60S ribosomal protein L24 - Homo sapiens (Human)

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P83731 (RL24_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 85. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
60S ribosomal protein L24

Alternative name(s):
60S ribosomal protein L30

Gene names

Name:

RPL24

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	157 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Sequence similarities

Belongs to the ribosomal protein L24e family.

Ontologies

Keywords
Molecular function	Ribonucleoprotein Ribosomal protein
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	endocrine pancreas development Traceable author statement. Source: Reactome mRNA metabolic process Traceable author statement. Source: Reactome translational elongation Traceable author statement. Source: Reactome translational termination Traceable author statement. Source: Reactome viral transcription Traceable author statement. Source: Reactome
Cellular component	cytosolic large ribosomal subunit Inferred from direct assay. Source: UniProtKB
Molecular function	RNA binding Traceable author statement. Source: ProtInc structural constituent of ribosome Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct
LYAR	Q9NX58	1	EBI-353146,EBI-713507
MAGEB2	O15479	1	EBI-353146,EBI-1057615
NAA38	O95777	1	EBI-353146,EBI-347779
NDRG1	Q92597	1	EBI-353146,EBI-716486

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 157

157

60S ribosomal protein L24

PRO_0000136867

Sites

Site

Not acetylated

Amino acid modifications

Modified residue

N6-acetyllysine Ref.13

Modified residue

N6-acetyllysine Ref.13

Modified residue

Phosphothreonine Ref.9 Ref.10 Ref.11

Modified residue

Phosphoserine Ref.10 Ref.11 Ref.12

Modified residue

N6-acetyllysine Ref.13

Sequences

Sequence

Length

Mass (Da)

Tools

P83731 [UniParc].

Last modified January 16, 2004. Version 1.
Checksum: 1D48EEB7C0652574
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FASTA

157

17,779

        10         20         30         40         50         60 
MKVELCSFSG YKIYPGHGRR YARTDGKVFQ FLNAKCESAF LSKRNPRQIN WTVLYRRKHK 

        70         80         90        100        110        120 
KGQSEEIQKK RTRRAVKFQR AITGASLADI MAKRNQKPEV RKAQREQAIR AAKEAKKAKQ 

       130        140        150 
ASKKTAMAAA KAPTKAAPKQ KIVKPVKVSA PRVGGKR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of cDNA clones encoding the human homologue of Saccharomyces cerevisiae ribosomal protein L30." Johnson K.R. Gene 123:283-285(1993) [PubMed: 8428672] [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(2002) [PubMed: 11875025] [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 (JUN-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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thymus.
[5]	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. Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[7]	Bienvenut W.V., Bilsland A.E., Keith W.N. Submitted (JAN-2010) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1-12; 28-44; 48-56 AND 81-93, LACK OF N-TERMINAL ACETYLATION, 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(1998) [PubMed: 9582194] [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(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83 AND SER-86, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-83 AND SER-86, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86, MASS SPECTROMETRY.
[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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27; LYS-77 AND LYS-93, MASS SPECTROMETRY.
[14]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00306332.
PIR	JN0549.
RefSeq	NP_000977.1. NM_000986.3.
UniGene	Hs.477028. Hs.547172. Hs.649475.
3D structure databases
ProteinModelPortal	P83731.
SMR	P83731. Positions 4-56.
ModBase	Search...
Protein-protein interaction databases
IntAct	P83731. 12 interactions.
MINT	MINT-5000278.
STRING	P83731.
PTM databases
PhosphoSite	P83731.
Polymorphism databases
DMDM	41393532.
Proteomic databases
PRIDE	P83731.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000394077; ENSP00000377640; ENSG00000114391.
GeneID	6152.
KEGG	hsa:6152.
UCSC	uc003dvh.1. human.
Organism-specific databases
CTD	6152.
GeneCards	GC03M101399.
H-InvDB	HIX0003512.
HGNC	HGNC:10325. RPL24.
MIM	604180. gene.
neXtProt	NX_P83731.
PharmGKB	PA34701.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG20423.
GeneTree	ENSGT00550000074809.
HOGENOM	HBG600564.
HOVERGEN	HBG001066.
InParanoid	P83731.
OMA	IHPGHGK.
OrthoDB	EOG46DM48.
PhylomeDB	P83731.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology. REACT_111217. Metabolism. REACT_15380. Diabetes pathways. REACT_17015. Metabolism of proteins. REACT_1762. 3' -UTR-mediated translational regulation. REACT_6167. Influenza Infection. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	P83731.
Bgee	P83731.
CleanEx	HS_RPL24.
Genevestigator	P83731.
GermOnline	ENSG00000114391. Homo sapiens.
Family and domain databases
InterPro	IPR023442. Ribosomal_L24e_CS. IPR023441. Ribosomal_L24e_dom. IPR000988. Ribosomal_L24e_rel. IPR011017. TRASH. [Graphical view]
Gene3D	G3DSA:2.30.170.20. Ribosomal_L24E. 1 hit.
KO	K02896.
PANTHER	PTHR10792. Ribosomal_L24E. 1 hit.
Pfam	PF01246. Ribosomal_L24e. 1 hit. [Graphical view]
SMART	SM00746. TRASH. 1 hit. [Graphical view]
PROSITE	PS01073. RIBOSOMAL_L24E. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	23893.
SOURCE	Search...

Entry information

Entry name

RL24_HUMAN

Accession

Primary (citable) accession number: P83731
Secondary accession number(s): B2R4Y3, P38663, Q6IBS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 16, 2004
Last sequence update:	January 16, 2004
Last modified:	January 25, 2012
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Ribosomal proteins

Ribosomal proteins families and list of entries

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents