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Protein

60S ribosomal protein L24

Gene

RPL24

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

Functioni

GO - Molecular functioni

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

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  4. SRP-dependent cotranslational protein targeting to membrane Source: Reactome
  5. translation Source: UniProtKB
  6. translational elongation Source: Reactome
  7. translational initiation Source: Reactome
  8. translational termination Source: Reactome
  9. viral life cycle Source: Reactome
  10. viral process Source: Reactome
  11. 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 L24
Alternative name(s):
60S ribosomal protein L30
Gene namesi
Name:RPL24
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:10325. RPL24.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. cytosolic large ribosomal subunit Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34701.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15715760S ribosomal protein L24PRO_0000136867Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271N6-acetyllysine1 Publication
Modified residuei77 – 771N6-acetyllysine1 Publication
Modified residuei83 – 831Phosphothreonine3 Publications
Modified residuei86 – 861Phosphoserine3 Publications
Modified residuei93 – 931N6-acetyllysine1 Publication
Modified residuei131 – 1311N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP83731.
PaxDbiP83731.
PRIDEiP83731.

PTM databases

PhosphoSiteiP83731.

Expressioni

Gene expression databases

BgeeiP83731.
CleanExiHS_RPL24.
ExpressionAtlasiP83731. baseline and differential.
GenevestigatoriP83731.

Organism-specific databases

HPAiHPA051653.

Interactioni

Protein-protein interaction databases

BioGridi112071. 123 interactions.
IntActiP83731. 25 interactions.
MINTiMINT-5000278.
STRINGi9606.ENSP00000377640.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CW1-157[»]
ProteinModelPortaliP83731.
SMRiP83731. Positions 1-107.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L24e family.Curated

Phylogenomic databases

eggNOGiCOG2075.
HOGENOMiHOG000184343.
HOVERGENiHBG001066.
InParanoidiP83731.
KOiK02896.
OMAiRTIECEF.
OrthoDBiEOG77HDH1.
PhylomeDBiP83731.
TreeFamiTF312933.

Family and domain databases

Gene3Di2.30.170.20. 1 hit.
InterProiIPR023442. Ribosomal_L24e_CS.
IPR023441. Ribosomal_L24e_dom.
IPR000988. Ribosomal_L24e_rel.
IPR011017. TRASH_dom.
[Graphical view]
PANTHERiPTHR10792. PTHR10792. 1 hit.
PfamiPF01246. Ribosomal_L24e. 1 hit.
[Graphical view]
SMARTiSM00746. TRASH. 1 hit.
[Graphical view]
PROSITEiPS01073. RIBOSOMAL_L24E. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P83731-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVELCSFSG YKIYPGHGRR YARTDGKVFQ FLNAKCESAF LSKRNPRQIN
60 70 80 90 100
WTVLYRRKHK KGQSEEIQKK RTRRAVKFQR AITGASLADI MAKRNQKPEV
110 120 130 140 150
RKAQREQAIR AAKEAKKAKQ ASKKTAMAAA KAPTKAAPKQ KIVKPVKVSA

PRVGGKR
Length:157
Mass (Da):17,779
Last modified:January 15, 2004 - v1
Checksum:i1D48EEB7C0652574
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94314 mRNA. Translation: AAC28251.1.
AB061828 Genomic DNA. Translation: BAB79466.1.
CR456729 mRNA. Translation: CAG33010.1.
AK311992 mRNA. Translation: BAG34930.1.
CH471052 Genomic DNA. Translation: EAW79780.1.
BC000690 mRNA. Translation: AAH00690.1.
BC070193 mRNA. Translation: AAH70193.1.
AB007177 Genomic DNA. Translation: BAA25836.1.
CCDSiCCDS33809.1.
PIRiJN0549.
RefSeqiNP_000977.1. NM_000986.3.
UniGeneiHs.477028.
Hs.649475.

Genome annotation databases

EnsembliENST00000394077; ENSP00000377640; ENSG00000114391.
GeneIDi6152.
KEGGihsa:6152.
UCSCiuc003dvh.1. human.

Polymorphism databases

DMDMi41393532.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M94314 mRNA. Translation: AAC28251.1.
AB061828 Genomic DNA. Translation: BAB79466.1.
CR456729 mRNA. Translation: CAG33010.1.
AK311992 mRNA. Translation: BAG34930.1.
CH471052 Genomic DNA. Translation: EAW79780.1.
BC000690 mRNA. Translation: AAH00690.1.
BC070193 mRNA. Translation: AAH70193.1.
AB007177 Genomic DNA. Translation: BAA25836.1.
CCDSiCCDS33809.1.
PIRiJN0549.
RefSeqiNP_000977.1. NM_000986.3.
UniGeneiHs.477028.
Hs.649475.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00CW1-157[»]
ProteinModelPortaliP83731.
SMRiP83731. Positions 1-107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112071. 123 interactions.
IntActiP83731. 25 interactions.
MINTiMINT-5000278.
STRINGi9606.ENSP00000377640.

PTM databases

PhosphoSiteiP83731.

Polymorphism databases

DMDMi41393532.

Proteomic databases

MaxQBiP83731.
PaxDbiP83731.
PRIDEiP83731.

Protocols and materials databases

DNASUi6152.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000394077; ENSP00000377640; ENSG00000114391.
GeneIDi6152.
KEGGihsa:6152.
UCSCiuc003dvh.1. human.

Organism-specific databases

CTDi6152.
GeneCardsiGC03M101399.
HGNCiHGNC:10325. RPL24.
HPAiHPA051653.
MIMi604180. gene.
neXtProtiNX_P83731.
PharmGKBiPA34701.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2075.
HOGENOMiHOG000184343.
HOVERGENiHBG001066.
InParanoidiP83731.
KOiK02896.
OMAiRTIECEF.
OrthoDBiEOG77HDH1.
PhylomeDBiP83731.
TreeFamiTF312933.

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.

Miscellaneous databases

ChiTaRSiRPL24. human.
GeneWikiiRPL24.
GenomeRNAii6152.
NextBioi23893.
PROiP83731.
SOURCEiSearch...

Gene expression databases

BgeeiP83731.
CleanExiHS_RPL24.
ExpressionAtlasiP83731. baseline and differential.
GenevestigatoriP83731.

Family and domain databases

Gene3Di2.30.170.20. 1 hit.
InterProiIPR023442. Ribosomal_L24e_CS.
IPR023441. Ribosomal_L24e_dom.
IPR000988. Ribosomal_L24e_rel.
IPR011017. TRASH_dom.
[Graphical view]
PANTHERiPTHR10792. PTHR10792. 1 hit.
PfamiPF01246. Ribosomal_L24e. 1 hit.
[Graphical view]
SMARTiSM00746. TRASH. 1 hit.
[Graphical view]
PROSITEiPS01073. RIBOSOMAL_L24E. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of cDNA clones encoding the human homologue of Saccharomyces cerevisiae ribosomal protein L30."
    Johnson K.R.
    Gene 123:283-285(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thymus.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon.
  7. Bienvenut W.V., Bilsland A.E., Keith W.N.
    Submitted (DEC-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-12; 28-44; 48-56 AND 81-93, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  8. "A map of 75 human ribosomal protein genes."
    Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N., Hudson T.J., Tanaka T., Page D.C.
    Genome Res. 8:509-523(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 132-157.
  9. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83 AND SER-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27; LYS-77 AND LYS-93, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83 AND SER-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRL24_HUMAN
AccessioniPrimary (citable) accession number: P83731
Secondary accession number(s): B2R4Y3, P38663, Q6IBS3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2004
Last sequence update: January 15, 2004
Last modified: March 31, 2015
This is version 118 of the entry and version 1 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 3
    Human chromosome 3: 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

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.