RT35_HUMAN
ID RT35_HUMAN Reviewed; 323 AA.
AC P82673; Q32LZ1; Q6P4C6; Q7L1M6; Q8NBP4; Q96AI0; Q9H044; Q9HC14; Q9P1R5;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=28S ribosomal protein S35, mitochondrial;
DE Short=MRP-S35;
DE Short=S35mt;
DE AltName: Full=28S ribosomal protein S28, mitochondrial;
DE Short=MRP-S28;
DE Short=S28mt;
DE AltName: Full=Mitochondrial small ribosomal subunit protein mS35 {ECO:0000303|PubMed:25838379};
DE Flags: Precursor;
GN Name=MRPS35 {ECO:0000312|HGNC:HGNC:16635};
GN Synonyms=MRPS28 {ECO:0000303|PubMed:11344316};
GN ORFNames=HDCMD11P, MDS023, PSEC0213;
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:AAG14958.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hematopoietic stem cell;
RA Huang C., Qian B., Tu Y., Gu W., Wang Y., Han Z., Chen Z.;
RT "Novel genes expressed in hematopoietic stem/progenitor cells from
RT myelodysplastic syndrome patients.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Teratocarcinoma;
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 MRNA] (ISOFORM 1).
RC TISSUE=Embryo;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAI09373.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon {ECO:0000312|EMBL:AAH17086.1},
RC Lung {ECO:0000312|EMBL:AAH63515.1}, and
RC Pancreas {ECO:0000312|EMBL:AAH28346.2};
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-323 (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAG14958.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 180-323 (ISOFORM 1).
RC TISSUE=Dendritic cell {ECO:0000312|EMBL:AAF65185.1};
RA Zhao Z., Huang X., Li N., Zhu X., Cao X.;
RT "A novel gene from human dendritic cells.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=11344316; DOI=10.1110/ps.35301;
RA Koc E.C., Burkhart W., Blackburn K., Koc H., Moseley A., Spremulli L.L.;
RT "Identification of four proteins from the small subunit of the mammalian
RT mitochondrial ribosome using a proteomics approach.";
RL Protein Sci. 10:471-481(2001).
RN [8]
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 [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), SUBUNIT, AND SUBCELLULAR
RP LOCATION.
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25838379}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000305};
CC IsoId=P82673-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=P82673-2; Sequence=VSP_054096, VSP_054097;
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mS35 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG14958.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF182422; AAG14958.1; ALT_FRAME; mRNA.
DR EMBL; AK075378; BAC11579.1; -; mRNA.
DR EMBL; AK075515; BAC11664.1; -; mRNA.
DR EMBL; BC015862; AAH15862.2; -; mRNA.
DR EMBL; BC017086; AAH17086.1; -; mRNA.
DR EMBL; BC028346; AAH28346.2; -; mRNA.
DR EMBL; BC063515; AAH63515.1; -; mRNA.
DR EMBL; BC109372; AAI09373.1; -; mRNA.
DR EMBL; AL512733; CAC21665.1; -; mRNA.
DR EMBL; AF068296; AAF65185.1; -; mRNA.
DR CCDS; CCDS53769.1; -. [P82673-2]
DR CCDS; CCDS8714.1; -. [P82673-1]
DR RefSeq; NP_001177793.1; NM_001190864.1. [P82673-2]
DR RefSeq; NP_068593.2; NM_021821.3. [P82673-1]
DR PDB; 3J9M; EM; 3.50 A; A1=1-323.
DR PDB; 6NU2; EM; 3.90 A; A1=52-323.
DR PDB; 6NU3; EM; 4.40 A; A1=1-323.
DR PDB; 6RW4; EM; 2.97 A; 1=1-323.
DR PDB; 6RW5; EM; 3.14 A; 1=1-323.
DR PDB; 6VLZ; EM; 2.97 A; A1=1-323.
DR PDB; 6VMI; EM; 2.96 A; A1=1-323.
DR PDB; 6ZM5; EM; 2.89 A; A1=1-323.
DR PDB; 6ZM6; EM; 2.59 A; A1=1-323.
DR PDB; 6ZS9; EM; 4.00 A; A1=1-323.
DR PDB; 6ZSA; EM; 4.00 A; A1=1-323.
DR PDB; 6ZSB; EM; 4.50 A; A1=1-323.
DR PDB; 6ZSC; EM; 3.50 A; A1=1-323.
DR PDB; 6ZSD; EM; 3.70 A; A1=1-323.
DR PDB; 6ZSE; EM; 5.00 A; A1=1-323.
DR PDB; 6ZSG; EM; 4.00 A; A1=1-323.
DR PDB; 7A5F; EM; 4.40 A; b6=1-323.
DR PDB; 7A5G; EM; 4.33 A; b6=1-323.
DR PDB; 7A5I; EM; 3.70 A; b6=1-323.
DR PDB; 7A5K; EM; 3.70 A; b6=1-323.
DR PDB; 7L08; EM; 3.49 A; A1=1-323.
DR PDB; 7OG4; EM; 3.80 A; A1=1-323.
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; P82673; -.
DR SMR; P82673; -.
DR BioGRID; 121919; 297.
DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR CORUM; P82673; -.
DR IntAct; P82673; 102.
DR MINT; P82673; -.
DR STRING; 9606.ENSP00000081029; -.
DR GlyGen; P82673; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P82673; -.
DR MetOSite; P82673; -.
DR PhosphoSitePlus; P82673; -.
DR BioMuta; MRPS35; -.
DR DMDM; 74708095; -.
DR EPD; P82673; -.
DR jPOST; P82673; -.
DR MassIVE; P82673; -.
DR MaxQB; P82673; -.
DR PaxDb; P82673; -.
DR PeptideAtlas; P82673; -.
DR PRIDE; P82673; -.
DR ProteomicsDB; 57712; -. [P82673-1]
DR ProteomicsDB; 57713; -. [P82673-2]
DR Antibodypedia; 24450; 123 antibodies from 24 providers.
DR DNASU; 60488; -.
DR Ensembl; ENST00000081029.8; ENSP00000081029.3; ENSG00000061794.13. [P82673-1]
DR Ensembl; ENST00000538315.5; ENSP00000445390.1; ENSG00000061794.13. [P82673-2]
DR GeneID; 60488; -.
DR KEGG; hsa:60488; -.
DR MANE-Select; ENST00000081029.8; ENSP00000081029.3; NM_021821.4; NP_068593.2.
DR UCSC; uc001rih.4; human. [P82673-1]
DR CTD; 60488; -.
DR DisGeNET; 60488; -.
DR GeneCards; MRPS35; -.
DR HGNC; HGNC:16635; MRPS35.
DR HPA; ENSG00000061794; Low tissue specificity.
DR MIM; 611995; gene.
DR neXtProt; NX_P82673; -.
DR OpenTargets; ENSG00000061794; -.
DR PharmGKB; PA31022; -.
DR VEuPathDB; HostDB:ENSG00000061794; -.
DR eggNOG; KOG3933; Eukaryota.
DR GeneTree; ENSGT00390000003443; -.
DR HOGENOM; CLU_060973_0_1_1; -.
DR InParanoid; P82673; -.
DR OMA; AHARDKF; -.
DR OrthoDB; 1339087at2759; -.
DR PhylomeDB; P82673; -.
DR TreeFam; TF318686; -.
DR PathwayCommons; P82673; -.
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; P82673; -.
DR SIGNOR; P82673; -.
DR BioGRID-ORCS; 60488; 406 hits in 1093 CRISPR screens.
DR ChiTaRS; MRPS35; human.
DR GeneWiki; MRPS35; -.
DR GenomeRNAi; 60488; -.
DR Pharos; P82673; Tdark.
DR PRO; PR:P82673; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P82673; protein.
DR Bgee; ENSG00000061794; Expressed in rectum and 202 other tissues.
DR ExpressionAtlas; P82673; baseline and differential.
DR Genevisible; P82673; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; ISS:UniProtKB.
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; IC:ComplexPortal.
DR InterPro; IPR039848; Ribosomal_S24/S35.
DR InterPro; IPR019349; Ribosomal_S24/S35_mit.
DR PANTHER; PTHR13490; PTHR13490; 1.
DR Pfam; PF10213; MRP-S28; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Mitochondrion;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000305"
FT CHAIN ?..323
FT /note="28S ribosomal protein S35, mitochondrial"
FT /id="PRO_0000046055"
FT REGION 31..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 257..321
FT /evidence="ECO:0000255"
FT COMPBIAS 43..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 176..194
FT /note="KLSSLNLDDHAKKKLIKLV -> PFKEAELRLCSVSTNSVIP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054096"
FT VAR_SEQ 195..323
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054097"
FT VARIANT 6
FT /note="L -> I (in dbSNP:rs35475802)"
FT /id="VAR_052051"
SQ SEQUENCE 323 AA; 36844 MW; B29F819E914F2B49 CRC64;
MAAAALPAWL SLQSRARTLR AFSTAVYSAT PVPTPSLPER TPGNERPPRR KALPPRTEKM
AVDQDWPSVY PVAAPFKPSA VPLPVRMGYP VKKGVPMAKE GNLELLKIPN FLHLTPVAIK
KHCEALKDFC TEWPAALDSD EKCEKHFPIE IDSTDYVSSG PSVRNPRARV VVLRVKLSSL
NLDDHAKKKL IKLVGERYCK TTDVLTIKTD RCPLRRQNYD YAVYLLTVLY HESWNTEEWE
KSKTEADMEE YIWENSSSER NILETLLQMK AAEKNMEINK EELLGTKEIE EYKKSVVSLK
NEEENENSIS QYKESVKRLL NVT
