TSR2_YEAST
ID TSR2_YEAST Reviewed; 205 AA.
AC Q06672; D6VZ69;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Pre-rRNA-processing protein TSR2;
DE AltName: Full=20S rRNA accumulation protein 2;
GN Name=TSR2 {ECO:0000312|SGD:S000004427}; OrderedLocusNames=YLR435W;
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] {ECO:0000312|EMBL:AAB67515.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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] {ECO:0000305}
RP INTERACTION WITH RPS26A.
RX PubMed=10688190; DOI=10.1038/35001009;
RA Uetz P., Giot L., Cagney G., Mansfield T.A., Judson R.S., Knight J.R.,
RA Lockshon D., Narayan V., Srinivasan M., Pochart P., Qureshi-Emili A.,
RA Li Y., Godwin B., Conover D., Kalbfleisch T., Vijayadamodar G., Yang M.,
RA Johnston M., Fields S., Rothberg J.M.;
RT "A comprehensive analysis of protein-protein interactions in Saccharomyces
RT cerevisiae.";
RL Nature 403:623-627(2000).
RN [4] {ECO:0000305}
RP FUNCTION, AND INTERACTION WITH RPS26A.
RX PubMed=12837249; DOI=10.1016/s0092-8674(03)00466-5;
RA Peng W.-T., Robinson M.D., Mnaimneh S., Krogan N.J., Cagney G.,
RA Morris Q.D., Davierwala A.P., Grigull J., Yang X., Zhang W., Mitsakakis N.,
RA Ryan O.W., Datta N., Jojic V., Pal C., Canadien V., Richards D.P.,
RA Beattie B., Wu L.F., Altschuler S.J., Roweis S., Frey B.J., Emili A.,
RA Greenblatt J.F., Hughes T.R.;
RT "A panoramic view of yeast noncoding RNA processing.";
RL Cell 113:919-933(2003).
RN [5] {ECO:0000305}
RP IDENTIFICATION OF PROBABLE INITIATION SITE.
RX PubMed=12748633; DOI=10.1038/nature01644;
RA Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT "Sequencing and comparison of yeast species to identify genes and
RT regulatory elements.";
RL Nature 423:241-254(2003).
RN [6] {ECO:0000305}
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 [7] {ECO:0000305}
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).
CC -!- FUNCTION: Required for 20S pre-rRNA processing.
CC {ECO:0000269|PubMed:12837249}.
CC -!- SUBUNIT: Interacts with RPS26A. {ECO:0000269|PubMed:10688190,
CC ECO:0000269|PubMed:12837249}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 13400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the TSR2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB67515.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U21094; AAB67515.1; ALT_INIT; Genomic_DNA.
DR EMBL; BK006945; DAA09735.1; -; Genomic_DNA.
DR PIR; S59404; S59404.
DR RefSeq; NP_013539.4; NM_001182323.3.
DR PDB; 6G03; NMR; -; A=1-152.
DR PDB; 6G04; NMR; -; A=1-152.
DR PDBsum; 6G03; -.
DR PDBsum; 6G04; -.
DR AlphaFoldDB; Q06672; -.
DR SMR; Q06672; -.
DR BioGRID; 31693; 198.
DR DIP; DIP-1584N; -.
DR IntAct; Q06672; 5.
DR MINT; Q06672; -.
DR STRING; 4932.YLR435W; -.
DR iPTMnet; Q06672; -.
DR MaxQB; Q06672; -.
DR PaxDb; Q06672; -.
DR PRIDE; Q06672; -.
DR EnsemblFungi; YLR435W_mRNA; YLR435W; YLR435W.
DR GeneID; 851154; -.
DR KEGG; sce:YLR435W; -.
DR SGD; S000004427; TSR2.
DR VEuPathDB; FungiDB:YLR435W; -.
DR eggNOG; KOG4032; Eukaryota.
DR GeneTree; ENSGT00390000012692; -.
DR HOGENOM; CLU_074896_0_1_1; -.
DR InParanoid; Q06672; -.
DR OMA; IEIMDYT; -.
DR BioCyc; YEAST:G3O-32492-MON; -.
DR PRO; PR:Q06672; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06672; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR InterPro; IPR019398; Pre-rRNA_process_TSR2.
DR PANTHER; PTHR21250; PTHR21250; 1.
DR Pfam; PF10273; WGG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; rRNA processing.
FT CHAIN 1..205
FT /note="Pre-rRNA-processing protein TSR2"
FT /id="PRO_0000076359"
FT REGION 144..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..176
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 4..8
FT /evidence="ECO:0007829|PDB:6G03"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:6G03"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:6G03"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:6G03"
FT HELIX 26..40
FT /evidence="ECO:0007829|PDB:6G03"
FT HELIX 44..51
FT /evidence="ECO:0007829|PDB:6G03"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:6G04"
FT HELIX 59..66
FT /evidence="ECO:0007829|PDB:6G03"
FT HELIX 68..71
FT /evidence="ECO:0007829|PDB:6G03"
FT TURN 72..76
FT /evidence="ECO:0007829|PDB:6G03"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:6G03"
FT HELIX 82..97
FT /evidence="ECO:0007829|PDB:6G03"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:6G03"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:6G04"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:6G03"
FT HELIX 136..140
FT /evidence="ECO:0007829|PDB:6G03"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:6G03"
SQ SEQUENCE 205 AA; 23713 MW; DF78941D3608EFCB CRC64;
MSTQYIDETA FVQAEQGKTN LMFSDEKQQA RFELGVSMVI YKWDALDVAV ENSWGGPDSA
EKRDWITGIV VDLFKNEKVV DAALIEETLL YAMIDEFETN VEDDSALPIA VEVINIYNDC
FNLNYNKVEK LYLEWQEKQR TKKSKRVVHI EGDDDEDDED VEDYDDEDED EEMDEVVPDL
VSSKPEPIVD EDGFELVQPK GRRKH
