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Protein

40S ribosomal protein S25

Gene

RPS25

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

Functioni

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • structural constituent of ribosome Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

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 S25
Gene namesi
Name:RPS25
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:10413. RPS25.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • cytosolic small ribosomal subunit Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleus Source: UniProtKB
  • ribosome Source: UniProtKB
  • small ribosomal subunit Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34817.

Polymorphism and mutation databases

BioMutaiRPS25.
DMDMi51338648.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12512540S ribosomal protein S25PRO_0000192869Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431N6-acetyllysineBy similarity
Modified residuei52 – 521N6-acetyllysine; alternate1 Publication
Modified residuei52 – 521N6-succinyllysine; alternateBy similarity
Modified residuei60 – 601N6-acetyllysine1 Publication
Modified residuei66 – 661N6-acetyllysine1 Publication
Modified residuei94 – 941N6-acetyllysine; alternate1 Publication
Modified residuei94 – 941N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP62851.
PaxDbiP62851.
PRIDEiP62851.

PTM databases

PhosphoSiteiP62851.

Expressioni

Gene expression databases

BgeeiP62851.
CleanExiHS_RPS25.
ExpressionAtlasiP62851. baseline and differential.
GenevestigatoriP62851.

Organism-specific databases

HPAiHPA031801.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
THAP1Q9NVV93EBI-353054,EBI-741515

Protein-protein interaction databases

BioGridi112144. 118 interactions.
IntActiP62851. 16 interactions.
MINTiMINT-5000124.
STRINGi9606.ENSP00000236900.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AZ1-125[»]
ProteinModelPortaliP62851.
SMRiP62851. Positions 41-115.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein S25e family.Curated

Phylogenomic databases

eggNOGiCOG4901.
GeneTreeiENSGT00390000004856.
HOGENOMiHOG000203673.
HOVERGENiHBG054579.
InParanoidiP62851.
KOiK02975.
OMAiDVPTYKY.
PhylomeDBiP62851.
TreeFamiTF314909.

Family and domain databases

InterProiIPR004977. Ribosomal_S25.
[Graphical view]
PANTHERiPTHR12850. PTHR12850. 1 hit.
PfamiPF03297. Ribosomal_S25. 1 hit.
[Graphical view]
ProDomiPD012268. Ribosomal_S25. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

P62851-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPKDDKKKK DAGKSAKKDK DPVNKSGGKA KKKKWSKGKV RDKLNNLVLF
60 70 80 90 100
DKATYDKLCK EVPNYKLITP AVVSERLKIR GSLARAALQE LLSKGLIKLV
110 120
SKHRAQVIYT RNTKGGDAPA AGEDA
Length:125
Mass (Da):13,742
Last modified:August 16, 2004 - v1
Checksum:iB8E05F04FCF2F1A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64716 mRNA. Translation: AAA16105.1.
AB061844 Genomic DNA. Translation: BAB79482.1.
AK311883 mRNA. Translation: BAG34824.1.
CH471065 Genomic DNA. Translation: EAW67426.1.
BC003537 mRNA. Translation: AAH03537.1.
BC004294 mRNA. Translation: AAH04294.1.
BC004986 mRNA. Translation: AAH04986.1.
CCDSiCCDS8406.1.
PIRiJQ1347.
RefSeqiNP_001019.1. NM_001028.2.
UniGeneiHs.512676.

Genome annotation databases

EnsembliENST00000527673; ENSP00000435096; ENSG00000118181.
ENST00000628770; ENSP00000486392; ENSG00000280831.
GeneIDi6230.
KEGGihsa:6230.
UCSCiuc001pun.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64716 mRNA. Translation: AAA16105.1.
AB061844 Genomic DNA. Translation: BAB79482.1.
AK311883 mRNA. Translation: BAG34824.1.
CH471065 Genomic DNA. Translation: EAW67426.1.
BC003537 mRNA. Translation: AAH03537.1.
BC004294 mRNA. Translation: AAH04294.1.
BC004986 mRNA. Translation: AAH04986.1.
CCDSiCCDS8406.1.
PIRiJQ1347.
RefSeqiNP_001019.1. NM_001028.2.
UniGeneiHs.512676.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V6Xelectron microscopy5.00AZ1-125[»]
ProteinModelPortaliP62851.
SMRiP62851. Positions 41-115.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112144. 118 interactions.
IntActiP62851. 16 interactions.
MINTiMINT-5000124.
STRINGi9606.ENSP00000236900.

PTM databases

PhosphoSiteiP62851.

Polymorphism and mutation databases

BioMutaiRPS25.
DMDMi51338648.

Proteomic databases

MaxQBiP62851.
PaxDbiP62851.
PRIDEiP62851.

Protocols and materials databases

DNASUi6230.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000527673; ENSP00000435096; ENSG00000118181.
ENST00000628770; ENSP00000486392; ENSG00000280831.
GeneIDi6230.
KEGGihsa:6230.
UCSCiuc001pun.2. human.

Organism-specific databases

CTDi6230.
GeneCardsiGC11M118886.
HGNCiHGNC:10413. RPS25.
HPAiHPA031801.
MIMi180465. gene.
neXtProtiNX_P62851.
PharmGKBiPA34817.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4901.
GeneTreeiENSGT00390000004856.
HOGENOMiHOG000203673.
HOVERGENiHBG054579.
InParanoidiP62851.
KOiK02975.
OMAiDVPTYKY.
PhylomeDBiP62851.
TreeFamiTF314909.

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

ChiTaRSiRPS25. human.
GeneWikiiRPS25.
GenomeRNAii6230.
NextBioi24185.
PROiP62851.
SOURCEiSearch...

Gene expression databases

BgeeiP62851.
CleanExiHS_RPS25.
ExpressionAtlasiP62851. baseline and differential.
GenevestigatoriP62851.

Family and domain databases

InterProiIPR004977. Ribosomal_S25.
[Graphical view]
PANTHERiPTHR12850. PTHR12850. 1 hit.
PfamiPF03297. Ribosomal_S25. 1 hit.
[Graphical view]
ProDomiPD012268. Ribosomal_S25. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing a cDNA encoding human ribosomal protein S25."
    Li M., Latoud C., Center M.S.
    Gene 107:329-333(1991) [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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Tongue.
  4. 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].
    Tissue: Pancreas and Skin.
  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 103-114.
    Tissue: Placenta.
  7. "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-52; LYS-60; LYS-66 AND LYS-94, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).

Entry informationi

Entry nameiRS25_HUMAN
AccessioniPrimary (citable) accession number: P62851
Secondary accession number(s): B2R4M7, P25111
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: May 27, 2015
This is version 111 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 11
    Human chromosome 11: 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.