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Protein

60S ribosomal protein L4

Gene

Rpl4

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

Functioni

GO - Molecular functioni

  • 5S rRNA binding Source: RGD
  • structural constituent of ribosome Source: InterPro

GO - Biological processi

  • brain development Source: RGD
  • brainstem development Source: RGD
  • cell differentiation Source: RGD
  • cellular response to organonitrogen compound Source: RGD
  • positive regulation of axon extension Source: RGD
  • positive regulation of axonogenesis Source: RGD
  • translation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L4
Alternative name(s):
60S ribosomal protein L1
Gene namesi
Name:Rpl4
Synonyms:Rpl1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi619824. Rpl4.

Subcellular locationi

GO - Cellular componenti

  • A band Source: RGD
  • cytosolic large ribosomal subunit Source: RGD
  • large ribosomal subunit Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 42142060S ribosomal protein L4PRO_0000129353Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei14 – 141N6-acetyllysineBy similarity
Modified residuei106 – 1061N6-acetyllysineBy similarity
Modified residuei259 – 2591N6-acetyllysineBy similarity
Modified residuei290 – 2901PhosphoserineCombined sources
Modified residuei295 – 2951PhosphoserineCombined sources
Modified residuei300 – 3001CitrullineBy similarity
Modified residuei333 – 3331N6-acetyllysineBy similarity
Modified residuei353 – 3531N6-acetyllysineBy similarity
Modified residuei364 – 3641N6-acetyllysineBy similarity
Modified residuei365 – 3651PhosphoserineBy similarity

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Phosphoprotein

Proteomic databases

PaxDbiP50878.
PRIDEiP50878.

PTM databases

iPTMnetiP50878.
PhosphoSiteiP50878.

Interactioni

Subunit structurei

May bind IPO9 with low affinity (By similarity). Interacts with RBM3.By similarity1 Publication

Protein-protein interaction databases

BioGridi249017. 4 interactions.
IntActiP50878. 1 interaction.
MINTiMINT-4566156.
STRINGi10116.ENSRNOP00000013462.

Structurei

3D structure databases

ProteinModelPortaliP50878.
SMRiP50878. Positions 7-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi307 – 421115Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein L4P family.Curated

Phylogenomic databases

eggNOGiKOG1475. Eukaryota.
COG0088. LUCA.
HOGENOMiHOG000107331.
HOVERGENiHBG001453.
InParanoidiP50878.
KOiK02930.
PhylomeDBiP50878.

Family and domain databases

Gene3Di3.40.1370.10. 1 hit.
InterProiIPR025755. Ribos_L4_C_dom.
IPR002136. Ribosomal_L4/L1e.
IPR013000. Ribosomal_L4/L1e_euk/arc_CS.
IPR023574. Ribosomal_L4_dom.
[Graphical view]
PfamiPF14374. Ribos_L4_asso_C. 1 hit.
PF00573. Ribosomal_L4. 1 hit.
[Graphical view]
SUPFAMiSSF52166. SSF52166. 1 hit.
PROSITEiPS00939. RIBOSOMAL_L1E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P50878-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MACARPLISV YSEKGESSGK NVTLPAVFKA PIRPDIVNFV HTNLRKNNRQ
60 70 80 90 100
PYAVSELAGH QTSAESWGTG RAVARIPRVR GGGTHRSGQG AFGNMCRGGR
110 120 130 140 150
MFAPTKTWRR WHRRVNTTQK RYAICSALAA SALPALVMSK GHCVEEVPEL
160 170 180 190 200
PLVVEDKVES YKKTKEAVQL LKKLKAWNDI KKVYASQRMR AGKGKMRNRR
210 220 230 240 250
RIQRRGPCII YNEDNGIIKA FRNIPGITLL NVSKLNILKL APGGHVGRFC
260 270 280 290 300
IWTESAFRKL DELYGTWRKA ASLKSNYNLP MHKMMNTDLS RILKSPEIQR
310 320 330 340 350
ALRAPRKKIH RRVLKKNPLK NLRIMLKLNP YAKTMRRNTI LRQARNHKLR
360 370 380 390 400
VKKLEAAAAA LAAKSEKIVP EKGAGDKKPA VGKKGKKPVD AKKLKKPAGK
410 420
KVVTKKPAEK KPTTEEKKSA A
Length:421
Mass (Da):47,257
Last modified:January 23, 2007 - v3
Checksum:i08C82C1D7A49AAC5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82180 mRNA. Translation: CAA57671.1.
PIRiJC4277.
RefSeqiNP_071955.1. NM_022510.1.
UniGeneiRn.1133.

Genome annotation databases

GeneIDi64302.
KEGGirno:64302.
UCSCiRGD:619824. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82180 mRNA. Translation: CAA57671.1.
PIRiJC4277.
RefSeqiNP_071955.1. NM_022510.1.
UniGeneiRn.1133.

3D structure databases

ProteinModelPortaliP50878.
SMRiP50878. Positions 7-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249017. 4 interactions.
IntActiP50878. 1 interaction.
MINTiMINT-4566156.
STRINGi10116.ENSRNOP00000013462.

PTM databases

iPTMnetiP50878.
PhosphoSiteiP50878.

Proteomic databases

PaxDbiP50878.
PRIDEiP50878.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64302.
KEGGirno:64302.
UCSCiRGD:619824. rat.

Organism-specific databases

CTDi6124.
RGDi619824. Rpl4.

Phylogenomic databases

eggNOGiKOG1475. Eukaryota.
COG0088. LUCA.
HOGENOMiHOG000107331.
HOVERGENiHBG001453.
InParanoidiP50878.
KOiK02930.
PhylomeDBiP50878.

Miscellaneous databases

NextBioi612934.
PROiP50878.

Family and domain databases

Gene3Di3.40.1370.10. 1 hit.
InterProiIPR025755. Ribos_L4_C_dom.
IPR002136. Ribosomal_L4/L1e.
IPR013000. Ribosomal_L4/L1e_euk/arc_CS.
IPR023574. Ribosomal_L4_dom.
[Graphical view]
PfamiPF14374. Ribos_L4_asso_C. 1 hit.
PF00573. Ribosomal_L4. 1 hit.
[Graphical view]
SUPFAMiSSF52166. SSF52166. 1 hit.
PROSITEiPS00939. RIBOSOMAL_L1E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The primary structures of rat ribosomal proteins L4 and L41."
    Chan Y.-L., Olvera J., Wool I.G.
    Biochem. Biophys. Res. Commun. 214:810-818(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "Cold stress-induced protein Rbm3 binds 60S ribosomal subunits, alters microRNA levels, and enhances global protein synthesis."
    Dresios J., Aschrafi A., Owens G.C., Vanderklish P.W., Edelman G.M., Mauro V.P.
    Proc. Natl. Acad. Sci. U.S.A. 102:1865-1870(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBM3.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-290 AND SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRL4_RAT
AccessioniPrimary (citable) accession number: P50878
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 98 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. 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.