RT29_HUMAN
ID RT29_HUMAN Reviewed; 398 AA.
AC P51398; B4DP59; B4DY62; E7EM60; Q13044; Q68CT7; Q96Q20;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=28S ribosomal protein S29, mitochondrial;
DE Short=MRP-S29;
DE Short=S29mt;
DE AltName: Full=Death-associated protein 3;
DE Short=DAP-3;
DE AltName: Full=Ionizing radiation resistance conferring protein;
DE AltName: Full=Mitochondrial small ribosomal subunit protein mS29 {ECO:0000303|PubMed:25838379};
DE Flags: Precursor;
GN Name=DAP3; Synonyms=MRPS29;
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] (ISOFORM 1).
RC TISSUE=Cervix carcinoma;
RA Henning K.A.;
RT "The molecular genetics of human diseases with defective DNA damage
RT processing.";
RL Thesis (1993), University of Stanford, United States.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=7499268; DOI=10.1074/jbc.270.46.27932;
RA Kissil J.L., Deiss L.P., Bayewitch M., Raveh T., Khaspekov G., Kimchi A.;
RT "Isolation of DAP3, a novel mediator of interferon-gamma-induced cell
RT death.";
RL J. Biol. Chem. 270:27932-27936(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon endothelium;
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]
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 [7]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-235.
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 to
RT the chromosomes and implications for human disorders.";
RL Genomics 77:65-70(2001).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=11162496; DOI=10.1006/bbrc.2000.4119;
RA Morgan C.J., Jacques C., Savagner F., Tourmen Y., Mirebeau D.P.,
RA Malthiery Y., Reynier P.;
RT "A conserved N-terminal sequence targets human DAP3 to mitochondria.";
RL Biochem. Biophys. Res. Commun. 280:177-181(2001).
RN [11]
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 [12]
RP INTERACTION WITH NOA1.
RX PubMed=19103604; DOI=10.1074/jbc.m807797200;
RA Tang T., Zheng B., Chen S.H., Murphy A.N., Kudlicka K., Zhou H.,
RA Farquhar M.G.;
RT "hNOA1 interacts with complex I and DAP3 and regulates mitochondrial
RT respiration and apoptosis.";
RL J. Biol. Chem. 284:5414-5424(2009).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-175 AND LYS-207, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [14]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH DELE1.
RX PubMed=20563667; DOI=10.1007/s10495-010-0519-3;
RA Harada T., Iwai A., Miyazaki T.;
RT "Identification of DELE, a novel DAP3-binding protein which is crucial for
RT death receptor-mediated apoptosis induction.";
RL Apoptosis 15:1247-1255(2010).
RN [15]
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 [16]
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 [17]
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 -!- FUNCTION: Involved in mediating interferon-gamma-induced cell death.
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 DELE1
CC (PubMed:20563667). Interacts with NOA1 (PubMed:19103604).
CC {ECO:0000269|PubMed:19103604, ECO:0000269|PubMed:20563667,
CC ECO:0000269|PubMed:25838379}.
CC -!- INTERACTION:
CC P51398; Q8NC60: NOA1; NbExp=5; IntAct=EBI-355912, EBI-717871;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11162496,
CC ECO:0000269|PubMed:20563667}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P51398-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51398-2; Sequence=VSP_042790;
CC Name=3;
CC IsoId=P51398-3; Sequence=VSP_044639;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mS29 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA57443.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U18321; AAA57443.1; ALT_FRAME; mRNA.
DR EMBL; X83544; CAA58535.1; -; mRNA.
DR EMBL; AK293117; BAF85806.1; -; mRNA.
DR EMBL; AK298201; BAG60471.1; -; mRNA.
DR EMBL; AK302281; BAG63624.1; -; mRNA.
DR EMBL; BT019494; AAV38301.1; -; mRNA.
DR EMBL; CR749790; CAH18651.1; -; mRNA.
DR EMBL; AL162734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53044.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53045.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53047.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53048.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53049.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53051.1; -; Genomic_DNA.
DR EMBL; BC107487; AAI07488.1; -; mRNA.
DR EMBL; BC107488; AAI07489.1; -; mRNA.
DR CCDS; CCDS1120.1; -. [P51398-1]
DR CCDS; CCDS55646.1; -. [P51398-3]
DR CCDS; CCDS55647.1; -. [P51398-2]
DR PIR; G01589; G01589.
DR RefSeq; NP_001186778.1; NM_001199849.1. [P51398-1]
DR RefSeq; NP_001186779.1; NM_001199850.1. [P51398-3]
DR RefSeq; NP_001186780.1; NM_001199851.1. [P51398-2]
DR RefSeq; NP_004623.1; NM_004632.3. [P51398-1]
DR RefSeq; NP_387506.1; NM_033657.2. [P51398-1]
DR RefSeq; XP_005245537.1; XM_005245480.2. [P51398-3]
DR RefSeq; XP_005245538.1; XM_005245481.2. [P51398-2]
DR RefSeq; XP_016857780.1; XM_017002291.1. [P51398-3]
DR RefSeq; XP_016857781.1; XM_017002292.1. [P51398-2]
DR RefSeq; XP_016857782.1; XM_017002293.1. [P51398-2]
DR PDB; 3J9M; EM; 3.50 A; AX=1-398.
DR PDB; 6NU2; EM; 3.90 A; AX=51-398.
DR PDB; 6NU3; EM; 4.40 A; AX=1-398.
DR PDB; 6RW4; EM; 2.97 A; X=1-398.
DR PDB; 6RW5; EM; 3.14 A; X=1-398.
DR PDB; 6VLZ; EM; 2.97 A; AX=1-398.
DR PDB; 6VMI; EM; 2.96 A; AX=1-398.
DR PDB; 6ZM5; EM; 2.89 A; AX=1-398.
DR PDB; 6ZM6; EM; 2.59 A; AX=1-398.
DR PDB; 6ZS9; EM; 4.00 A; AX=51-398.
DR PDB; 6ZSA; EM; 4.00 A; AX=51-398.
DR PDB; 6ZSB; EM; 4.50 A; AX=51-398.
DR PDB; 6ZSC; EM; 3.50 A; AX=51-398.
DR PDB; 6ZSD; EM; 3.70 A; AX=51-398.
DR PDB; 6ZSE; EM; 5.00 A; AX=51-398.
DR PDB; 6ZSG; EM; 4.00 A; AX=51-398.
DR PDB; 7A5F; EM; 4.40 A; X6=1-398.
DR PDB; 7A5G; EM; 4.33 A; X6=1-398.
DR PDB; 7A5I; EM; 3.70 A; X6=1-398.
DR PDB; 7A5K; EM; 3.70 A; X6=1-398.
DR PDB; 7L08; EM; 3.49 A; AX=1-398.
DR PDB; 7OG4; EM; 3.80 A; AX=1-398.
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; P51398; -.
DR SMR; P51398; -.
DR BioGRID; 113587; 303.
DR ComplexPortal; CPX-5225; 28S mitochondrial small ribosomal subunit.
DR CORUM; P51398; -.
DR IntAct; P51398; 103.
DR MINT; P51398; -.
DR STRING; 9606.ENSP00000357320; -.
DR ChEMBL; CHEMBL4295776; -.
DR GlyGen; P51398; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P51398; -.
DR PhosphoSitePlus; P51398; -.
DR SwissPalm; P51398; -.
DR BioMuta; DAP3; -.
DR DMDM; 1706299; -.
DR EPD; P51398; -.
DR jPOST; P51398; -.
DR MassIVE; P51398; -.
DR MaxQB; P51398; -.
DR PaxDb; P51398; -.
DR PeptideAtlas; P51398; -.
DR PRIDE; P51398; -.
DR ProteomicsDB; 16866; -.
DR ProteomicsDB; 56303; -. [P51398-1]
DR ProteomicsDB; 56304; -. [P51398-2]
DR Antibodypedia; 1656; 488 antibodies from 38 providers.
DR DNASU; 7818; -.
DR Ensembl; ENST00000343043.7; ENSP00000341692.3; ENSG00000132676.16. [P51398-1]
DR Ensembl; ENST00000368336.10; ENSP00000357320.5; ENSG00000132676.16. [P51398-1]
DR Ensembl; ENST00000421487.6; ENSP00000412605.2; ENSG00000132676.16. [P51398-3]
DR Ensembl; ENST00000471642.6; ENSP00000476592.1; ENSG00000132676.16. [P51398-2]
DR Ensembl; ENST00000535183.5; ENSP00000445003.1; ENSG00000132676.16. [P51398-2]
DR GeneID; 7818; -.
DR KEGG; hsa:7818; -.
DR MANE-Select; ENST00000368336.10; ENSP00000357320.5; NM_004632.4; NP_004623.1.
DR UCSC; uc001flq.4; human. [P51398-1]
DR CTD; 7818; -.
DR DisGeNET; 7818; -.
DR GeneCards; DAP3; -.
DR HGNC; HGNC:2673; DAP3.
DR HPA; ENSG00000132676; Low tissue specificity.
DR MIM; 602074; gene.
DR neXtProt; NX_P51398; -.
DR OpenTargets; ENSG00000132676; -.
DR PharmGKB; PA27141; -.
DR VEuPathDB; HostDB:ENSG00000132676; -.
DR eggNOG; KOG3928; Eukaryota.
DR GeneTree; ENSGT00390000015248; -.
DR HOGENOM; CLU_048181_0_0_1; -.
DR InParanoid; P51398; -.
DR OMA; DITNYDW; -.
DR OrthoDB; 1593937at2759; -.
DR PhylomeDB; P51398; -.
DR TreeFam; TF313726; -.
DR PathwayCommons; P51398; -.
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; P51398; -.
DR SIGNOR; P51398; -.
DR BioGRID-ORCS; 7818; 498 hits in 1105 CRISPR screens.
DR ChiTaRS; DAP3; human.
DR GeneWiki; DAP3; -.
DR GenomeRNAi; 7818; -.
DR Pharos; P51398; Tbio.
DR PRO; PR:P51398; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P51398; protein.
DR Bgee; ENSG00000132676; Expressed in body of pancreas and 203 other tissues.
DR ExpressionAtlas; P51398; baseline and differential.
DR Genevisible; P51398; 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:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:ProtInc.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR019368; Ribosomal_S23/S29_mit.
DR InterPro; IPR008092; Ribosomal_S29_mit.
DR PANTHER; PTHR12810; PTHR12810; 1.
DR Pfam; PF10236; DAP3; 1.
DR PRINTS; PR01716; DEATHASSOCP3.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis; GTP-binding;
KW Mitochondrion; Nucleotide-binding; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 22..398
FT /note="28S ribosomal protein S29, mitochondrial"
FT /id="PRO_0000087717"
FT REGION 39..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 100
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:25838379"
FT BINDING 128..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000305|PubMed:25838379"
FT MOD_RES 175
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 207
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 16..56
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042790"
FT VAR_SEQ 57..90
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044639"
FT VARIANT 240
FT /note="V -> F (in dbSNP:rs57692591)"
FT /id="VAR_061811"
FT CONFLICT 157
FT /note="D -> Y (in Ref. 3; BAG63624)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 398 AA; 45566 MW; 778AF183FA04DEC8 CRC64;
MMLKGITRLI SRIHKLDPGR FLHMGTQARQ SIAAHLDNQV PVESPRAISR TNENDPAKHG
DQHEGQHYNI SPQDLETVFP HGLPPRFVMQ VKTFSEACLM VRKPALELLH YLKNTSFAYP
AIRYLLYGEK GTGKTLSLCH VIHFCAKQDW LILHIPDAHL WVKNCRDLLQ SSYNKQRFDQ
PLEASTWLKN FKTTNERFLN QIKVQEKYVW NKRESTEKGS PLGEVVEQGI TRVRNATDAV
GIVLKELKRQ SSLGMFHLLV AVDGINALWG RTTLKREDKS PIAPEELALV HNLRKMMKND
WHGGAIVSAL SQTGSLFKPR KAYLPQELLG KEGFDALDPF IPILVSNYNP KEFESCIQYY
LENNWLQHEK APTEEGKKEL LFLSNANPSL LERHCAYL
