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60S ribosomal protein L3 (HIV-1 TAR RNA-binding protein B) (TARBP-B) (Large ribosomal subunit protein uL3)

 RL3_HUMAN               Reviewed;         403 AA.
P39023; B2RDV9; Q15548; Q5I0G0;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
18-JUL-2018, entry version 193.
RecName: Full=60S ribosomal protein L3;
AltName: Full=HIV-1 TAR RNA-binding protein B;
Short=TARBP-B;
AltName: Full=Large ribosomal subunit protein uL3 {ECO:0000303|PubMed:24524803};
Name=RPL3; ORFNames=OK/SW-cl.32;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Leffers H.;
"Complete coding sequence of human ribosomal protein L3 mRNA.";
Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-
reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Colon, Lung, Muscle, Ovary, PNS, Skin, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-403.
Still I.H.;
Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-277.
PubMed=7576925; DOI=10.1089/aid.1995.11.663;
Reddy T.R., Suhasini M., Rappaport J., Looney D.J., Kraus G.,
Wong-Staal F.;
"Molecular cloning and characterization of a TAR-binding nuclear
factor from T cells.";
AIDS Res. Hum. Retroviruses 11:663-669(1995).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 328-398.
PubMed=9582194;
Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
Hudson T.J., Tanaka T., Page D.C.;
"A map of 75 human ribosomal protein genes.";
Genome Res. 8:509-523(1998).
[10]
PROTEIN SEQUENCE OF 2-13, IDENTIFICATION BY MASS SPECTROMETRY,
FUNCTION, AND SUBUNIT.
PubMed=12962325; DOI=10.1023/A:1025068419698;
Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,
Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B.,
Karpova G.G.;
"Characterization and analysis of posttranslational modifications of
the human large cytoplasmic ribosomal subunit proteins by mass
spectrometry and Edman sequencing.";
J. Protein Chem. 22:249-258(2003).
[11]
SUBCELLULAR LOCATION.
PubMed=16963496; DOI=10.1093/nar/gkl603;
Sekiguchi T., Hayano T., Yanagida M., Takahashi N., Nishimoto T.;
"NOP132 is required for proper nucleolus localization of DEAD-box RNA
helicase DDX47.";
Nucleic Acids Res. 34:4593-4608(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[14]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-294 AND LYS-366, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
INTERACTION WITH METTL18.
PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
"A newly uncovered group of distantly related lysine
methyltransferases preferentially interact with molecular chaperones
to regulate their activity.";
PLoS Genet. 9:E1003210-E1003210(2013).
[20]
NOMENCLATURE.
PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
Williamson J.R., Wilson D., Yonath A., Yusupov M.;
"A new system for naming ribosomal proteins.";
Curr. Opin. Struct. Biol. 24:165-169(2014).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-294, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-399, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[24]
INTERACTION WITH DHX33.
PubMed=26100019; DOI=10.1128/MCB.00315-15;
Zhang Y., You J., Wang X., Weber J.;
"The DHX33 RNA Helicase Promotes mRNA Translation Initiation.";
Mol. Cell. Biol. 35:2918-2931(2015).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-39; LYS-224; LYS-226;
LYS-286; LYS-366; LYS-386; LYS-393 AND LYS-399, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[27]
STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
PubMed=23636399; DOI=10.1038/nature12104;
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
Wilson D.N., Beckmann R.;
"Structures of the human and Drosophila 80S ribosome.";
Nature 497:80-85(2013).
[28]
VARIANT ARG-11.
PubMed=22431104; DOI=10.1002/humu.22081;
Gazda H.T., Preti M., Sheen M.R., O'Donohue M.F., Vlachos A.,
Davies S.M., Kattamis A., Doherty L., Landowski M., Buros C.,
Ghazvinian R., Sieff C.A., Newburger P.E., Niewiadomska E.,
Matysiak M., Glader B., Atsidaftos E., Lipton J.M., Gleizes P.E.,
Beggs A.H.;
"Frameshift mutation in p53 regulator RPL26 is associated with
multiple physical abnormalities and a specific pre-ribosomal RNA
processing defect in diamond-blackfan anemia.";
Hum. Mutat. 33:1037-1044(2012).
-!- FUNCTION: The L3 protein is a component of the large subunit of
cytoplasmic ribosomes. {ECO:0000305|PubMed:12962325}.
-!- SUBUNIT: Component of the large ribosomal subunit (Probable).
Interacts with METTL18 (PubMed:23349634). Interacts with DHX33
(PubMed:26100019). {ECO:0000269|PubMed:23349634,
ECO:0000269|PubMed:26100019, ECO:0000305|PubMed:12962325}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:16963496}. Cytoplasm
{ECO:0000269|PubMed:16963496}.
-!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
{ECO:0000305}.
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EMBL; X73460; CAA51839.1; -; mRNA.
EMBL; AB062291; BAB93474.1; -; mRNA.
EMBL; CR456566; CAG30452.1; -; mRNA.
EMBL; AK315693; BAG38056.1; -; mRNA.
EMBL; AL022326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002408; AAH02408.1; -; mRNA.
EMBL; BC006483; AAH06483.1; -; mRNA.
EMBL; BC008003; AAH08003.1; -; mRNA.
EMBL; BC012146; AAH12146.1; -; mRNA.
EMBL; BC012786; AAH12786.1; -; mRNA.
EMBL; BC013674; AAH13674.1; -; mRNA.
EMBL; BC014017; AAH14017.1; -; mRNA.
EMBL; BC015032; AAH15032.1; -; mRNA.
EMBL; BC015767; AAH15767.1; -; mRNA.
EMBL; BC063662; AAH63662.1; -; mRNA.
EMBL; BC088373; AAH88373.1; -; mRNA.
EMBL; BC107711; AAI07712.1; -; mRNA.
EMBL; M90054; AAA60291.1; -; mRNA.
EMBL; L22453; AAA91344.1; -; mRNA.
EMBL; AB007166; BAA25828.1; -; Genomic_DNA.
CCDS; CCDS13988.1; -.
PIR; S34195; S34195.
RefSeq; NP_000958.1; NM_000967.3.
UniGene; Hs.119598; -.
PDB; 4UG0; EM; -; LB=1-403.
PDB; 4V6X; EM; 5.00 A; CB=1-403.
PDB; 5AJ0; EM; 3.50 A; AB=1-403.
PDB; 5LKS; EM; 3.60 A; LB=1-403.
PDB; 5T2C; EM; 3.60 A; E=1-403.
PDB; 6EK0; EM; 2.90 A; LB=1-403.
PDBsum; 4UG0; -.
PDBsum; 4V6X; -.
PDBsum; 5AJ0; -.
PDBsum; 5LKS; -.
PDBsum; 5T2C; -.
PDBsum; 6EK0; -.
ProteinModelPortal; P39023; -.
SMR; P39023; -.
BioGrid; 112042; 190.
CORUM; P39023; -.
IntAct; P39023; 67.
MINT; P39023; -.
STRING; 9606.ENSP00000346001; -.
DrugBank; DB02494; Alpha-Hydroxy-Beta-Phenyl-Propionic Acid.
DrugBank; DB07374; Anisomycin.
DrugBank; DB04865; Omacetaxine mepesuccinate.
DrugBank; DB08437; Puromycin.
iPTMnet; P39023; -.
PhosphoSitePlus; P39023; -.
SwissPalm; P39023; -.
BioMuta; RPL3; -.
DMDM; 730565; -.
SWISS-2DPAGE; P39023; -.
EPD; P39023; -.
MaxQB; P39023; -.
PaxDb; P39023; -.
PeptideAtlas; P39023; -.
PRIDE; P39023; -.
ProteomicsDB; 55309; -.
TopDownProteomics; P39023; -.
DNASU; 6122; -.
Ensembl; ENST00000216146; ENSP00000346001; ENSG00000100316.
GeneID; 6122; -.
KEGG; hsa:6122; -.
UCSC; uc003axi.4; human.
CTD; 6122; -.
DisGeNET; 6122; -.
EuPathDB; HostDB:ENSG00000100316.15; -.
GeneCards; RPL3; -.
H-InvDB; HIX0172339; -.
HGNC; HGNC:10332; RPL3.
HPA; HPA003365; -.
HPA; HPA055361; -.
MIM; 604163; gene.
neXtProt; NX_P39023; -.
OpenTargets; ENSG00000100316; -.
PharmGKB; PA34713; -.
eggNOG; KOG0746; Eukaryota.
eggNOG; COG0087; LUCA.
GeneTree; ENSGT00390000017606; -.
HOGENOM; HOG000107319; -.
HOVERGEN; HBG001864; -.
InParanoid; P39023; -.
KO; K02925; -.
OMA; HQRTEYN; -.
OrthoDB; EOG091G086T; -.
PhylomeDB; P39023; -.
TreeFam; TF300555; -.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-156902; Peptide chain elongation.
Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-HSA-192823; Viral mRNA Translation.
Reactome; R-HSA-2408557; Selenocysteine synthesis.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-HSA-72764; Eukaryotic Translation Termination.
Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
ChiTaRS; RPL3; human.
GeneWiki; RPL3; -.
GenomeRNAi; 6122; -.
PRO; PR:P39023; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100316; -.
CleanEx; HS_RPL3; -.
ExpressionAtlas; P39023; baseline and differential.
Genevisible; P39023; HS.
GO; GO:0005737; C:cytoplasm; HDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0022625; C:cytosolic large ribosomal subunit; HDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0008097; F:5S rRNA binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
GO; GO:0006412; P:translation; IBA:GO_Central.
GO; GO:0006413; P:translational initiation; TAS:Reactome.
InterPro; IPR000597; Ribosomal_L3.
InterPro; IPR019926; Ribosomal_L3_CS.
InterPro; IPR009000; Transl_B-barrel_sf.
Pfam; PF00297; Ribosomal_L3; 1.
SUPFAM; SSF50447; SSF50447; 1.
PROSITE; PS00474; RIBOSOMAL_L3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Isopeptide bond; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Ribonucleoprotein;
Ribosomal protein; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12962325}.
CHAIN 2 403 60S ribosomal protein L3.
/FTId=PRO_0000077227.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 136 136 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27659}.
MOD_RES 286 286 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P27659}.
MOD_RES 294 294 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 304 304 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 366 366 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 373 373 N6-acetyllysine.
{ECO:0000250|UniProtKB:P27659}.
CROSSLNK 39 39 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 224 224 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 226 226 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 286 286 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 294 294 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 366 366 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 386 386 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 393 393 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 399 399 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
VARIANT 11 11 H -> R (rare variant found in a Diamond-
Blackfan anemia patient; unknown
pathological significance).
{ECO:0000269|PubMed:22431104}.
/FTId=VAR_069220.
CONFLICT 22 22 S -> T (in Ref. 8; AAA91344).
{ECO:0000305}.
CONFLICT 260 260 A -> V (in Ref. 8; AAA91344).
{ECO:0000305}.
SEQUENCE 403 AA; 46109 MW; A607CEE75CF62148 CRC64;
MSHRKFSAPR HGSLGFLPRK RSSRHRGKVK SFPKDDPSKP VHLTAFLGYK AGMTHIVREV
DRPGSKVNKK EVVEAVTIVE TPPMVVVGIV GYVETPRGLR TFKTVFAEHI SDECKRRFYK
NWHKSKKKAF TKYCKKWQDE DGKKQLEKDF SSMKKYCQVI RVIAHTQMRL LPLRQKKAHL
MEIQVNGGTV AEKLDWARER LEQQVPVNQV FGQDEMIDVI GVTKGKGYKG VTSRWHTKKL
PRKTHRGLRK VACIGAWHPA RVAFSVARAG QKGYHHRTEI NKKIYKIGQG YLIKDGKLIK
NNASTDYDLS DKSINPLGGF VHYGEVTNDF VMLKGCVVGT KKRVLTLRKS LLVQTKRRAL
EKIDLKFIDT TSKFGHGRFQ TMEEKKAFMG PLKKDRIAKE EGA


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