YBP1_YEAST
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 03-AUG-2022, entry version 146.
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}.
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; 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; P38315; -.
DR PRIDE; P38315; -.
DR EnsemblFungi; YBR216C_mRNA; YBR216C; YBR216C.
DR GeneID; 852517; -.
DR KEGG; sce:YBR216C; -.
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 BioCyc; YEAST:G3O-29153-MON; -.
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; PTHR28020; 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
