Ribosomal_L5_CS.
IPR022803. Ribosomal_L5_domain.
IPR031310. Ribosomal_L5_N.
[Graphical view]
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

  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. Bienvenut W.V., von Kriegsheim A., Kolch W.
    Submitted (JUN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 39-52 AND 170-178, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fibroblast.

Entry informationi

Entry nameiRL11_RAT
AccessioniPrimary (citable) accession number: P62914
Secondary accession number(s): P25121, P39026, Q9Y674
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Ribosomal proteins
    Ribosomal proteins families and list of entries
  2. 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.