RS7A_YEAST
ID RS7A_YEAST Reviewed; 190 AA.
AC P26786; D6W2F7; Q08502;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=40S ribosomal protein S7-A {ECO:0000303|PubMed:9559554};
DE AltName: Full=RP30;
DE AltName: Full=RP40;
DE AltName: Full=Small ribosomal subunit protein eS7-A {ECO:0000303|PubMed:24524803};
GN Name=RPS7A {ECO:0000303|PubMed:9559554}; Synonyms=RPS30;
GN OrderedLocusNames=YOR096W; ORFNames=YOR3177W;
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].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-26, AND ACETYLATION AT SER-2 BY NATA.
RX PubMed=1544921; DOI=10.1016/s0021-9258(18)42785-8;
RA Takakura H., Tsunasawa S., Miyagi M., Warner J.R.;
RT "NH2-terminal acetylation of ribosomal proteins of Saccharomyces
RT cerevisiae.";
RL J. Biol. Chem. 267:5442-5445(1992).
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, AND ACETYLATION AT SER-2 BY NATA.
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 LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP FUNCTION, INTERACTION WITH MPP10 AND SNORNA U3, IDENTIFICATION IN SSU
RP PROCESSOME, AND SUBCELLULAR LOCATION.
RX PubMed=15590835; DOI=10.1128/ec.3.6.1619-1626.2004;
RA Bernstein K.A., Gallagher J.E.G., Mitchell B.M., Granneman S.,
RA Baserga S.J.;
RT "The small-subunit processome is a ribosome assembly intermediate.";
RL Eukaryot. Cell 3:1619-1626(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [11]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-124, AND IDENTIFICATION BY
RP MASS 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 [12]
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 [13]
RP X-RAY CRYSTALLOGRAPHY (3.00 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 (PubMed:22096102). eS7 is involved in nucleolar processing of
CC pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835).
CC {ECO:0000269|PubMed:15590835, ECO:0000305|PubMed:22096102}.
CC -!- SUBUNIT: Component of the small ribosomal subunit (SSU). 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) (PubMed:9559554, PubMed:22096102).
CC Interacts with snoRNA U3. uS11 interacts with MPP10. Component of the
CC ribosomal small subunit (SSU) processome composed of at least 40
CC protein subunits and snoRNA U3 (PubMed:15590835).
CC {ECO:0000269|PubMed:15590835, ECO:0000269|PubMed:22096102,
CC ECO:0000305|PubMed:9559554}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus,
CC nucleolus {ECO:0000269|PubMed:15590835}.
CC -!- PTM: N-terminally acetylated by acetyltransferase NatA.
CC {ECO:0000269|PubMed:10601260, ECO:0000269|PubMed:1544921}.
CC -!- MISCELLANEOUS: Present with 41000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- MISCELLANEOUS: There are 2 genes for eS7 in yeast. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS7 family.
CC {ECO:0000305}.
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DR EMBL; X94335; CAA64018.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z75004; CAA99293.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10873.1; -; Genomic_DNA.
DR PIR; S66981; S66981.
DR RefSeq; NP_014739.1; NM_001183515.1.
DR PDB; 3J6X; EM; 6.10 A; S7=1-190.
DR PDB; 3J6Y; EM; 6.10 A; S7=1-190.
DR PDB; 3J77; EM; 6.20 A; S7=1-190.
DR PDB; 3J78; EM; 6.30 A; S7=1-190.
DR PDB; 4U3M; X-ray; 3.00 A; S7/s7=2-190.
DR PDB; 4U3N; X-ray; 3.20 A; S7/s7=2-190.
DR PDB; 4U3U; X-ray; 2.90 A; S7/s7=2-190.
DR PDB; 4U4N; X-ray; 3.10 A; S7/s7=2-190.
DR PDB; 4U4O; X-ray; 3.60 A; S7/s7=2-190.
DR PDB; 4U4Q; X-ray; 3.00 A; S7/s7=2-190.
DR PDB; 4U4R; X-ray; 2.80 A; S7/s7=2-190.
DR PDB; 4U4U; X-ray; 3.00 A; S7/s7=2-190.
DR PDB; 4U4Y; X-ray; 3.20 A; S7/s7=2-190.
DR PDB; 4U4Z; X-ray; 3.10 A; S7/s7=2-190.
DR PDB; 4U50; X-ray; 3.20 A; S7/s7=2-190.
DR PDB; 4U51; X-ray; 3.20 A; S7/s7=2-190.
DR PDB; 4U52; X-ray; 3.00 A; S7/s7=2-190.
DR PDB; 4U53; X-ray; 3.30 A; S7/s7=2-190.
DR PDB; 4U55; X-ray; 3.20 A; S7/s7=2-190.
DR PDB; 4U56; X-ray; 3.45 A; S7/s7=2-190.
DR PDB; 4U6F; X-ray; 3.10 A; S7/s7=2-190.
DR PDB; 4V88; X-ray; 3.00 A; AH/CH=1-190.
DR PDB; 4V8Y; EM; 4.30 A; AH=1-190.
DR PDB; 4V8Z; EM; 6.60 A; AH=1-190.
DR PDB; 4V92; EM; 3.70 A; H=4-187.
DR PDB; 5DAT; X-ray; 3.15 A; S7/s7=2-190.
DR PDB; 5DC3; X-ray; 3.25 A; S7/s7=2-190.
DR PDB; 5DGE; X-ray; 3.45 A; S7/s7=2-190.
DR PDB; 5DGF; X-ray; 3.30 A; S7/s7=2-190.
DR PDB; 5DGV; X-ray; 3.10 A; S7/s7=2-190.
DR PDB; 5FCI; X-ray; 3.40 A; S7/s7=2-190.
DR PDB; 5FCJ; X-ray; 3.10 A; S7/s7=2-190.
DR PDB; 5I4L; X-ray; 3.10 A; S7/s7=2-187.
DR PDB; 5JUO; EM; 4.00 A; EB=1-190.
DR PDB; 5JUP; EM; 3.50 A; EB=1-190.
DR PDB; 5JUS; EM; 4.20 A; EB=1-190.
DR PDB; 5JUT; EM; 4.00 A; EB=1-190.
DR PDB; 5JUU; EM; 4.00 A; EB=1-190.
DR PDB; 5LL6; EM; 3.90 A; U=1-190.
DR PDB; 5LYB; X-ray; 3.25 A; S7/s7=2-187.
DR PDB; 5M1J; EM; 3.30 A; H2=4-187.
DR PDB; 5MC6; EM; 3.80 A; U=1-190.
DR PDB; 5MEI; X-ray; 3.50 A; I/s7=2-187.
DR PDB; 5NDG; X-ray; 3.70 A; S7/s7=3-187.
DR PDB; 5NDV; X-ray; 3.30 A; S7/s7=2-187.
DR PDB; 5NDW; X-ray; 3.70 A; S7/s7=4-187.
DR PDB; 5OBM; X-ray; 3.40 A; S7/s7=2-187.
DR PDB; 5ON6; X-ray; 3.10 A; I/s7=2-187.
DR PDB; 5TBW; X-ray; 3.00 A; I/s7=2-187.
DR PDB; 5TGA; X-ray; 3.30 A; S7/s7=2-187.
DR PDB; 5TGM; X-ray; 3.50 A; S7/s7=2-187.
DR PDB; 5TZS; EM; 5.10 A; 7=1-190.
DR PDB; 5WLC; EM; 3.80 A; L7=1-190.
DR PDB; 5WYJ; EM; 8.70 A; SI=1-190.
DR PDB; 5WYK; EM; 4.50 A; SI=1-190.
DR PDB; 6EML; EM; 3.60 A; U=1-190.
DR PDB; 6FAI; EM; 3.40 A; H=1-190.
DR PDB; 6GQ1; EM; 4.40 A; x=4-187.
DR PDB; 6GQB; EM; 3.90 A; x=4-187.
DR PDB; 6GQV; EM; 4.00 A; x=4-187.
DR PDB; 6HHQ; X-ray; 3.10 A; I/s7=1-190.
DR PDB; 6I7O; EM; 5.30 A; U/Ub=3-187.
DR PDB; 6KE6; EM; 3.40 A; SI=1-190.
DR PDB; 6LQP; EM; 3.20 A; SI=1-190.
DR PDB; 6LQQ; EM; 4.10 A; SI=1-190.
DR PDB; 6LQR; EM; 8.60 A; SI=1-190.
DR PDB; 6LQS; EM; 3.80 A; SI=1-190.
DR PDB; 6LQT; EM; 4.90 A; SI=1-190.
DR PDB; 6LQU; EM; 3.70 A; SI=1-190.
DR PDB; 6Q8Y; EM; 3.10 A; U=4-187.
DR PDB; 6RBD; EM; 3.47 A; H=1-190.
DR PDB; 6RBE; EM; 3.80 A; H=1-190.
DR PDB; 6S47; EM; 3.28 A; BI=2-190.
DR PDB; 6SNT; EM; 2.80 A; H=1-190.
DR PDB; 6SV4; EM; 3.30 A; U/Ub/Uc=1-190.
DR PDB; 6T4Q; EM; 2.60 A; SH=4-187.
DR PDB; 6T7I; EM; 3.20 A; SH=1-190.
DR PDB; 6T7T; EM; 3.10 A; SH=1-190.
DR PDB; 6T83; EM; 4.00 A; Hb/i=1-190.
DR PDB; 6TB3; EM; 2.80 A; U=4-187.
DR PDB; 6TNU; EM; 3.10 A; U=4-187.
DR PDB; 6WDR; EM; 3.70 A; H=4-187.
DR PDB; 6WOO; EM; 2.90 A; HH=4-187.
DR PDB; 6XIQ; EM; 4.20 A; x=1-190.
DR PDB; 6XIR; EM; 3.20 A; x=1-190.
DR PDB; 6Y7C; EM; 3.80 A; H=1-190.
DR PDB; 6Z6J; EM; 3.40 A; SH=1-190.
DR PDB; 6Z6K; EM; 3.40 A; SH=1-190.
DR PDB; 6ZCE; EM; 5.30 A; I=1-190.
DR PDB; 6ZQA; EM; 4.40 A; DH=1-190.
DR PDB; 6ZQB; EM; 3.90 A; DH=1-190.
DR PDB; 6ZQC; EM; 3.80 A; DH=1-190.
DR PDB; 6ZQD; EM; 3.80 A; DH=1-190.
DR PDB; 6ZQE; EM; 7.10 A; DH=1-190.
DR PDB; 6ZQF; EM; 4.90 A; DH=1-190.
DR PDB; 6ZQG; EM; 3.50 A; DH=1-190.
DR PDB; 6ZU9; EM; 6.20 A; U=1-190.
DR PDB; 6ZVI; EM; 3.00 A; p=3-187.
DR PDB; 7A1G; EM; 3.00 A; U=4-187.
DR PDB; 7AJT; EM; 4.60 A; DH=1-190.
DR PDB; 7AJU; EM; 3.80 A; DH=1-190.
DR PDB; 7B7D; EM; 3.30 A; U=4-187.
DR PDB; 7D4I; EM; 4.00 A; SI=1-190.
DR PDB; 7D5T; EM; 6.00 A; SI=1-190.
DR PDB; 7D63; EM; 12.30 A; SI=1-190.
DR PDB; 7NRC; EM; 3.90 A; SU=4-187.
DR PDB; 7NRD; EM; 4.36 A; SU=3-187.
DR PDBsum; 3J6X; -.
DR PDBsum; 3J6Y; -.
DR PDBsum; 3J77; -.
DR PDBsum; 3J78; -.
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; 4V88; -.
DR PDBsum; 4V8Y; -.
DR PDBsum; 4V8Z; -.
DR PDBsum; 4V92; -.
DR PDBsum; 5DAT; -.
DR PDBsum; 5DC3; -.
DR PDBsum; 5DGE; -.
DR PDBsum; 5DGF; -.
DR PDBsum; 5DGV; -.
DR PDBsum; 5FCI; -.
DR PDBsum; 5FCJ; -.
DR PDBsum; 5I4L; -.
DR PDBsum; 5JUO; -.
DR PDBsum; 5JUP; -.
DR PDBsum; 5JUS; -.
DR PDBsum; 5JUT; -.
DR PDBsum; 5JUU; -.
DR PDBsum; 5LL6; -.
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; 5TBW; -.
DR PDBsum; 5TGA; -.
DR PDBsum; 5TGM; -.
DR PDBsum; 5TZS; -.
DR PDBsum; 5WLC; -.
DR PDBsum; 5WYJ; -.
DR PDBsum; 5WYK; -.
DR PDBsum; 6EML; -.
DR PDBsum; 6FAI; -.
DR PDBsum; 6GQ1; -.
DR PDBsum; 6GQB; -.
DR PDBsum; 6GQV; -.
DR PDBsum; 6HHQ; -.
DR PDBsum; 6I7O; -.
DR PDBsum; 6KE6; -.
DR PDBsum; 6LQP; -.
DR PDBsum; 6LQQ; -.
DR PDBsum; 6LQR; -.
DR PDBsum; 6LQS; -.
DR PDBsum; 6LQT; -.
DR PDBsum; 6LQU; -.
DR PDBsum; 6Q8Y; -.
DR PDBsum; 6RBD; -.
DR PDBsum; 6RBE; -.
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; 6WDR; -.
DR PDBsum; 6WOO; -.
DR PDBsum; 6XIQ; -.
DR PDBsum; 6XIR; -.
DR PDBsum; 6Y7C; -.
DR PDBsum; 6Z6J; -.
DR PDBsum; 6Z6K; -.
DR PDBsum; 6ZCE; -.
DR PDBsum; 6ZQA; -.
DR PDBsum; 6ZQB; -.
DR PDBsum; 6ZQC; -.
DR PDBsum; 6ZQD; -.
DR PDBsum; 6ZQE; -.
DR PDBsum; 6ZQF; -.
DR PDBsum; 6ZQG; -.
DR PDBsum; 6ZU9; -.
DR PDBsum; 6ZVI; -.
DR PDBsum; 7A1G; -.
DR PDBsum; 7AJT; -.
DR PDBsum; 7AJU; -.
DR PDBsum; 7B7D; -.
DR PDBsum; 7D4I; -.
DR PDBsum; 7D5T; -.
DR PDBsum; 7D63; -.
DR PDBsum; 7NRC; -.
DR PDBsum; 7NRD; -.
DR AlphaFoldDB; P26786; -.
DR SMR; P26786; -.
DR BioGRID; 34494; 635.
DR DIP; DIP-2592N; -.
DR IntAct; P26786; 66.
DR MINT; P26786; -.
DR STRING; 4932.YOR096W; -.
DR iPTMnet; P26786; -.
DR MaxQB; P26786; -.
DR PaxDb; P26786; -.
DR PRIDE; P26786; -.
DR TopDownProteomics; P26786; -.
DR EnsemblFungi; YOR096W_mRNA; YOR096W; YOR096W.
DR GeneID; 854263; -.
DR KEGG; sce:YOR096W; -.
DR SGD; S000005622; RPS7A.
DR VEuPathDB; FungiDB:YOR096W; -.
DR eggNOG; KOG3320; Eukaryota.
DR GeneTree; ENSGT00390000014122; -.
DR HOGENOM; CLU_088621_1_2_1; -.
DR InParanoid; P26786; -.
DR OMA; AAYHKVQ; -.
DR BioCyc; YEAST:G3O-33629-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-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
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 PRO; PR:P26786; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P26786; protein.
DR GO; GO:0030686; C:90S preribosome; HDA:SGD.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:SGD.
DR GO; GO:0002181; P:cytoplasmic translation; NAS:SGD.
DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IBA:GO_Central.
DR GO; GO:0042254; P:ribosome biogenesis; IGI:SGD.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR InterPro; IPR000554; Ribosomal_S7e.
DR PANTHER; PTHR11278; PTHR11278; 1.
DR Pfam; PF01251; Ribosomal_S7e; 1.
DR PROSITE; PS00948; RIBOSOMAL_S7E; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Nucleus; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Ribosome biogenesis; rRNA processing; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:1544921"
FT CHAIN 2..190
FT /note="40S ribosomal protein S7-A"
FT /id="PRO_0000174212"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:10601260,
FT ECO:0000269|PubMed:1544921"
FT CROSSLNK 124
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 24
FT /note="F -> E (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 4..8
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 9..12
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 15..28
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 56..62
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:6FAI"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:6ZVI"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:6FAI"
FT STRAND 135..142
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:6RBD"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:6ZVI"
FT HELIX 166..177
FT /evidence="ECO:0007829|PDB:6ZVI"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:6ZVI"
SQ SEQUENCE 190 AA; 21622 MW; 0096C3D7B6A196A3 CRC64;
MSAPQAKILS QAPTELELQV AQAFVELENS SPELKAELRP LQFKSIREID VAGGKKALAI
FVPVPSLAGF HKVQTKLTRE LEKKFQDRHV IFLAERRILP KPSRTSRQVQ KRPRSRTLTA
VHDKILEDLV FPTEIVGKRV RYLVGGNKIQ KVLLDSKDVQ QIDYKLESFQ AVYNKLTGKQ
IVFEIPSETH
