BFR1_YEAST
ID BFR1_YEAST Reviewed; 470 AA.
AC P38934; D6W2Q7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Nuclear segregation protein BFR1;
DE AltName: Full=Brefeldin A resistance protein 1;
GN Name=BFR1; OrderedLocusNames=YOR198C;
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.
RC STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX PubMed=8070655; DOI=10.1093/genetics/137.2.423;
RA Jackson C.L., Kepes F.;
RT "BFR1, a multicopy suppressor of brefeldin A-induced lethality, is
RT implicated in secretion and nuclear segregation in Saccharomyces
RT cerevisiae.";
RL Genetics 137:423-437(1994).
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 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-336, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=YAL6B;
RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA Jensen O.N.;
RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT pathway.";
RL Mol. Cell. Proteomics 4:310-327(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-336, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-336, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-336 AND SER-369, AND
RP IDENTIFICATION BY 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: Implicated in secretion, nuclear segregation and in
CC maintenance of cell size.
CC -!- DOMAIN: Three regions of the protein are predicted to form a coiled-
CC coil. It may adopt a rod-shaped rather than a globular configuration.
CC -!- MISCELLANEOUS: Present with 33400 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
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DR EMBL; U06870; AAA19589.1; -; Unassigned_DNA.
DR EMBL; Z75106; CAA99411.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10973.1; -; Genomic_DNA.
DR PIR; S47887; S47887.
DR RefSeq; NP_014841.1; NM_001183617.1.
DR AlphaFoldDB; P38934; -.
DR SMR; P38934; -.
DR BioGRID; 34596; 1373.
DR DIP; DIP-4128N; -.
DR IntAct; P38934; 48.
DR MINT; P38934; -.
DR STRING; 4932.YOR198C; -.
DR CarbonylDB; P38934; -.
DR iPTMnet; P38934; -.
DR UCD-2DPAGE; P38934; -.
DR MaxQB; P38934; -.
DR PaxDb; P38934; -.
DR PRIDE; P38934; -.
DR EnsemblFungi; YOR198C_mRNA; YOR198C; YOR198C.
DR GeneID; 854373; -.
DR KEGG; sce:YOR198C; -.
DR SGD; S000005724; BFR1.
DR VEuPathDB; FungiDB:YOR198C; -.
DR eggNOG; ENOG502QRKP; Eukaryota.
DR HOGENOM; CLU_023943_2_0_1; -.
DR InParanoid; P38934; -.
DR OMA; NFRAGVG; -.
DR BioCyc; YEAST:G3O-33706-MON; -.
DR ChiTaRS; BFR1; yeast.
DR PRO; PR:P38934; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P38934; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:SGD.
DR GO; GO:0042175; C:nuclear outer membrane-endoplasmic reticulum membrane network; IDA:SGD.
DR GO; GO:0005844; C:polysome; IDA:SGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IMP:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0008298; P:intracellular mRNA localization; IMP:SGD.
DR GO; GO:0051321; P:meiotic cell cycle; IMP:SGD.
DR GO; GO:0045048; P:protein insertion into ER membrane; IMP:SGD.
DR GO; GO:0035269; P:protein O-linked mannosylation; IMP:SGD.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:SGD.
DR InterPro; IPR039604; Bfr1.
DR PANTHER; PTHR31027; PTHR31027; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Phosphoprotein; Reference proteome.
FT CHAIN 1..470
FT /note="Nuclear segregation protein BFR1"
FT /id="PRO_0000064919"
FT REGION 346..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 17..178
FT /evidence="ECO:0000255"
FT COILED 237..281
FT /evidence="ECO:0000255"
FT COILED 398..469
FT /evidence="ECO:0000255"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 336
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15665377,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 470 AA; 54639 MW; 7F46E360CE3A9BF6 CRC64;
MSSQQHKFKR PDVSVRDKKL DTLNVQLKKI DTEIGLIRKQ IDQHQVNDTT QQERKKLQDK
NKEIIKIQAD LKTRRSNIHD SIKQLDAQIK RKNNQIEEKL GKKAKFSSTA EAKQRINEIE
ESIASGDLSL VQEKLLVKEM QSLNKLIKDL VNIEPIRKSV DADKAKINQL KEELNGLNPK
DVSNQFEENQ QKLNDIHSKT QGVYDKRQTL FNKRAALYKK RDELYSQIRQ IRADFDNEFK
SFRAKLDKER LKREEEQRLS KLLEQKDVDM GKLQEKLTHA KIPAFTYEIG AIENSLLVLD
PTYVKPKKNI LPDLSSNALE TKPARKVVAD DLVLVTPKKD DFVNVAPSKS KKYKKKNQQK
NTENEQPASI FNKVDGKFTL EPTLIATLAE LDVTVPINSD DVKITVEQLK KKHEELLSKQ
EEQTKQNIES VEKEIEKLNL DYSNKEQQVK KELEEKRLKE QEESEKDKEN
