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YBP2_YEAST
ID   YBP2_YEAST              Reviewed;         641 AA.
AC   P53169; D6VU81;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 142.
DE   RecName: Full=YAP1-binding protein 2 {ECO:0000303|PubMed:15075262};
DE   AltName: Full=YBP1 homolog protein 1 {ECO:0000303|PubMed:15075262};
GN   Name=YBP2 {ECO:0000303|PubMed:15075262};
GN   Synonyms=YBH1 {ECO:0000303|PubMed:15075262};
GN   OrderedLocusNames=YGL060W {ECO:0000312|SGD:S000003028};
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 204508 / S288c;
RX   PubMed=9234674;
RX   DOI=10.1002/(sici)1097-0061(199707)13:9<861::aid-yea125>3.0.co;2-9;
RA   Feuermann M., de Montigny J., Potier S., Souciet J.-L.;
RT   "The characterization of two new clusters of duplicated genes suggests a
RT   'Lego' organization of the yeast Saccharomyces cerevisiae chromosomes.";
RL   Yeast 13:861-869(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169869;
RA   Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA   Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA   Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA   Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA   Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA   Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA   Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA   Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA   Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA   Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA   Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA   Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA   Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA   Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA   Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA   Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA   Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA   Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA   Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA   Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA   Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA   Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL   Nature 387:81-84(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, AND ALKYLATING STRESS INDUCED EXPRESSION.
RX   PubMed=9990050; DOI=10.1073/pnas.96.4.1486;
RA   Jelinsky S.A., Samson L.D.;
RT   "Global response of Saccharomyces cerevisiae to an alkylating agent.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:1486-1491(1999).
RN   [5]
RP   FUNCTION, AND STRESS INDUCED EXPRESSION.
RX   PubMed=11570514; DOI=10.1007/s002940100237;
RA   de Jesus Ferreira M.C., Bao X., Laize V., Hohmann S.;
RT   "Transposon mutagenesis reveals novel loci affecting tolerance to salt
RT   stress and growth at low temperature.";
RL   Curr. Genet. 40:27-39(2001).
RN   [6]
RP   FUNCTION.
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   [7]
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   [8]
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   [9]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
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 activation of YAP1. Acts in a
CC       parallele pathway to YBP1. {ECO:0000269|PubMed:11570514,
CC       ECO:0000269|PubMed:12743123, ECO:0000269|PubMed:15075262,
CC       ECO:0000269|PubMed:9990050}.
CC   -!- INTERACTION:
CC       P53169; Q05080: HOF1; NbExp=2; IntAct=EBI-23796, EBI-5412;
CC       P53169; Q08273: HRT1; NbExp=3; IntAct=EBI-23796, EBI-31686;
CC       P53169; P43603: LSB3; NbExp=2; IntAct=EBI-23796, EBI-22980;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:15075262}.
CC   -!- DISRUPTION PHENOTYPE: Increases sensitivity to H(2)O(2) and decreases
CC       activation of YAP1-dependent gene expression.
CC       {ECO:0000269|PubMed:15075262}.
CC   -!- MISCELLANEOUS: Present with 3900 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the YBP1 family. {ECO:0000305}.
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DR   EMBL; Z72582; CAA96763.1; -; Genomic_DNA.
DR   EMBL; BK006941; DAA08042.1; -; Genomic_DNA.
DR   PIR; S64064; S64064.
DR   RefSeq; NP_011455.1; NM_001180925.1.
DR   AlphaFoldDB; P53169; -.
DR   BioGRID; 33187; 150.
DR   DIP; DIP-2073N; -.
DR   IntAct; P53169; 8.
DR   MINT; P53169; -.
DR   STRING; 4932.YGL060W; -.
DR   iPTMnet; P53169; -.
DR   MaxQB; P53169; -.
DR   PaxDb; P53169; -.
DR   PRIDE; P53169; -.
DR   EnsemblFungi; YGL060W_mRNA; YGL060W; YGL060W.
DR   GeneID; 852820; -.
DR   KEGG; sce:YGL060W; -.
DR   SGD; S000003028; YBP2.
DR   VEuPathDB; FungiDB:YGL060W; -.
DR   eggNOG; ENOG502QWJN; Eukaryota.
DR   GeneTree; ENSGT00940000176740; -.
DR   HOGENOM; CLU_024514_0_0_1; -.
DR   InParanoid; P53169; -.
DR   OMA; NGNPKEC; -.
DR   BioCyc; YEAST:G3O-30568-MON; -.
DR   PRO; PR:P53169; -.
DR   Proteomes; UP000002311; Chromosome VII.
DR   RNAct; P53169; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0000776; C:kinetochore; IDA:SGD.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central.
DR   GO; GO:0007052; P:mitotic spindle organization; IGI:SGD.
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..641
FT                   /note="YAP1-binding protein 2"
FT                   /id="PRO_0000066151"
SQ   SEQUENCE   641 AA;  73102 MW;  AB39654DC55F024A CRC64;
     MYNEQVNSGK SIKEKERYLD ALLKILKDNP VTLKEIGWDL PKGLLQFFSR KNINVNIHLV
     FSPLVSSVME CFNELAINGN PKECLLTACE LVSTLHIVLT ETGDSDEENE DLNDSNRNDA
     SNITDELSVI TPEIGHYMAK NTVEFIPNLK IYVLFEFMSL LLKRVDTLYP SKFLAMVTSA
     IIKYVTTNVQ AMDDPHFILR IVYNFCTNYS PAQPSASLTD GISTNDLEKI HDDESALQKK
     LLANLSVFVI SNCLKNHPGN IDKIYFKTLM HKKTDENEID ASVLQICHQY YEYVTSLDVH
     MKELLEKCLV ESRSIYNSLL MNPAASTPEF KEEINQLVYE VSYAYQIKKL ADEKNLELDQ
     YGVVILSAIH YSKNGTHLLP QIDIQSAIYL YLRCTTASLF SEIYENKFLE SSVRYWLWVS
     TTETSTEKIK CALQELPGHI TTAFLQMLLM KTCNESNNDT KLTEITLLRR LLYLMPESTS
     FTFIFETLLH CPYITAKIAV LDILRDMMIR SPEAANRDET VGLIEQQNPG NTANSVPIMP
     TLPPRPYITI NEDRMASIHS IALICFSAAK QKKRTQGDLL LVLTYMKFFV SLRNKWDLGL
     LTLINKEISE SFQGEGEPEL AFINISNNTL GEYIEEMNIR S
 
 
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