RL35A_YEAST
ID RL35A_YEAST Reviewed; 120 AA.
AC P0CX84; D6VRG2; P39741; P39930;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=60S ribosomal protein L35-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=Large ribosomal subunit protein uL29-A {ECO:0000303|PubMed:24524803};
GN Name=RPL35A {ECO:0000303|PubMed:9559554}; Synonyms=SOS1;
GN OrderedLocusNames=YDL191W; ORFNames=D1249;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8513501; DOI=10.1016/0092-8674(93)90646-8;
RA Zhong T., Arndt K.T.;
RT "The yeast SIS1 protein, a DnaJ homolog, is required for the initiation of
RT translation.";
RL Cell 73:1175-1186(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8896272;
RX DOI=10.1002/(sici)1097-0061(199609)12:10b<1065::aid-yea995>3.0.co;2-f;
RA Verhasselt P., Voet M., Mathys J., Volckaert G.;
RT "The sequence of 23 kb surrounding the SNF3 locus on the left arm of yeast
RT chromosome IV reveals the location of five known genes and characterizes at
RT least six new open reading frames including putative genes for ribosomal
RT protein L35 and a sugar transport protein.";
RL Yeast 12:1065-1070(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [4]
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 [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 MASS SPECTROMETRY, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=11983894; DOI=10.1073/pnas.082119899;
RA Lee S.-W., Berger S.J., Martinovic S., Pasa-Tolic L., Anderson G.A.,
RA Shen Y., Zhao R., Smith R.D.;
RT "Direct mass spectrometric analysis of intact proteins of the yeast large
RT ribosomal subunit using capillary LC/FTICR.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:5942-5947(2002).
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 SER-13 AND SER-50, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [9]
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 [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 2-60, 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 STRUCTURE BY ELECTRON MICROSCOPY (8.60 ANGSTROMS).
RX PubMed=19933108; DOI=10.1126/science.1178535;
RA Becker T., Bhushan S., Jarasch A., Armache J.P., Funes S., Jossinet F.,
RA Gumbart J., Mielke T., Berninghausen O., Schulten K., Westhof E.,
RA Gilmore R., Mandon E.C., Beckmann R.;
RT "Structure of monomeric yeast and mammalian Sec61 complexes interacting
RT with the translating ribosome.";
RL Science 326:1369-1373(2009).
RN [14]
RP STRUCTURE BY ELECTRON MICROSCOPY (8.80 ANGSTROMS).
RX PubMed=20980660; DOI=10.1073/pnas.1009999107;
RA Armache J.P., Jarasch A., Anger A.M., Villa E., Becker T., Bhushan S.,
RA Jossinet F., Habeck M., Dindar G., Franckenberg S., Marquez V., Mielke T.,
RA Thomm M., Berninghausen O., Beatrix B., Soding J., Westhof E., Wilson D.N.,
RA Beckmann R.;
RT "Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome
RT at 5.5-A resolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:19748-19753(2010).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS).
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 [16]
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS), SUBUNIT, AND 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).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (8.10 ANGSTROMS).
RX PubMed=23142985; DOI=10.1038/nsmb.2425;
RA Greber B.J., Boehringer D., Montellese C., Ban N.;
RT "Cryo-EM structures of Arx1 and maturation factors Rei1 and Jjj1 bound to
RT the 60S ribosomal subunit.";
RL Nat. Struct. Mol. Biol. 19:1228-1233(2012).
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). uL29 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 -!- MASS SPECTROMETRY: Mass=13769.991; Method=Electrospray;
CC Note=Monoisotopic mass.; Evidence={ECO:0000269|PubMed:11983894};
CC -!- MISCELLANEOUS: There are 2 genes for uL29 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL29 family.
CC {ECO:0000305}.
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DR EMBL; M82913; AAA34492.1; -; Genomic_DNA.
DR EMBL; X83276; CAA58256.1; -; Genomic_DNA.
DR EMBL; Z74239; CAA98768.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11722.1; -; Genomic_DNA.
DR PIR; S30770; S30770.
DR RefSeq; NP_010090.1; NM_001180251.2.
DR RefSeq; NP_010145.1; NM_001180196.2.
DR PDB; 2WW9; EM; 8.60 A; N=1-120.
DR PDB; 2WWA; EM; 8.90 A; N=1-120.
DR PDB; 2WWB; EM; 6.48 A; N=1-120.
DR PDB; 3J6X; EM; 6.10 A; 75=1-120.
DR PDB; 3J6Y; EM; 6.10 A; 75=1-120.
DR PDB; 3J77; EM; 6.20 A; 85=1-120.
DR PDB; 3J78; EM; 6.30 A; 85=1-120.
DR PDB; 3JCT; EM; 3.08 A; h=1-120.
DR PDB; 4U3M; X-ray; 3.00 A; O5/o5=2-120.
DR PDB; 4U3N; X-ray; 3.20 A; O5/o5=2-120.
DR PDB; 4U3U; X-ray; 2.90 A; O5/o5=2-120.
DR PDB; 4U4N; X-ray; 3.10 A; O5/o5=2-120.
DR PDB; 4U4O; X-ray; 3.60 A; O5/o5=2-120.
DR PDB; 4U4Q; X-ray; 3.00 A; O5/o5=2-120.
DR PDB; 4U4R; X-ray; 2.80 A; O5/o5=2-120.
DR PDB; 4U4U; X-ray; 3.00 A; O5/o5=2-120.
DR PDB; 4U4Y; X-ray; 3.20 A; O5/o5=2-120.
DR PDB; 4U4Z; X-ray; 3.10 A; O5/o5=2-120.
DR PDB; 4U50; X-ray; 3.20 A; O5/o5=2-120.
DR PDB; 4U51; X-ray; 3.20 A; O5/o5=2-120.
DR PDB; 4U52; X-ray; 3.00 A; O5/o5=2-120.
DR PDB; 4U53; X-ray; 3.30 A; O5/o5=2-120.
DR PDB; 4U55; X-ray; 3.20 A; O5/o5=2-120.
DR PDB; 4U56; X-ray; 3.45 A; O5/o5=2-120.
DR PDB; 4U6F; X-ray; 3.10 A; O5/o5=2-120.
DR PDB; 4V4B; EM; 11.70 A; BX=1-120.
DR PDB; 4V6I; EM; 8.80 A; Bc=1-120.
DR PDB; 4V7F; EM; 8.70 A; Z=1-120.
DR PDB; 4V7R; X-ray; 4.00 A; Bc/Dc=1-120.
DR PDB; 4V88; X-ray; 3.00 A; Bh/Dh=1-120.
DR PDB; 4V8T; EM; 8.10 A; h=1-120.
DR PDB; 4V91; EM; 3.70 A; h=1-120.
DR PDB; 5APN; EM; 3.91 A; h=1-120.
DR PDB; 5APO; EM; 3.41 A; h=1-120.
DR PDB; 5DAT; X-ray; 3.15 A; O5/o5=2-120.
DR PDB; 5DC3; X-ray; 3.25 A; O5/o5=2-120.
DR PDB; 5DGE; X-ray; 3.45 A; O5/o5=2-120.
DR PDB; 5DGF; X-ray; 3.30 A; O5/o5=2-120.
DR PDB; 5DGV; X-ray; 3.10 A; O5/o5=2-120.
DR PDB; 5FCI; X-ray; 3.40 A; O5/o5=2-120.
DR PDB; 5FCJ; X-ray; 3.10 A; O5/o5=2-120.
DR PDB; 5FL8; EM; 9.50 A; h=1-120.
DR PDB; 5GAK; EM; 3.88 A; j=1-120.
DR PDB; 5H4P; EM; 3.07 A; h=1-120.
DR PDB; 5I4L; X-ray; 3.10 A; O5/o5=2-120.
DR PDB; 5JCS; EM; 9.50 A; h=1-120.
DR PDB; 5JUO; EM; 4.00 A; MA=1-120.
DR PDB; 5JUP; EM; 3.50 A; MA=1-120.
DR PDB; 5JUS; EM; 4.20 A; MA=1-120.
DR PDB; 5JUT; EM; 4.00 A; MA=1-120.
DR PDB; 5JUU; EM; 4.00 A; MA=1-120.
DR PDB; 5LYB; X-ray; 3.25 A; O5/o5=2-120.
DR PDB; 5M1J; EM; 3.30 A; h5=2-120.
DR PDB; 5MC6; EM; 3.80 A; BP=1-120.
DR PDB; 5MEI; X-ray; 3.50 A; AI/DJ=2-120.
DR PDB; 5NDG; X-ray; 3.70 A; O5/o5=2-120.
DR PDB; 5NDV; X-ray; 3.30 A; O5/o5=2-120.
DR PDB; 5NDW; X-ray; 3.70 A; O5/o5=2-120.
DR PDB; 5OBM; X-ray; 3.40 A; O5/o5=2-120.
DR PDB; 5ON6; X-ray; 3.10 A; AI/DJ=2-120.
DR PDB; 5T62; EM; 3.30 A; u=1-120.
DR PDB; 5T6R; EM; 4.50 A; u=1-120.
DR PDB; 5TBW; X-ray; 3.00 A; AI/DJ=2-120.
DR PDB; 5TGA; X-ray; 3.30 A; O5/o5=2-120.
DR PDB; 5TGM; X-ray; 3.50 A; O5/o5=2-120.
DR PDB; 5Z3G; EM; 3.65 A; l=1-120.
DR PDB; 6C0F; EM; 3.70 A; h=1-120.
DR PDB; 6CB1; EM; 4.60 A; h=1-120.
DR PDB; 6ELZ; EM; 3.30 A; h=1-120.
DR PDB; 6EM1; EM; 3.60 A; h=1-120.
DR PDB; 6EM3; EM; 3.20 A; h=1-120.
DR PDB; 6EM4; EM; 4.10 A; h=1-120.
DR PDB; 6EM5; EM; 4.30 A; h=1-120.
DR PDB; 6FT6; EM; 3.90 A; h=1-120.
DR PDB; 6GQ1; EM; 4.40 A; h=2-120.
DR PDB; 6GQB; EM; 3.90 A; h=2-120.
DR PDB; 6GQV; EM; 4.00 A; h=2-120.
DR PDB; 6HD7; EM; 3.40 A; j=1-120.
DR PDB; 6HHQ; X-ray; 3.10 A; AI/DJ=1-120.
DR PDB; 6I7O; EM; 5.30 A; BP/YP=2-120.
DR PDB; 6M62; EM; 3.20 A; h=1-120.
DR PDB; 6N8J; EM; 3.50 A; h=1-120.
DR PDB; 6N8K; EM; 3.60 A; h=1-120.
DR PDB; 6N8L; EM; 3.60 A; h=1-120.
DR PDB; 6N8M; EM; 3.50 A; u=1-120.
DR PDB; 6N8N; EM; 3.80 A; u=1-120.
DR PDB; 6N8O; EM; 3.50 A; u=1-120.
DR PDB; 6OIG; EM; 3.80 A; h=2-120.
DR PDB; 6Q8Y; EM; 3.10 A; BP=2-120.
DR PDB; 6QIK; EM; 3.10 A; Z=1-120.
DR PDB; 6QT0; EM; 3.40 A; Z=1-120.
DR PDB; 6QTZ; EM; 3.50 A; Z=1-120.
DR PDB; 6R84; EM; 3.60 A; j=2-120.
DR PDB; 6R86; EM; 3.40 A; j=2-120.
DR PDB; 6R87; EM; 3.40 A; j=2-120.
DR PDB; 6RI5; EM; 3.30 A; Z=1-120.
DR PDB; 6RZZ; EM; 3.20 A; Z=1-120.
DR PDB; 6S05; EM; 3.90 A; Z=1-120.
DR PDB; 6S47; EM; 3.28 A; Aj=2-120.
DR PDB; 6SNT; EM; 2.80 A; ai=1-120.
DR PDB; 6SV4; EM; 3.30 A; BP/YP/ZP=1-120.
DR PDB; 6T4Q; EM; 2.60 A; Lh=2-120.
DR PDB; 6T7I; EM; 3.20 A; Lh=1-120.
DR PDB; 6T7T; EM; 3.10 A; Lh=1-120.
DR PDB; 6T83; EM; 4.00 A; S/hb=1-120.
DR PDB; 6TB3; EM; 2.80 A; BP=2-120.
DR PDB; 6TNU; EM; 3.10 A; BP=2-120.
DR PDB; 6WOO; EM; 2.90 A; h=3-118.
DR PDB; 6XIQ; EM; 4.20 A; h=1-120.
DR PDB; 6XIR; EM; 3.20 A; h=1-120.
DR PDB; 6YLG; EM; 3.00 A; h=1-120.
DR PDB; 6YLH; EM; 3.10 A; h=1-120.
DR PDB; 6YLX; EM; 3.90 A; h=1-120.
DR PDB; 6YLY; EM; 3.80 A; h=1-120.
DR PDB; 6Z6J; EM; 3.40 A; Lh=1-120.
DR PDB; 6Z6K; EM; 3.40 A; Lh=1-120.
DR PDB; 7AZY; EM; 2.88 A; D=1-120.
DR PDB; 7B7D; EM; 3.30 A; Ld=2-120.
DR PDB; 7BT6; EM; 3.12 A; h=1-120.
DR PDB; 7BTB; EM; 3.22 A; h=1-120.
DR PDB; 7NRC; EM; 3.90 A; Lj=2-120.
DR PDB; 7NRD; EM; 4.36 A; Lj=2-120.
DR PDB; 7OF1; EM; 3.10 A; h=1-120.
DR PDB; 7OH3; EM; 3.40 A; h=1-120.
DR PDB; 7OHP; EM; 3.90 A; h=1-120.
DR PDB; 7OHQ; EM; 3.10 A; h=1-120.
DR PDB; 7OHR; EM; 4.72 A; h=1-120.
DR PDB; 7OHS; EM; 4.38 A; h=1-120.
DR PDB; 7OHU; EM; 3.70 A; h=1-120.
DR PDB; 7OHV; EM; 3.90 A; h=1-120.
DR PDB; 7OHW; EM; 3.50 A; h=1-120.
DR PDB; 7OHX; EM; 3.30 A; h=1-120.
DR PDB; 7OHY; EM; 3.90 A; h=1-120.
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; 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; P0CX84; -.
DR SMR; P0CX84; -.
DR BioGRID; 31854; 281.
DR BioGRID; 31925; 206.
DR IntAct; P0CX84; 5.
DR MINT; P0CX84; -.
DR STRING; 4932.YDL136W; -.
DR iPTMnet; P0CX84; -.
DR MaxQB; P0CX84; -.
DR PaxDb; P0CX84; -.
DR PRIDE; P0CX84; -.
DR EnsemblFungi; YDL136W_mRNA; YDL136W; YDL136W.
DR EnsemblFungi; YDL191W_mRNA; YDL191W; YDL191W.
DR GeneID; 851336; -.
DR GeneID; 851419; -.
DR KEGG; sce:YDL136W; -.
DR KEGG; sce:YDL191W; -.
DR SGD; S000002350; RPL35A.
DR VEuPathDB; FungiDB:YDL136W; -.
DR VEuPathDB; FungiDB:YDL191W; -.
DR eggNOG; KOG3436; Eukaryota.
DR HOGENOM; CLU_110381_1_1_1; -.
DR InParanoid; P0CX84; -.
DR OMA; VMNQKAR; -.
DR BioCyc; YEAST:G3O-29576-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; P0CX84; -.
DR PRO; PR:P0CX84; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P0CX84; protein.
DR ExpressionAtlas; P0CX84; baseline and differential.
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:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR Gene3D; 1.10.287.310; -; 1.
DR HAMAP; MF_00374; Ribosomal_L29; 1.
DR InterPro; IPR001854; Ribosomal_L29/L35.
DR InterPro; IPR036049; Ribosomal_L29/L35_sf.
DR InterPro; IPR018254; Ribosomal_L29_CS.
DR InterPro; IPR045059; RL35.
DR PANTHER; PTHR45722; PTHR45722; 1.
DR Pfam; PF00831; Ribosomal_L29; 1.
DR SUPFAM; SSF46561; SSF46561; 1.
DR TIGRFAMs; TIGR00012; L29; 1.
DR PROSITE; PS00579; RIBOSOMAL_L29; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11983894"
FT CHAIN 2..120
FT /note="60S ribosomal protein L35-A"
FT /id="PRO_0000130552"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 14..33
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 43..69
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:6EM3"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:6EM3"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:6EM3"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6EM3"
SQ SEQUENCE 120 AA; 13910 MW; D8AC9DF157AD2AD6 CRC64;
MAGVKAYELR TKSKEQLASQ LVDLKKELAE LKVQKLSRPS LPKIKTVRKS IACVLTVINE
QQREAVRQLY KGKKYQPKDL RAKKTRALRR ALTKFEASQV TEKQRKKQIA FPQRKYAIKA
