RT14_HUMAN
ID RT14_HUMAN Reviewed; 128 AA.
AC O60783; Q5R358;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=28S ribosomal protein S14, mitochondrial;
DE Short=MRP-S14;
DE Short=S14mt;
DE AltName: Full=Mitochondrial small ribosomal subunit protein uS14m {ECO:0000303|PubMed:25838379};
GN Name=MRPS14 {ECO:0000312|HGNC:HGNC:14049};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAB41269.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Rhodes S.;
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:Z99297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAH09788.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow {ECO:0000269|PubMed:15489334};
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=10938081; DOI=10.1074/jbc.m003596200;
RA Koc E.C., Burkhart W., Blackburn K., Moseley A., Koc H., Spremulli L.L.;
RT "A proteomics approach to the identification of mammalian mitochondrial
RT small subunit ribosomal proteins.";
RL J. Biol. Chem. 275:32585-32591(2000).
RN [5]
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., Buerckstuemmer T.,
RA 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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [7]
RP INVOLVEMENT IN COXPD38, AND VARIANT COXPD38 CYS-108.
RX PubMed=30358850; DOI=10.1093/hmg/ddy374;
RA Jackson C.B., Huemer M., Bolognini R., Martin F., Szinnai G., Donner B.C.,
RA Richter U., Battersby B.J., Nuoffer J.M., Suomalainen A., Schaller A.;
RT "A variant in MRPS14 (uS14m) causes perinatal hypertrophic cardiomyopathy
RT with neonatal lactic acidosis, growth retardation, dysmorphic features and
RT neurological involvement.";
RL Hum. Mol. Genet. 28:639-649(2019).
RN [8] {ECO:0007744|PDB:3J9M}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=25838379; DOI=10.1126/science.aaa1193;
RA Amunts A., Brown A., Toots J., Scheres S.H., Ramakrishnan V.;
RT "Ribosome. The structure of the human mitochondrial ribosome.";
RL Science 348:95-98(2015).
CC -!- SUBUNIT: Component of the mitochondrial small ribosomal subunit (mt-
CC SSU). Mature mammalian 55S mitochondrial ribosomes consist of a small
CC (28S) and a large (39S) subunit. The 28S small subunit contains a 12S
CC ribosomal RNA (12S mt-rRNA) and 30 different proteins. The 39S large
CC subunit contains a 16S rRNA (16S mt-rRNA), a copy of mitochondrial
CC valine transfer RNA (mt-tRNA(Val)), which plays an integral structural
CC role, and 52 different proteins (PubMed:25838379). Interacts with LIAT1
CC (By similarity). {ECO:0000250|UniProtKB:Q9CR88,
CC ECO:0000269|PubMed:25838379}.
CC -!- INTERACTION:
CC O60783; P22607: FGFR3; NbExp=3; IntAct=EBI-1045956, EBI-348399;
CC O60783; P06396: GSN; NbExp=3; IntAct=EBI-1045956, EBI-351506;
CC O60783; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-1045956, EBI-741480;
CC O60783; Q9Y649; NbExp=3; IntAct=EBI-1045956, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25838379}.
CC -!- DISEASE: Combined oxidative phosphorylation deficiency 38 (COXPD38)
CC [MIM:618378]: An autosomal recessive disorder due to mitochondrial
CC dysfunction and characterized by perinatal hypertrophic cardiomyopathy,
CC growth retardation, muscle hypotonia, elevated lactate, dysmorphy and
CC intellectual disability. {ECO:0000269|PubMed:30358850}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS14 family.
CC {ECO:0000305}.
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DR EMBL; AL049705; CAB41269.1; -; mRNA.
DR EMBL; Z99297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC009788; AAH09788.1; -; mRNA.
DR CCDS; CCDS1316.1; -.
DR RefSeq; NP_071383.1; NM_022100.2.
DR PDB; 3J9M; EM; 3.50 A; AK=1-128.
DR PDB; 6NU2; EM; 3.90 A; AK=28-128.
DR PDB; 6NU3; EM; 4.40 A; AK=1-128.
DR PDB; 6RW4; EM; 2.97 A; K=1-128.
DR PDB; 6RW5; EM; 3.14 A; K=1-128.
DR PDB; 6VLZ; EM; 2.97 A; AK=1-128.
DR PDB; 6VMI; EM; 2.96 A; AK=1-128.
DR PDB; 6ZM5; EM; 2.89 A; AK=1-128.
DR PDB; 6ZM6; EM; 2.59 A; AK=1-128.
DR PDB; 6ZS9; EM; 4.00 A; AK=1-128.
DR PDB; 6ZSA; EM; 4.00 A; AK=1-128.
DR PDB; 6ZSB; EM; 4.50 A; AK=1-128.
DR PDB; 6ZSC; EM; 3.50 A; AK=1-128.
DR PDB; 6ZSD; EM; 3.70 A; AK=1-128.
DR PDB; 6ZSE; EM; 5.00 A; AK=1-128.
DR PDB; 6ZSG; EM; 4.00 A; AK=1-128.
DR PDB; 7A5F; EM; 4.40 A; K6=1-128.
DR PDB; 7A5G; EM; 4.33 A; K6=1-128.
DR PDB; 7A5I; EM; 3.70 A; K6=1-128.
DR PDB; 7A5K; EM; 3.70 A; K6=1-128.
DR PDB; 7L08; EM; 3.49 A; AK=1-128.
DR PDB; 7OG4; EM; 3.80 A; AK=1-128.
DR PDBsum; 3J9M; -.
DR PDBsum; 6NU2; -.
DR PDBsum; 6NU3; -.
DR PDBsum; 6RW4; -.
DR PDBsum; 6RW5; -.
DR PDBsum; 6VLZ; -.
DR PDBsum; 6VMI; -.
DR PDBsum; 6ZM5; -.
DR PDBsum; 6ZM6; -.
DR PDBsum; 6ZS9; -.
DR PDBsum; 6ZSA; -.
DR PDBsum; 6ZSB; -.
DR PDBsum; 6ZSC; -.
DR PDBsum; 6ZSD; -.
DR PDBsum; 6ZSE; -.
DR PDBsum; 6ZSG; -.
DR PDBsum; 7A5F; -.
DR PDBsum; 7A5G; -.
DR PDBsum; 7A5I; -.
DR PDBsum; 7A5K; -.
DR PDBsum; 7L08; -.
DR PDBsum; 7OG4; -.
DR AlphaFoldDB; O60783; -.
DR SMR; O60783; -.
DR BioGRID; 121999; 221.
DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR CORUM; O60783; -.
DR IntAct; O60783; 58.
DR MINT; O60783; -.
DR STRING; 9606.ENSP00000420714; -.
DR GlyGen; O60783; 1 site, 1 O-linked glycan (1 site).
DR SwissPalm; O60783; -.
DR BioMuta; MRPS14; -.
DR EPD; O60783; -.
DR jPOST; O60783; -.
DR MassIVE; O60783; -.
DR MaxQB; O60783; -.
DR PaxDb; O60783; -.
DR PeptideAtlas; O60783; -.
DR PRIDE; O60783; -.
DR ProteomicsDB; 49596; -.
DR TopDownProteomics; O60783; -.
DR Antibodypedia; 63335; 56 antibodies from 14 providers.
DR DNASU; 63931; -.
DR Ensembl; ENST00000476371.1; ENSP00000420714.1; ENSG00000120333.4.
DR GeneID; 63931; -.
DR KEGG; hsa:63931; -.
DR MANE-Select; ENST00000476371.1; ENSP00000420714.1; NM_022100.3; NP_071383.1.
DR UCSC; uc001gkk.4; human.
DR CTD; 63931; -.
DR DisGeNET; 63931; -.
DR GeneCards; MRPS14; -.
DR HGNC; HGNC:14049; MRPS14.
DR HPA; ENSG00000120333; Low tissue specificity.
DR MalaCards; MRPS14; -.
DR MIM; 611978; gene.
DR MIM; 618378; phenotype.
DR neXtProt; NX_O60783; -.
DR OpenTargets; ENSG00000120333; -.
DR PharmGKB; PA30998; -.
DR VEuPathDB; HostDB:ENSG00000120333; -.
DR eggNOG; KOG1741; Eukaryota.
DR GeneTree; ENSGT00390000015663; -.
DR HOGENOM; CLU_139869_1_0_1; -.
DR InParanoid; O60783; -.
DR OMA; FGLCRNQ; -.
DR OrthoDB; 1612572at2759; -.
DR PhylomeDB; O60783; -.
DR TreeFam; TF320418; -.
DR PathwayCommons; O60783; -.
DR Reactome; R-HSA-5368286; Mitochondrial translation initiation.
DR Reactome; R-HSA-5389840; Mitochondrial translation elongation.
DR Reactome; R-HSA-5419276; Mitochondrial translation termination.
DR SignaLink; O60783; -.
DR SIGNOR; O60783; -.
DR BioGRID-ORCS; 63931; 535 hits in 1092 CRISPR screens.
DR ChiTaRS; MRPS14; human.
DR GenomeRNAi; 63931; -.
DR Pharos; O60783; Tdark.
DR PRO; PR:O60783; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O60783; protein.
DR Bgee; ENSG00000120333; Expressed in tendon of biceps brachii and 202 other tissues.
DR ExpressionAtlas; O60783; baseline and differential.
DR Genevisible; O60783; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005761; C:mitochondrial ribosome; NAS:UniProtKB.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IMP:UniProtKB.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR InterPro; IPR001209; Ribosomal_S14.
DR PANTHER; PTHR19836; PTHR19836; 1.
DR Pfam; PF00253; Ribosomal_S14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Mitochondrion;
KW Primary mitochondrial disease; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..128
FT /note="28S ribosomal protein S14, mitochondrial"
FT /id="PRO_0000131013"
FT VARIANT 108
FT /note="R -> C (in COXPD38; dbSNP:rs990763738)"
FT /evidence="ECO:0000269|PubMed:30358850"
FT /id="VAR_082116"
SQ SEQUENCE 128 AA; 15139 MW; FFF3F3C70214EDE4 CRC64;
MAAFMLGSLL RTFKQMVPSS ASGQVRSHYV DWRMWRDVKR RKMAYEYADE RLRINSLRKN
TILPKILQDV ADEEIAALPR DSCPVRIRNR CVMTSRPRGV KRRWRLSRIV FRHLADHGQL
SGIQRATW
