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P36578 (RL4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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

Names and origin

Protein namesRecommended name:
60S ribosomal protein L4
Alternative name(s):
60S ribosomal protein L1
Gene names
Name:RPL4
Synonyms:RPL1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length427 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Subunit structure

May bind IPO9 with low affinity. Interacts with RBM3 By similarity. Ref.9

Post-translational modification

Citrullinated by PADI4 By similarity.

Sequence similarities

Belongs to the ribosomal protein L4P family.

Ontologies

Keywords
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
Citrullination
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

translation

Non-traceable author statement PubMed 12962325. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

cytosolic large ribosomal subunit

Inferred from direct assay PubMed 12962325. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay PubMed 21630459PubMed 22720776. Source: UniProt

ribonucleoprotein complex

Inferred from direct assay PubMed 18809582. Source: MGI

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 23275563. Source: IntAct

structural constituent of ribosome

Non-traceable author statement PubMed 12962325. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HTTP428582EBI-348313,EBI-466029

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 42742660S ribosomal protein L4
PRO_0000129350

Regions

Compositional bias364 – 42764Lys-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.12
Modified residue141N6-acetyllysine Ref.13
Modified residue1061N6-acetyllysine Ref.13
Modified residue2591N6-acetyllysine By similarity
Modified residue2951Phosphoserine Ref.10 Ref.14
Modified residue3001Citrulline By similarity
Modified residue3331N6-acetyllysine Ref.13
Modified residue3531N6-acetyllysine By similarity
Modified residue3641N6-acetyllysine By similarity
Modified residue3651Phosphoserine Ref.10 Ref.14

Experimental info

Sequence conflict31C → V in AAA60281. Ref.1
Sequence conflict361I → M in AAA60281. Ref.1
Sequence conflict631S → R in AAA60281. Ref.1
Sequence conflict1471V → F in AAA60281. Ref.1
Sequence conflict2011Missing in AAA60281. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P36578 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: 4785ED31699CD792

FASTA42747,697
        10         20         30         40         50         60 
MACARPLISV YSEKGESSGK NVTLPAVFKA PIRPDIVNFV HTNLRKNNRQ PYAVSELAGH 

        70         80         90        100        110        120 
QTSAESWGTG RAVARIPRVR GGGTHRSGQG AFGNMCRGGR MFAPTKTWRR WHRRVNTTQK 

       130        140        150        160        170        180 
RYAICSALAA SALPALVMSK GHRIEEVPEL PLVVEDKVEG YKKTKEAVLL LKKLKAWNDI 

       190        200        210        220        230        240 
KKVYASQRMR AGKGKMRNRR RIQRRGPCII YNEDNGIIKA FRNIPGITLL NVSKLNILKL 

       250        260        270        280        290        300 
APGGHVGRFC IWTESAFRKL DELYGTWRKA ASLKSNYNLP MHKMINTDLS RILKSPEIQR 

       310        320        330        340        350        360 
ALRAPRKKIH RRVLKKNPLK NLRIMLKLNP YAKTMRRNTI LRQARNHKLR VDKAAAAAAA 

       370        380        390        400        410        420 
LQAKSDEKAA VAGKKPVVGK KGKKAAVGVK KQKKPLVGKK AAATKKPAPE KKPAEKKPTT 


EEKKPAA 

« Hide

References

« Hide 'large scale' references
[1]"Human ribosomal protein L4: cloning and sequencing of the cDNA and primary structure of the protein."
Bagni C., Mariottini P., Annesi F., Amaldi F.
Biochim. Biophys. Acta 1216:475-478(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]Bagni C.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]Kato S.
Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Lymphoma.
[4]"The human ribosomal protein genes: sequencing and comparative analysis of 73 genes."
Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S., Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.
Genome Res. 12:379-390(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Skeletal muscle.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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].
Tissue: Colon, Embryonic stem cell, Eye, Hippocampus, Muscle, Pancreas and Skin.
[8]Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
Submitted (MAY-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-13, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: T-cell.
[9]"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.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14; LYS-106 AND LYS-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295 AND SER-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Structures of the human and Drosophila 80S ribosome."
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.
Nature 497:80-85(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L20868 mRNA. Translation: AAA60281.2.
D23660 mRNA. Translation: BAA04887.1.
AB061820 Genomic DNA. Translation: BAB79458.1.
AK291117 mRNA. Translation: BAF83806.1.
AK291859 mRNA. Translation: BAF84548.1.
CH471082 Genomic DNA. Translation: EAW77776.1.
BC001365 mRNA. Translation: AAH01365.1.
BC005817 mRNA. Translation: AAH05817.1.
BC007748 mRNA. Translation: AAH07748.1.
BC007996 mRNA. Translation: AAH07996.1.
BC009888 mRNA. Translation: AAH09888.1.
BC010151 mRNA. Translation: AAH10151.1.
BC014653 mRNA. Translation: AAH14653.1.
BC066925 mRNA. Translation: AAH66925.1.
BC095427 mRNA. Translation: AAH95427.1.
CCDSCCDS10218.1.
PIRT09551.
RefSeqNP_000959.2. NM_000968.3.
UniGeneHs.186350.
Hs.644628.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00C1-427[»]
ProteinModelPortalP36578.
SMRP36578. Positions 4-371.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112044. 151 interactions.
DIPDIP-27559N.
IntActP36578. 33 interactions.
MINTMINT-1034893.
STRING9606.ENSP00000311430.

PTM databases

PhosphoSiteP36578.

Polymorphism databases

DMDM22002063.

2D gel databases

SWISS-2DPAGEP36578.

Proteomic databases

MaxQBP36578.
PaxDbP36578.
PRIDEP36578.

Protocols and materials databases

DNASU6124.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307961; ENSP00000311430; ENSG00000174444.
GeneID6124.
KEGGhsa:6124.
UCSCuc002apv.3. human.

Organism-specific databases

CTD6124.
GeneCardsGC15M066790.
HGNCHGNC:10353. RPL4.
HPAHPA034600.
MIM180479. gene.
neXtProtNX_P36578.
PharmGKBPA34749.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0088.
HOVERGENHBG001453.
InParanoidP36578.
KOK02930.
OMAKAKMLKP.
OrthoDBEOG73RBBP.
PhylomeDBP36578.
TreeFamTF300593.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressP36578.
BgeeP36578.
CleanExHS_RPL4.
GenevestigatorP36578.

Family and domain databases

Gene3D3.40.1370.10. 1 hit.
InterProIPR025755. Ribos_L4_C_dom.
IPR002136. Ribosomal_L4/L1e.
IPR013000. Ribosomal_L4/L1e_euk/arc_CS.
IPR023574. Ribosomal_L4_dom.
[Graphical view]
PfamPF14374. Ribos_L4_asso_C. 1 hit.
PF00573. Ribosomal_L4. 1 hit.
[Graphical view]
SUPFAMSSF52166. SSF52166. 1 hit.
PROSITEPS00939. RIBOSOMAL_L1E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPL4. human.
GeneWikiRibosomal_protein_L4.
GenomeRNAi6124.
NextBio23787.
PMAP-CutDBP36578.
PROP36578.
SOURCESearch...

Entry information

Entry nameRL4_HUMAN
AccessionPrimary (citable) accession number: P36578
Secondary accession number(s): A8K502 expand/collapse secondary AC list , P39029, Q4VBR0, Q969Z9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 146 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM