DENR_YEAST
ID DENR_YEAST Reviewed; 198 AA.
AC P47089; D6VWJ0;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Translation machinery-associated protein 22;
DE AltName: Full=Density-regulated protein homolog;
GN Name=TMA22; Synonyms=RBF22; OrderedLocusNames=YJR014W;
GN ORFNames=J1446, YJR83.12;
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=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP DOMAIN.
RX PubMed=10093218; DOI=10.1007/pl00006472;
RA Aravind L., Koonin E.V.;
RT "Novel predicted RNA-binding domains associated with the translation
RT machinery.";
RL J. Mol. Evol. 48:291-302(1999).
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBUNIT.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
RN [8]
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).
CC -!- SUBUNIT: Interacts with the 40S ribosomal subunit.
CC {ECO:0000269|PubMed:16702403}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The SUI1 domain may be involved in RNA binding.
CC {ECO:0000269|PubMed:10093218}.
CC -!- MISCELLANEOUS: Present with 21600 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the DENR family. {ECO:0000305}.
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DR EMBL; Z49514; CAA89538.1; -; Genomic_DNA.
DR EMBL; X87611; CAA60937.1; -; Genomic_DNA.
DR EMBL; AY557898; AAS56224.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08806.1; -; Genomic_DNA.
DR PIR; S55203; S55203.
DR RefSeq; NP_012548.1; NM_001181672.1.
DR AlphaFoldDB; P47089; -.
DR SMR; P47089; -.
DR BioGRID; 33770; 174.
DR DIP; DIP-6768N; -.
DR IntAct; P47089; 10.
DR MINT; P47089; -.
DR STRING; 4932.YJR014W; -.
DR iPTMnet; P47089; -.
DR MaxQB; P47089; -.
DR PaxDb; P47089; -.
DR PRIDE; P47089; -.
DR EnsemblFungi; YJR014W_mRNA; YJR014W; YJR014W.
DR GeneID; 853471; -.
DR KEGG; sce:YJR014W; -.
DR SGD; S000003775; TMA22.
DR VEuPathDB; FungiDB:YJR014W; -.
DR eggNOG; KOG3239; Eukaryota.
DR GeneTree; ENSGT00390000014349; -.
DR HOGENOM; CLU_073511_0_1_1; -.
DR InParanoid; P47089; -.
DR OMA; VIYCGVC; -.
DR BioCyc; YEAST:G3O-31659-MON; -.
DR PRO; PR:P47089; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P47089; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; ISS:SGD.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central.
DR GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
DR InterPro; IPR005873; DENR_eukaryotes.
DR InterPro; IPR001950; SUI1.
DR InterPro; IPR036877; SUI1_dom_sf.
DR Pfam; PF01253; SUI1; 1.
DR SUPFAM; SSF55159; SSF55159; 1.
DR TIGRFAMs; TIGR01159; DRP1; 1.
DR PROSITE; PS50296; SUI1; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..198
FT /note="Translation machinery-associated protein 22"
FT /id="PRO_0000130609"
FT DOMAIN 99..170
FT /note="SUI1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00200"
SQ SEQUENCE 198 AA; 22495 MW; 778A38A6BD28E40C CRC64;
MLREVIYCGI CSYPPEYCEF SGKLKRCKVW LSENHADLYA KLYGTDDNTQ EVEAVTNKLA
ESSIGEAREE KLEKDLLKIQ KKQENREQRE LAKKLSSKVI IKREARTKRK FIVAISGLEV
FDIDMKKLAK TFASRFATGC SVSKNAEKKE EVVIQGDVMD EVETYIHSLL EEKGLKDVKV
ETIDAKKKKK PAAEGAAK
