RL17A_YEAST
ID RL17A_YEAST Reviewed; 184 AA.
AC P05740; D6VX21;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=60S ribosomal protein L17-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=L20A;
DE AltName: Full=Large ribosomal subunit protein uL22-A {ECO:0000303|PubMed:24524803};
DE AltName: Full=YL17;
GN Name=RPL17A {ECO:0000303|PubMed:9559554}; Synonyms=RPL17, RPL20A;
GN OrderedLocusNames=YKL180W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
RX PubMed=8154185; DOI=10.1002/yea.320091208;
RA Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J.,
RA Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
RT "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI
RT from Saccharomyces cerevisiae reveals 23 open reading frames including the
RT FAS1 gene.";
RL Yeast 9:1343-1348(1993).
RN [4]
RP PARTIAL PROTEIN SEQUENCE OF 2-41, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=18782943; DOI=10.1007/bf00341461;
RA Otaka E., Higo K., Itoh T.;
RT "Yeast ribosomal proteins. VIII. Isolation of two proteins and sequence
RT characterization of twenty-four proteins from cytoplasmic ribosomes.";
RL Mol. Gen. Genet. 195:544-546(1984).
RN [5]
RP NOMENCLATURE, AND SUBUNIT.
RX PubMed=9559554;
RX DOI=10.1002/(sici)1097-0061(19980330)14:5<471::aid-yea241>3.0.co;2-u;
RA Planta R.J., Mager W.H.;
RT "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.";
RL Yeast 14:471-477(1998).
RN [6]
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=10601260; DOI=10.1074/jbc.274.52.37035;
RA Arnold R.J., Polevoda B., Reilly J.P., Sherman F.;
RT "The action of N-terminal acetyltransferases on yeast ribosomal proteins.";
RL J. Biol. Chem. 274:37035-37040(1999).
RN [7]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-70, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-46, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
RN [10]
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 [11]
RP 3D-STRUCTURE MODELING OF 6-152, AND ELECTRON MICROSCOPY.
RX PubMed=11701127; DOI=10.1016/s0092-8674(01)00539-6;
RA Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G.,
RA Frank J.;
RT "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-
RT ribosome and subunit-subunit interactions.";
RL Cell 107:373-386(2001).
RN [12]
RP 3D-STRUCTURE MODELING, AND ELECTRON MICROSCOPY.
RX PubMed=14976550; DOI=10.1038/sj.emboj.7600102;
RA Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R.,
RA Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.;
RT "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome
RT facilitate tRNA translocation.";
RL EMBO J. 23:1008-1019(2004).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 80S RIBOSOME.
RX PubMed=21109664; DOI=10.1126/science.1194294;
RA Ben-Shem A., Jenner L., Yusupova G., Yusupov M.;
RT "Crystal structure of the eukaryotic ribosome.";
RL Science 330:1203-1209(2010).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 80S RIBOSOME, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=22096102; DOI=10.1126/science.1212642;
RA Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., Yusupova G.,
RA Yusupov M.;
RT "The structure of the eukaryotic ribosome at 3.0 A resolution.";
RL Science 334:1524-1529(2011).
CC -!- FUNCTION: Component of the ribosome, a large ribonucleoprotein complex
CC responsible for the synthesis of proteins in the cell. The small
CC ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the
CC encoded message by selecting cognate aminoacyl-transfer RNA (tRNA)
CC molecules. The large subunit (LSU) contains the ribosomal catalytic
CC site termed the peptidyl transferase center (PTC), which catalyzes the
CC formation of peptide bonds, thereby polymerizing the amino acids
CC delivered by tRNAs into a polypeptide chain. The nascent polypeptides
CC leave the ribosome through a tunnel in the LSU and interact with
CC protein factors that function in enzymatic processing, targeting, and
CC the membrane insertion of nascent chains at the exit of the ribosomal
CC tunnel. {ECO:0000305|PubMed:22096102}.
CC -!- SUBUNIT: Component of the large ribosomal subunit (LSU). Mature yeast
CC ribosomes consist of a small (40S) and a large (60S) subunit. The 40S
CC small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33
CC different proteins (encoded by 57 genes). The large 60S subunit
CC contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different
CC proteins (encoded by 81 genes). uL22 is associated with the polypeptide
CC exit tunnel (PubMed:9559554, PubMed:22096102).
CC {ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:22096102}.
CC -!- MISCELLANEOUS: There are 2 genes for uL22 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL22 family.
CC {ECO:0000305}.
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DR EMBL; Z28180; CAA82023.1; -; Genomic_DNA.
DR EMBL; Z28179; CAA82022.1; -; Genomic_DNA.
DR EMBL; X74151; CAA52258.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA08987.1; -; Genomic_DNA.
DR PIR; S38012; S38012.
DR RefSeq; NP_012741.1; NM_001179746.1.
DR PDB; 2WW9; EM; 8.60 A; I=1-184.
DR PDB; 2WWA; EM; 8.90 A; I=1-184.
DR PDB; 2WWB; EM; 6.48 A; I=1-184.
DR PDB; 3J6X; EM; 6.10 A; 57=1-184.
DR PDB; 3J6Y; EM; 6.10 A; 57=1-184.
DR PDB; 3J77; EM; 6.20 A; 67=1-184.
DR PDB; 3J78; EM; 6.30 A; 67=1-184.
DR PDB; 3JCT; EM; 3.08 A; P=1-184.
DR PDB; 4U3M; X-ray; 3.00 A; M7/m7=2-184.
DR PDB; 4U3N; X-ray; 3.20 A; M7/m7=2-184.
DR PDB; 4U3U; X-ray; 2.90 A; M7/m7=2-184.
DR PDB; 4U4N; X-ray; 3.10 A; M7/m7=2-184.
DR PDB; 4U4O; X-ray; 3.60 A; M7/m7=2-184.
DR PDB; 4U4Q; X-ray; 3.00 A; M7/m7=2-184.
DR PDB; 4U4R; X-ray; 2.80 A; M7/m7=2-184.
DR PDB; 4U4U; X-ray; 3.00 A; M7/m7=2-184.
DR PDB; 4U4Y; X-ray; 3.20 A; M7/m7=2-184.
DR PDB; 4U4Z; X-ray; 3.10 A; M7/m7=2-184.
DR PDB; 4U50; X-ray; 3.20 A; M7/m7=2-184.
DR PDB; 4U51; X-ray; 3.20 A; M7/m7=2-184.
DR PDB; 4U52; X-ray; 3.00 A; M7/m7=2-184.
DR PDB; 4U53; X-ray; 3.30 A; M7/m7=2-184.
DR PDB; 4U55; X-ray; 3.20 A; M7/m7=2-184.
DR PDB; 4U56; X-ray; 3.45 A; M7/m7=2-184.
DR PDB; 4U6F; X-ray; 3.10 A; M7/m7=2-184.
DR PDB; 4V4B; EM; 11.70 A; BN=2-184.
DR PDB; 4V6I; EM; 8.80 A; BV=1-170.
DR PDB; 4V7F; EM; 8.70 A; U=1-184.
DR PDB; 4V7R; X-ray; 4.00 A; BQ/DQ=1-184.
DR PDB; 4V88; X-ray; 3.00 A; BP/DP=1-184.
DR PDB; 4V8T; EM; 8.10 A; P=1-184.
DR PDB; 4V8Y; EM; 4.30 A; BP=2-184.
DR PDB; 4V8Z; EM; 6.60 A; BP=2-184.
DR PDB; 4V91; EM; 3.70 A; P=1-184.
DR PDB; 5APN; EM; 3.91 A; P=1-184.
DR PDB; 5APO; EM; 3.41 A; P=1-184.
DR PDB; 5DAT; X-ray; 3.15 A; M7/m7=2-184.
DR PDB; 5DC3; X-ray; 3.25 A; M7/m7=2-184.
DR PDB; 5DGE; X-ray; 3.45 A; M7/m7=2-184.
DR PDB; 5DGF; X-ray; 3.30 A; M7/m7=2-184.
DR PDB; 5DGV; X-ray; 3.10 A; M7/m7=2-184.
DR PDB; 5FCI; X-ray; 3.40 A; M7/m7=2-184.
DR PDB; 5FCJ; X-ray; 3.10 A; M7/m7=2-184.
DR PDB; 5FL8; EM; 9.50 A; P=1-184.
DR PDB; 5GAK; EM; 3.88 A; R=1-184.
DR PDB; 5H4P; EM; 3.07 A; P=1-184.
DR PDB; 5I4L; X-ray; 3.10 A; M7/m7=2-184.
DR PDB; 5JCS; EM; 9.50 A; P=1-184.
DR PDB; 5JUO; EM; 4.00 A; U=1-184.
DR PDB; 5JUP; EM; 3.50 A; U=1-184.
DR PDB; 5JUS; EM; 4.20 A; U=1-184.
DR PDB; 5JUT; EM; 4.00 A; U=1-184.
DR PDB; 5JUU; EM; 4.00 A; U=1-184.
DR PDB; 5LYB; X-ray; 3.25 A; M7/m7=2-184.
DR PDB; 5M1J; EM; 3.30 A; P5=2-184.
DR PDB; 5MC6; EM; 3.80 A; AX=1-184.
DR PDB; 5MEI; X-ray; 3.50 A; CR/x=2-184.
DR PDB; 5NDG; X-ray; 3.70 A; M7/m7=1-184.
DR PDB; 5NDV; X-ray; 3.30 A; M7/m7=1-184.
DR PDB; 5NDW; X-ray; 3.70 A; M7/m7=1-184.
DR PDB; 5OBM; X-ray; 3.40 A; M7/m7=1-184.
DR PDB; 5ON6; X-ray; 3.10 A; CR/x=2-184.
DR PDB; 5T62; EM; 3.30 A; c=1-184.
DR PDB; 5T6R; EM; 4.50 A; c=1-184.
DR PDB; 5TBW; X-ray; 3.00 A; CR/x=2-184.
DR PDB; 5TGA; X-ray; 3.30 A; M7/m7=2-184.
DR PDB; 5TGM; X-ray; 3.50 A; M7/m7=2-184.
DR PDB; 5Z3G; EM; 3.65 A; T=1-184.
DR PDB; 6C0F; EM; 3.70 A; P=1-184.
DR PDB; 6CB1; EM; 4.60 A; P=1-184.
DR PDB; 6ELZ; EM; 3.30 A; P=1-184.
DR PDB; 6EM1; EM; 3.60 A; P=1-184.
DR PDB; 6EM3; EM; 3.20 A; P=1-184.
DR PDB; 6EM4; EM; 4.10 A; P=1-184.
DR PDB; 6EM5; EM; 4.30 A; P=1-184.
DR PDB; 6FT6; EM; 3.90 A; P=1-184.
DR PDB; 6GQ1; EM; 4.40 A; P=2-184.
DR PDB; 6GQB; EM; 3.90 A; P=2-184.
DR PDB; 6GQV; EM; 4.00 A; P=2-184.
DR PDB; 6HD7; EM; 3.40 A; R=1-184.
DR PDB; 6HHQ; X-ray; 3.10 A; CR/x=1-184.
DR PDB; 6I7O; EM; 5.30 A; AX/XX=1-184.
DR PDB; 6M62; EM; 3.20 A; P=1-184.
DR PDB; 6N8J; EM; 3.50 A; P=1-184.
DR PDB; 6N8K; EM; 3.60 A; P=1-184.
DR PDB; 6N8L; EM; 3.60 A; P=1-184.
DR PDB; 6N8M; EM; 3.50 A; c=1-184.
DR PDB; 6N8N; EM; 3.80 A; c=1-184.
DR PDB; 6N8O; EM; 3.50 A; c=1-184.
DR PDB; 6OIG; EM; 3.80 A; P=2-184.
DR PDB; 6Q8Y; EM; 3.10 A; AX=2-184.
DR PDB; 6QIK; EM; 3.10 A; U=2-155.
DR PDB; 6QT0; EM; 3.40 A; U=1-184.
DR PDB; 6QTZ; EM; 3.50 A; U=1-184.
DR PDB; 6R84; EM; 3.60 A; 5=2-184.
DR PDB; 6R86; EM; 3.40 A; 5=2-184.
DR PDB; 6R87; EM; 3.40 A; 5=2-184.
DR PDB; 6RI5; EM; 3.30 A; U=1-184.
DR PDB; 6RZZ; EM; 3.20 A; U=1-184.
DR PDB; 6S05; EM; 3.90 A; U=1-184.
DR PDB; 6S47; EM; 3.28 A; AR=2-184.
DR PDB; 6SNT; EM; 2.80 A; v=1-184.
DR PDB; 6SV4; EM; 3.30 A; AX/XX/zX=1-184.
DR PDB; 6T4Q; EM; 2.60 A; LP=2-184.
DR PDB; 6T7I; EM; 3.20 A; LP=1-184.
DR PDB; 6T7T; EM; 3.10 A; LP=1-184.
DR PDB; 6T83; EM; 4.00 A; A/Py=1-184.
DR PDB; 6TB3; EM; 2.80 A; AX=2-184.
DR PDB; 6TNU; EM; 3.10 A; AX=2-184.
DR PDB; 6WOO; EM; 2.90 A; P=3-182.
DR PDB; 6XIQ; EM; 4.20 A; P=1-184.
DR PDB; 6XIR; EM; 3.20 A; P=1-184.
DR PDB; 6YLG; EM; 3.00 A; P=1-184.
DR PDB; 6YLH; EM; 3.10 A; P=1-184.
DR PDB; 6YLX; EM; 3.90 A; P=1-184.
DR PDB; 6YLY; EM; 3.80 A; P=1-184.
DR PDB; 6Z6J; EM; 3.40 A; LP=1-184.
DR PDB; 6Z6K; EM; 3.40 A; LP=1-184.
DR PDB; 7AZY; EM; 2.88 A; y=1-184.
DR PDB; 7B7D; EM; 3.30 A; LR=2-184.
DR PDB; 7BT6; EM; 3.12 A; P=1-184.
DR PDB; 7BTB; EM; 3.22 A; P=1-184.
DR PDB; 7NRC; EM; 3.90 A; LR=2-184.
DR PDB; 7NRD; EM; 4.36 A; LR=2-184.
DR PDB; 7OF1; EM; 3.10 A; P=1-184.
DR PDB; 7OH3; EM; 3.40 A; P=1-184.
DR PDB; 7OHP; EM; 3.90 A; P=1-184.
DR PDB; 7OHQ; EM; 3.10 A; P=1-184.
DR PDB; 7OHR; EM; 4.72 A; P=1-184.
DR PDB; 7OHS; EM; 4.38 A; P=1-184.
DR PDB; 7OHU; EM; 3.70 A; P=1-184.
DR PDB; 7OHV; EM; 3.90 A; P=1-184.
DR PDB; 7OHW; EM; 3.50 A; P=1-184.
DR PDB; 7OHX; EM; 3.30 A; P=1-184.
DR PDB; 7OHY; EM; 3.90 A; P=1-184.
DR PDBsum; 2WW9; -.
DR PDBsum; 2WWA; -.
DR PDBsum; 2WWB; -.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
DR PDBsum; 3JCT; -.
DR PDBsum; 4U3M; -.
DR PDBsum; 4U3N; -.
DR PDBsum; 4U3U; -.
DR PDBsum; 4U4N; -.
DR PDBsum; 4U4O; -.
DR PDBsum; 4U4Q; -.
DR PDBsum; 4U4R; -.
DR PDBsum; 4U4U; -.
DR PDBsum; 4U4Y; -.
DR PDBsum; 4U4Z; -.
DR PDBsum; 4U50; -.
DR PDBsum; 4U51; -.
DR PDBsum; 4U52; -.
DR PDBsum; 4U53; -.
DR PDBsum; 4U55; -.
DR PDBsum; 4U56; -.
DR PDBsum; 4U6F; -.
DR PDBsum; 4V4B; -.
DR PDBsum; 4V6I; -.
DR PDBsum; 4V7F; -.
DR PDBsum; 4V7R; -.
DR PDBsum; 4V88; -.
DR PDBsum; 4V8T; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V91; -.
DR PDBsum; 5APN; -.
DR PDBsum; 5APO; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5DGF; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5FL8; -.
DR PDBsum; 5GAK; -.
DR PDBsum; 5H4P; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5JCS; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 5LYB; -.
DR PDBsum; 5M1J; -.
DR PDBsum; 5MC6; -.
DR PDBsum; 5MEI; -.
DR PDBsum; 5NDG; -.
DR PDBsum; 5NDV; -.
DR PDBsum; 5NDW; -.
DR PDBsum; 5OBM; -.
DR PDBsum; 5ON6; -.
DR PDBsum; 5T62; -.
DR PDBsum; 5T6R; -.
DR PDBsum; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 5Z3G; -.
DR PDBsum; 6C0F; -.
DR PDBsum; 6CB1; -.
DR PDBsum; 6ELZ; -.
DR PDBsum; 6EM1; -.
DR PDBsum; 6EM3; -.
DR PDBsum; 6EM4; -.
DR PDBsum; 6EM5; -.
DR PDBsum; 6FT6; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HD7; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6M62; -.
DR PDBsum; 6N8J; -.
DR PDBsum; 6N8K; -.
DR PDBsum; 6N8L; -.
DR PDBsum; 6N8M; -.
DR PDBsum; 6N8N; -.
DR PDBsum; 6N8O; -.
DR PDBsum; 6OIG; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6QIK; -.
DR PDBsum; 6QT0; -.
DR PDBsum; 6QTZ; -.
DR PDBsum; 6R84; -.
DR PDBsum; 6R86; -.
DR PDBsum; 6R87; -.
DR PDBsum; 6RI5; -.
DR PDBsum; 6RZZ; -.
DR PDBsum; 6S05; -.
DR PDBsum; 6S47; -.
DR PDBsum; 6SNT; -.
DR PDBsum; 6SV4; -.
DR PDBsum; 6T4Q; -.
DR PDBsum; 6T7I; -.
DR PDBsum; 6T7T; -.
DR PDBsum; 6T83; -.
DR PDBsum; 6TB3; -.
DR PDBsum; 6TNU; -.
DR PDBsum; 6WOO; -.
DR PDBsum; 6XIQ; -.
DR PDBsum; 6XIR; -.
DR PDBsum; 6YLG; -.
DR PDBsum; 6YLH; -.
DR PDBsum; 6YLX; -.
DR PDBsum; 6YLY; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 7AZY; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7BT6; -.
DR PDBsum; 7BTB; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR PDBsum; 7OF1; -.
DR PDBsum; 7OH3; -.
DR PDBsum; 7OHP; -.
DR PDBsum; 7OHQ; -.
DR PDBsum; 7OHR; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHU; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR PDBsum; 7OHX; -.
DR PDBsum; 7OHY; -.
DR AlphaFoldDB; P05740; -.
DR SMR; P05740; -.
DR BioGRID; 33959; 210.
DR DIP; DIP-5529N; -.
DR IntAct; P05740; 59.
DR MINT; P05740; -.
DR STRING; 4932.YKL180W; -.
DR CarbonylDB; P05740; -.
DR iPTMnet; P05740; -.
DR MaxQB; P05740; -.
DR PaxDb; P05740; -.
DR PRIDE; P05740; -.
DR EnsemblFungi; YKL180W_mRNA; YKL180W; YKL180W.
DR GeneID; 853674; -.
DR KEGG; sce:YKL180W; -.
DR SGD; S000001663; RPL17A.
DR VEuPathDB; FungiDB:YKL180W; -.
DR eggNOG; KOG3353; Eukaryota.
DR GeneTree; ENSGT00950000183010; -.
DR HOGENOM; CLU_083987_0_0_1; -.
DR InParanoid; P05740; -.
DR OMA; REPDNIT; -.
DR BioCyc; YEAST:G3O-31946-MON; -.
DR Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR EvolutionaryTrace; P05740; -.
DR PRO; PR:P05740; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P05740; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:SGD.
DR GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IGI:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; IDA:SGD.
DR CDD; cd00336; Ribosomal_L22; 1.
DR Gene3D; 3.90.470.10; -; 1.
DR InterPro; IPR001063; Ribosomal_L22.
DR InterPro; IPR018260; Ribosomal_L22/L17_CS.
DR InterPro; IPR005721; Ribosomal_L22/L17_euk/arc.
DR InterPro; IPR036394; Ribosomal_L22/L17_sf.
DR PANTHER; PTHR11593; PTHR11593; 1.
DR Pfam; PF00237; Ribosomal_L22; 1.
DR SUPFAM; SSF54843; SSF54843; 1.
DR TIGRFAMs; TIGR01038; uL22_arch_euk; 1.
DR PROSITE; PS00464; RIBOSOMAL_L22; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:18782943"
FT CHAIN 2..184
FT /note="60S ribosomal protein L17-A"
FT /id="PRO_0000125347"
FT MOD_RES 70
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CROSSLNK 46
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 104..114
FT /note="AKGLDATKLYV -> VCQEYYMFSTR (in Ref. 3; CAA52258)"
FT /evidence="ECO:0000305"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 26..34
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 41..52
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 85..105
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 112..121
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:6EM3"
SQ SEQUENCE 184 AA; 20549 MW; B8902DD90714671D CRC64;
MARYGATSTN PAKSASARGS YLRVSFKNTR ETAQAINGWE LTKAQKYLEQ VLDHQRAIPF
RRFNSSIGRT AQGKEFGVTK ARWPAKSVKF VQGLLQNAAA NAEAKGLDAT KLYVSHIQVN
QAPKQRRRTY RAHGRINKYE SSPSHIELVV TEKEEAVAKA AEKKVVRLTS RQRGRIAAQK
RIAA
