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RL7B_YEAST
ID   RL7B_YEAST              Reviewed;         244 AA.
AC   Q12213; D6W3H1;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 178.
DE   RecName: Full=60S ribosomal protein L7-B {ECO:0000303|PubMed:9559554};
DE   AltName: Full=L6;
DE   AltName: Full=Large ribosomal subunit protein uL30-B {ECO:0000303|PubMed:24524803};
DE   AltName: Full=RP11;
DE   AltName: Full=YL8;
GN   Name=RPL7B {ECO:0000303|PubMed:9559554}; Synonyms=RPL6B, YL8B;
GN   OrderedLocusNames=YPL198W;
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=A364A / ATCC 22244;
RX   PubMed=8536309; DOI=10.1007/bf00311877;
RA   Mizuta K., Hashimoto T., Otaka E.;
RT   "The evolutionary relationships between homologs of ribosomal YL8 protein
RT   and YL8-like proteins.";
RL   Curr. Genet. 28:19-25(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(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   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   [5]
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   [6]
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   [7]
RP   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   [8]
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).
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) (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: Present with 7080 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- MISCELLANEOUS: There are 2 genes for uL30 in yeast. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uL30 family.
CC       {ECO:0000305}.
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DR   EMBL; D25232; BAA04957.1; -; Genomic_DNA.
DR   EMBL; Z73554; CAA97911.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11237.1; -; Genomic_DNA.
DR   PIR; S55910; S55910.
DR   RefSeq; NP_015126.1; NM_001184012.1.
DR   AlphaFoldDB; Q12213; -.
DR   SMR; Q12213; -.
DR   BioGRID; 35986; 122.
DR   IntAct; Q12213; 108.
DR   MINT; Q12213; -.
DR   STRING; 4932.YPL198W; -.
DR   iPTMnet; Q12213; -.
DR   MaxQB; Q12213; -.
DR   PaxDb; Q12213; -.
DR   PRIDE; Q12213; -.
DR   EnsemblFungi; YPL198W_mRNA; YPL198W; YPL198W.
DR   GeneID; 855903; -.
DR   KEGG; sce:YPL198W; -.
DR   SGD; S000006119; RPL7B.
DR   VEuPathDB; FungiDB:YPL198W; -.
DR   eggNOG; KOG3184; Eukaryota.
DR   GeneTree; ENSGT00950000182878; -.
DR   HOGENOM; CLU_055156_0_2_1; -.
DR   InParanoid; Q12213; -.
DR   OMA; TKKTNHF; -.
DR   BioCyc; YEAST:G3O-34090-MON; -.
DR   PRO; PR:Q12213; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q12213; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0003723; F:RNA 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:0000470; P:maturation of LSU-rRNA; IMP:SGD.
DR   GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central.
DR   GO; GO:0042273; P:ribosomal large subunit biogenesis; IDA:SGD.
DR   CDD; cd01657; Ribosomal_L7_archeal_euk; 1.
DR   Gene3D; 3.30.1390.20; -; 2.
DR   InterPro; IPR036919; L30_ferredoxin-like_sf.
DR   InterPro; IPR018038; Ribosomal_L30_CS.
DR   InterPro; IPR016082; Ribosomal_L30_ferredoxin-like.
DR   InterPro; IPR012988; Ribosomal_L30_N.
DR   InterPro; IPR039699; Ribosomal_L7/L30.
DR   InterPro; IPR005998; Ribosomal_L7_euk.
DR   InterPro; IPR035808; Ribosomal_L7_euk_arc.
DR   PANTHER; PTHR11524; PTHR11524; 1.
DR   Pfam; PF00327; Ribosomal_L30; 1.
DR   Pfam; PF08079; Ribosomal_L30_N; 1.
DR   SUPFAM; SSF55129; SSF55129; 1.
DR   TIGRFAMs; TIGR01310; uL30_euk; 1.
DR   PROSITE; PS00634; RIBOSOMAL_L30; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT   CHAIN           1..244
FT                   /note="60S ribosomal protein L7-B"
FT                   /id="PRO_0000104652"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   244 AA;  27696 MW;  27F8FC0EE61EC266 CRC64;
     MSTEKILTPE SQLKKTKAQQ KTAEQIAAER AARKAANKEK RAIILERNAA YQKEYETAER
     NIIQAKRDAK AAGSYYVEAQ HKLVFVVRIK GINKIPPKPR KVLQLLRLTR INSGTFVKVT
     KATLELLKLI EPYVAYGYPS YSTIRQLVYK RGFGKINKQR VPLSDNAIIE ANLGKYGILS
     IDDLIHEIIT VGPHFKQANN FLWPFKLSNP SGGWGVPRKF KHFIQGGSFG NREEFINKLV
     KAMN
 
 
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