位置:首页 > 蛋白库 > YD131_YEAST
YD131_YEAST
ID   YD131_YEAST             Reviewed;         556 AA.
AC   Q03899; D6VSB7;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=F-box protein YDR131C;
GN   OrderedLocusNames=YDR131C;
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=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(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   PROTEIN SEQUENCE OF 132-148 AND 521-529, IDENTIFICATION IN SCF COMPLEX, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=10582239; DOI=10.1098/rstb.1999.0497;
RA   Willems A.R., Goh T., Taylor L., Chernushevich I., Shevchenko A., Tyers M.;
RT   "SCF ubiquitin protein ligases and phosphorylation-dependent proteolysis.";
RL   Philos. Trans. R. Soc. Lond., B, Biol. Sci. 354:1533-1550(1999).
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   INTERACTION WITH SKP1, AND RECONSTITUTION OF THE SCF(YDR131C) 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).
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}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with SKP1. Component of the probable SCF(YDR131C)
CC       complex containing CDC53, SKP1, RBX1 and YDR131C.
CC       {ECO:0000269|PubMed:10582239, ECO:0000269|PubMed:14747994}.
CC   -!- INTERACTION:
CC       Q03899; P52286: SKP1; NbExp=4; IntAct=EBI-36201, EBI-4090;
CC   -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:14562095}.
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; Z48179; CAA88212.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11977.1; -; Genomic_DNA.
DR   PIR; S51858; S51858.
DR   RefSeq; NP_010416.1; NM_001180439.1.
DR   AlphaFoldDB; Q03899; -.
DR   BioGRID; 32187; 55.
DR   ComplexPortal; CPX-3681; SCF-Ydr131c ubiquitin ligase complex.
DR   DIP; DIP-867N; -.
DR   IntAct; Q03899; 18.
DR   STRING; 4932.YDR131C; -.
DR   MaxQB; Q03899; -.
DR   PaxDb; Q03899; -.
DR   PRIDE; Q03899; -.
DR   EnsemblFungi; YDR131C_mRNA; YDR131C; YDR131C.
DR   GeneID; 851709; -.
DR   KEGG; sce:YDR131C; -.
DR   SGD; S000002538; YDR131C.
DR   VEuPathDB; FungiDB:YDR131C; -.
DR   eggNOG; ENOG502QTK4; Eukaryota.
DR   HOGENOM; CLU_020929_1_0_1; -.
DR   InParanoid; Q03899; -.
DR   OMA; DEHQRCN; -.
DR   BioCyc; YEAST:G3O-29730-MON; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q03899; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q03899; protein.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:SGD.
DR   GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; ISA:SGD.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IGI:SGD.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:ComplexPortal.
DR   InterPro; IPR001810; F-box_dom.
DR   PROSITE; PS50181; FBOX; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Reference proteome; Ubl conjugation pathway;
KW   Vacuole.
FT   CHAIN           1..556
FT                   /note="F-box protein YDR131C"
FT                   /id="PRO_0000253804"
FT   DOMAIN          1..44
FT                   /note="F-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
SQ   SEQUENCE   556 AA;  65243 MW;  7004D9665DAE2CEF CRC64;
     MFDKLPYEIF KQIAWRIPQE DKISLTYVCK RSYESIIPFI YQNLFLNETY HINGDYDNSF
     GTCYWSVLNF HYIDEDDSNT KNDMSNRRLA KVKFSYFERT LAESPKRLCP LINRIRCTWH
     LNEDVMTNVL KLLSEYGSNL KFVDQFVRSS VNKGLEPLSK QLKTLTLTPP TLMPTHNSVS
     GSYLNKIDRL LLKCDLSRLE KLSIHINALK YFKNTGSPMK IKALVLNLRP DTLNLAEYDA
     SDDFLKELEY IDIFDASTLR QLEILSWYSR DDFPSGEEGG FDRLYVKWGL EGFWKFPNIE
     KLSLASLVYS EFFLMNCLAV FHNLKILKLD YMGKFDFDVS LINFLSKQVC GKKLQRFDIH
     CQLNHRLFFP MTDNPLTRLN FDGFCPCSTC KNTIHEVILK KIFPETRSKL LKNPNKFQAH
     NFFYQMFFEN KIMPYTNIID NESPAMGWDS VPIETFVRKF NENLQSTIEN TENITVNKIT
     REDAISLYHL YLHYLKDVFK VFEQSLPNLE YLTINGIPTK IIQVDELQRC AVPLFYNNGY
     KSNSVYELVD AEALFS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025