RM28_HUMAN
ID RM28_HUMAN Reviewed; 256 AA.
AC Q13084; B2RCM4; D3DU46; Q4TT39; Q96S26; Q9BQD8; Q9BR04;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 4.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=39S ribosomal protein L28, mitochondrial;
DE Short=L28mt;
DE Short=MRP-L28;
DE AltName: Full=Melanoma antigen p15;
DE AltName: Full=Melanoma-associated antigen recognized by T-lymphocytes;
DE AltName: Full=Mitochondrial large ribosomal subunit protein bL28m {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL28; Synonyms=MAAT1;
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 [LARGE SCALE MRNA], AND VARIANT TYR-27.
RC TISSUE=Skeletal muscle;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11157797; DOI=10.1093/hmg/10.4.339;
RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C.,
RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.;
RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of
RT the short arm of human chromosome 16.";
RL Hum. Mol. Genet. 10:339-352(2001).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TYR-27.
RC TISSUE=Lung, and Placenta;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 82-256, SYNTHESIS OF 137-146, AND VARIANT
RP GLU-160.
RC TISSUE=Melanoma;
RX PubMed=7751637;
RA Robbins P.F., El-Gamil M., Li Y.F., Topalian S.L., Rivoltini L.,
RA Sakaguchi K., Appella E., Kawakami Y., Rosenberg S.A.;
RT "Cloning of a new gene encoding an antigen recognized by melanoma-specific
RT HLA-A24-restricted tumor-infiltrating lymphocytes.";
RL J. Immunol. 154:5944-5950(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-256.
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP IDENTIFICATION.
RX PubMed=11551941; DOI=10.1074/jbc.m106510200;
RA Koc E.C., Burkhart W., Blackburn K., Moyer M.B., Schlatzer D.M.,
RA Moseley A., Spremulli L.L.;
RT "The large subunit of the mammalian mitochondrial ribosome. Analysis of the
RT complement of ribosomal proteins present.";
RL J. Biol. Chem. 276:43958-43969(2001).
RN [9]
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 [10]
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 [11] {ECO:0007744|PDB:3J7Y}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=25278503; DOI=10.1126/science.1258026;
RA Brown A., Amunts A., Bai X.C., Sugimoto Y., Edwards P.C., Murshudov G.,
RA Scheres S.H., Ramakrishnan V.;
RT "Structure of the large ribosomal subunit from human mitochondria.";
RL Science 346:718-722(2014).
RN [12] {ECO:0007744|PDB:5OOL, ECO:0007744|PDB:5OOM}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS), SUBCELLULAR LOCATION,
RP AND SUBUNIT.
RX PubMed=28892042; DOI=10.1038/nsmb.3464;
RA Brown A., Rathore S., Kimanius D., Aibara S., Bai X.C., Rorbach J.,
RA Amunts A., Ramakrishnan V.;
RT "Structures of the human mitochondrial ribosome in native states of
RT assembly.";
RL Nat. Struct. Mol. Biol. 24:866-869(2017).
CC -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC LSU) (PubMed:28892042, PubMed:25278503, PubMed:11551941). Mature
CC mammalian 55S mitochondrial ribosomes consist of a small (28S) and a
CC large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA
CC (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains
CC a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA
CC (mt-tRNA(Val)), which plays an integral structural role, and 52
CC different proteins (PubMed:11551941, PubMed:25278503). Interacts with
CC OXA1L. {ECO:0000250|UniProtKB:Q2HJJ1, ECO:0000269|PubMed:11551941,
CC ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:28892042,
CC ECO:0000305|PubMed:11551941}.
CC -!- INTERACTION:
CC Q13084; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-723426, EBI-11096309;
CC Q13084; Q8N9N5: BANP; NbExp=3; IntAct=EBI-723426, EBI-744695;
CC Q13084; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-723426, EBI-5278764;
CC Q13084; Q01850: CDR2; NbExp=3; IntAct=EBI-723426, EBI-1181367;
CC Q13084; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-723426, EBI-744099;
CC Q13084; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-723426, EBI-10175124;
CC Q13084; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-723426, EBI-2549423;
CC Q13084; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-723426, EBI-747204;
CC Q13084; Q659C4-6: LARP1B; NbExp=3; IntAct=EBI-723426, EBI-12036449;
CC Q13084; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-723426, EBI-726510;
CC Q13084; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-723426, EBI-10271199;
CC Q13084; O60437: PPL; NbExp=3; IntAct=EBI-723426, EBI-368321;
CC Q13084; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-723426, EBI-748391;
CC Q13084; Q10587: TEF; NbExp=3; IntAct=EBI-723426, EBI-2796967;
CC Q13084; O43734: TRAF3IP2; NbExp=3; IntAct=EBI-723426, EBI-744798;
CC Q13084; Q9BUZ4: TRAF4; NbExp=4; IntAct=EBI-723426, EBI-3650647;
CC Q13084; Q63HK5: TSHZ3; NbExp=3; IntAct=EBI-723426, EBI-9053916;
CC Q13084; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-723426, EBI-3918381;
CC Q13084; O95045-2: UPP2; NbExp=3; IntAct=EBI-723426, EBI-11528386;
CC Q13084; O75604: USP2; NbExp=3; IntAct=EBI-723426, EBI-743272;
CC Q13084; A0A024R8A9: USP20; NbExp=3; IntAct=EBI-723426, EBI-14096082;
CC Q13084; Q8N720: ZNF655; NbExp=3; IntAct=EBI-723426, EBI-625509;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:28892042}.
CC -!- TISSUE SPECIFICITY: Found in a variety of normal tissues including
CC spleen, testes, thymus, liver, kidney, brain, adrenal, lung and retinal
CC tissue.
CC -!- MISCELLANEOUS: Potentially represents an important therapeutic reagent
CC for HLA-A24 patients. This antigen is recognized by tumor-infiltrating
CC lymphocyte (TIL) 1290 in the context of HLA-A24.
CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL28 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50181.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAK61226.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK315180; BAG37621.1; -; mRNA.
DR EMBL; AE006463; AAK61226.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z97634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85827.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85829.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85832.1; -; Genomic_DNA.
DR EMBL; CH471112; EAW85834.1; -; Genomic_DNA.
DR EMBL; BC000507; AAH00507.2; -; mRNA.
DR EMBL; BC000990; AAH00990.2; -; mRNA.
DR EMBL; U19796; AAC50181.1; ALT_INIT; mRNA.
DR EMBL; BT009857; AAP88859.1; -; mRNA.
DR CCDS; CCDS32349.1; -.
DR RefSeq; NP_006419.2; NM_006428.4.
DR RefSeq; XP_005255098.1; XM_005255041.1.
DR RefSeq; XP_011520653.1; XM_011522351.2.
DR PDB; 3J7Y; EM; 3.40 A; X=1-256.
DR PDB; 5OOL; EM; 3.06 A; X=1-256.
DR PDB; 5OOM; EM; 3.03 A; X=1-256.
DR PDB; 6I9R; EM; 3.90 A; X=1-256.
DR PDB; 6NU2; EM; 3.90 A; X=2-244.
DR PDB; 6NU3; EM; 4.40 A; X=2-244.
DR PDB; 6VLZ; EM; 2.97 A; X=1-256.
DR PDB; 6VMI; EM; 2.96 A; X=1-256.
DR PDB; 6ZM5; EM; 2.89 A; X=1-256.
DR PDB; 6ZM6; EM; 2.59 A; X=1-256.
DR PDB; 6ZS9; EM; 4.00 A; XX=1-256.
DR PDB; 6ZSA; EM; 4.00 A; XX=1-256.
DR PDB; 6ZSB; EM; 4.50 A; XX=1-256.
DR PDB; 6ZSC; EM; 3.50 A; XX=1-256.
DR PDB; 6ZSD; EM; 3.70 A; XX=1-256.
DR PDB; 6ZSE; EM; 5.00 A; XX=1-256.
DR PDB; 6ZSG; EM; 4.00 A; XX=1-256.
DR PDB; 7A5F; EM; 4.40 A; X3=1-256.
DR PDB; 7A5G; EM; 4.33 A; X3=1-256.
DR PDB; 7A5H; EM; 3.30 A; X=1-256.
DR PDB; 7A5I; EM; 3.70 A; X3=1-256.
DR PDB; 7A5J; EM; 3.10 A; X=1-256.
DR PDB; 7A5K; EM; 3.70 A; X3=1-256.
DR PDB; 7L08; EM; 3.49 A; X=1-256.
DR PDB; 7L20; EM; 3.15 A; X=1-256.
DR PDB; 7O9K; EM; 3.10 A; X=1-256.
DR PDB; 7O9M; EM; 2.50 A; X=1-256.
DR PDB; 7ODR; EM; 2.90 A; X=1-256.
DR PDB; 7ODS; EM; 3.10 A; X=1-256.
DR PDB; 7ODT; EM; 3.10 A; X=1-256.
DR PDB; 7OF0; EM; 2.20 A; X=1-256.
DR PDB; 7OF2; EM; 2.70 A; X=1-256.
DR PDB; 7OF3; EM; 2.70 A; X=1-256.
DR PDB; 7OF4; EM; 2.70 A; X=1-256.
DR PDB; 7OF5; EM; 2.90 A; X=1-256.
DR PDB; 7OF6; EM; 2.60 A; X=1-256.
DR PDB; 7OF7; EM; 2.50 A; X=1-256.
DR PDB; 7OG4; EM; 3.80 A; XX=1-256.
DR PDB; 7OI6; EM; 5.70 A; X=1-256.
DR PDB; 7OI7; EM; 3.50 A; X=1-256.
DR PDB; 7OI8; EM; 3.50 A; X=1-256.
DR PDB; 7OI9; EM; 3.30 A; X=1-256.
DR PDB; 7OIA; EM; 3.20 A; X=1-256.
DR PDB; 7OIB; EM; 3.30 A; X=1-256.
DR PDB; 7OIC; EM; 3.10 A; X=1-256.
DR PDB; 7OID; EM; 3.70 A; X=1-256.
DR PDB; 7OIE; EM; 3.50 A; X=1-256.
DR PDB; 7PD3; EM; 3.40 A; X=1-256.
DR PDB; 7QH6; EM; 3.08 A; X=1-256.
DR PDBsum; 3J7Y; -.
DR PDBsum; 5OOL; -.
DR PDBsum; 5OOM; -.
DR PDBsum; 6I9R; -.
DR PDBsum; 6NU2; -.
DR PDBsum; 6NU3; -.
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; 7A5H; -.
DR PDBsum; 7A5I; -.
DR PDBsum; 7A5J; -.
DR PDBsum; 7A5K; -.
DR PDBsum; 7L08; -.
DR PDBsum; 7L20; -.
DR PDBsum; 7O9K; -.
DR PDBsum; 7O9M; -.
DR PDBsum; 7ODR; -.
DR PDBsum; 7ODS; -.
DR PDBsum; 7ODT; -.
DR PDBsum; 7OF0; -.
DR PDBsum; 7OF2; -.
DR PDBsum; 7OF3; -.
DR PDBsum; 7OF4; -.
DR PDBsum; 7OF5; -.
DR PDBsum; 7OF6; -.
DR PDBsum; 7OF7; -.
DR PDBsum; 7OG4; -.
DR PDBsum; 7OI6; -.
DR PDBsum; 7OI7; -.
DR PDBsum; 7OI8; -.
DR PDBsum; 7OI9; -.
DR PDBsum; 7OIA; -.
DR PDBsum; 7OIB; -.
DR PDBsum; 7OIC; -.
DR PDBsum; 7OID; -.
DR PDBsum; 7OIE; -.
DR PDBsum; 7PD3; -.
DR PDBsum; 7QH6; -.
DR AlphaFoldDB; Q13084; -.
DR SMR; Q13084; -.
DR BioGRID; 115824; 225.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q13084; -.
DR DIP; DIP-61135N; -.
DR IntAct; Q13084; 101.
DR MINT; Q13084; -.
DR STRING; 9606.ENSP00000199706; -.
DR GlyGen; Q13084; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13084; -.
DR PhosphoSitePlus; Q13084; -.
DR SwissPalm; Q13084; -.
DR BioMuta; MRPL28; -.
DR DMDM; 85695426; -.
DR EPD; Q13084; -.
DR jPOST; Q13084; -.
DR MassIVE; Q13084; -.
DR MaxQB; Q13084; -.
DR PaxDb; Q13084; -.
DR PeptideAtlas; Q13084; -.
DR PRIDE; Q13084; -.
DR ProteomicsDB; 59138; -.
DR Antibodypedia; 22648; 281 antibodies from 33 providers.
DR DNASU; 10573; -.
DR Ensembl; ENST00000199706.13; ENSP00000199706.7; ENSG00000086504.18.
DR Ensembl; ENST00000389675.6; ENSP00000374326.2; ENSG00000086504.18.
DR Ensembl; ENST00000648346.1; ENSP00000497004.1; ENSG00000086504.18.
DR GeneID; 10573; -.
DR KEGG; hsa:10573; -.
DR MANE-Select; ENST00000199706.13; ENSP00000199706.7; NM_006428.5; NP_006419.2.
DR UCSC; uc002cgs.3; human.
DR CTD; 10573; -.
DR DisGeNET; 10573; -.
DR GeneCards; MRPL28; -.
DR HGNC; HGNC:14484; MRPL28.
DR HPA; ENSG00000086504; Low tissue specificity.
DR MIM; 604853; gene.
DR neXtProt; NX_Q13084; -.
DR PharmGKB; PA30515; -.
DR VEuPathDB; HostDB:ENSG00000086504; -.
DR eggNOG; KOG3279; Eukaryota.
DR GeneTree; ENSGT00390000017359; -.
DR InParanoid; Q13084; -.
DR OMA; LKNRACD; -.
DR OrthoDB; 1558223at2759; -.
DR PhylomeDB; Q13084; -.
DR TreeFam; TF313040; -.
DR PathwayCommons; Q13084; -.
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; Q13084; -.
DR SIGNOR; Q13084; -.
DR BioGRID-ORCS; 10573; 404 hits in 1071 CRISPR screens.
DR ChiTaRS; MRPL28; human.
DR GeneWiki; MRPL28; -.
DR GenomeRNAi; 10573; -.
DR Pharos; Q13084; Tdark.
DR PRO; PR:Q13084; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q13084; protein.
DR Bgee; ENSG00000086504; Expressed in apex of heart and 197 other tissues.
DR ExpressionAtlas; Q13084; baseline and differential.
DR Genevisible; Q13084; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome.
DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005761; C:mitochondrial ribosome; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA: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 GO; GO:0006412; P:translation; NAS:UniProtKB.
DR Gene3D; 2.30.170.40; -; 1.
DR InterPro; IPR034704; L28p-like.
DR InterPro; IPR026569; Ribo_L28/L24.
DR InterPro; IPR037147; Ribo_L28/L24_sf.
DR PANTHER; PTHR13528; PTHR13528; 1.
DR Pfam; PF00830; Ribosomal_L28; 1.
DR SUPFAM; SSF143800; SSF143800; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..55
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 56..256
FT /note="39S ribosomal protein L28, mitochondrial"
FT /id="PRO_0000030506"
FT VARIANT 27
FT /note="H -> Y (in dbSNP:rs3194151)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_054219"
FT VARIANT 160
FT /note="D -> E (in dbSNP:rs11557302)"
FT /evidence="ECO:0000269|PubMed:7751637"
FT /id="VAR_052024"
FT VARIANT 230
FT /note="Y -> C (in dbSNP:rs13226)"
FT /id="VAR_061806"
FT CONFLICT 147
FT /note="K -> KASG (in Ref. 2; AAK61226)"
FT /evidence="ECO:0000305"
FT CONFLICT 148..150
FT /note="TPK -> ASG (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="R -> T (in Ref. 6; AAC50181)"
FT /evidence="ECO:0000305"
FT HELIX 8..10
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 11..16
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 20..23
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:5OOM"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 73..77
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 129..138
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 156..171
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 181..190
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 202..205
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 208..219
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 226..243
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 256 AA; 30157 MW; 6578FD1E98FC5A6E CRC64;
MPLHKYPVWL WKRLQLREGI CSRLPGHYLR SLEEERTPTP VHYRPHGAKF KINPKNGQRE
RVEDVPIPIY FPPESQRGLW GGEGWILGQI YANNDKLSKR LKKVWKPQLF EREFYSEILD
KKFTVTVTMR TLDLIDEAYG LDFYILKTPK EDLCSKFGMD LKRGMLLRLA RQDPQLHPED
PERRAAIYDK YKEFAIPEEE AEWVGLTLEE AIEKQRLLEE KDPVPLFKIY VAELIQQLQQ
QALSEPAVVQ KRASGQ
