Full text data of MRPS16
MRPS16
(RPMS16)
[Confidence: low (only semi-automatic identification from reviews)]
28S ribosomal protein S16, mitochondrial; MRP-S16; S16mt; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
28S ribosomal protein S16, mitochondrial; MRP-S16; S16mt; Flags: Precursor
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y3D3
ID RT16_HUMAN Reviewed; 137 AA.
AC Q9Y3D3; Q96Q60;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=28S ribosomal protein S16, mitochondrial;
DE Short=MRP-S16;
DE Short=S16mt;
DE Flags: Precursor;
GN Name=MRPS16; Synonyms=RPMS16; ORFNames=CGI-132;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11402041; DOI=10.1074/jbc.M103236200;
RA Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA Watanabe K.;
RT "Proteomic analysis of the mammalian mitochondrial ribosome.
RT Identification of protein components in the 28S small subunit.";
RL J. Biol. Chem. 276:33181-33195(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-35.
RX PubMed=11543634; DOI=10.1006/geno.2001.6622;
RA Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S.,
RA Watanabe K., Tanaka T.;
RT "The human mitochondrial ribosomal protein genes: mapping of 54 genes
RT to the chromosomes and implications for human disorders.";
RL Genomics 77:65-70(2001).
RN [5]
RP IDENTIFICATION.
RX PubMed=11279123; DOI=10.1074/jbc.M100727200;
RA Koc E.C., Burkhart W., Blackburn K., Moseley A., Spremulli L.L.;
RT "The small subunit of the mammalian mitochondrial ribosome:
RT identification of the full complement of ribosomal proteins present.";
RL J. Biol. Chem. 276:19363-19374(2001).
RN [6]
RP INVOLVEMENT IN COXPD2.
RX PubMed=15505824; DOI=10.1002/ana.20282;
RA Miller C., Saada A., Shaul N., Shabtai N., Ben-Shalom E., Shaag A.,
RA Hershkovitz E., Elpeleg O.;
RT "Defective mitochondrial translation caused by a ribosomal protein
RT (MRPS16) mutation.";
RL Ann. Neurol. 56:734-738(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- SUBUNIT: Component of the mitochondrial ribosome small subunit
CC (28S) which comprises a 12S rRNA and about 30 distinct proteins.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 2 (COXPD2)
CC [MIM:610498]: A mitochondrial disease resulting in fatal neonatal
CC metabolic acidosis with agenesis of the corpus callosum. Note=The
CC disease is caused by mutations affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the ribosomal protein S16P family.
CC -!- WEB RESOURCE: Name=GeneReviews;
CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/MRPS16";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF151890; AAD34127.1; -; mRNA.
DR EMBL; AB049948; BAB41001.1; -; mRNA.
DR EMBL; BC021106; AAH21106.1; -; mRNA.
DR EMBL; AB051351; BAB54941.1; -; Genomic_DNA.
DR RefSeq; NP_057149.1; NM_016065.3.
DR UniGene; Hs.180312; -.
DR ProteinModelPortal; Q9Y3D3; -.
DR SMR; Q9Y3D3; 17-91.
DR IntAct; Q9Y3D3; 3.
DR MINT; MINT-6488773; -.
DR STRING; 9606.ENSP00000362036; -.
DR PhosphoSite; Q9Y3D3; -.
DR DMDM; 13633952; -.
DR PaxDb; Q9Y3D3; -.
DR PRIDE; Q9Y3D3; -.
DR DNASU; 51021; -.
DR Ensembl; ENST00000372945; ENSP00000362036; ENSG00000182180.
DR GeneID; 51021; -.
DR KEGG; hsa:51021; -.
DR UCSC; uc001jts.1; human.
DR CTD; 51021; -.
DR GeneCards; GC10M075008; -.
DR HGNC; HGNC:14048; MRPS16.
DR MIM; 609204; gene.
DR MIM; 610498; phenotype.
DR neXtProt; NX_Q9Y3D3; -.
DR Orphanet; 254920; Combined oxidative phosphorylation defect type 2.
DR PharmGKB; PA31000; -.
DR eggNOG; COG0228; -.
DR HOGENOM; HOG000246720; -.
DR HOVERGEN; HBG017758; -.
DR InParanoid; Q9Y3D3; -.
DR KO; K02959; -.
DR OrthoDB; EOG7P02KX; -.
DR GeneWiki; MRPS16; -.
DR GenomeRNAi; 51021; -.
DR NextBio; 53544; -.
DR PRO; PR:Q9Y3D3; -.
DR ArrayExpress; Q9Y3D3; -.
DR Bgee; Q9Y3D3; -.
DR CleanEx; HS_MRPS16; -.
DR Genevestigator; Q9Y3D3; -.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR Gene3D; 3.30.1320.10; -; 1.
DR InterPro; IPR000307; Ribosomal_S16.
DR InterPro; IPR023803; Ribosomal_S16_dom.
DR PANTHER; PTHR12919; PTHR12919; 1.
DR Pfam; PF00886; Ribosomal_S16; 1.
DR SUPFAM; SSF54565; SSF54565; 1.
DR TIGRFAMs; TIGR00002; S16; 1.
DR PROSITE; PS00732; RIBOSOMAL_S16; FALSE_NEG.
PE 1: Evidence at protein level;
KW Complete proteome; Mitochondrion; Phosphoprotein; Polymorphism;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Transit peptide.
FT TRANSIT 1 34 Mitochondrion (Potential).
FT CHAIN 35 137 28S ribosomal protein S16, mitochondrial.
FT /FTId=PRO_0000030618.
FT MOD_RES 130 130 Phosphothreonine.
FT VARIANT 12 12 Y -> H (in dbSNP:rs7905009).
FT /FTId=VAR_031525.
SQ SEQUENCE 137 AA; 15345 MW; C12B14B1B357F8D6 CRC64;
MVHLTTLLCK AYRGGHLTIR LALGGCTNRP FYRIVAAHNK CPRDGRFVEQ LGSYDPLPNS
HGEKLVALNL DRIRHWIGCG AHLSKPMEKL LGLAGFFPLH PMMITNAERL RRKRAREVLL
ASQKTDAEAT DTEATET
//
ID RT16_HUMAN Reviewed; 137 AA.
AC Q9Y3D3; Q96Q60;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 118.
DE RecName: Full=28S ribosomal protein S16, mitochondrial;
DE Short=MRP-S16;
DE Short=S16mt;
DE Flags: Precursor;
GN Name=MRPS16; Synonyms=RPMS16; ORFNames=CGI-132;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11402041; DOI=10.1074/jbc.M103236200;
RA Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA Watanabe K.;
RT "Proteomic analysis of the mammalian mitochondrial ribosome.
RT Identification of protein components in the 28S small subunit.";
RL J. Biol. Chem. 276:33181-33195(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 6-35.
RX PubMed=11543634; DOI=10.1006/geno.2001.6622;
RA Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S.,
RA Watanabe K., Tanaka T.;
RT "The human mitochondrial ribosomal protein genes: mapping of 54 genes
RT to the chromosomes and implications for human disorders.";
RL Genomics 77:65-70(2001).
RN [5]
RP IDENTIFICATION.
RX PubMed=11279123; DOI=10.1074/jbc.M100727200;
RA Koc E.C., Burkhart W., Blackburn K., Moseley A., Spremulli L.L.;
RT "The small subunit of the mammalian mitochondrial ribosome:
RT identification of the full complement of ribosomal proteins present.";
RL J. Biol. Chem. 276:19363-19374(2001).
RN [6]
RP INVOLVEMENT IN COXPD2.
RX PubMed=15505824; DOI=10.1002/ana.20282;
RA Miller C., Saada A., Shaul N., Shabtai N., Ben-Shalom E., Shaag A.,
RA Hershkovitz E., Elpeleg O.;
RT "Defective mitochondrial translation caused by a ribosomal protein
RT (MRPS16) mutation.";
RL Ann. Neurol. 56:734-738(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-130, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
CC -!- SUBUNIT: Component of the mitochondrial ribosome small subunit
CC (28S) which comprises a 12S rRNA and about 30 distinct proteins.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 2 (COXPD2)
CC [MIM:610498]: A mitochondrial disease resulting in fatal neonatal
CC metabolic acidosis with agenesis of the corpus callosum. Note=The
CC disease is caused by mutations affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the ribosomal protein S16P family.
CC -!- WEB RESOURCE: Name=GeneReviews;
CC URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/MRPS16";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF151890; AAD34127.1; -; mRNA.
DR EMBL; AB049948; BAB41001.1; -; mRNA.
DR EMBL; BC021106; AAH21106.1; -; mRNA.
DR EMBL; AB051351; BAB54941.1; -; Genomic_DNA.
DR RefSeq; NP_057149.1; NM_016065.3.
DR UniGene; Hs.180312; -.
DR ProteinModelPortal; Q9Y3D3; -.
DR SMR; Q9Y3D3; 17-91.
DR IntAct; Q9Y3D3; 3.
DR MINT; MINT-6488773; -.
DR STRING; 9606.ENSP00000362036; -.
DR PhosphoSite; Q9Y3D3; -.
DR DMDM; 13633952; -.
DR PaxDb; Q9Y3D3; -.
DR PRIDE; Q9Y3D3; -.
DR DNASU; 51021; -.
DR Ensembl; ENST00000372945; ENSP00000362036; ENSG00000182180.
DR GeneID; 51021; -.
DR KEGG; hsa:51021; -.
DR UCSC; uc001jts.1; human.
DR CTD; 51021; -.
DR GeneCards; GC10M075008; -.
DR HGNC; HGNC:14048; MRPS16.
DR MIM; 609204; gene.
DR MIM; 610498; phenotype.
DR neXtProt; NX_Q9Y3D3; -.
DR Orphanet; 254920; Combined oxidative phosphorylation defect type 2.
DR PharmGKB; PA31000; -.
DR eggNOG; COG0228; -.
DR HOGENOM; HOG000246720; -.
DR HOVERGEN; HBG017758; -.
DR InParanoid; Q9Y3D3; -.
DR KO; K02959; -.
DR OrthoDB; EOG7P02KX; -.
DR GeneWiki; MRPS16; -.
DR GenomeRNAi; 51021; -.
DR NextBio; 53544; -.
DR PRO; PR:Q9Y3D3; -.
DR ArrayExpress; Q9Y3D3; -.
DR Bgee; Q9Y3D3; -.
DR CleanEx; HS_MRPS16; -.
DR Genevestigator; Q9Y3D3; -.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0006412; P:translation; NAS:UniProtKB.
DR Gene3D; 3.30.1320.10; -; 1.
DR InterPro; IPR000307; Ribosomal_S16.
DR InterPro; IPR023803; Ribosomal_S16_dom.
DR PANTHER; PTHR12919; PTHR12919; 1.
DR Pfam; PF00886; Ribosomal_S16; 1.
DR SUPFAM; SSF54565; SSF54565; 1.
DR TIGRFAMs; TIGR00002; S16; 1.
DR PROSITE; PS00732; RIBOSOMAL_S16; FALSE_NEG.
PE 1: Evidence at protein level;
KW Complete proteome; Mitochondrion; Phosphoprotein; Polymorphism;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Transit peptide.
FT TRANSIT 1 34 Mitochondrion (Potential).
FT CHAIN 35 137 28S ribosomal protein S16, mitochondrial.
FT /FTId=PRO_0000030618.
FT MOD_RES 130 130 Phosphothreonine.
FT VARIANT 12 12 Y -> H (in dbSNP:rs7905009).
FT /FTId=VAR_031525.
SQ SEQUENCE 137 AA; 15345 MW; C12B14B1B357F8D6 CRC64;
MVHLTTLLCK AYRGGHLTIR LALGGCTNRP FYRIVAAHNK CPRDGRFVEQ LGSYDPLPNS
HGEKLVALNL DRIRHWIGCG AHLSKPMEKL LGLAGFFPLH PMMITNAERL RRKRAREVLL
ASQKTDAEAT DTEATET
//
MIM
609204
*RECORD*
*FIELD* NO
609204
*FIELD* TI
*609204 MITOCHONDRIAL RIBOSOMAL PROTEIN S16: MRPS16
*FIELD* TX
DESCRIPTION
Mammalian mitochondria carry out the synthesis of 13 polypeptides that
read moreare essential for oxidative phosphorylation. Mitochondrial ribosomes are
composed of small (28S) and large (39S) subunits. MRPS16 is a component
of the small subunit, which contains a 12S rRNA (MTRNR1; 561000) and
about 30 proteins. In mitochondrial ribosomes, the RNA molecules are
transcribed from the mitochondrial DNA, but the ribosomal proteins, such
as MRPS16, are encoded by the nuclear genome. They are synthesized in
the cytoplasm and imported into the mitochondria (Kenmochi et al., 2001;
Koc et al., 2001).
CLONING
By proteolytic digestion of whole bovine 28S subunits, followed by
peptide analysis and EST database analysis, Koc et al. (2001) identified
human MRPS16. The deduced 137-amino acid protein has a calculated
molecular mass of 15.3 kD. Following cleavage of the N-terminal 34-amino
acid mitochondrial import signal, the mature protein has a calculated
molecular mass of 11.5 kD. MRPS16 homologs were identified in mouse,
Drosophila, C. elegans, yeast, and E. coli genomes. Mouse and human
MRPS16 share 91.1% amino acid identity.
MAPPING
By radiation hybrid analysis and genomic sequence analysis, Kenmochi et
al. (2001) mapped the MRPS16 gene to chromosome 10q22.1.
MOLECULAR GENETICS
In a patient with combined oxidative phosphorylation deficiency (COXPD2;
610498) manifesting as agenesis of the corpus callosum, dysmorphism, and
fatal neonatal lactic acidosis, Miller et al. (2004) identified a
homozygous nonsense mutation in the MRPS16 gene (609204.0001), resulting
in a defect in mitochondrial translation.
NOMENCLATURE
Koc et al. (2001) proposed that mitochondrial ribosomal proteins with
prokaryotic homologs, such as MRPS16, be given the same number as the
corresponding ribosomal protein in E. coli. Since there are 21 proteins
in the bacterial ribosome, novel mammalian mitochondrial ribosomal
proteins without prokaryotic homologs are designated MRPS22 and above.
*FIELD* AV
.0001
COMBINED OXIDATIVE PHOSPHORYLATION DEFICIENCY 2
MRPS16, ARG111TER
In a patient with combined oxidative phosphorylation deficiency (610498)
manifesting as agenesis of the corpus callosum, dysmorphism, and fatal
neonatal lactic acidosis, Miller et al. (2004) identified a homozygous
331C-T transition in the MRPS16 gene, resulting in an arg111-to-ter
(R111X) substitution. The abundance of the 12S rRNA transcript was
markedly decreased to 12% of control values, which may be an indirect
result of the MRPS16 mutation. The parents were consanguineous and
heterozygous for the mutation.
*FIELD* RF
1. Kenmochi, N.; Suzuki, T.; Uechi, T.; Magoori, M.; Kuniba, M.; Higa,
S.; Watanabe, K.; Tanaka, T.: The human mitochondrial ribosomal protein
genes: mapping of 54 genes to the chromosomes and implications for
human disorders. Genomics 77: 65-70, 2001.
2. Koc, E. C.; Burkhart, W.; Blackburn, K.; Moseley, A.; Spremulli,
L. L.: The small subunit of the mammalian mitochondrial ribosome:
identification of the full complement of ribosomal proteins present. J.
Biol. Chem. 276: 19363-19374, 2001.
3. Miller, C.; Saada, A.; Shaul, N.; Shabtai, N.; Ben-Shalom, E.;
Shaag, A.; Hershkovitz, E.; Elpeleg, O.: Defective mitochondrial
translation caused by a ribosomal protein (MRPS16) mutation. Ann.
Neurol. 56: 734-738, 2004.
*FIELD* CN
Cassandra L. Kniffin - updated: 6/2/2005
*FIELD* CD
Patricia A. Hartz: 2/14/2005
*FIELD* ED
carol: 10/18/2006
ckniffin: 10/18/2006
wwang: 6/15/2005
wwang: 6/13/2005
ckniffin: 6/2/2005
mgross: 2/14/2005
*RECORD*
*FIELD* NO
609204
*FIELD* TI
*609204 MITOCHONDRIAL RIBOSOMAL PROTEIN S16: MRPS16
*FIELD* TX
DESCRIPTION
Mammalian mitochondria carry out the synthesis of 13 polypeptides that
read moreare essential for oxidative phosphorylation. Mitochondrial ribosomes are
composed of small (28S) and large (39S) subunits. MRPS16 is a component
of the small subunit, which contains a 12S rRNA (MTRNR1; 561000) and
about 30 proteins. In mitochondrial ribosomes, the RNA molecules are
transcribed from the mitochondrial DNA, but the ribosomal proteins, such
as MRPS16, are encoded by the nuclear genome. They are synthesized in
the cytoplasm and imported into the mitochondria (Kenmochi et al., 2001;
Koc et al., 2001).
CLONING
By proteolytic digestion of whole bovine 28S subunits, followed by
peptide analysis and EST database analysis, Koc et al. (2001) identified
human MRPS16. The deduced 137-amino acid protein has a calculated
molecular mass of 15.3 kD. Following cleavage of the N-terminal 34-amino
acid mitochondrial import signal, the mature protein has a calculated
molecular mass of 11.5 kD. MRPS16 homologs were identified in mouse,
Drosophila, C. elegans, yeast, and E. coli genomes. Mouse and human
MRPS16 share 91.1% amino acid identity.
MAPPING
By radiation hybrid analysis and genomic sequence analysis, Kenmochi et
al. (2001) mapped the MRPS16 gene to chromosome 10q22.1.
MOLECULAR GENETICS
In a patient with combined oxidative phosphorylation deficiency (COXPD2;
610498) manifesting as agenesis of the corpus callosum, dysmorphism, and
fatal neonatal lactic acidosis, Miller et al. (2004) identified a
homozygous nonsense mutation in the MRPS16 gene (609204.0001), resulting
in a defect in mitochondrial translation.
NOMENCLATURE
Koc et al. (2001) proposed that mitochondrial ribosomal proteins with
prokaryotic homologs, such as MRPS16, be given the same number as the
corresponding ribosomal protein in E. coli. Since there are 21 proteins
in the bacterial ribosome, novel mammalian mitochondrial ribosomal
proteins without prokaryotic homologs are designated MRPS22 and above.
*FIELD* AV
.0001
COMBINED OXIDATIVE PHOSPHORYLATION DEFICIENCY 2
MRPS16, ARG111TER
In a patient with combined oxidative phosphorylation deficiency (610498)
manifesting as agenesis of the corpus callosum, dysmorphism, and fatal
neonatal lactic acidosis, Miller et al. (2004) identified a homozygous
331C-T transition in the MRPS16 gene, resulting in an arg111-to-ter
(R111X) substitution. The abundance of the 12S rRNA transcript was
markedly decreased to 12% of control values, which may be an indirect
result of the MRPS16 mutation. The parents were consanguineous and
heterozygous for the mutation.
*FIELD* RF
1. Kenmochi, N.; Suzuki, T.; Uechi, T.; Magoori, M.; Kuniba, M.; Higa,
S.; Watanabe, K.; Tanaka, T.: The human mitochondrial ribosomal protein
genes: mapping of 54 genes to the chromosomes and implications for
human disorders. Genomics 77: 65-70, 2001.
2. Koc, E. C.; Burkhart, W.; Blackburn, K.; Moseley, A.; Spremulli,
L. L.: The small subunit of the mammalian mitochondrial ribosome:
identification of the full complement of ribosomal proteins present. J.
Biol. Chem. 276: 19363-19374, 2001.
3. Miller, C.; Saada, A.; Shaul, N.; Shabtai, N.; Ben-Shalom, E.;
Shaag, A.; Hershkovitz, E.; Elpeleg, O.: Defective mitochondrial
translation caused by a ribosomal protein (MRPS16) mutation. Ann.
Neurol. 56: 734-738, 2004.
*FIELD* CN
Cassandra L. Kniffin - updated: 6/2/2005
*FIELD* CD
Patricia A. Hartz: 2/14/2005
*FIELD* ED
carol: 10/18/2006
ckniffin: 10/18/2006
wwang: 6/15/2005
wwang: 6/13/2005
ckniffin: 6/2/2005
mgross: 2/14/2005
MIM
610498
*RECORD*
*FIELD* NO
610498
*FIELD* TI
#610498 COMBINED OXIDATIVE PHOSPHORYLATION DEFICIENCY 2; COXPD2
;;CORPUS CALLOSUM, AGENESIS OF, WITH DYSMORPHISM AND FATAL LACTIC ACIDOSIS
read more*FIELD* TX
A number sign (#) is used with this entry because combined oxidative
phosphorylation deficiency-2 (COXPD2) can be caused by homozygous
mutation in the MRPS16 gene (609204) on chromosome 10q22.
For a discussion of genetic heterogeneity of combined oxidative
phosphorylation deficiency, see COXPD1 (609060).
CLINICAL FEATURES
Miller et al. (2004) reported an infant, born of consanguineous parents,
with agenesis of the corpus callosum, dysmorphism, and fatal neonatal
lactic acidosis. The patient was small at birth, with dysmorphic facies,
low-set ears, nonpitting edema of the limbs, brachydactyly, and
redundant skin over the neck. She died of intractable metabolic acidosis
at age 3 days. Analysis of mitochondrial respiratory chain enzymes
showed severe defects in complexes I, II+III, IV, and V, but complex II,
which is solely encoded by the nuclear genome, was normal. Miller et al.
(2004) noted that certain dysmorphic features of the patient may have
been due to other factors, since she was born of consanguineous parents,
but concluded that the major defect was in the mitochondrial translation
apparatus.
MOLECULAR GENETICS
In a patient with combined oxidative phosphorylation deficiency, Miller
et al. (2004) identified a homozygous mutation in the MRPS16 gene
(609204.0001). The abundance of the 12S rRNA transcript was markedly
decreased to 12% of control values, which may be an indirect result of
the MRPS16 mutation. The parents were heterozygous for the mutation.
*FIELD* RF
1. Miller, C.; Saada, A.; Shaul, N.; Shabtai, N.; Ben-Shalom, E.;
Shaag, A.; Hershkovitz, E.; Elpeleg, O.: Defective mitochondrial
translation caused by a ribosomal protein (MRPS16) mutation. Ann.
Neurol. 56: 734-738, 2004.
*FIELD* CS
INHERITANCE:
Autosomal recessive
GROWTH:
[Other];
Small for gestational age
HEAD AND NECK:
[Face];
Dysmorphic facies;
[Ears];
Low-set ears;
[Neck];
Redundant skin over the neck
CARDIOVASCULAR:
[Vascular];
Patent ductus arteriosus
ABDOMEN:
[Gastrointestinal];
Poor feeding
SKELETAL:
[Hands];
Brachydactyly
MUSCLE, SOFT TISSUE:
Edema, nonpitting
NEUROLOGIC:
[Central nervous system];
Lethargy, neonatal;
Hypotonia, neonatal;
Decreased spontaneous movements;
Agenesis of the corpus callosum;
Dilated ventricles
METABOLIC FEATURES:
Lactic acidosis
LABORATORY ABNORMALITIES:
Increased serum lactate;
Abnormal liver function tests;
Decreased activity of mitochondrial respiratory complexes I, II+III,
IV, and V;
Normal complex II activity
MISCELLANEOUS:
Onset at birth;
Genetic heterogeneity (see COXPD1, 609060)
MOLECULAR BASIS:
Caused by mutation in the mitochondrial ribosomal protein S16 (MRPS16,
609204.0001)
*FIELD* CD
Cassandra L. Kniffin: 10/18/2006
*FIELD* ED
ckniffin: 10/18/2006
*FIELD* CD
Cassandra L. Kniffin: 10/16/2006
*FIELD* ED
carol: 07/21/2011
carol: 10/18/2006
ckniffin: 10/18/2006
*RECORD*
*FIELD* NO
610498
*FIELD* TI
#610498 COMBINED OXIDATIVE PHOSPHORYLATION DEFICIENCY 2; COXPD2
;;CORPUS CALLOSUM, AGENESIS OF, WITH DYSMORPHISM AND FATAL LACTIC ACIDOSIS
read more*FIELD* TX
A number sign (#) is used with this entry because combined oxidative
phosphorylation deficiency-2 (COXPD2) can be caused by homozygous
mutation in the MRPS16 gene (609204) on chromosome 10q22.
For a discussion of genetic heterogeneity of combined oxidative
phosphorylation deficiency, see COXPD1 (609060).
CLINICAL FEATURES
Miller et al. (2004) reported an infant, born of consanguineous parents,
with agenesis of the corpus callosum, dysmorphism, and fatal neonatal
lactic acidosis. The patient was small at birth, with dysmorphic facies,
low-set ears, nonpitting edema of the limbs, brachydactyly, and
redundant skin over the neck. She died of intractable metabolic acidosis
at age 3 days. Analysis of mitochondrial respiratory chain enzymes
showed severe defects in complexes I, II+III, IV, and V, but complex II,
which is solely encoded by the nuclear genome, was normal. Miller et al.
(2004) noted that certain dysmorphic features of the patient may have
been due to other factors, since she was born of consanguineous parents,
but concluded that the major defect was in the mitochondrial translation
apparatus.
MOLECULAR GENETICS
In a patient with combined oxidative phosphorylation deficiency, Miller
et al. (2004) identified a homozygous mutation in the MRPS16 gene
(609204.0001). The abundance of the 12S rRNA transcript was markedly
decreased to 12% of control values, which may be an indirect result of
the MRPS16 mutation. The parents were heterozygous for the mutation.
*FIELD* RF
1. Miller, C.; Saada, A.; Shaul, N.; Shabtai, N.; Ben-Shalom, E.;
Shaag, A.; Hershkovitz, E.; Elpeleg, O.: Defective mitochondrial
translation caused by a ribosomal protein (MRPS16) mutation. Ann.
Neurol. 56: 734-738, 2004.
*FIELD* CS
INHERITANCE:
Autosomal recessive
GROWTH:
[Other];
Small for gestational age
HEAD AND NECK:
[Face];
Dysmorphic facies;
[Ears];
Low-set ears;
[Neck];
Redundant skin over the neck
CARDIOVASCULAR:
[Vascular];
Patent ductus arteriosus
ABDOMEN:
[Gastrointestinal];
Poor feeding
SKELETAL:
[Hands];
Brachydactyly
MUSCLE, SOFT TISSUE:
Edema, nonpitting
NEUROLOGIC:
[Central nervous system];
Lethargy, neonatal;
Hypotonia, neonatal;
Decreased spontaneous movements;
Agenesis of the corpus callosum;
Dilated ventricles
METABOLIC FEATURES:
Lactic acidosis
LABORATORY ABNORMALITIES:
Increased serum lactate;
Abnormal liver function tests;
Decreased activity of mitochondrial respiratory complexes I, II+III,
IV, and V;
Normal complex II activity
MISCELLANEOUS:
Onset at birth;
Genetic heterogeneity (see COXPD1, 609060)
MOLECULAR BASIS:
Caused by mutation in the mitochondrial ribosomal protein S16 (MRPS16,
609204.0001)
*FIELD* CD
Cassandra L. Kniffin: 10/18/2006
*FIELD* ED
ckniffin: 10/18/2006
*FIELD* CD
Cassandra L. Kniffin: 10/16/2006
*FIELD* ED
carol: 07/21/2011
carol: 10/18/2006
ckniffin: 10/18/2006