Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P62273 (RS29_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
40S ribosomal protein S29
Gene names
Name:RPS29
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length56 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Cofactor

Binds 1 zinc ion per subunit Potential.

Sequence similarities

Belongs to the ribosomal protein S14P family.

Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   LigandMetal-binding
Zinc
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
   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

Inferred by curator PubMed 15883184Ref.6. 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.6. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

small ribosomal subunit

Inferred from direct assay PubMed 15883184. Source: UniProtKB

   Molecular_functionstructural constituent of ribosome

Inferred from direct assay PubMed 15883184. Source: UniProtKB

zinc ion binding

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P62273-1)

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: P62273-2)

The sequence of this isoform differs from the canonical sequence as follows:
     54-56: KLD → KKDLSCLPWHCLWR

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6 Ref.7
Chain2 – 565540S ribosomal protein S29
PRO_0000131019

Sites

Metal binding211Zinc Potential
Metal binding241Zinc Potential
Metal binding391Zinc Potential
Metal binding421Zinc Potential

Amino acid modifications

Modified residue481N6-acetyllysine Ref.9

Natural variations

Alternative sequence54 – 563KLD → KKDLSCLPWHCLWR in isoform 2.
VSP_042844

Sequences

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

Last modified January 23, 2007. Version 2.
Checksum: 41325122B493EFF9

FASTA566,677
        10         20         30         40         50 
MGHQQLYWSH PRKFGQGSRS CRVCSNRHGL IRKYGLNMCR QCFRQYAKDI GFIKLD 

« Hide

Isoform 2 [UniParc].

Checksum: 4B12A162293EE2F4
Show »

FASTA678,087

References

« Hide 'large scale' references
[1]"Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human ribosomal protein mRNAs."
Frigerio J.-M., Dagorn J.-C., Iovanna J.L.
Biochim. Biophys. Acta 1262:64-68(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Colon.
[2]"The S29 ribosomal protein increases tumor suppressor activity of K rev-1 gene on v-K ras-transformed NIH3T3 cells."
Kondoh N., Noda M., Fisher R.J., Schweinfest C.W., Papas T.S., Kondoh A., Samuel K.P., Oikawa T.
Biochim. Biophys. Acta 1313:41-46(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Colon.
[3]"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] (ISOFORM 1).
[4]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1 AND 2).
Tissue: Blood, Bone marrow and Eye.
[6]"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 2-11.
Tissue: Placenta.
[7]Bienvenut W.V., Murray L., Brunton V.G., Frame M.C.
Submitted (FEB-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-12 AND 49-56, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon adenocarcinoma.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-54.
[9]"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-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"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].
[11]"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
U14973 mRNA. Translation: AAA85661.1.
L31610 mRNA. Translation: AAB27426.1.
AB061847 Genomic DNA. Translation: BAB79485.1.
AL139099 Genomic DNA. No translation available.
BC015974 mRNA. Translation: AAH15974.2.
BC032813 mRNA. Translation: AAH32813.1.
BC035313 mRNA. Translation: AAH35313.1.
AB007165 Genomic DNA. Translation: BAA25827.1.
PIRS55919.
RefSeqNP_001023.1. NM_001032.4.
NP_001025172.1. NM_001030001.2.
UniGeneHs.156367.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZKQelectron microscopy8.70n1-56[»]
3J3Aelectron microscopy5.00d1-56[»]
ProteinModelPortalP62273.
SMRP62273. Positions 4-56.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112149. 78 interactions.
IntActP62273. 7 interactions.
MINTMINT-4133209.
STRING9606.ENSP00000379339.

PTM databases

PhosphoSiteP62273.

Polymorphism databases

DMDM50403626.

Proteomic databases

PaxDbP62273.
PRIDEP62273.

Protocols and materials databases

DNASU6235.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000245458; ENSP00000245458; ENSG00000213741. [P62273-1]
ENST00000396020; ENSP00000379339; ENSG00000213741. [P62273-2]
GeneID6235.
KEGGhsa:6235.
UCSCuc001wwl.4. human. [P62273-2]
uc001wwm.4. human. [P62273-1]

Organism-specific databases

CTD6235.
GeneCardsGC14M050043.
HGNCHGNC:10419. RPS29.
HPAHPA004107.
MIM603633. gene.
neXtProtNX_P62273.
PharmGKBPA34826.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0199.
HOVERGENHBG004459.
KOK02980.
OMACFREKAA.
OrthoDBEOG78D7P4.
PhylomeDBP62273.
TreeFamTF300217.

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

BgeeP62273.
CleanExHS_RPS29.
GenevestigatorP62273.

Family and domain databases

InterProIPR001209. Ribosomal_S14.
IPR018271. Ribosomal_S14_CS.
[Graphical view]
PfamPF00253. Ribosomal_S14. 1 hit.
[Graphical view]
PROSITEPS00527. RIBOSOMAL_S14. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRPS29.
GenomeRNAi6235.
NextBio24205.
PROP62273.
SOURCESearch...

Entry information

Entry nameRS29_HUMAN
AccessionPrimary (citable) accession number: P62273
Secondary accession number(s): A8MZ73, P30054
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 99 of the entry and version 2 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 14

Human chromosome 14: entries, gene names and cross-references to MIM