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P62847 (RS24_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 117. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S24
Gene names
Name:RPS24
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length133 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for processing of pre-rRNA and maturation of 40S ribosomal subunits. Ref.12

Tissue specificity

Mature tissues, such as adult brain, skeletal muscle, heart, and kidney, express low levels, whereas tissues and organs with significant populations of proliferating cells, such as fetal brain, placenta, bone marrow, and various glandular organs, contain significantly higher levels. Ref.11

Involvement in disease

Diamond-Blackfan anemia 3 (DBA3) [MIM:610629]: A form of Diamond-Blackfan anemia, a congenital non-regenerative hypoplastic anemia that usually presents early in infancy. Diamond-Blackfan anemia is characterized by a moderate to severe macrocytic anemia, erythroblastopenia, and an increased risk of developing leukemia. 30 to 40% of Diamond-Blackfan anemia patients present with short stature and congenital anomalies, the most frequent being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and urogenital anomalies.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11

Sequence similarities

Belongs to the ribosomal protein S24e family.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   DiseaseDiamond-Blackfan anemia
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
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

erythrocyte homeostasis

Inferred from mutant phenotype Ref.11Ref.12. Source: UniProtKB

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)

Inferred from Biological aspect of Ancestor. Source: RefGenome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

rRNA processing

Inferred from mutant phenotype Ref.12PubMed 18697920. Source: UniProtKB

ribosomal small subunit biogenesis

Inferred from mutant phenotype Ref.12PubMed 18697920. Source: UniProtKB

translation

Inferred by curator PubMed 15883184Ref.10. 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 small ribosomal subunit

Inferred from direct assay PubMed 15883184Ref.10. Source: UniProtKB

nucleolus

Inferred from Biological aspect of Ancestor. Source: RefGenome

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

small ribosomal subunit

Inferred from direct assay PubMed 15883184. Source: UniProtKB

   Molecular_functionnucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

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

structural constituent of ribosome

Non-traceable author statement PubMed 18412286. Source: UniProtKB

translation initiation factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P62847-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P62847-2)

The sequence of this isoform differs from the canonical sequence as follows:
     131-133: Missing.
Isoform 3 (identifier: P62847-3)

The sequence of this isoform differs from the canonical sequence as follows:
     131-133: PKE → KK
Isoform 4 (identifier: P62847-4)

The sequence of this isoform differs from the canonical sequence as follows:
     131-133: PKE → MRELGLGVQA...PPSCLSGLGH
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13313340S ribosomal protein S24 HAMAP-Rule MF_00545
PRO_0000137623

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9 Ref.13 Ref.16 Ref.17
Modified residue91Phosphothreonine Ref.14

Natural variations

Alternative sequence131 – 1333Missing in isoform 2.
VSP_005724
Alternative sequence131 – 1333PKE → KK in isoform 3.
VSP_039113
Alternative sequence131 – 1333PKE → MRELGLGVQALGRISQEERC TDVKNSKARESRGVVWQVEV PGPWSVWTCGRLRRGCGKYL QVAVTWRKTENREQCCQACL LERALVRNGAFMSPASPAPA GSPHPVDGDLVLHLPEALSA TLTLSPHIQAINKSFGPFFE IHQESSCFSPPSCLSGLGH in isoform 4.
VSP_045672

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 16, 2004. Version 1.
Checksum: CE9065C0764D60A6

FASTA13315,423
        10         20         30         40         50         60 
MNDTVTIRTR KFMTNRLLQR KQMVIDVLHP GKATVPKTEI REKLAKMYKT TPDVIFVFGF 

        70         80         90        100        110        120 
RTHFGGGKTT GFGMIYDSLD YAKKNEPKHR LARHGLYEKK KTSRKQRKER KNRMKKVRGT 

       130 
AKANVGAGKK PKE 

« Hide

Isoform 2 [UniParc] [UniParc].

Checksum: E0764D60A6DD576E
Show »

FASTA13015,069
Isoform 3 [UniParc].

Checksum: 107190764D60A6DD
Show »

FASTA13215,325
Isoform 4 [UniParc].

Checksum: 611E080AF85103CD
Show »

FASTA28932,431

References

« Hide 'large scale' references
[1]"A cDNA encoding human ribosomal protein S24."
Brown S.J., Jewell A., Maki C.G., Roufa D.J.
Gene 91:293-296(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"The gene encoding human ribosomal protein S24 and tissue-specific expression of differentially spliced mRNAs."
Xu W.-B., Roufa D.J.
Gene 169:257-262(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[3]"Full-length cDNA libraries and normalization."
Li W.B., Gruber C., Jessee J., Polayes D.
Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Placenta.
[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. 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] (ISOFORMS 1 AND 2).
Tissue: Brain and Thymus.
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Retina.
[6]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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].
[8]"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] (ISOFORM 2).
Tissue: Kidney and Muscle.
[9]Quadroni M.
Submitted (OCT-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-8; 50-61; 69-83 AND 119-132, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[10]"Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry."
Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K., Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.
Eur. J. Biochem. 239:144-149(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 69-83.
Tissue: Placenta.
[11]"Ribosomal protein S24 gene is mutated in Diamond-Blackfan anemia."
Gazda H.T., Grabowska A., Merida-Long L.B., Latawiec E., Schneider H.E., Lipton J.M., Vlachos A., Atsidaftos E., Ball S.E., Orfali K.A., Niewiadomska E., Da Costa L., Tchernia G., Niemeyer C., Meerpohl J.J., Stahl J., Schratt G., Glader B. expand/collapse author list , Backer K., Wong C., Nathan D.G., Beggs A.H., Sieff C.A.
Am. J. Hum. Genet. 79:1110-1118(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN DBA3, TISSUE SPECIFICITY.
[12]"Mutation of ribosomal protein RPS24 in Diamond-Blackfan anemia results in a ribosome biogenesis disorder."
Choesmel V., Fribourg S., Aguissa-Toure A.H., Pinaud N., Legrand P., Gazda H.T., Gleizes P.E.
Hum. Mol. Genet. 17:1253-1263(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"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 MET-1, 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 THR-9, 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]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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) OF 80S RIBOSOME.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M31520 mRNA. Translation: AAA36588.1.
U12202 Genomic DNA. Translation: AAB08007.1.
U12202 Genomic DNA. Translation: AAB08006.1.
BX336465 mRNA. No translation available.
AK311776 mRNA. Translation: BAG34719.1.
AK311910 mRNA. Translation: BAG34851.1.
BX537975 mRNA. Translation: CAD97939.1.
AL512628 Genomic DNA. Translation: CAI16467.1.
AL512628 Genomic DNA. Translation: CAI16468.1.
CH471083 Genomic DNA. Translation: EAW54623.1.
CH471083 Genomic DNA. Translation: EAW54625.1.
BC000523 mRNA. Translation: AAH00523.1.
BC003149 mRNA. No translation available.
BC071926 mRNA. Translation: AAH71926.1.
CCDSCCDS44443.1. [P62847-4]
CCDS7355.1.
CCDS7356.1. [P62847-2]
PIRJC4671.
JH0213.
RefSeqNP_001017.1. NM_001026.4. [P62847-1]
NP_001135755.1. NM_001142283.1. [P62847-3]
NP_001135757.1. NM_001142285.1. [P62847-4]
NP_148982.1. NM_033022.3. [P62847-2]
UniGeneHs.280130.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3J3Aelectron microscopy5.00Y1-133[»]
ProteinModelPortalP62847.
SMRP62847. Positions 3-128.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112143. 164 interactions.
IntActP62847. 22 interactions.
MINTMINT-4719640.
STRING9606.ENSP00000414321.

PTM databases

PhosphoSiteP62847.

Polymorphism databases

DMDM51338645.

Proteomic databases

MaxQBP62847.
PaxDbP62847.
PRIDEP62847.

Protocols and materials databases

DNASU6229.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360830; ENSP00000354074; ENSG00000138326. [P62847-2]
ENST00000372360; ENSP00000361435; ENSG00000138326. [P62847-1]
ENST00000440692; ENSP00000414321; ENSG00000138326. [P62847-4]
GeneID6229.
KEGGhsa:6229.
UCSCuc001jzp.3. human.
uc010qlo.2. human. [P62847-3]

Organism-specific databases

CTD6229.
GeneCardsGC10P079793.
GeneReviewsRPS24.
HGNCHGNC:10411. RPS24.
HPAHPA003364.
MIM602412. gene.
610629. phenotype.
neXtProtNX_P62847.
Orphanet124. Blackfan-Diamond anemia.
PharmGKBPA34815.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2004.
HOGENOMHOG000186306.
HOVERGENHBG000969.
InParanoidP62847.
KOK02974.
OMATENREQC.
OrthoDBEOG7PS1J8.
PhylomeDBP62847.
TreeFamTF314134.

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

ArrayExpressP62847.
BgeeP62847.
CleanExHS_RPS24.
GenevestigatorP62847.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
HAMAPMF_00545. Ribosomal_S24e.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR012678. Ribosomal_L23/L15e_core_dom.
IPR001976. Ribosomal_S24e.
IPR018098. Ribosomal_S24e_CS.
[Graphical view]
PANTHERPTHR10496. PTHR10496. 1 hit.
PfamPF01282. Ribosomal_S24e. 1 hit.
[Graphical view]
ProDomPD006052. Ribosomal_S24e. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF54189. SSF54189. 1 hit.
PROSITEPS00529. RIBOSOMAL_S24E. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRPS24. human.
GeneWikiRPS24.
GenomeRNAi6229.
NextBio24179.
PROP62847.
SOURCESearch...

Entry information

Entry nameRS24_HUMAN
AccessionPrimary (citable) accession number: P62847
Secondary accession number(s): E7EPK6 expand/collapse secondary AC list , P16632, Q5T0P7, Q5T0P8, Q7Z3D1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 9, 2014
This is version 117 of the entry and version 1 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 10

Human chromosome 10: entries, gene names and cross-references to MIM