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Protein

60S ribosomal protein L4

Gene

RPL4

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiR-BTA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-BTA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-BTA-6791226. Major pathway of rRNA processing in the nucleolus.
R-BTA-72689. Formation of a pool of free 40S subunits.
R-BTA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-BTA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-BTA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L4
Gene namesi
Name:RPL4
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 10

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 42242160S ribosomal protein L4PRO_0000129348Add
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 residuei266 – 2661PhosphothreonineBy similarity
Modified residuei290 – 2901PhosphoserineBy similarity
Modified residuei295 – 2951PhosphoserineBy similarity
Modified residuei300 – 3001CitrullineBy similarity
Modified residuei333 – 3331N6-acetyllysineBy similarity
Modified residuei353 – 3531N6-acetyllysineBy similarity
Modified residuei361 – 3611N6-acetyllysine; alternateBy similarity
Cross-linki361 – 361Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Modified residuei362 – 3621PhosphoserineBy similarity

Post-translational modificationi

Citrullinated by PADI4.By similarity

Keywords - PTMi

Acetylation, Citrullination, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ58DW0.
PeptideAtlasiQ58DW0.
PRIDEiQ58DW0.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000006866.

Structurei

3D structure databases

ProteinModelPortaliQ58DW0.
SMRiQ58DW0. Positions 7-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi361 – 41959Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein L4P family.Curated

Phylogenomic databases

eggNOGiKOG1475. Eukaryota.
COG0088. LUCA.
GeneTreeiENSGT00390000018145.
HOGENOMiHOG000107331.
HOVERGENiHBG001453.
InParanoidiQ58DW0.
KOiK02930.
OMAiFQACARP.
OrthoDBiEOG73RBBP.
TreeFamiTF300593.

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.

Q58DW0-1 [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 GHRIEEVPEL
160 170 180 190 200
PLVVEDKVEG YKKTKEAVLL LKKLKAWNDI KKVYASQRMR AGKGKMRNRR
210 220 230 240 250
RIQRRGPCII YNEDNGIIKA FRNIPGITLL NVSKLNILKL APGGHVGRFC
260 270 280 290 300
IWTESAFRKL DELYGTWRKA ASLKSNYNLP MHKMLNTDLS RILKSPEIQR
310 320 330 340 350
ALRAPRKKIH RRVLKKNPLK NLRIMLKLNP YAKTMRRNTI LRQARNHKIR
360 370 380 390 400
MDKAAAALEA KSDQKGVQGK KPVVGNKEKK AVGDKKLKKP VVGKKAAGTK
410 420
KPAAEKKPTE KKPTSEEKKA AA
Length:422
Mass (Da):47,412
Last modified:January 23, 2007 - v3
Checksum:iADC3F06A6EA3F8E3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021487 mRNA. Translation: AAX46334.1.
BC102521 mRNA. Translation: AAI02522.1.
RefSeqiNP_001014894.1. NM_001014894.1.
UniGeneiBt.48893.

Genome annotation databases

EnsembliENSBTAT00000006866; ENSBTAP00000006866; ENSBTAG00000005211.
GeneIDi510547.
KEGGibta:510547.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021487 mRNA. Translation: AAX46334.1.
BC102521 mRNA. Translation: AAI02522.1.
RefSeqiNP_001014894.1. NM_001014894.1.
UniGeneiBt.48893.

3D structure databases

ProteinModelPortaliQ58DW0.
SMRiQ58DW0. Positions 7-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000006866.

Proteomic databases

PaxDbiQ58DW0.
PeptideAtlasiQ58DW0.
PRIDEiQ58DW0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000006866; ENSBTAP00000006866; ENSBTAG00000005211.
GeneIDi510547.
KEGGibta:510547.

Organism-specific databases

CTDi6124.

Phylogenomic databases

eggNOGiKOG1475. Eukaryota.
COG0088. LUCA.
GeneTreeiENSGT00390000018145.
HOGENOMiHOG000107331.
HOVERGENiHBG001453.
InParanoidiQ58DW0.
KOiK02930.
OMAiFQACARP.
OrthoDBiEOG73RBBP.
TreeFamiTF300593.

Enzyme and pathway databases

ReactomeiR-BTA-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-BTA-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-BTA-6791226. Major pathway of rRNA processing in the nucleolus.
R-BTA-72689. Formation of a pool of free 40S subunits.
R-BTA-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-BTA-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-BTA-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.

Entry informationi

Entry nameiRL4_BOVIN
AccessioniPrimary (citable) accession number: Q58DW0
Secondary accession number(s): Q3T088
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 74 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.