Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

40S ribosomal protein S29

Gene

RPS29

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

Functioni

Cofactori

Zn2+CuratedNote: Binds 1 zinc ion per subunit.Curated

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi21 – 211ZincSequence Analysis
Metal bindingi24 – 241ZincSequence Analysis
Metal bindingi39 – 391ZincSequence Analysis
Metal bindingi42 – 421ZincSequence Analysis

GO - Molecular functioni

  1. structural constituent of ribosome Source: UniProtKB
  2. zinc ion binding 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

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
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_1979. Translation initiation complex formation.
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_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Names & Taxonomyi

Protein namesi
Recommended name:
40S ribosomal protein S29
Gene namesi
Name:RPS29
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:10419. RPS29.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. cytosolic small ribosomal subunit Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. focal adhesion Source: UniProtKB
  6. small ribosomal subunit Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Diamond-Blackfan anemia 131 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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 malignancy. 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.

See also OMIM:615909
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti31 – 311I → F in DBA13; results in reduced protein expression; results in pre-rRNA processing defect. 1 Publication
VAR_071328
Natural varianti50 – 501I → T in DBA13; results in reduced protein expression; results in pre-rRNA processing defect. 1 Publication
VAR_071329

Keywords - Diseasei

Diamond-Blackfan anemia, Disease mutation

Organism-specific databases

MIMi615909. phenotype.
Orphaneti124. Blackfan-Diamond anemia.
PharmGKBiPA34826.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 565540S ribosomal protein S29PRO_0000131019Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei48 – 481N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP62273.
PaxDbiP62273.
PRIDEiP62273.

PTM databases

PhosphoSiteiP62273.

Expressioni

Gene expression databases

BgeeiP62273.
CleanExiHS_RPS29.
GenevestigatoriP62273.

Organism-specific databases

HPAiHPA004107.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
DDX56Q9NY931EBI-1054121,EBI-372376
EIF1BO607391EBI-1054121,EBI-1043343
EIF4A2Q142401EBI-1054121,EBI-73473
EXT2Q930631EBI-1054121,EBI-1047761
STYXL1Q9Y6J81EBI-1054121,EBI-1044511

Protein-protein interaction databases

BioGridi112149. 52 interactions.
IntActiP62273. 7 interactions.
MINTiMINT-4133209.
STRINGi9606.ENSP00000379339.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZKQelectron microscopy8.70n1-56[»]
4V6Xelectron microscopy5.00d1-56[»]
ProteinModelPortaliP62273.
SMRiP62273. Positions 4-56.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S14P family.Curated

Phylogenomic databases

eggNOGiCOG0199.
GeneTreeiENSGT00390000005814.
HOVERGENiHBG004459.
InParanoidiP62273.
KOiK02980.
OMAiCFREKAA.
OrthoDBiEOG78D7P4.
PhylomeDBiP62273.
TreeFamiTF300217.

Family and domain databases

InterProiIPR001209. Ribosomal_S14.
IPR018271. Ribosomal_S14_CS.
[Graphical view]
PfamiPF00253. Ribosomal_S14. 1 hit.
[Graphical view]
PROSITEiPS00527. RIBOSOMAL_S14. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P62273-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGHQQLYWSH PRKFGQGSRS CRVCSNRHGL IRKYGLNMCR QCFRQYAKDI

GFIKLD
Length:56
Mass (Da):6,677
Last modified:January 23, 2007 - v2
Checksum:i41325122B493EFF9
GO
Isoform 2 (identifier: P62273-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:67
Mass (Da):8,087
Checksum:i4B12A162293EE2F4
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti31 – 311I → F in DBA13; results in reduced protein expression; results in pre-rRNA processing defect. 1 Publication
VAR_071328
Natural varianti50 – 501I → T in DBA13; results in reduced protein expression; results in pre-rRNA processing defect. 1 Publication
VAR_071329

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei54 – 563KLD → KKDLSCLPWHCLWR in isoform 2. 1 PublicationVSP_042844

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32072.1. [P62273-2]
CCDS9685.1. [P62273-1]
PIRiS55919.
RefSeqiNP_001023.1. NM_001032.4. [P62273-1]
NP_001025172.1. NM_001030001.2. [P62273-2]
UniGeneiHs.156367.

Genome annotation databases

EnsembliENST00000245458; ENSP00000245458; ENSG00000213741. [P62273-1]
ENST00000396020; ENSP00000379339; ENSG00000213741. [P62273-2]
ENST00000611563; ENSP00000479892; ENSG00000213741. [P62273-1]
GeneIDi6235.
KEGGihsa:6235.
UCSCiuc001wwl.4. human. [P62273-2]
uc001wwm.4. human. [P62273-1]

Polymorphism databases

DMDMi50403626.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS32072.1. [P62273-2]
CCDS9685.1. [P62273-1]
PIRiS55919.
RefSeqiNP_001023.1. NM_001032.4. [P62273-1]
NP_001025172.1. NM_001030001.2. [P62273-2]
UniGeneiHs.156367.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZKQelectron microscopy8.70n1-56[»]
4V6Xelectron microscopy5.00d1-56[»]
ProteinModelPortaliP62273.
SMRiP62273. Positions 4-56.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112149. 52 interactions.
IntActiP62273. 7 interactions.
MINTiMINT-4133209.
STRINGi9606.ENSP00000379339.

PTM databases

PhosphoSiteiP62273.

Polymorphism databases

DMDMi50403626.

Proteomic databases

MaxQBiP62273.
PaxDbiP62273.
PRIDEiP62273.

Protocols and materials databases

DNASUi6235.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000245458; ENSP00000245458; ENSG00000213741. [P62273-1]
ENST00000396020; ENSP00000379339; ENSG00000213741. [P62273-2]
ENST00000611563; ENSP00000479892; ENSG00000213741. [P62273-1]
GeneIDi6235.
KEGGihsa:6235.
UCSCiuc001wwl.4. human. [P62273-2]
uc001wwm.4. human. [P62273-1]

Organism-specific databases

CTDi6235.
GeneCardsiGC14M050043.
HGNCiHGNC:10419. RPS29.
HPAiHPA004107.
MIMi603633. gene.
615909. phenotype.
neXtProtiNX_P62273.
Orphaneti124. Blackfan-Diamond anemia.
PharmGKBiPA34826.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0199.
GeneTreeiENSGT00390000005814.
HOVERGENiHBG004459.
InParanoidiP62273.
KOiK02980.
OMAiCFREKAA.
OrthoDBiEOG78D7P4.
PhylomeDBiP62273.
TreeFamiTF300217.

Enzyme and pathway databases

ReactomeiREACT_1079. Formation of the ternary complex, and subsequently, the 43S complex.
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_1979. Translation initiation complex formation.
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_931. Ribosomal scanning and start codon recognition.
REACT_9491. Viral mRNA Translation.

Miscellaneous databases

GeneWikiiRPS29.
GenomeRNAii6235.
NextBioi24205.
PROiP62273.
SOURCEiSearch...

Gene expression databases

BgeeiP62273.
CleanExiHS_RPS29.
GenevestigatoriP62273.

Family and domain databases

InterProiIPR001209. Ribosomal_S14.
IPR018271. Ribosomal_S14_CS.
[Graphical view]
PfamiPF00253. Ribosomal_S14. 1 hit.
[Graphical view]
PROSITEiPS00527. RIBOSOMAL_S14. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
  12. "Whole-exome sequencing and functional studies identify RPS29 as a novel gene mutated in multicase Diamond-Blackfan anemia families."
    Mirabello L., Macari E.R., Jessop L., Ellis S.R., Myers T., Giri N., Taylor A.M., McGrath K.E., Humphries J.M., Ballew B.J., Yeager M., Boland J.F., He J., Hicks B.D., Burdett L., Alter B.P., Zon L., Savage S.A.
    Blood 124:24-32(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN DBA13, VARIANTS DBA13 PHE-31 AND THR-50, CHARACTERIZATION OF VARIANTS DBA13 PHE-31 AND THR-50.

Entry informationi

Entry nameiRS29_HUMAN
AccessioniPrimary (citable) accession number: P62273
Secondary accession number(s): A8MZ73, P30054
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: January 23, 2007
Last modified: February 4, 2015
This is version 108 of the entry and version 2 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 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Ribosomal proteins
    Ribosomal proteins families and list of entries
  7. 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.