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CUB1_YEAST
ID   CUB1_YEAST              Reviewed;         551 AA.
AC   Q08977; D6W3A9; Q05760; Q7LGU3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Cu(2+) suppressing and bleomycin sensitive protein 1;
GN   Name=CUB1; OrderedLocusNames=YPL260W;
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=9169875;
RA   Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA   Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA   Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA   Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA   DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA   Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA   Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA   Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA   Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA   Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA   Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA   Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA   Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA   Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA   Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA   Vo D.H., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL   Nature 387:103-105(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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-156.
RX   PubMed=3040736; DOI=10.1016/s0021-9258(18)45347-1;
RA   Wu M., Tzagoloff A.;
RT   "Mitochondrial and cytoplasmic fumarases in Saccharomyces cerevisiae are
RT   encoded by a single nuclear gene FUM1.";
RL   J. Biol. Chem. 262:12275-12282(1987).
RN   [4]
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   [5]
RP   PHOSPHORYLATION.
RX   PubMed=16172400; DOI=10.1073/pnas.0501046102;
RA   Budovskaya Y.V., Stephan J.S., Deminoff S.J., Herman P.K.;
RT   "An evolutionary proteomics approach identifies substrates of the cAMP-
RT   dependent protein kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13933-13938(2005).
RN   [6]
RP   INDUCTION.
RX   PubMed=22842922; DOI=10.1038/ncb2549;
RA   Tkach J.M., Yimit A., Lee A.Y., Riffle M., Costanzo M., Jaschob D.,
RA   Hendry J.A., Ou J., Moffat J., Boone C., Davis T.N., Nislow C., Brown G.W.;
RT   "Dissecting DNA damage response pathways by analysing protein localization
RT   and abundance changes during DNA replication stress.";
RL   Nat. Cell Biol. 14:966-976(2012).
RN   [7]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND SUBUNIT.
RX   DOI=10.1016/j.plgene.2015.11.002;
RA   Firestone K., Awonusi D., Panfair D., Roland D., Ramamurthy A.,
RA   Kusmierczyk A.R.;
RT   "YPL260W, a high-copy suppressor of a copper-sensitive phenotype in yeast,
RT   is linked to DNA repair and proteasome function.";
RL   Plant Gene 5:38-48(2016).
CC   -!- FUNCTION: Involved in bleomycin tolerance with links to DNA repair
CC       and/or proteasome function. {ECO:0000269|Ref.7}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|Ref.7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- INDUCTION: Expression is induced in response to DNA replication stress.
CC       {ECO:0000269|PubMed:22842922}.
CC   -!- PTM: Phosphorylated by PKA in vitro. {ECO:0000269|PubMed:16172400}.
CC   -!- DISRUPTION PHENOTYPE: Leads to sensitivity to bleomycin (Ref.7).
CC       Bleomycin sensnsitivity is even increased when CUB1 deletion is
CC       combined with proteasome mutants including PRE9 or UMP1 disruptions
CC       (Ref.7). Suppresses the copper tolerance induced by the proteasome
CC       subunit PRE9 disuption (Ref.7). Leads to synthetic sickness with
CC       deletion of RAD6 on media containing bleomycin, but not hydroxyurea
CC       (HU) (Ref.7). {ECO:0000269|Ref.7}.
CC   -!- SIMILARITY: Belongs to the CUB1 family. {ECO:0000305}.
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DR   EMBL; Z73615; CAA97990.1; -; Genomic_DNA.
DR   EMBL; Z73617; CAA97996.1; -; Genomic_DNA.
DR   EMBL; J02802; AAA66910.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11175.1; -; Genomic_DNA.
DR   PIR; S65293; S65293.
DR   RefSeq; NP_015063.1; NM_001184074.1.
DR   AlphaFoldDB; Q08977; -.
DR   SMR; Q08977; -.
DR   BioGRID; 35952; 113.
DR   DIP; DIP-2002N; -.
DR   IntAct; Q08977; 4.
DR   MINT; Q08977; -.
DR   STRING; 4932.YPL260W; -.
DR   iPTMnet; Q08977; -.
DR   MaxQB; Q08977; -.
DR   PaxDb; Q08977; -.
DR   PRIDE; Q08977; -.
DR   EnsemblFungi; YPL260W_mRNA; YPL260W; YPL260W.
DR   GeneID; 855867; -.
DR   KEGG; sce:YPL260W; -.
DR   SGD; S000006181; CUB1.
DR   VEuPathDB; FungiDB:YPL260W; -.
DR   eggNOG; ENOG502QPV0; Eukaryota.
DR   HOGENOM; CLU_026648_1_0_1; -.
DR   InParanoid; Q08977; -.
DR   OMA; KQDRTTY; -.
DR   BioCyc; YEAST:G3O-34145-MON; -.
DR   PRO; PR:Q08977; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q08977; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   InterPro; IPR018810; UPF0662.
DR   PANTHER; PTHR28086; PTHR28086; 1.
DR   Pfam; PF10303; DUF2408; 3.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..551
FT                   /note="Cu(2+) suppressing and bleomycin sensitive protein
FT                   1"
FT                   /id="PRO_0000255978"
FT   REGION          513..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          174..213
FT                   /evidence="ECO:0000255"
FT   COILED          249..300
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        535..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        90
FT                   /note="D -> G (in Ref. 3; AAA66910)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        128
FT                   /note="E -> K (in Ref. 3; AAA66910)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   551 AA;  62780 MW;  9DF384D00D58EDC8 CRC64;
     MFASAGQQHP QIVPKEEESI LNYLLEVRSS LAKLKQNRTQ YLNSKDVQTT YQHVLTKVRE
     LDDIRKNSHE TPAKSAATLI HSTELHNRVD SVLDDVFQLL SLCFLTVGLK NSAPATYASL
     STVESLLEHL NESNVFTHHD LSPIKERLEE ISKIVEQKNS SPAYDEDGND DRLREIDNER
     KKNKIEEDLL LRAKLKHCKD EYDILEGKLE EIDPSLSTVM EKLFRIRRGL LSLVASAKKT
     MSKSDINTNS LLQEQNDLQT NNESLTDDKH LVSQEYVHEK LSVLKNELSE LESNRDDSGK
     FKSLESHQVA EKGQSVLNGL LDDCHDLVND LSHQKNGGLT LDPYLQPIYE QLIDIKTTLE
     NLMITRRWTL RETDLFSYQK KLNEIDNKRI NGKFPTKSQD SKGQSILLYL LRRCYAIIYK
     LLESSEPVSE ALQPIHNQLS TVRRCLLELK RMGGVNNERE LYPYQMKLAS LDNLRTEGIF
     YDSDGNIPEG QGILNALLAE CFDILHELKV EAEEKAQNST SSDGSDDDDN GESGIDSNSN
     DSEPESEYQQ E
 
 
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