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P36578

- RL4_HUMAN

UniProt

P36578 - RL4_HUMAN

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Protein

60S ribosomal protein L4

Gene
RPL4, RPL1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein binding Source: IntAct
  3. RNA binding Source: ProtInc
  4. structural constituent of ribosome Source: UniProtKB

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. mRNA metabolic process Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  5. RNA metabolic process Source: Reactome
  6. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  7. translation Source: UniProtKB
  8. translational elongation Source: Reactome
  9. translational initiation Source: Reactome
  10. translational termination Source: Reactome
  11. viral life cycle Source: Reactome
  12. viral process Source: Reactome
  13. viral transcription Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L4
Alternative name(s):
60S ribosomal protein L1
Gene namesi
Name:RPL4
Synonyms:RPL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:10353. RPL4.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. cytosolic large ribosomal subunit Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProt
  5. nucleolus Source: HPA
  6. nucleus Source: UniProt
  7. ribonucleoprotein complex Source: MGI
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34749.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 42742660S ribosomal protein L4PRO_0000129350Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei14 – 141N6-acetyllysine1 Publication
Modified residuei106 – 1061N6-acetyllysine1 Publication
Modified residuei259 – 2591N6-acetyllysine By similarity
Modified residuei295 – 2951Phosphoserine2 Publications
Modified residuei300 – 3001Citrulline By similarity
Modified residuei333 – 3331N6-acetyllysine1 Publication
Modified residuei353 – 3531N6-acetyllysine By similarity
Modified residuei364 – 3641N6-acetyllysine By similarity
Modified residuei365 – 3651Phosphoserine2 Publications

Post-translational modificationi

Citrullinated by PADI4 By similarity.

Keywords - PTMi

Acetylation, Citrullination, Phosphoprotein

Proteomic databases

MaxQBiP36578.
PaxDbiP36578.
PRIDEiP36578.

2D gel databases

SWISS-2DPAGEP36578.

PTM databases

PhosphoSiteiP36578.

Miscellaneous databases

PMAP-CutDBP36578.

Expressioni

Gene expression databases

ArrayExpressiP36578.
BgeeiP36578.
CleanExiHS_RPL4.
GenevestigatoriP36578.

Organism-specific databases

HPAiHPA034600.

Interactioni

Subunit structurei

May bind IPO9 with low affinity. Interacts with RBM3 By similarity.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
HTTP428582EBI-348313,EBI-466029

Protein-protein interaction databases

BioGridi112044. 139 interactions.
DIPiDIP-27559N.
IntActiP36578. 33 interactions.
MINTiMINT-1034893.
STRINGi9606.ENSP00000311430.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Belectron microscopy5.00C1-427[»]
ProteinModelPortaliP36578.
SMRiP36578. Positions 4-371.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi364 – 42764Lys-richAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0088.
HOVERGENiHBG001453.
InParanoidiP36578.
KOiK02930.
OMAiKAKMLKP.
OrthoDBiEOG73RBBP.
PhylomeDBiP36578.
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.

P36578-1 [UniParc]FASTAAdd to Basket

« Hide

MACARPLISV YSEKGESSGK NVTLPAVFKA PIRPDIVNFV HTNLRKNNRQ    50
PYAVSELAGH QTSAESWGTG RAVARIPRVR GGGTHRSGQG AFGNMCRGGR 100
MFAPTKTWRR WHRRVNTTQK RYAICSALAA SALPALVMSK GHRIEEVPEL 150
PLVVEDKVEG YKKTKEAVLL LKKLKAWNDI KKVYASQRMR AGKGKMRNRR 200
RIQRRGPCII YNEDNGIIKA FRNIPGITLL NVSKLNILKL APGGHVGRFC 250
IWTESAFRKL DELYGTWRKA ASLKSNYNLP MHKMINTDLS RILKSPEIQR 300
ALRAPRKKIH RRVLKKNPLK NLRIMLKLNP YAKTMRRNTI LRQARNHKLR 350
VDKAAAAAAA LQAKSDEKAA VAGKKPVVGK KGKKAAVGVK KQKKPLVGKK 400
AAATKKPAPE KKPAEKKPTT EEKKPAA 427
Length:427
Mass (Da):47,697
Last modified:January 23, 2007 - v5
Checksum:i4785ED31699CD792
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31C → V in AAA60281. 1 Publication
Sequence conflicti36 – 361I → M in AAA60281. 1 Publication
Sequence conflicti63 – 631S → R in AAA60281. 1 Publication
Sequence conflicti147 – 1471V → F in AAA60281. 1 Publication
Sequence conflicti201 – 2011Missing in AAA60281. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS10218.1.
PIRiT09551.
RefSeqiNP_000959.2. NM_000968.3.
UniGeneiHs.186350.
Hs.644628.

Genome annotation databases

EnsembliENST00000307961; ENSP00000311430; ENSG00000174444.
GeneIDi6124.
KEGGihsa:6124.
UCSCiuc002apv.3. human.

Polymorphism databases

DMDMi22002063.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS10218.1.
PIRi T09551.
RefSeqi NP_000959.2. NM_000968.3.
UniGenei Hs.186350.
Hs.644628.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3J3B electron microscopy 5.00 C 1-427 [» ]
ProteinModelPortali P36578.
SMRi P36578. Positions 4-371.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112044. 139 interactions.
DIPi DIP-27559N.
IntActi P36578. 33 interactions.
MINTi MINT-1034893.
STRINGi 9606.ENSP00000311430.

PTM databases

PhosphoSitei P36578.

Polymorphism databases

DMDMi 22002063.

2D gel databases

SWISS-2DPAGE P36578.

Proteomic databases

MaxQBi P36578.
PaxDbi P36578.
PRIDEi P36578.

Protocols and materials databases

DNASUi 6124.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000307961 ; ENSP00000311430 ; ENSG00000174444 .
GeneIDi 6124.
KEGGi hsa:6124.
UCSCi uc002apv.3. human.

Organism-specific databases

CTDi 6124.
GeneCardsi GC15M066790.
HGNCi HGNC:10353. RPL4.
HPAi HPA034600.
MIMi 180479. gene.
neXtProti NX_P36578.
PharmGKBi PA34749.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0088.
HOVERGENi HBG001453.
InParanoidi P36578.
KOi K02930.
OMAi KAKMLKP.
OrthoDBi EOG73RBBP.
PhylomeDBi P36578.
TreeFami TF300593.

Enzyme and pathway databases

Reactomei REACT_115902. SRP-dependent cotranslational protein targeting to membrane.
REACT_1404. Peptide chain elongation.
REACT_1797. Formation of a pool of free 40S subunits.
REACT_1986. Eukaryotic Translation Termination.
REACT_2085. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_75768. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_79. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

ChiTaRSi RPL4. human.
GeneWikii Ribosomal_protein_L4.
GenomeRNAii 6124.
NextBioi 23787.
PMAP-CutDB P36578.
PROi P36578.
SOURCEi Search...

Gene expression databases

ArrayExpressi P36578.
Bgeei P36578.
CleanExi HS_RPL4.
Genevestigatori P36578.

Family and domain databases

Gene3Di 3.40.1370.10. 1 hit.
InterProi IPR025755. Ribos_L4_C_dom.
IPR002136. Ribosomal_L4/L1e.
IPR013000. Ribosomal_L4/L1e_euk/arc_CS.
IPR023574. Ribosomal_L4_dom.
[Graphical view ]
Pfami PF14374. Ribos_L4_asso_C. 1 hit.
PF00573. Ribosomal_L4. 1 hit.
[Graphical view ]
SUPFAMi SSF52166. SSF52166. 1 hit.
PROSITEi PS00939. RIBOSOMAL_L1E. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL4_HUMAN
AccessioniPrimary (citable) accession number: P36578
Secondary accession number(s): A8K502
, P39029, Q4VBR0, Q969Z9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 147 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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