ID   YBP1_YEAST              Reviewed;         674 AA.
AC   P38315; D6VQL2;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   08-NOV-2023, entry version 150.
DE   RecName: Full=YAP1-binding protein 1;
DE   AltName: Full=Activator of YAP1;
GN   Name=YBP1 {ECO:0000303|PubMed:12743123};
GN   OrderedLocusNames=YBR216C {ECO:0000312|SGD:S000000420};
GN   ORFNames=YBR1505 {ECO:0000312|SGD:S000000420};
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.
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, AND INTERACTION WITH NUP116.
RX   PubMed=11283351; DOI=10.1073/pnas.061034498;
RA   Ito T., Chiba T., Ozawa R., Yoshida M., Hattori M., Sakaki Y.;
RT   "A comprehensive two-hybrid analysis to explore the yeast protein
RT   interactome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4569-4574(2001).
RN   [4]
RP   FUNCTION, AND OXIDATIVE STRESS RESPONSE.
RX   PubMed=12743123; DOI=10.1074/jbc.m303542200;
RA   Veal E.A., Ross S.J., Malakasi P., Peacock E., Morgan B.A.;
RT   "Ybp1 is required for the hydrogen peroxide-induced oxidation of the Yap1
RT   transcription factor.";
RL   J. Biol. Chem. 278:30896-30904(2003).
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   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH YAP1.
RX   PubMed=15075262; DOI=10.1128/ec.3.2.318-330.2004;
RA   Gulshan K., Rovinsky S.A., Moye-Rowley W.S.;
RT   "YBP1 and its homologue YBP2/YBH1 influence oxidative-stress tolerance by
RT   nonidentical mechanisms in Saccharomyces cerevisiae.";
RL   Eukaryot. Cell 3:318-330(2004).
CC   -!- FUNCTION: Involved in oxidative stress response and redox homeostasis.
CC       Required for hydrogen peroxide-induced oxidation and nuclear
CC       localization (activation) of YAP1. Functions probably in concert with
CC       HYP1/GPX3, the actual YAP1 modifying enzyme. YBP1 is not required for
CC       HYP1/GPX3-independent, diamide-induced oxidation of YAP1.
CC       {ECO:0000269|PubMed:11283351, ECO:0000269|PubMed:12743123,
CC       ECO:0000269|PubMed:15075262}.
CC   -!- SUBUNIT: Interacts with YAP1. Forms a peroxide stress induced complex
CC       with YAP1 in the cytoplasm. Systematic proteome-wide 2-hybrid
CC       interaction studies suggest that YAP1, HYR1/GPX3, and YBP1 all interact
CC       with the nuclear pore complex subunit NUP116, which is involved in
CC       nucleocytoplasmic transport. {ECO:0000269|PubMed:11283351,
CC       ECO:0000269|PubMed:15075262}.
CC   -!- INTERACTION:
CC       P38315; P19880: YAP1; NbExp=3; IntAct=EBI-20985, EBI-31265;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:15075262}.
CC   -!- MISCELLANEOUS: Present with 3100 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the YBP1 family. {ECO:0000305}.
CC   -!- CAUTION: YBP1 encoded by the widely used laboratory strain W303-1a is
CC       only partially functional, probably due to four amino acid
CC       substitutions. {ECO:0000305}.
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DR   EMBL; Z36085; CAA85180.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07332.1; -; Genomic_DNA.
DR   PIR; S46092; S46092.
DR   RefSeq; NP_009775.3; NM_001178564.3.
DR   AlphaFoldDB; P38315; -.
DR   BioGRID; 32913; 113.
DR   DIP; DIP-4499N; -.
DR   IntAct; P38315; 19.
DR   MINT; P38315; -.
DR   STRING; 4932.YBR216C; -.
DR   iPTMnet; P38315; -.
DR   MaxQB; P38315; -.
DR   PaxDb; 4932-YBR216C; -.
DR   PeptideAtlas; P38315; -.
DR   EnsemblFungi; YBR216C_mRNA; YBR216C; YBR216C.
DR   GeneID; 852517; -.
DR   KEGG; sce:YBR216C; -.
DR   AGR; SGD:S000000420; -.
DR   SGD; S000000420; YBP1.
DR   VEuPathDB; FungiDB:YBR216C; -.
DR   eggNOG; ENOG502QWJN; Eukaryota.
DR   GeneTree; ENSGT00940000176740; -.
DR   HOGENOM; CLU_024514_0_0_1; -.
DR   InParanoid; P38315; -.
DR   OMA; LTYEIGW; -.
DR   OrthoDB; 2731083at2759; -.
DR   BioCyc; YEAST:G3O-29153-MONOMER; -.
DR   BioGRID-ORCS; 852517; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P38315; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38315; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   InterPro; IPR013877; YAP-bd/ALF4/Glomulin.
DR   InterPro; IPR040347; YBP1/2.
DR   PANTHER; PTHR28020; YAP1-BINDING PROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR28020:SF1; YAP1-BINDING PROTEIN 1-RELATED; 1.
DR   Pfam; PF08568; Kinetochor_Ybp2; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Reference proteome; Stress response.
FT   CHAIN           1..674
FT                   /note="YAP1-binding protein 1"
FT                   /id="PRO_0000066150"
FT   VARIANT         7
FT                   /note="I -> L (in strain: W303-1a)"
FT   VARIANT         328
FT                   /note="F -> V (in strain: W303-1a)"
FT   VARIANT         343
FT                   /note="K -> E (in strain: W303-1a)"
FT   VARIANT         570
FT                   /note="N -> D (in strain: W303-1a)"
SQ   SEQUENCE   674 AA;  77741 MW;  31F2B200CE34B32D CRC64;
     MEPIDDILFE VTDAFKTQKE DLLELVTLID IYGEQVNQEG SYEEKTRFIE TLNTLLEDNP
     STTGEIGWDL PKGLLKFLSK DNVDVNGRLG TNMIVQGVMK CFYAISIQGE PKKCLITGLE
     LLSSLCSKDF SKSDQQNKED FVDKKANTLP PEGVIENSSN RKDFPSYGES KSSNEFFLKL
     KSYILFEFIG ASLKRISTLF PSKYLGAAVS TIEKFVYSHA DTFEDALFLL RRVYTFCRNY
     IPPDPPKDIQ LNEDFTREMF DKVVEEESEL QVRLLRRLCT FGISTPIKTV TTNADVKYYC
     ALNQQKFELS AYYTEYLELF CRYYQMAFSL DVDIEGEFQN VIKECRIIYK SVPQEISAVN
     DEAKLVLERM VYKLAYTFEV QKAAKEKNVG LDYNGVILFS GIHYLETNQH LVKEMNITDA
     IYLYLRFTTP SLYSKVYYNV AVESVSRYWL WYAITTEPLE DVKKELKNLS VFVTKTLLHV
     LLQKNCIQVN QQLRMITFTL LTRLLCLIPE KVAFEFILDV LKTSPLPLAK TSVLCVFKDL
     SRRRISTKDN DSETDLIVEK LSKLKVNDSN KAQQSNIRHY IQLDSSKMKA VHDCCLQTIQ
     DSFTADAKKS DILLLLTYLN IFIVLKKTWD EDLLKIVCSK IDSNLKSVEP DKLPKYKEIV
     DKNESLNDYF TGIK
//