UFO1_YEAST
ID UFO1_YEAST Reviewed; 668 AA.
AC Q04511; D6W0J5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Ubiquitin ligase complex F-box protein UFO1;
GN Name=UFO1; OrderedLocusNames=YML088W;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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]
RP FUNCTION IN HO DEGRADATION.
RX PubMed=10963670; DOI=10.1073/pnas.97.18.10077;
RA Kaplun L., Ivantsiv Y., Kornitzer D., Raveh D.;
RT "Functions of the DNA damage response pathway target Ho endonuclease of
RT yeast for degradation via the ubiquitin-26S proteasome system.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10077-10082(2000).
RN [4]
RP INTERACTION WITH SKP1.
RX PubMed=11283612; DOI=10.1038/35070067;
RA Seol J.H., Shevchenko A., Shevchenko A., Deshaies R.J.;
RT "Skp1 forms multiple protein complexes, including RAVE, a regulator of V-
RT ATPase assembly.";
RL Nat. Cell Biol. 3:384-391(2001).
RN [5]
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 [6]
RP INTERACTION WITH SKP1, AND RECONSTITUTION OF THE SCF(UFO1) COMPLEX.
RX PubMed=14747994; DOI=10.1002/prot.10620;
RA Kus B.M., Caldon C.E., Andorn-Broza R., Edwards A.M.;
RT "Functional interaction of 13 yeast SCF complexes with a set of yeast E2
RT enzymes in vitro.";
RL Proteins 54:455-467(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-514, 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-511 AND THR-514, 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: Substrate recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex which mediates the
CC ubiquitination and subsequent proteasomal degradation of target
CC proteins. Probably recognizes and binds to phosphorylated target
CC proteins (By similarity). {ECO:0000250, ECO:0000269|PubMed:10963670}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with SKP1. Component of the probable SCF(UFO1)
CC complex containing CDC53, SKP1, RBX1 and UFO1.
CC {ECO:0000269|PubMed:11283612, ECO:0000269|PubMed:14747994}.
CC -!- INTERACTION:
CC Q04511; P52286: SKP1; NbExp=6; IntAct=EBI-20020, EBI-4090;
CC -!- MISCELLANEOUS: Present with 639 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z46660; CAA86650.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09809.1; -; Genomic_DNA.
DR PIR; S49639; S49639.
DR RefSeq; NP_013622.1; NM_001182447.1.
DR AlphaFoldDB; Q04511; -.
DR SMR; Q04511; -.
DR BioGRID; 35053; 190.
DR ComplexPortal; CPX-3243; SCF-Ufo1 ubiquitin ligase complex.
DR DIP; DIP-1953N; -.
DR IntAct; Q04511; 5.
DR MINT; Q04511; -.
DR STRING; 4932.YML088W; -.
DR iPTMnet; Q04511; -.
DR MaxQB; Q04511; -.
DR PaxDb; Q04511; -.
DR PRIDE; Q04511; -.
DR EnsemblFungi; YML088W_mRNA; YML088W; YML088W.
DR GeneID; 854886; -.
DR KEGG; sce:YML088W; -.
DR SGD; S000004553; UFO1.
DR VEuPathDB; FungiDB:YML088W; -.
DR eggNOG; KOG0274; Eukaryota.
DR HOGENOM; CLU_425266_0_0_1; -.
DR InParanoid; Q04511; -.
DR OMA; CTTPQGC; -.
DR BioCyc; YEAST:G3O-32676-MON; -.
DR Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q04511; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04511; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:SGD.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISA:SGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:SGD.
DR GO; GO:0071406; P:cellular response to methylmercury; IMP:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IMP:SGD.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR003903; UIM_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12937; F-box-like; 1.
DR SMART; SM00256; FBOX; 1.
DR SMART; SM00726; UIM; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS50330; UIM; 3.
PE 1: Evidence at protein level;
KW Phosphoprotein; Reference proteome; Repeat; Ubl conjugation pathway.
FT CHAIN 1..668
FT /note="Ubiquitin ligase complex F-box protein UFO1"
FT /id="PRO_0000119970"
FT DOMAIN 5..51
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT DOMAIN 547..566
FT /note="UIM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 583..602
FT /note="UIM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT DOMAIN 651..668
FT /note="UIM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00213"
FT REGION 564..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 599..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 511
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 514
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 668 AA; 76860 MW; 10CA467CF9417FBC CRC64;
MERPGLVLQD LPPEILINIF SHLDEKDLFT LQELSTHFRN LIHDEELWKN LFKSRVHTTH
FPTFSQSSKF SVEYIERTRG LHHWQHNKAI RTKYTIIPTR NWDQPSIERI VFDYPRVAAY
NDGTITILQL QNHKRQKKFK KLIYIPCTTP QGCSTMDFNI NAAVFGRFDG RVFGKLLSNK
SYLTPVMEFT GRHSAGVTAI CNSESWDTSR EDWSVSGSEN GEIIWWCENK LVKMWKVSNR
VIWKLAFFKD WTLIMDDEKL YIIHQMQELH SIDIPKDLDE QPMRVRFFKM DFGSMTLVLA
DLNNVYTISV NPNGNFGNLR KLEMPEQICA VEIDEKTSQR EQNWQFAGDD GCYISLLTTQ
NTLYIINIRD LSSSGLKVQC KISFDEQVYV SQVTNLIVVV ALPNVLQILN AMTGELIKTV
LKTEKFPEFL KVSQDKIIMG SGNVLNYLKF VSSDSKKHHH STKGKNTVSN KWNETLNTEL
QYYDEDEDLR RKRQSEISRL IDAYGGDLEL SGDTDEENDI QLRIALLESQ EAQARNQAEA
GEPVGDDEDE QLRRALEESQ LIYETQTNSS ANHGNNTNDE IDEDDEEFLR AIRQSRVEDE
RRRHLRNHTT GRRNGPLSDD NFATYGAAES SERTSTENTI GSSVGVDASN NVDEDLQLAI
ALSLSEIN
