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Protein

60S ribosomal protein L4

Gene

Rpl4

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

Functioni

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

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 L4
Gene namesi
Name:Rpl4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1915141. Rpl4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 41941860S ribosomal protein L4PRO_0000129351Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei14 – 141N6-acetyllysineBy similarity
Modified residuei106 – 1061N6-acetyllysineBy similarity
Modified residuei259 – 2591N6-acetyllysine1 Publication
Modified residuei295 – 2951Phosphoserine1 Publication
Modified residuei300 – 3001Citrulline1 Publication
Modified residuei333 – 3331N6-acetyllysineBy similarity
Modified residuei353 – 3531N6-acetyllysine1 Publication
Modified residuei364 – 3641N6-acetyllysine1 Publication
Modified residuei365 – 3651PhosphoserineBy similarity

Post-translational modificationi

Citrullinated by PADI4.1 Publication

Keywords - PTMi

Acetylation, Citrullination, Phosphoprotein

Proteomic databases

MaxQBiQ9D8E6.
PaxDbiQ9D8E6.
PRIDEiQ9D8E6.

PTM databases

PhosphoSiteiQ9D8E6.

Expressioni

Gene expression databases

BgeeiQ9D8E6.
CleanExiMM_RPL4.
ExpressionAtlasiQ9D8E6. baseline and differential.
GenevisibleiQ9D8E6. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi212515. 7 interactions.
IntActiQ9D8E6. 9 interactions.
MINTiMINT-1859608.
STRINGi10090.ENSMUSP00000034966.

Structurei

3D structure databases

ProteinModelPortaliQ9D8E6.
SMRiQ9D8E6. Positions 4-266.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi307 – 419113Lys-richAdd
BLAST

Sequence similaritiesi

Belongs to the ribosomal protein L4P family.Curated

Phylogenomic databases

eggNOGiCOG0088.
GeneTreeiENSGT00390000018145.
HOGENOMiHOG000107331.
HOVERGENiHBG001453.
InParanoidiQ9D8E6.
KOiK02930.
OMAiFQACARP.
OrthoDBiEOG73RBBP.
PhylomeDBiQ9D8E6.
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.

Q9D8E6-1 [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 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
VKKLEAAATA LATKSEKVVP EKGTADKKPA VGKKGKKVDA KKQKPAGKKV
410
VAKKPAEKKP TTEEKKPAA
Length:419
Mass (Da):47,154
Last modified:January 23, 2007 - v3
Checksum:iE736E656A60BE85B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti161 – 1611Y → F in BAB27375 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008098 mRNA. Translation: BAB25458.1.
AK011068 mRNA. Translation: BAB27375.1.
BC003459 mRNA. Translation: AAH03459.1.
CCDSiCCDS40667.1.
RefSeqiNP_077174.1. NM_024212.4.
UniGeneiMm.280083.

Genome annotation databases

EnsembliENSMUST00000034966; ENSMUSP00000034966; ENSMUSG00000032399.
GeneIDi67891.
KEGGimmu:67891.
UCSCiuc009qbn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008098 mRNA. Translation: BAB25458.1.
AK011068 mRNA. Translation: BAB27375.1.
BC003459 mRNA. Translation: AAH03459.1.
CCDSiCCDS40667.1.
RefSeqiNP_077174.1. NM_024212.4.
UniGeneiMm.280083.

3D structure databases

ProteinModelPortaliQ9D8E6.
SMRiQ9D8E6. Positions 4-266.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi212515. 7 interactions.
IntActiQ9D8E6. 9 interactions.
MINTiMINT-1859608.
STRINGi10090.ENSMUSP00000034966.

PTM databases

PhosphoSiteiQ9D8E6.

Proteomic databases

MaxQBiQ9D8E6.
PaxDbiQ9D8E6.
PRIDEiQ9D8E6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034966; ENSMUSP00000034966; ENSMUSG00000032399.
GeneIDi67891.
KEGGimmu:67891.
UCSCiuc009qbn.1. mouse.

Organism-specific databases

CTDi6124.
MGIiMGI:1915141. Rpl4.

Phylogenomic databases

eggNOGiCOG0088.
GeneTreeiENSGT00390000018145.
HOGENOMiHOG000107331.
HOVERGENiHBG001453.
InParanoidiQ9D8E6.
KOiK02930.
OMAiFQACARP.
OrthoDBiEOG73RBBP.
PhylomeDBiQ9D8E6.
TreeFamiTF300593.

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

ChiTaRSiRpl4. mouse.
NextBioi325862.
PROiQ9D8E6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D8E6.
CleanExiMM_RPL4.
ExpressionAtlasiQ9D8E6. baseline and differential.
GenevisibleiQ9D8E6. MM.

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 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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryonic liver and Small intestine.
  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].
  3. Kanor S., Quadroni M., Bienvenut W.V.
    Submitted (MAR-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 165-171 AND 353-363, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Skeletal muscle.
  4. "Importins fulfill a dual function as nuclear import receptors and cytoplasmic chaperones for exposed basic domains."
    Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.
    EMBO J. 21:377-386(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IPO9.
  5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-259; LYS-353 AND LYS-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. Cited for: CITRULLINATION AT ARG-300.

Entry informationi

Entry nameiRL4_MOUSE
AccessioniPrimary (citable) accession number: Q9D8E6
Secondary accession number(s): Q9CY08
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 26, 2002
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 122 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, Direct protein sequencing, 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.