DSF2_YEAST
ID DSF2_YEAST Reviewed; 736 AA.
AC P38213; D6VQ08;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Protein DSF2;
DE AltName: Full=Deletion suppressor of MPT5 mutation protein 2;
GN Name=DSF2; OrderedLocusNames=YBR007C; ORFNames=YBR0113;
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=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 205 AND 327.
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 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 [4]
RP DISRUPTION PHENOTYPE.
RX PubMed=16328373; DOI=10.1007/s00438-005-0064-x;
RA Ohkuni K., Kikuchi Y., Hara K., Taneda T., Hayashi N., Kikuchi A.;
RT "Suppressor analysis of the mpt5/htr1/uth4/puf5 deletion in Saccharomyces
RT cerevisiae.";
RL Mol. Genet. Genomics 275:81-88(2006).
RN [5]
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).
RN [6]
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 -!- DISRUPTION PHENOTYPE: Rescues temperature-sensitivity of MPT5 deletion.
CC Partially suppresses the hydroxyurea (HU) sensitivity of MPT5 deletion.
CC {ECO:0000269|PubMed:16328373}.
CC -!- MISCELLANEOUS: Present with 377 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z35876; CAA84944.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07128.2; -; Genomic_DNA.
DR PIR; S45859; S45859.
DR RefSeq; NP_009561.2; NM_001178355.2.
DR AlphaFoldDB; P38213; -.
DR SMR; P38213; -.
DR BioGRID; 32708; 49.
DR IntAct; P38213; 9.
DR MINT; P38213; -.
DR STRING; 4932.YBR007C; -.
DR iPTMnet; P38213; -.
DR MaxQB; P38213; -.
DR PaxDb; P38213; -.
DR PRIDE; P38213; -.
DR EnsemblFungi; YBR007C_mRNA; YBR007C; YBR007C.
DR GeneID; 852292; -.
DR KEGG; sce:YBR007C; -.
DR SGD; S000000211; DSF2.
DR VEuPathDB; FungiDB:YBR007C; -.
DR eggNOG; ENOG502QW3C; Eukaryota.
DR HOGENOM; CLU_364101_0_0_1; -.
DR InParanoid; P38213; -.
DR OMA; CLSGTIW; -.
DR BioCyc; YEAST:G3O-28994-MON; -.
DR PRO; PR:P38213; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38213; protein.
DR GO; GO:0005934; C:cellular bud tip; HDA:SGD.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR SMART; SM00671; SEL1; 1.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..736
FT /note="Protein DSF2"
FT /id="PRO_0000202467"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..381
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 205
FT /note="S -> R (in Ref. 1; CAA84944)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="P -> T (in Ref. 1; CAA84944)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 736 AA; 82336 MW; 1238CEB4AA38EA52 CRC64;
MNQNLKNTSW ADRIGSDDQE RKANSSEVSQ SPPPNNSFES SMDSQFSYAH SNKSSISFES
IQTTERLLDK LDLSLEDELI LQEALLEEEN ASRNSQLSQT SGPTLCMPAS EFPSLRYRTN
PSPTYIQARD RSLIIDNLKE KDSTLRGKYS SGKVERHLPV KSRYSYIVEE DYDSETFSGM
KPQMNRNEKD YKYPNLENGN RSTNSPNPFN FEKYRIENTR LHHLYPTLIS DNNTSVDNNA
NSKNNRTTSN NINTSTKTDR ISEKQSCPNE FTTTQKSNCL YRNGSSTSTN TSFSEVGQLS
KPKTQSSFES ESSSFSKLKL TKSDTTPIKP SPKRSNSSTS TITKTNTMTN DISLPPTPPY
KAHKKKTSLN SLKKLFKSPR TRAKNKKDLE SEGSSPIRSA TNSLDFSGEN IQLPSTSSTI
NNSSPHLARY IFPPNPVFHF KTASTPQSST DKKKNSKARP NRTHLRTFSD FHTTEKDSKI
GELSALTEQS NKPYHPKVRR RTLSLDGMLP NNSTQCMDSF SHKKEGSNAT SKCGKLKFHP
EPYDNDESSH IGQAITMRHQ GKLEESAQRL KKACACGNKT AFLLYGLALR HGCGVDKNLK
LSLGYLMAAT DIKSFAAEVL DLDINPLNFA SMDDIPDIAP EPTAPALYEC GMAYLKGLGM
DHPDERKGLK FLEKAALLGH VDSMCLSGTI WSKTSNVKKR DLARAAAWFR IADKKGANLL
GSDWIYKEKY MKQGPK
