BRX1_YEAST
ID BRX1_YEAST Reviewed; 291 AA.
AC Q08235; D6W1Z1;
DT 09-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Ribosome biogenesis protein BRX1;
GN Name=BRX1; OrderedLocusNames=YOL077C;
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=9178509;
RX DOI=10.1002/(sici)1097-0061(199705)13:6<583::aid-yea111>3.0.co;2-y;
RA Tzermia M., Katsoulou C., Alexandraki D.;
RT "Sequence analysis of a 33.2 kb segment from the left arm of yeast
RT chromosome XV reveals eight known genes and ten new open reading frames
RT including homologues of ABC transporters, inositol phosphatases and human
RT expressed sequence tags.";
RL Yeast 13:583-589(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, AND SEQUENCE REVISION TO 161.
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11843177; DOI=10.1515/bc.2001.199;
RA Kaser A., Bogengruber E., Hallegger M., Doppler E., Lepperdinger G.,
RA Jantsch M., Breitenbach M., Kreil G.;
RT "Brix from Xenopus laevis and brx1p from yeast define a new family of
RT proteins involved in the biogenesis of large ribosomal subunits.";
RL Biol. Chem. 382:1637-1647(2001).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Required for biogenesis of the 60S ribosomal subunit.
CC {ECO:0000269|PubMed:11843177}.
CC -!- SUBUNIT: Part of a complex that includes BRX1, RPF1, RPF2 and SSF1 or
CC SSF2.
CC -!- INTERACTION:
CC Q08235; P36049: EBP2; NbExp=5; IntAct=EBI-3775, EBI-6289;
CC Q08235; P43586: LOC1; NbExp=3; IntAct=EBI-3775, EBI-22906;
CC Q08235; P39744: NOC2; NbExp=4; IntAct=EBI-3775, EBI-29259;
CC Q08235; P21304: PWP1; NbExp=3; IntAct=EBI-3775, EBI-14328;
CC Q08235; Q05022: RRP5; NbExp=3; IntAct=EBI-3775, EBI-16011;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11843177,
CC ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 13200 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the BRX1 family. {ECO:0000305}.
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DR EMBL; Z74819; CAA99087.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10707.2; -; Genomic_DNA.
DR PIR; S66770; S66770.
DR RefSeq; NP_014565.2; NM_001183331.2.
DR PDB; 5Z1G; X-ray; 2.29 A; B/D=26-259.
DR PDB; 5Z3G; EM; 3.65 A; a=1-291.
DR PDB; 6C0F; EM; 3.70 A; b=1-291.
DR PDB; 6CB1; EM; 4.60 A; b=1-291.
DR PDB; 6ELZ; EM; 3.30 A; A=1-291.
DR PDB; 6EM1; EM; 3.60 A; A=1-291.
DR PDB; 6EM3; EM; 3.20 A; A=1-291.
DR PDB; 6EM4; EM; 4.10 A; A=1-291.
DR PDB; 6EM5; EM; 4.30 A; A=1-291.
DR PDB; 7OHR; EM; 4.72 A; A=1-291.
DR PDB; 7OHS; EM; 4.38 A; A=1-291.
DR PDB; 7OHV; EM; 3.90 A; A=1-291.
DR PDB; 7OHW; EM; 3.50 A; A=1-291.
DR PDBsum; 5Z1G; -.
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; 7OHR; -.
DR PDBsum; 7OHS; -.
DR PDBsum; 7OHV; -.
DR PDBsum; 7OHW; -.
DR AlphaFoldDB; Q08235; -.
DR SMR; Q08235; -.
DR BioGRID; 34325; 307.
DR DIP; DIP-6317N; -.
DR IntAct; Q08235; 74.
DR MINT; Q08235; -.
DR STRING; 4932.YOL077C; -.
DR iPTMnet; Q08235; -.
DR MaxQB; Q08235; -.
DR PaxDb; Q08235; -.
DR PRIDE; Q08235; -.
DR EnsemblFungi; YOL077C_mRNA; YOL077C; YOL077C.
DR GeneID; 854078; -.
DR KEGG; sce:YOL077C; -.
DR SGD; S000005437; BRX1.
DR VEuPathDB; FungiDB:YOL077C; -.
DR eggNOG; KOG2971; Eukaryota.
DR GeneTree; ENSGT00390000014467; -.
DR HOGENOM; CLU_048373_2_1_1; -.
DR InParanoid; Q08235; -.
DR OMA; GPTVKMH; -.
DR BioCyc; YEAST:G3O-33481-MON; -.
DR PRO; PR:Q08235; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08235; protein.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0030687; C:preribosome, large subunit precursor; IDA:SGD.
DR GO; GO:0008097; F:5S rRNA binding; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0042134; F:rRNA primary transcript binding; IDA:SGD.
DR GO; GO:0000464; P:endonucleolytic cleavage in ITS1 upstream of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000465; P:exonucleolytic trimming to generate mature 5'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR InterPro; IPR007109; Brix.
DR InterPro; IPR026532; BRX1.
DR PANTHER; PTHR13634; PTHR13634; 1.
DR Pfam; PF04427; Brix; 1.
DR SMART; SM00879; Brix; 1.
DR PROSITE; PS50833; BRIX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome;
KW Ribosome biogenesis.
FT CHAIN 1..291
FT /note="Ribosome biogenesis protein BRX1"
FT /id="PRO_0000120235"
FT DOMAIN 31..232
FT /note="Brix"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00034"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT CONFLICT 161
FT /note="G -> C (in Ref. 1 and 2; CAA99087)"
FT /evidence="ECO:0000305"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:5Z1G"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:5Z1G"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:5Z1G"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:5Z1G"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:5Z1G"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:5Z1G"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:5Z1G"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:5Z1G"
FT STRAND 109..118
FT /evidence="ECO:0007829|PDB:5Z1G"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:5Z1G"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:5Z1G"
FT HELIX 147..160
FT /evidence="ECO:0007829|PDB:5Z1G"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:5Z1G"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:5Z1G"
FT STRAND 185..194
FT /evidence="ECO:0007829|PDB:5Z1G"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:5Z1G"
FT STRAND 218..231
FT /evidence="ECO:0007829|PDB:5Z1G"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:5Z1G"
FT HELIX 245..253
FT /evidence="ECO:0007829|PDB:5Z1G"
SQ SEQUENCE 291 AA; 33531 MW; 31466853EF0E7301 CRC64;
MSSIYKALAG KSKDNKSEKK QGNVKQFMNK QRTLLISSRG VNYRHRHLIQ DLSGLLPHSR
KEPKLDTKKD LQQLNEIAEL YNCNNVLFFE ARKHQDLYLW LSKPPNGPTI KFYIQNLHTM
DELNFTGNCL KGSRPVLSFD QRFESSPHYQ LIKELLVHNF GVPPNARKSK PFIDHVMSFS
IVDDKIWVRT YEISHSTKNK EEYEDGEEDI SLVEIGPRFV MTVILILEGS FGGPKIYENK
QYVSPNVVRA QIKQQAAEEA KSRAEAAVER KIKRRENVLA ADPLSNDALF K
