DUF1_YEAST
ID DUF1_YEAST Reviewed; 1116 AA.
AC Q99247; D6W1Y1;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=DUB-associated factor 1 {ECO:0000303|PubMed:21070969};
GN Name=DUF1 {ECO:0000303|PubMed:21070969}; OrderedLocusNames=YOL087C;
GN ORFNames=O0944;
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].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8533473; DOI=10.1002/yea.320111009;
RA Zumstein E., Pearson B.M., Kalogeropoulos A., Schweizer M.;
RT "A 29.425 kb segment on the left arm of yeast chromosome XV contains more
RT than twice as many unknown as known open reading frames.";
RL Yeast 11:975-986(1995).
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 FUNCTION.
RX PubMed=10407277;
RX DOI=10.1002/(sici)1097-0061(199907)15:10b<973::aid-yea402>3.0.co;2-l;
RA Rieger K.-J., El-Alama M., Stein G., Bradshaw C., Slonimski P.P.,
RA Maundrell K.;
RT "Chemotyping of yeast mutants using robotics.";
RL Yeast 15:973-986(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-693, 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-668, 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).
RN [9]
RP UBIQUITIN-BINDING, AND DOMAIN.
RX PubMed=21070969; DOI=10.1016/j.molcel.2010.10.018;
RA Pashkova N., Gakhar L., Winistorfer S.C., Yu L., Ramaswamy S., Piper R.C.;
RT "WD40 repeat propellers define a ubiquitin-binding domain that regulates
RT turnover of F box proteins.";
RL Mol. Cell 40:433-443(2010).
CC -!- FUNCTION: Ubiquitin-binding protein involved in the resistance to
CC phenanthroline, sanguinarine, nordihydroguaiaretic acid (NDGA),
CC isopropyl (N-3-chloro-phenyl)-carbamate (IPCPC) and guanosine 5'-O-(2-
CC thiodiphosphate). {ECO:0000269|PubMed:10407277,
CC ECO:0000303|PubMed:21070969}.
CC -!- SUBUNIT: Interacts (via its WD repeats) with ubiquitin.
CC {ECO:0000269|PubMed:21070969}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- DOMAIN: The N-terminal WD repeats are involved in ubiquitin-binding.
CC {ECO:0000269|PubMed:21070969}.
CC -!- MISCELLANEOUS: Present with 589 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X83121; CAA58192.1; -; Genomic_DNA.
DR EMBL; Z74829; CAA99099.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10697.1; -; Genomic_DNA.
DR PIR; S57382; S57382.
DR RefSeq; NP_014554.1; NM_001183341.1.
DR AlphaFoldDB; Q99247; -.
DR BioGRID; 34315; 121.
DR DIP; DIP-6391N; -.
DR IntAct; Q99247; 29.
DR MINT; Q99247; -.
DR STRING; 4932.YOL087C; -.
DR iPTMnet; Q99247; -.
DR MaxQB; Q99247; -.
DR PaxDb; Q99247; -.
DR PRIDE; Q99247; -.
DR EnsemblFungi; YOL087C_mRNA; YOL087C; YOL087C.
DR GeneID; 854066; -.
DR KEGG; sce:YOL087C; -.
DR SGD; S000005447; DUF1.
DR VEuPathDB; FungiDB:YOL087C; -.
DR eggNOG; KOG0308; Eukaryota.
DR HOGENOM; CLU_297547_0_0_1; -.
DR InParanoid; Q99247; -.
DR OMA; WDIVSCE; -.
DR BioCyc; YEAST:G3O-33488-MON; -.
DR Reactome; R-SCE-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR PRO; PR:Q99247; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q99247; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR021772; WDR48/Bun107.
DR Pfam; PF11816; DUF3337; 1.
DR SMART; SM00320; WD40; 4.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..1116
FT /note="DUB-associated factor 1"
FT /id="PRO_0000235919"
FT REPEAT 21..62
FT /note="WD 1"
FT REPEAT 91..132
FT /note="WD 2"
FT REPEAT 160..200
FT /note="WD 3"
FT REPEAT 219..262
FT /note="WD 4"
FT REPEAT 266..305
FT /note="WD 5"
FT REPEAT 387..426
FT /note="WD 6"
FT REPEAT 428..466
FT /note="WD 7"
FT REGION 578..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..599
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 747..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 668
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 693
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
SQ SEQUENCE 1116 AA; 125382 MW; 0691CFEA2B0D09F6 CRC64;
MNQLTVSYGL ISPDYCTSQD AHILPITKIL YPDIPGKNYF LTSGRDGSII LHKNTQLSNE
PETAATTIKN DAIRMQVHSD WASDLIHVNM KNSDPSAGDT FISVSHDFSI VLISVNAQLT
TWDKKIIGDH DDYIKCIVPI HYEMSNDYEL EEQEGGPDNV HDGINNGIVV DEQNNFLFVT
GGLDRKIKLW CLSSGPEKMA TLLHTFDNAQ SNDTGSIYSM SPIIPKYSFD DNQTSRPFDF
VAGDCNGDLI FYSCKYRKEV IRIQNAHRTN IKVVRTLDDS TRLISTSSDG VINVWDLNCR
HDQTTGALQL PKKIGSWSWD SSIWCVQGTS LDKLYFGDSQ GNVMRANLSS YEDAKLTRIF
KPDHHHHHHH HHEHEEQNIS TTDAKVKKYG GILDIALLPN EKLLFSFCTD SNLNVLDLTN
NHFSVNEGGF ALTRSSLLTN RRHVITENTK GQMQRWDIVS CELLNTFDSS EGSFDDIVMK
YTSKEILSHW CTVSVKVGML FVKINPKFLK TEVYGSALKD YQVVNNIEIN SDERYNLGKI
VINSLFNEFI SYEVQKDKLL RKKIFSLKKK DLTNSLTLDT GYNSESKKNN KDKKRKSTFK
ISSTLSIGNT NSSGTPPNSA PATPVMAETI VLEEQPLLQS ASDKAIDDSL ELVQPLPASK
KPYFRTQSSG SLLSRKFKSF RSTSGRATTG LNTPEEPKGI LPDTPHVIND DSAFPQAINT
TQQSKDATPE SMLWNHPFKL EQKLSAISSQ DLPSNNTHNK LRSSENSRAN STSTLEGNEK
KKPEFMPDLL EQIQESYKQQ YMNTSSLKYL TKRLPVTKII KASSCPIIRV KSATLVLVHL
WKEGSCGGRV LFSTLLPPSH VDNETVSGGK ENSKPPDDEE VDLQAVDDDK LGKYDLIDGE
LGSRLNRRQI FEQLEENLPY WFAKALFRDI KTVEEQPKLN FLIMPWSSVG GSEAAGNENK
KKFISASDTT ESSGNDSSDS SLGNGNEAVS PSTQQQFHNM LKFGRPKTSE QELNPTDLPR
ISEANVKLVA PGMIRVKKIK LYVADRFETK TPEMKAKMEP SLWLDLLCRG QVLDNDMTLN
TVRTLYWKSQ GDIVLEYRRK VHNSPLVHEV NGNEGK
