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Protein

28S ribosomal protein S23, mitochondrial

Gene

MRPS23

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

Functioni

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. mitochondrial translation Source: Reactome
  2. mitochondrial translational elongation Source: Reactome
  3. mitochondrial translational initiation Source: Reactome
  4. mitochondrial translational termination Source: Reactome
  5. organelle organization Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_267634. Mitochondrial translation initiation.
REACT_268133. Mitochondrial translation elongation.
REACT_268261. Mitochondrial translation termination.

Names & Taxonomyi

Protein namesi
Recommended name:
28S ribosomal protein S23, mitochondrial
Short name:
MRP-S23
Short name:
S23mt
Gene namesi
Name:MRPS23
ORF Names:CGI-138, HSPC329
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:14509. MRPS23.

Subcellular locationi

GO - Cellular componenti

  1. intermediate filament cytoskeleton Source: HPA
  2. mitochondrial inner membrane Source: Reactome
  3. mitochondrion Source: HPA
  4. nuclear membrane Source: HPA
  5. ribosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31011.

Polymorphism and mutation databases

BioMutaiMRPS23.
DMDMi31077184.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 19019028S ribosomal protein S23, mitochondrialPRO_0000087705Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei102 – 1021N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9Y3D9.
PaxDbiQ9Y3D9.
PeptideAtlasiQ9Y3D9.
PRIDEiQ9Y3D9.

PTM databases

PhosphoSiteiQ9Y3D9.

Expressioni

Gene expression databases

BgeeiQ9Y3D9.
CleanExiHS_MRPS23.
ExpressionAtlasiQ9Y3D9. baseline and differential.
GenevestigatoriQ9Y3D9.

Organism-specific databases

HPAiHPA023453.

Interactioni

Subunit structurei

Component of the mitochondrial ribosome small subunit (28S) which comprises a 12S rRNA and about 30 distinct proteins.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
USHBP1Q8N6Y03EBI-1054270,EBI-739895

Protein-protein interaction databases

BioGridi119657. 38 interactions.
IntActiQ9Y3D9. 9 interactions.
STRINGi9606.ENSP00000320184.

Structurei

3D structure databases

ProteinModelPortaliQ9Y3D9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiNOG81280.
GeneTreeiENSGT00390000009030.
HOGENOMiHOG000059557.
HOVERGENiHBG044512.
InParanoidiQ9Y3D9.
KOiK17402.
OMAiFSRTRNL.
OrthoDBiEOG7TBC3P.
PhylomeDBiQ9Y3D9.
TreeFamiTF106116.

Family and domain databases

InterProiIPR019520. Ribosomal_S23/Rsm25.
IPR023611. Ribosomal_S23/S25_mit.
[Graphical view]
PANTHERiPTHR15925. PTHR15925. 1 hit.
PfamiPF10484. MRP-S23. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y3D9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGSRLETVG SIFSRTRDLV RAGVLKEKPL WFDVYDAFPP LREPVFQRPR
60 70 80 90 100
VRYGKAKAPI QDIWYHEDRI RAKFYSVYGS GQRAFDLFNP NFKSTCQRFV
110 120 130 140 150
EKYTELQKLG ETDEEKLFVE TGKALLAEGV ILRRVGEART QHGGSHVSRK
160 170 180 190
SEHLSVRPQT ALEENETQKE VPQDQHLEAP ADQSKGLLPP
Length:190
Mass (Da):21,771
Last modified:May 23, 2003 - v2
Checksum:i0A50DEDA9BFB74AF
GO

Sequence cautioni

The sequence AAD34133.1 differs from that shown. Reason: Frameshift at position 138. Curated
The sequence AAF29007.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111S → C in AAD34133 (PubMed:10810093).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151896 mRNA. Translation: AAD34133.1. Frameshift.
AF161447 mRNA. Translation: AAF29007.1. Frameshift.
AK312729 mRNA. Translation: BAG35600.1.
CH471109 Genomic DNA. Translation: EAW94503.1.
BC000242 mRNA. Translation: AAH00242.1.
AB061206 Genomic DNA. Translation: BAB54956.1.
CCDSiCCDS11598.1.
RefSeqiNP_057154.2. NM_016070.3.
UniGeneiHs.5836.

Genome annotation databases

EnsembliENST00000313608; ENSP00000320184; ENSG00000181610.
GeneIDi51649.
KEGGihsa:51649.
UCSCiuc002ivc.3. human.

Polymorphism and mutation databases

BioMutaiMRPS23.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151896 mRNA. Translation: AAD34133.1. Frameshift.
AF161447 mRNA. Translation: AAF29007.1. Frameshift.
AK312729 mRNA. Translation: BAG35600.1.
CH471109 Genomic DNA. Translation: EAW94503.1.
BC000242 mRNA. Translation: AAH00242.1.
AB061206 Genomic DNA. Translation: BAB54956.1.
CCDSiCCDS11598.1.
RefSeqiNP_057154.2. NM_016070.3.
UniGeneiHs.5836.

3D structure databases

ProteinModelPortaliQ9Y3D9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119657. 38 interactions.
IntActiQ9Y3D9. 9 interactions.
STRINGi9606.ENSP00000320184.

PTM databases

PhosphoSiteiQ9Y3D9.

Polymorphism and mutation databases

BioMutaiMRPS23.
DMDMi31077184.

Proteomic databases

MaxQBiQ9Y3D9.
PaxDbiQ9Y3D9.
PeptideAtlasiQ9Y3D9.
PRIDEiQ9Y3D9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000313608; ENSP00000320184; ENSG00000181610.
GeneIDi51649.
KEGGihsa:51649.
UCSCiuc002ivc.3. human.

Organism-specific databases

CTDi51649.
GeneCardsiGC17M055916.
HGNCiHGNC:14509. MRPS23.
HPAiHPA023453.
MIMi611985. gene.
neXtProtiNX_Q9Y3D9.
PharmGKBiPA31011.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG81280.
GeneTreeiENSGT00390000009030.
HOGENOMiHOG000059557.
HOVERGENiHBG044512.
InParanoidiQ9Y3D9.
KOiK17402.
OMAiFSRTRNL.
OrthoDBiEOG7TBC3P.
PhylomeDBiQ9Y3D9.
TreeFamiTF106116.

Enzyme and pathway databases

ReactomeiREACT_267634. Mitochondrial translation initiation.
REACT_268133. Mitochondrial translation elongation.
REACT_268261. Mitochondrial translation termination.

Miscellaneous databases

GenomeRNAii51649.
NextBioi55600.
PROiQ9Y3D9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y3D9.
CleanExiHS_MRPS23.
ExpressionAtlasiQ9Y3D9. baseline and differential.
GenevestigatoriQ9Y3D9.

Family and domain databases

InterProiIPR019520. Ribosomal_S23/Rsm25.
IPR023611. Ribosomal_S23/S25_mit.
[Graphical view]
PANTHERiPTHR15925. PTHR15925. 1 hit.
PfamiPF10484. MRP-S23. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  2. "Human partial CDS from CD34+ stem cells."
    Ye M., Zhang Q.-H., Zhou J., Shen Y., Wu X.-Y., Guan Z.Q., Wang L., Fan H.-Y., Mao Y.-F., Dai M., Huang Q.-H., Chen S.-J., Chen Z.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Umbilical cord blood.
  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].
  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: Eye.
  6. "The human mitochondrial ribosomal protein genes: mapping of 54 genes to the chromosomes and implications for human disorders."
    Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S., Watanabe K., Tanaka T.
    Genomics 77:65-70(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-98.
  7. "A proteomics approach to the identification of mammalian mitochondrial small subunit ribosomal proteins."
    Koc E.C., Burkhart W., Blackburn K., Moseley A., Koc H., Spremulli L.L.
    J. Biol. Chem. 275:32585-32591(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  8. "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-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRT23_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3D9
Secondary accession number(s): B2R6V3
, Q96Q24, Q9BWH8, Q9P053
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 23, 2003
Last modified: April 29, 2015
This is version 117 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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.