RL28_HUMAN
ID RL28_HUMAN Reviewed; 137 AA.
AC P46779; B2R4A6; B4DEP9; C9JB50; E9PB24; G5E9L2; Q6IAY0; Q96FX1; Q9BWQ0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=60S ribosomal protein L28;
DE AltName: Full=Large ribosomal subunit protein eL28 {ECO:0000303|PubMed:24524803};
GN Name=RPL28;
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=Colon;
RX PubMed=7772601; DOI=10.1016/0167-4781(95)00045-i;
RA Frigerio J.-M., Dagorn J.-C., Iovanna J.L.;
RT "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9, S10
RT and S29 human ribosomal protein mRNAs.";
RL Biochim. Biophys. Acta 1262:64-68(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Hippocampus;
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 GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=B-cell, Kidney, Prostatic adenocarcinoma, and Uterus;
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 [7]
RP PROTEIN SEQUENCE OF 2-11; 23-33; 40-58; 72-79 AND 120-127, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Hepatoma, and Ovarian carcinoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A., Lilla S., Lempens A.,
RA Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND
RP SUBUNIT.
RX PubMed=12962325; DOI=10.1023/a:1025068419698;
RA Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,
RA Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B., Karpova G.G.;
RT "Characterization and analysis of posttranslational modifications of the
RT human large cytoplasmic ribosomal subunit proteins by mass spectrometry and
RT Edman sequencing.";
RL J. Protein Chem. 22:249-258(2003).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [13]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-58 AND LYS-65, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [16]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
RN [17] {ECO:0007744|PDB:6LQM, ECO:0007744|PDB:6LSR, ECO:0007744|PDB:6LSS, ECO:0007744|PDB:6LU8}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.09 ANGSTROMS), FUNCTION, AND SUBUNIT.
RX PubMed=32669547; DOI=10.1038/s41467-020-17237-x;
RA Liang X., Zuo M.Q., Zhang Y., Li N., Ma C., Dong M.Q., Gao N.;
RT "Structural snapshots of human pre-60S ribosomal particles before and after
RT nuclear export.";
RL Nat. Commun. 11:3542-3542(2020).
CC -!- FUNCTION: Component of the large ribosomal subunit (PubMed:12962325,
CC PubMed:23636399, PubMed:32669547). The ribosome is a large
CC ribonucleoprotein complex responsible for the synthesis of proteins in
CC the cell (PubMed:12962325, PubMed:23636399, PubMed:32669547).
CC {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:32669547,
CC ECO:0000305|PubMed:12962325}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (PubMed:12962325,
CC PubMed:23636399, PubMed:32669547). {ECO:0000269|PubMed:23636399,
CC ECO:0000269|PubMed:32669547, ECO:0000305|PubMed:12962325}.
CC -!- INTERACTION:
CC P46779; P05067: APP; NbExp=3; IntAct=EBI-366357, EBI-77613;
CC P46779; O95273: CCNDBP1; NbExp=7; IntAct=EBI-366357, EBI-748961;
CC P46779; P43146: DCC; NbExp=3; IntAct=EBI-366357, EBI-1222919;
CC P46779; P10636: MAPT; NbExp=4; IntAct=EBI-366357, EBI-366182;
CC P46779; P36578: RPL4; NbExp=2; IntAct=EBI-366357, EBI-348313;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P46779-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P46779-2; Sequence=VSP_043026;
CC Name=3;
CC IsoId=P46779-3; Sequence=VSP_046173;
CC Name=4;
CC IsoId=P46779-4; Sequence=VSP_047026;
CC Name=5;
CC IsoId=P46779-5; Sequence=VSP_047027;
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL28 family.
CC {ECO:0000305}.
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DR EMBL; U14969; AAA85657.1; -; mRNA.
DR EMBL; CR457024; CAG33305.1; -; mRNA.
DR EMBL; AK311760; BAG34703.1; -; mRNA.
DR EMBL; AK293736; BAG57160.1; -; mRNA.
DR EMBL; AC020922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW72374.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW72375.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW72376.1; -; Genomic_DNA.
DR EMBL; BC010173; AAH10173.1; -; mRNA.
DR EMBL; BC010182; AAH10182.1; -; mRNA.
DR EMBL; BC011582; AAH11582.1; -; mRNA.
DR EMBL; BG777550; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS12924.1; -. [P46779-1]
DR CCDS; CCDS46189.1; -. [P46779-3]
DR CCDS; CCDS46190.1; -. [P46779-2]
DR CCDS; CCDS46191.1; -. [P46779-4]
DR CCDS; CCDS46192.1; -. [P46779-5]
DR PIR; S55915; S55915.
DR RefSeq; NP_000982.2; NM_000991.4. [P46779-1]
DR RefSeq; NP_001129606.1; NM_001136134.1. [P46779-2]
DR RefSeq; NP_001129607.1; NM_001136135.1. [P46779-3]
DR RefSeq; NP_001129608.1; NM_001136136.1. [P46779-5]
DR RefSeq; NP_001129609.1; NM_001136137.1. [P46779-4]
DR PDB; 4UG0; EM; -; Lr=1-137.
DR PDB; 4V6X; EM; 5.00 A; Cr=1-137.
DR PDB; 5AJ0; EM; 3.50 A; At=1-137.
DR PDB; 5LKS; EM; 3.60 A; Lr=1-137.
DR PDB; 5T2C; EM; 3.60 A; k=1-137.
DR PDB; 6IP5; EM; 3.90 A; 2k=1-137.
DR PDB; 6IP6; EM; 4.50 A; 2k=1-137.
DR PDB; 6IP8; EM; 3.90 A; 2k=1-137.
DR PDB; 6LQM; EM; 3.09 A; l=1-137.
DR PDB; 6LSR; EM; 3.13 A; l=1-137.
DR PDB; 6LSS; EM; 3.23 A; l=1-137.
DR PDB; 6LU8; EM; 3.13 A; l=1-137.
DR PDB; 6OLE; EM; 3.10 A; r=2-123.
DR PDB; 6OLF; EM; 3.90 A; r=2-123.
DR PDB; 6OLG; EM; 3.40 A; At=2-123.
DR PDB; 6OLI; EM; 3.50 A; r=2-123.
DR PDB; 6OLZ; EM; 3.90 A; At=2-123.
DR PDB; 6OM0; EM; 3.10 A; r=2-123.
DR PDB; 6OM7; EM; 3.70 A; r=2-123.
DR PDB; 6QZP; EM; 2.90 A; Lr=2-126.
DR PDB; 6W6L; EM; 3.84 A; r=1-137.
DR PDB; 6XA1; EM; 2.80 A; Lr=2-126.
DR PDB; 6Y0G; EM; 3.20 A; Lr=1-137.
DR PDB; 6Y2L; EM; 3.00 A; Lr=1-137.
DR PDB; 6Y57; EM; 3.50 A; Lr=1-137.
DR PDB; 6Y6X; EM; 2.80 A; Lr=2-126.
DR PDB; 6Z6L; EM; 3.00 A; Lr=1-137.
DR PDB; 6Z6M; EM; 3.10 A; Lr=1-137.
DR PDB; 6Z6N; EM; 2.90 A; Lr=1-137.
DR PDB; 6ZM7; EM; 2.70 A; Lr=1-137.
DR PDB; 6ZME; EM; 3.00 A; Lr=1-137.
DR PDB; 6ZMI; EM; 2.60 A; Lr=1-137.
DR PDB; 6ZMO; EM; 3.10 A; Lr=1-137.
DR PDB; 7BHP; EM; 3.30 A; Lr=1-137.
DR PDBsum; 4UG0; -.
DR PDBsum; 4V6X; -.
DR PDBsum; 5AJ0; -.
DR PDBsum; 5LKS; -.
DR PDBsum; 5T2C; -.
DR PDBsum; 6IP5; -.
DR PDBsum; 6IP6; -.
DR PDBsum; 6IP8; -.
DR PDBsum; 6LQM; -.
DR PDBsum; 6LSR; -.
DR PDBsum; 6LSS; -.
DR PDBsum; 6LU8; -.
DR PDBsum; 6OLE; -.
DR PDBsum; 6OLF; -.
DR PDBsum; 6OLG; -.
DR PDBsum; 6OLI; -.
DR PDBsum; 6OLZ; -.
DR PDBsum; 6OM0; -.
DR PDBsum; 6OM7; -.
DR PDBsum; 6QZP; -.
DR PDBsum; 6W6L; -.
DR PDBsum; 6XA1; -.
DR PDBsum; 6Y0G; -.
DR PDBsum; 6Y2L; -.
DR PDBsum; 6Y57; -.
DR PDBsum; 6Y6X; -.
DR PDBsum; 6Z6L; -.
DR PDBsum; 6Z6M; -.
DR PDBsum; 6Z6N; -.
DR PDBsum; 6ZM7; -.
DR PDBsum; 6ZME; -.
DR PDBsum; 6ZMI; -.
DR PDBsum; 6ZMO; -.
DR PDBsum; 7BHP; -.
DR AlphaFoldDB; P46779; -.
DR SMR; P46779; -.
DR BioGRID; 112077; 387.
DR ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR CORUM; P46779; -.
DR IntAct; P46779; 141.
DR MINT; P46779; -.
DR STRING; 9606.ENSP00000452909; -.
DR GlyGen; P46779; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P46779; -.
DR MetOSite; P46779; -.
DR PhosphoSitePlus; P46779; -.
DR SwissPalm; P46779; -.
DR BioMuta; RPL28; -.
DR EPD; P46779; -.
DR jPOST; P46779; -.
DR MassIVE; P46779; -.
DR MaxQB; P46779; -.
DR PaxDb; P46779; -.
DR PeptideAtlas; P46779; -.
DR PRIDE; P46779; -.
DR ProteomicsDB; 19127; -.
DR ProteomicsDB; 33973; -.
DR ProteomicsDB; 55761; -. [P46779-1]
DR ProteomicsDB; 55762; -. [P46779-2]
DR ProteomicsDB; 9416; -.
DR TopDownProteomics; P46779-1; -. [P46779-1]
DR Antibodypedia; 46430; 181 antibodies from 25 providers.
DR DNASU; 6158; -.
DR Ensembl; ENST00000344063.7; ENSP00000342787.3; ENSG00000108107.15. [P46779-1]
DR Ensembl; ENST00000428193.6; ENSP00000391665.2; ENSG00000108107.15. [P46779-4]
DR Ensembl; ENST00000431533.6; ENSP00000400596.2; ENSG00000108107.15. [P46779-5]
DR Ensembl; ENST00000558815.5; ENSP00000452909.1; ENSG00000108107.15. [P46779-3]
DR Ensembl; ENST00000559463.5; ENSP00000453319.1; ENSG00000108107.15. [P46779-1]
DR Ensembl; ENST00000560583.5; ENSP00000453029.1; ENSG00000108107.15. [P46779-2]
DR GeneID; 6158; -.
DR KEGG; hsa:6158; -.
DR MANE-Select; ENST00000344063.7; ENSP00000342787.3; NM_000991.5; NP_000982.2.
DR UCSC; uc002qkv.4; human. [P46779-1]
DR CTD; 6158; -.
DR DisGeNET; 6158; -.
DR GeneCards; RPL28; -.
DR HGNC; HGNC:10330; RPL28.
DR HPA; ENSG00000108107; Low tissue specificity.
DR MIM; 603638; gene.
DR neXtProt; NX_P46779; -.
DR OpenTargets; ENSG00000108107; -.
DR PharmGKB; PA34710; -.
DR VEuPathDB; HostDB:ENSG00000108107; -.
DR eggNOG; KOG3412; Eukaryota.
DR GeneTree; ENSGT00390000008732; -.
DR HOGENOM; CLU_106801_1_0_1; -.
DR InParanoid; P46779; -.
DR OMA; SHDLAWE; -.
DR PhylomeDB; P46779; -.
DR TreeFam; TF300173; -.
DR PathwayCommons; P46779; -.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-156902; Peptide chain elongation.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-HSA-192823; Viral mRNA Translation.
DR Reactome; R-HSA-2408557; Selenocysteine synthesis.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-HSA-72764; Eukaryotic Translation Termination.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR SignaLink; P46779; -.
DR SIGNOR; P46779; -.
DR BioGRID-ORCS; 6158; 620 hits in 1091 CRISPR screens.
DR ChiTaRS; RPL28; human.
DR GeneWiki; 60S_ribosomal_protein_L28; -.
DR GenomeRNAi; 6158; -.
DR Pharos; P46779; Tbio.
DR PRO; PR:P46779; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P46779; protein.
DR Bgee; ENSG00000108107; Expressed in adult organism and 205 other tissues.
DR ExpressionAtlas; P46779; baseline and differential.
DR Genevisible; P46779; HS.
DR GO; GO:0044297; C:cell body; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IC:ComplexPortal.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IPI:ComplexPortal.
DR GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR GO; GO:0030425; C:dendrite; IDA:ParkinsonsUK-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:FlyBase.
DR GO; GO:0002181; P:cytoplasmic translation; IC:FlyBase.
DR GO; GO:0006412; P:translation; TAS:ProtInc.
DR InterPro; IPR029004; L28e/Mak16.
DR InterPro; IPR002672; Ribosomal_L28e.
DR PANTHER; PTHR10544; PTHR10544; 1.
DR Pfam; PF01778; Ribosomal_L28e; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12962325, ECO:0000269|Ref.7,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..137
FT /note="60S ribosomal protein L28"
FT /id="PRO_0000122389"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:12962325, ECO:0000269|Ref.7,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 65
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 69..137
FT /note="GQRKPATSYVRTTINKNARATLSSIRHMIRKNKYRPDLRMAAIRRASAILRS
FT QKPVMVKRKRTRPTKSS -> E (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_047026"
FT VAR_SEQ 70..137
FT /note="QRKPATSYVRTTINKNARATLSSIRHMIRKNKYRPDLRMAAIRRASAILRSQ
FT KPVMVKRKRTRPTKSS -> EFCLVWARERPLSRVWEL (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_047027"
FT VAR_SEQ 109..137
FT /note="AAIRRASAILRSQKPVMVKRKRTRPTKSS -> VSWGLGIRLGETGQCCGEG
FT PPTTGCNMGWRGMDSCFQPTPHTQHWPRGRLVECMG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043026"
FT VAR_SEQ 109..137
FT /note="AAIRRASAILRSQKPVMVKRKRTRPTKSS -> DMLASTGSGLCCSVAVQPW
FT ASSSTSLCLRTLICNMRVDRPYYSGLMRRLNVQNLLDCAHKS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046173"
FT VARIANT 66
FT /note="R -> L (in dbSNP:rs13502)"
FT /id="VAR_034460"
FT CONFLICT 84
FT /note="K -> R (in Ref. 6; AAH10182)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="S -> T (in Ref. 1; AAA85657)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 137 AA; 15748 MW; 44DCDE45473D7C7B CRC64;
MSAHLQWMVV RNCSSFLIKR NKQTYSTEPN NLKARNSFRY NGLIHRKTVG VEPAADGKGV
VVVIKRRSGQ RKPATSYVRT TINKNARATL SSIRHMIRKN KYRPDLRMAA IRRASAILRS
QKPVMVKRKR TRPTKSS
