ID   RL29_HUMAN              Reviewed;         159 AA.
AC   P47914; A8K0H3; B2R4M8; Q6IPY3;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   27-MAR-2024, entry version 208.
DE   RecName: Full=Large ribosomal subunit protein eL29 {ECO:0000303|PubMed:24524803};
DE   AltName: Full=60S ribosomal protein L29;
DE   AltName: Full=Cell surface heparin-binding protein HIP;
GN   Name=RPL29;
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].
RA   Law P.T., Tsui S.K., Lee C.Y., Waye M.M.;
RL   Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8597591; DOI=10.1016/0167-4781(95)00224-3;
RA   Law P.T., Tsui S.K.W., Lam W.Y., Luk S.C., Hwang D.M., Liew C.C.,
RA   Lee C.-Y., Fung K.-P., Waye M.M.Y.;
RT   "A novel cDNA encoding a human homologue of ribosomal protein L29.";
RL   Biochim. Biophys. Acta 1305:105-108(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8662616; DOI=10.1074/jbc.271.20.11817;
RA   Liu S., Smith S.E., Julian J., Rohde L.H., Karin N.J., Carson D.D.;
RT   "cDNA cloning and expression of HIP, a novel cell surface heparan
RT   sulfate/heparin-binding protein of human uterine epithelial cells and cell
RT   lines.";
RL   J. Biol. Chem. 271:11817-11823(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Cerebellum;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Ovary, and Pancreas;
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   PROTEIN SEQUENCE OF 2-15, IDENTIFICATION BY MASS SPECTROMETRY, METHYLATION
RP   AT LYS-5, FUNCTION, AND 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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Lymphoblast;
RX   PubMed=14654843; DOI=10.1038/nature02166;
RA   Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT   "Proteomic characterization of the human centrosome by protein correlation
RT   profiling.";
RL   Nature 426:570-574(2003).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-33, AND IDENTIFICATION BY MASS
RP   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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, 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   [10]
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   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-142, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142, AND IDENTIFICATION BY
RP   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   [15]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT LYS-5, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Colon carcinoma;
RX   PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
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 (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   [18] {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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}.
CC   -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL29 family.
CC       {ECO:0000305}.
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DR   EMBL; U10248; AAC50499.1; -; mRNA.
DR   EMBL; Z49148; CAA89008.1; -; mRNA.
DR   EMBL; U49083; AAC50647.1; -; mRNA.
DR   EMBL; AK289538; BAF82227.1; -; mRNA.
DR   EMBL; AK311884; BAG34825.1; -; mRNA.
DR   EMBL; BC008926; AAH08926.1; -; mRNA.
DR   EMBL; BC070190; AAH70190.1; -; mRNA.
DR   EMBL; BC070481; AAH70481.1; -; mRNA.
DR   EMBL; BC071663; AAH71663.1; -; mRNA.
DR   CCDS; CCDS2845.1; -.
DR   PIR; S65784; S65784.
DR   RefSeq; NP_000983.1; NM_000992.2.
DR   PDB; 4UG0; EM; -; Lb=1-159.
DR   PDB; 4V6X; EM; 5.00 A; Cb=1-159.
DR   PDB; 5AJ0; EM; 3.50 A; Ab=1-159.
DR   PDB; 5T2C; EM; 3.60 A; V=1-159.
DR   PDB; 6IP5; EM; 3.90 A; 2V=1-159.
DR   PDB; 6IP6; EM; 4.50 A; 2V=1-159.
DR   PDB; 6IP8; EM; 3.90 A; 2V=1-159.
DR   PDB; 6LQM; EM; 3.09 A; C=1-159.
DR   PDB; 6LSR; EM; 3.13 A; C=1-159.
DR   PDB; 6LSS; EM; 3.23 A; C=1-159.
DR   PDB; 6LU8; EM; 3.13 A; C=1-159.
DR   PDB; 6OLE; EM; 3.10 A; c=2-122.
DR   PDB; 6OLF; EM; 3.90 A; c=2-122.
DR   PDB; 6OLG; EM; 3.40 A; Ab=2-122.
DR   PDB; 6OLI; EM; 3.50 A; c=2-122.
DR   PDB; 6OLZ; EM; 3.90 A; Ab=2-119.
DR   PDB; 6OM0; EM; 3.10 A; c=2-122.
DR   PDB; 6OM7; EM; 3.70 A; c=2-122.
DR   PDB; 6QZP; EM; 2.90 A; Lb=2-122.
DR   PDB; 6W6L; EM; 3.84 A; c=1-159.
DR   PDB; 6XA1; EM; 2.80 A; Lb=2-122.
DR   PDB; 6Y0G; EM; 3.20 A; Lb=1-159.
DR   PDB; 6Y2L; EM; 3.00 A; Lb=1-159.
DR   PDB; 6Y57; EM; 3.50 A; Lb=1-159.
DR   PDB; 6Y6X; EM; 2.80 A; Lb=2-122.
DR   PDB; 6Z6L; EM; 3.00 A; Lb=1-159.
DR   PDB; 6Z6M; EM; 3.10 A; Lb=1-159.
DR   PDB; 6Z6N; EM; 2.90 A; Lb=1-159.
DR   PDB; 6ZM7; EM; 2.70 A; Lb=1-159.
DR   PDB; 6ZME; EM; 3.00 A; Lb=1-159.
DR   PDB; 6ZMI; EM; 2.60 A; Lb=1-159.
DR   PDB; 6ZMO; EM; 3.10 A; Lb=1-159.
DR   PDB; 7BHP; EM; 3.30 A; Lb=1-159.
DR   PDB; 7F5S; EM; 2.72 A; Lb=1-159.
DR   PDB; 7OW7; EM; 2.20 A; V=1-159.
DR   PDB; 7QVP; EM; 3.00 A; Lb/Mb=1-159.
DR   PDB; 7XNX; EM; 2.70 A; Lb=1-159.
DR   PDB; 7XNY; EM; 2.50 A; Lb=1-159.
DR   PDB; 8A3D; EM; 1.67 A; V=1-159.
DR   PDB; 8FL6; EM; 2.62 A; LM=1-159.
DR   PDB; 8FL7; EM; 2.55 A; LM=1-159.
DR   PDB; 8FL9; EM; 2.75 A; LM=1-159.
DR   PDB; 8FLA; EM; 2.63 A; LM=1-159.
DR   PDB; 8FLB; EM; 2.55 A; LM=1-159.
DR   PDB; 8FLC; EM; 2.76 A; LM=1-159.
DR   PDB; 8FLD; EM; 2.58 A; LM=1-159.
DR   PDB; 8FLE; EM; 2.48 A; LM=1-159.
DR   PDB; 8FLF; EM; 2.65 A; LM=1-159.
DR   PDB; 8G5Y; EM; 2.29 A; Lb=1-159.
DR   PDB; 8G60; EM; 2.54 A; Lb=1-159.
DR   PDB; 8G61; EM; 2.94 A; Lb=1-159.
DR   PDB; 8G6J; EM; 2.80 A; Lb=1-159.
DR   PDB; 8GLP; EM; 1.67 A; Lb=1-159.
DR   PDB; 8IDT; EM; 2.80 A; C=1-159.
DR   PDB; 8IDY; EM; 3.00 A; C=1-159.
DR   PDB; 8IE3; EM; 3.30 A; C=1-159.
DR   PDB; 8INE; EM; 3.20 A; C=1-159.
DR   PDB; 8INF; EM; 3.00 A; C=1-159.
DR   PDB; 8INK; EM; 3.20 A; A=1-159.
DR   PDB; 8IPD; EM; 3.20 A; A=1-159.
DR   PDB; 8IPX; EM; 4.30 A; A=1-159.
DR   PDB; 8IPY; EM; 3.20 A; A=1-159.
DR   PDB; 8JDJ; EM; 2.50 A; g=1-159.
DR   PDB; 8JDK; EM; 2.26 A; g=1-159.
DR   PDB; 8JDL; EM; 2.42 A; g=1-159.
DR   PDB; 8JDM; EM; 2.67 A; g=1-159.
DR   PDBsum; 4UG0; -.
DR   PDBsum; 4V6X; -.
DR   PDBsum; 5AJ0; -.
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   PDBsum; 7F5S; -.
DR   PDBsum; 7OW7; -.
DR   PDBsum; 7QVP; -.
DR   PDBsum; 7XNX; -.
DR   PDBsum; 7XNY; -.
DR   PDBsum; 8A3D; -.
DR   PDBsum; 8FL6; -.
DR   PDBsum; 8FL7; -.
DR   PDBsum; 8FL9; -.
DR   PDBsum; 8FLA; -.
DR   PDBsum; 8FLB; -.
DR   PDBsum; 8FLC; -.
DR   PDBsum; 8FLD; -.
DR   PDBsum; 8FLE; -.
DR   PDBsum; 8FLF; -.
DR   PDBsum; 8G5Y; -.
DR   PDBsum; 8G60; -.
DR   PDBsum; 8G61; -.
DR   PDBsum; 8G6J; -.
DR   PDBsum; 8GLP; -.
DR   PDBsum; 8IDT; -.
DR   PDBsum; 8IDY; -.
DR   PDBsum; 8IE3; -.
DR   PDBsum; 8INE; -.
DR   PDBsum; 8INF; -.
DR   PDBsum; 8INK; -.
DR   PDBsum; 8IPD; -.
DR   PDBsum; 8IPX; -.
DR   PDBsum; 8IPY; -.
DR   PDBsum; 8JDJ; -.
DR   PDBsum; 8JDK; -.
DR   PDBsum; 8JDL; -.
DR   PDBsum; 8JDM; -.
DR   AlphaFoldDB; P47914; -.
DR   EMDB; EMD-0948; -.
DR   EMDB; EMD-0963; -.
DR   EMDB; EMD-0964; -.
DR   EMDB; EMD-0978; -.
DR   EMDB; EMD-10668; -.
DR   EMDB; EMD-10674; -.
DR   EMDB; EMD-10690; -.
DR   EMDB; EMD-10709; -.
DR   EMDB; EMD-11098; -.
DR   EMDB; EMD-11099; -.
DR   EMDB; EMD-11100; -.
DR   EMDB; EMD-11288; -.
DR   EMDB; EMD-11289; -.
DR   EMDB; EMD-11292; -.
DR   EMDB; EMD-11299; -.
DR   EMDB; EMD-12189; -.
DR   EMDB; EMD-13094; -.
DR   EMDB; EMD-14181; -.
DR   EMDB; EMD-15113; -.
DR   EMDB; EMD-29268; -.
DR   EMDB; EMD-29269; -.
DR   EMDB; EMD-29271; -.
DR   EMDB; EMD-29272; -.
DR   EMDB; EMD-29273; -.
DR   EMDB; EMD-29274; -.
DR   EMDB; EMD-29275; -.
DR   EMDB; EMD-29276; -.
DR   EMDB; EMD-29277; -.
DR   EMDB; EMD-29757; -.
DR   EMDB; EMD-29758; -.
DR   EMDB; EMD-29759; -.
DR   EMDB; EMD-29760; -.
DR   EMDB; EMD-29771; -.
DR   EMDB; EMD-31465; -.
DR   EMDB; EMD-33329; -.
DR   EMDB; EMD-33330; -.
DR   EMDB; EMD-35370; -.
DR   EMDB; EMD-35371; -.
DR   EMDB; EMD-35375; -.
DR   EMDB; EMD-35596; -.
DR   EMDB; EMD-35597; -.
DR   EMDB; EMD-35599; -.
DR   EMDB; EMD-35639; -.
DR   EMDB; EMD-35649; -.
DR   EMDB; EMD-35651; -.
DR   EMDB; EMD-3883; -.
DR   EMDB; EMD-40205; -.
DR   EMDB; EMD-9701; -.
DR   EMDB; EMD-9702; -.
DR   EMDB; EMD-9703; -.
DR   SMR; P47914; -.
DR   BioGRID; 112078; 333.
DR   ComplexPortal; CPX-5183; 60S cytosolic large ribosomal subunit.
DR   ComplexPortal; CPX-7664; 60S cytosolic large ribosomal subunit, testis-specific variant.
DR   ComplexPortal; CPX-7665; 60S cytosolic large ribosomal subunit, striated muscle variant.
DR   CORUM; P47914; -.
DR   IntAct; P47914; 66.
DR   MINT; P47914; -.
DR   STRING; 9606.ENSP00000294189; -.
DR   GlyGen; P47914; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; P47914; -.
DR   PhosphoSitePlus; P47914; -.
DR   SwissPalm; P47914; -.
DR   BioMuta; RPL29; -.
DR   EPD; P47914; -.
DR   jPOST; P47914; -.
DR   MassIVE; P47914; -.
DR   MaxQB; P47914; -.
DR   PaxDb; 9606-ENSP00000418868; -.
DR   PeptideAtlas; P47914; -.
DR   ProteomicsDB; 55822; -.
DR   Pumba; P47914; -.
DR   TopDownProteomics; P47914; -.
DR   Antibodypedia; 31146; 87 antibodies from 23 providers.
DR   DNASU; 6159; -.
DR   Ensembl; ENST00000294189.11; ENSP00000294189.4; ENSG00000162244.12.
DR   Ensembl; ENST00000466397.5; ENSP00000418868.1; ENSG00000162244.12.
DR   Ensembl; ENST00000475248.5; ENSP00000417048.1; ENSG00000162244.12.
DR   Ensembl; ENST00000479017.5; ENSP00000418153.1; ENSG00000162244.12.
DR   Ensembl; ENST00000492277.5; ENSP00000418346.1; ENSG00000162244.12.
DR   Ensembl; ENST00000495383.5; ENSP00000420673.1; ENSG00000162244.12.
DR   GeneID; 6159; -.
DR   KEGG; hsa:6159; -.
DR   MANE-Select; ENST00000294189.11; ENSP00000294189.4; NM_000992.3; NP_000983.1.
DR   UCSC; uc003dcs.4; human.
DR   AGR; HGNC:10331; -.
DR   CTD; 6159; -.
DR   DisGeNET; 6159; -.
DR   GeneCards; RPL29; -.
DR   HGNC; HGNC:10331; RPL29.
DR   HPA; ENSG00000162244; Low tissue specificity.
DR   MIM; 601832; gene.
DR   neXtProt; NX_P47914; -.
DR   OpenTargets; ENSG00000162244; -.
DR   PharmGKB; PA34711; -.
DR   VEuPathDB; HostDB:ENSG00000162244; -.
DR   eggNOG; KOG3504; Eukaryota.
DR   GeneTree; ENSGT00390000007084; -.
DR   HOGENOM; CLU_139508_0_0_1; -.
DR   InParanoid; P47914; -.
DR   OMA; LISGHHY; -.
DR   OrthoDB; 4737989at2759; -.
DR   PhylomeDB; P47914; -.
DR   TreeFam; TF313858; -.
DR   PathwayCommons; P47914; -.
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; P47914; -.
DR   SIGNOR; P47914; -.
DR   BioGRID-ORCS; 6159; 304 hits in 1089 CRISPR screens.
DR   ChiTaRS; RPL29; human.
DR   GeneWiki; RPL29; -.
DR   GenomeRNAi; 6159; -.
DR   Pharos; P47914; Tbio.
DR   PRO; PR:P47914; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; P47914; Protein.
DR   Bgee; ENSG00000162244; Expressed in stromal cell of endometrium and 110 other cell types or tissues.
DR   ExpressionAtlas; P47914; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; NAS:ComplexPortal.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR   GO; GO:0022626; C:cytosolic ribosome; IDA:FlyBase.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR   GO; GO:0008201; F:heparin binding; TAS:ProtInc.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
DR   GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central.
DR   GO; GO:0007566; P:embryo implantation; TAS:ProtInc.
DR   GO; GO:0006412; P:translation; TAS:ProtInc.
DR   Gene3D; 6.10.140.1730; -; 1.
DR   InterPro; IPR002673; Ribosomal_eL29.
DR   PANTHER; PTHR12884; 60S RIBOSOMAL PROTEIN L29; 1.
DR   PANTHER; PTHR12884:SF23; 60S RIBOSOMAL PROTEIN L29; 1.
DR   Pfam; PF01779; Ribosomal_L29e; 1.
DR   Genevisible; P47914; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   Heparin-binding; Methylation; Phosphoprotein; Reference proteome; Repeat;
KW   Ribonucleoprotein; Ribosomal protein.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:12962325"
FT   CHAIN           2..159
FT                   /note="Large ribosomal subunit protein eL29"
FT                   /id="PRO_0000219134"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..22
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         5
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000269|PubMed:12962325,
FT                   ECO:0007744|PubMed:24129315"
FT   MOD_RES         31
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         33
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:19608861"
FT   MOD_RES         142
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   CONFLICT        5
FT                   /note="K -> R (in Ref. 4; BAF82227)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        120
FT                   /note="R -> A (in Ref. 2; CAA89008)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   159 AA;  17752 MW;  2A0C31984EF4FF95 CRC64;
     MAKSKNHTTH NQSRKWHRNG IKKPRSQRYE SLKGVDPKFL RNMRFAKKHN KKGLKKMQAN
     NAKAMSARAE AIKALVKPKE VKPKIPKGVS RKLDRLAYIA HPKLGKRARA RIAKGLRLCR
     PKAKAKAKAK DQTKAQAAAP ASVPAQAPKR TQAPTKASE
//