RT31_HUMAN
ID RT31_HUMAN Reviewed; 395 AA.
AC Q92665; B2RCS3; Q5VYC8; Q8WTV8;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=28S ribosomal protein S31, mitochondrial;
DE Short=MRP-S31;
DE Short=S31mt;
DE AltName: Full=Imogen 38;
DE AltName: Full=Mitochondrial small ribosomal subunit protein mS31 {ECO:0000303|PubMed:25838379};
DE Flags: Precursor;
GN Name=MRPS31; Synonyms=IMOGN38;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ASN-279.
RC TISSUE=Skin;
RX PubMed=8567980; DOI=10.1172/jci118448;
RA Arden S.D., Roep B.O., Neophytou P.I., Usac E.F., Duinkerken G.,
RA de Vries R.R.P., Hutton J.C.;
RT "Imogen 38: a novel 38-kD islet mitochondrial autoantigen recognized by T
RT cells from a newly diagnosed type 1 diabetic patient.";
RL J. Clin. Invest. 97:551-561(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [6] {ECO:0000305}
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: identification
RT of the full complement of ribosomal proteins present.";
RL J. Biol. Chem. 276:19363-19374(2001).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [9]
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 [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), 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. {ECO:0000269|PubMed:25838379}.
CC -!- INTERACTION:
CC Q92665; P40763: STAT3; NbExp=2; IntAct=EBI-720602, EBI-518675;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11279123}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mS31 family. {ECO:0000305}.
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DR EMBL; Z68747; CAA92951.1; -; mRNA.
DR EMBL; AK315248; BAG37670.1; -; mRNA.
DR EMBL; AL355132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161614; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471075; EAX08629.1; -; Genomic_DNA.
DR EMBL; BC022045; AAH22045.1; -; mRNA.
DR CCDS; CCDS9372.1; -.
DR RefSeq; NP_005821.2; NM_005830.3.
DR PDB; 3J9M; EM; 3.50 A; AY=1-395.
DR PDB; 6NU2; EM; 3.90 A; AY=276-383.
DR PDB; 6NU3; EM; 4.40 A; AY=1-395.
DR PDB; 6RW4; EM; 2.97 A; Y=1-395.
DR PDB; 6RW5; EM; 3.14 A; Y=1-395.
DR PDB; 6VLZ; EM; 2.97 A; AY=1-395.
DR PDB; 6VMI; EM; 2.96 A; AY=1-395.
DR PDB; 6ZM5; EM; 2.89 A; AY=1-395.
DR PDB; 6ZM6; EM; 2.59 A; AY=1-395.
DR PDB; 6ZS9; EM; 4.00 A; AY=1-395.
DR PDB; 6ZSA; EM; 4.00 A; AY=1-395.
DR PDB; 6ZSB; EM; 4.50 A; AY=1-395.
DR PDB; 6ZSC; EM; 3.50 A; AY=1-395.
DR PDB; 6ZSD; EM; 3.70 A; AY=1-395.
DR PDB; 6ZSE; EM; 5.00 A; AY=1-395.
DR PDB; 6ZSG; EM; 4.00 A; AY=1-395.
DR PDB; 7A5F; EM; 4.40 A; Y6=1-395.
DR PDB; 7A5G; EM; 4.33 A; Y6=1-395.
DR PDB; 7A5I; EM; 3.70 A; Y6=1-395.
DR PDB; 7A5K; EM; 3.70 A; Y6=1-395.
DR PDB; 7L08; EM; 3.49 A; AY=1-395.
DR PDB; 7OG4; EM; 3.80 A; AY=1-395.
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; Q92665; -.
DR SMR; Q92665; -.
DR BioGRID; 115534; 279.
DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR CORUM; Q92665; -.
DR IntAct; Q92665; 115.
DR MINT; Q92665; -.
DR STRING; 9606.ENSP00000315397; -.
DR iPTMnet; Q92665; -.
DR MetOSite; Q92665; -.
DR PhosphoSitePlus; Q92665; -.
DR BioMuta; MRPS31; -.
DR DMDM; 93186129; -.
DR EPD; Q92665; -.
DR jPOST; Q92665; -.
DR MassIVE; Q92665; -.
DR MaxQB; Q92665; -.
DR PaxDb; Q92665; -.
DR PeptideAtlas; Q92665; -.
DR PRIDE; Q92665; -.
DR ProteomicsDB; 75398; -.
DR Antibodypedia; 23335; 166 antibodies from 26 providers.
DR DNASU; 10240; -.
DR Ensembl; ENST00000323563.8; ENSP00000315397.6; ENSG00000102738.8.
DR GeneID; 10240; -.
DR KEGG; hsa:10240; -.
DR MANE-Select; ENST00000323563.8; ENSP00000315397.6; NM_005830.4; NP_005821.2.
DR UCSC; uc001uxm.5; human.
DR CTD; 10240; -.
DR DisGeNET; 10240; -.
DR GeneCards; MRPS31; -.
DR HGNC; HGNC:16632; MRPS31.
DR HPA; ENSG00000102738; Low tissue specificity.
DR MIM; 611992; gene.
DR neXtProt; NX_Q92665; -.
DR OpenTargets; ENSG00000102738; -.
DR PharmGKB; PA31019; -.
DR VEuPathDB; HostDB:ENSG00000102738; -.
DR eggNOG; ENOG502QSX9; Eukaryota.
DR GeneTree; ENSGT00390000010017; -.
DR HOGENOM; CLU_052666_0_0_1; -.
DR InParanoid; Q92665; -.
DR OMA; FDEGYDN; -.
DR OrthoDB; 1584591at2759; -.
DR PhylomeDB; Q92665; -.
DR TreeFam; TF324305; -.
DR PathwayCommons; Q92665; -.
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; Q92665; -.
DR SIGNOR; Q92665; -.
DR BioGRID-ORCS; 10240; 289 hits in 1075 CRISPR screens.
DR ChiTaRS; MRPS31; human.
DR GenomeRNAi; 10240; -.
DR Pharos; Q92665; Tdark.
DR PRO; PR:Q92665; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q92665; protein.
DR Bgee; ENSG00000102738; Expressed in bronchial epithelial cell and 207 other tissues.
DR Genevisible; Q92665; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IC:ComplexPortal.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR InterPro; IPR026299; MRP-S31.
DR PANTHER; PTHR13231; PTHR13231; 1.
DR Pfam; PF15433; MRP-S31; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..65
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 66..395
FT /note="28S ribosomal protein S31, mitochondrial"
FT /id="PRO_0000030594"
FT REGION 70..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 241
FT /note="T -> M (in dbSNP:rs1854421)"
FT /id="VAR_052049"
FT VARIANT 279
FT /note="D -> N (in dbSNP:rs13508)"
FT /evidence="ECO:0000269|PubMed:8567980"
FT /id="VAR_061812"
FT CONFLICT 80
FT /note="T -> I (in Ref. 5; AAH22045)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="T -> A (in Ref. 5; AAH22045)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 45318 MW; 01ED04983ED56818 CRC64;
MFPRVSTFLP LRPLSRHPLS SGSPETSAAA IMLLTVRHGT VRYRSSALLA RTKNNIQRYF
GTNSVICSKK DKQSVRTEET SKETSESQDS EKENTKKDLL GIIKGMKVEL STVNVRTTKP
PKRRPLKSLE ATLGRLRRAT EYAPKKRIEP LSPELVAAAS AVADSLPFDK QTTKSELLSQ
LQQHEEESRA QRDAKRPKIS FSNIISDMKV ARSATARVRS RPELRIQFDE GYDNYPGQEK
TDDLKKRKNI FTGKRLNIFD MMAVTKEAPE TDTSPSLWDV EFAKQLATVN EQPLQNGFEE
LIQWTKEGKL WEFPINNEAG FDDDGSEFHE HIFLEKHLES FPKQGPIRHF MELVTCGLSK
NPYLSVKQKV EHIEWFRNYF NEKKDILKES NIQFN
