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Database: UniProt
Entry: DIA2_YEAST
LinkDB: DIA2_YEAST
Original site: DIA2_YEAST 
ID   DIA2_YEAST              Reviewed;         732 AA.
AC   Q08496; D6W2E3; O00034; Q7LGN4;
DT   18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   18-SEP-2019, entry version 162.
DE   RecName: Full=Protein DIA2;
DE   AltName: Full=Digs into agar protein 2;
GN   Name=DIA2; OrderedLocusNames=YOR080W; ORFNames=YOR29-31;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9133743;
RX   DOI=10.1002/(SICI)1097-0061(19970330)13:4<379::AID-YEA85>3.3.CO;2-7;
RA   Valens M., Bohn C., Daignan-Fornier B., Dang V.-D.,
RA   Bolotin-Fukuhara M.;
RT   "The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the
RT   presence of two tRNAs and 24 new open reading frames.";
RL   Yeast 13:379-390(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
RA   Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
RA   Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
RA   Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
RA   Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
RA   Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
RA   Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
RA   Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
RA   Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
RA   Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
RA   Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
RA   Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
RA   Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
RA   Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
RA   Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
RA   Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(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.,
RA   Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and
RT   now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   DOMAIN, AND FUNCTION.
RX   PubMed=10582239; DOI=10.1098/rstb.1999.0497;
RA   Willems A.R., Goh T., Taylor L., Chernushevich I., Shevchenko A.,
RA   Tyers M.;
RT   "SCF ubiquitin protein ligases and phosphorylation-dependent
RT   proteolysis.";
RL   Philos. Trans. R. Soc. Lond., B, Biol. Sci. 354:1533-1550(1999).
RN   [5]
RP   FUNCTION.
RX   PubMed=11063681;
RA   Palecek S.P., Parikh A.S., Kron S.J.;
RT   "Genetic analysis reveals that FLO11 upregulation and cell
RT   polarization independently regulate invasive growth in Saccharomyces
RT   cerevisiae.";
RL   Genetics 156:1005-1023(2000).
RN   [6]
RP   FUNCTION.
RX   PubMed=15620357; DOI=10.1016/j.cell.2004.11.052;
RA   Bao M.Z., Schwartz M.A., Cantin G.T., Yates J.R. III, Madhani H.D.;
RT   "Pheromone-dependent destruction of the Tec1 transcription factor is
RT   required for MAP kinase signaling specificity in yeast.";
RL   Cell 119:991-1000(2004).
RN   [7]
RP   FUNCTION.
RX   PubMed=15579722; DOI=10.1534/genetics.104.029033;
RA   Sarin S., Ross K.E., Boucher L., Green Y., Tyers M., Cohen-Fix O.;
RT   "Uncovering novel cell cycle players through the inactivation of
RT   securin in budding yeast.";
RL   Genetics 168:1763-1771(2004).
RN   [8]
RP   FUNCTION.
RX   PubMed=14993228; DOI=10.1074/jbc.m313746200;
RA   Serrano R., Bernal D., Simon E., Arino J.;
RT   "Copper and iron are the limiting factors for growth of the yeast
RT   Saccharomyces cerevisiae in an alkaline environment.";
RL   J. Biol. Chem. 279:19698-19704(2004).
RN   [9]
RP   INTERACTION WITH SKP1, AND RECONSTITUTION OF THE SCF(DIA2) 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
RT   E2 enzymes in vitro.";
RL   Proteins 54:455-467(2004).
RN   [10]
RP   FUNCTION.
RX   PubMed=16487579; DOI=10.1016/j.cell.2005.12.036;
RA   Pan X., Ye P., Yuan D.S., Wang X., Bader J.S., Boeke J.D.;
RT   "A DNA integrity network in the yeast Saccharomyces cerevisiae.";
RL   Cell 124:1069-1081(2006).
RN   [11]
RP   IDENTIFICATION IN THE SCF(DIA2) COMPLEX, AND FUNCTION OF THE SCF(DIA2)
RP   COMPLEX.
RX   PubMed=16421250; DOI=10.1091/mbc.e05-09-0884;
RA   Koepp D.M., Kile A.C., Swaminathan S., Rodriguez-Rivera V.;
RT   "The F-box protein Dia2 regulates DNA replication.";
RL   Mol. Biol. Cell 17:1540-1548(2006).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-393, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth
RT   phosphoproteome analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [13]
RP   IDENTIFICATION OF INITIATION SITE.
RC   STRAIN=ATCC 208353 / W303-1A;
RX   PubMed=19913425; DOI=10.1016/j.cub.2009.09.062;
RA   Morohashi H., Maculins T., Labib K.;
RT   "The amino-terminal TPR domain of Dia2 tethers SCF(Dia2) to the
RT   replisome progression complex.";
RL   Curr. Biol. 19:1943-1949(2009).
CC   -!- FUNCTION: F-box protein 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). The SCF(DIA2) complex is specifically
CC       involved in the pheromone induced degradation of phosphorylated
CC       TEC1. The SCF(DIA2) complex binds to DNA replication origins.
CC       Involved in DNA replication, genome stability, and the control of
CC       cell cycle, probably through its association to replication
CC       origins to facilitate the ubiquitination of another origin-binding
CC       protein. Required for invasive growth and growth under alkaline
CC       conditions. {ECO:0000250, ECO:0000269|PubMed:10582239,
CC       ECO:0000269|PubMed:11063681, ECO:0000269|PubMed:14993228,
CC       ECO:0000269|PubMed:15579722, ECO:0000269|PubMed:15620357,
CC       ECO:0000269|PubMed:16421250, ECO:0000269|PubMed:16487579}.
CC   -!- SUBUNIT: Component of the SCF(DIA2) complex containing CDC53,
CC       SKP1, RBX1 and DIA2. Interacts with SKP1.
CC       {ECO:0000269|PubMed:14747994, ECO:0000269|PubMed:16421250}.
CC   -!- INTERACTION:
CC       Q01454:CTF4; NbExp=5; IntAct=EBI-31943, EBI-5209;
CC       P29469:MCM2; NbExp=4; IntAct=EBI-31943, EBI-10533;
CC       P25588:MRC1; NbExp=11; IntAct=EBI-31943, EBI-412442;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the DIA2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA94565.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=CAA99273.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=CAA99275.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; Z70678; CAA94565.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z74988; CAA99273.1; ALT_INIT; Genomic_DNA.
DR   EMBL; Z74989; CAA99275.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK006948; DAA10859.2; -; Genomic_DNA.
DR   PIR; S66963; S66963.
DR   RefSeq; NP_014723.2; NM_001183499.1.
DR   BioGrid; 34479; 671.
DR   ComplexPortal; CPX-3250; SCF-Dia2 ubiquitin ligase complex.
DR   DIP; DIP-6496N; -.
DR   IntAct; Q08496; 46.
DR   MINT; Q08496; -.
DR   STRING; 4932.YOR080W; -.
DR   iPTMnet; Q08496; -.
DR   PaxDb; Q08496; -.
DR   PRIDE; Q08496; -.
DR   EnsemblFungi; YOR080W_mRNA; YOR080W; YOR080W.
DR   GeneID; 854247; -.
DR   KEGG; sce:YOR080W; -.
DR   EuPathDB; FungiDB:YOR080W; -.
DR   SGD; S000005606; DIA2.
DR   HOGENOM; HOG000142330; -.
DR   InParanoid; Q08496; -.
DR   KO; K15068; -.
DR   OMA; CKGYLRT; -.
DR   BioCyc; YEAST:G3O-33617-MONOMER; -.
DR   Reactome; R-SCE-8951664; Neddylation.
DR   Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:Q08496; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0019005; C:SCF ubiquitin ligase complex; IDA:SGD.
DR   GO; GO:0003688; F:DNA replication origin binding; IDA:SGD.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0043624; P:cellular protein complex disassembly; IMP:SGD.
DR   GO; GO:0030466; P:chromatin silencing at silent mating-type cassette; IMP:SGD.
DR   GO; GO:0006348; P:chromatin silencing at telomere; IMP:SGD.
DR   GO; GO:0001403; P:invasive growth in response to glucose limitation; IGI:SGD.
DR   GO; GO:0016567; P:protein ubiquitination; IMP:SGD.
DR   GO; GO:0006275; P:regulation of DNA replication; IMP:SGD.
DR   GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:SGD.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 3.80.10.10; -; 2.
DR   InterPro; IPR036047; F-box-like_dom_sf.
DR   InterPro; IPR001810; F-box_dom.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR013026; TPR-contain_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF00646; F-box; 1.
DR   Pfam; PF00560; LRR_1; 1.
DR   SMART; SM00256; FBOX; 1.
DR   SMART; SM00367; LRR_CC; 3.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF81383; SSF81383; 1.
DR   PROSITE; PS50181; FBOX; 1.
DR   PROSITE; PS51450; LRR; 4.
DR   PROSITE; PS50293; TPR_REGION; 2.
PE   1: Evidence at protein level;
KW   Cell cycle; Complete proteome; Leucine-rich repeat; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; TPR repeat;
KW   Ubl conjugation pathway.
FT   CHAIN         1    732       Protein DIA2.
FT                                /FTId=PRO_0000233003.
FT   REPEAT       15     48       TPR 1.
FT   REPEAT       78    111       TPR 2.
FT   REPEAT      113    145       TPR 3.
FT   DOMAIN      204    251       F-box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00080}.
FT   REPEAT      425    449       LRR 1.
FT   REPEAT      480    505       LRR 2.
FT   REPEAT      509    532       LRR 3.
FT   REPEAT      550    574       LRR 4.
FT   REPEAT      579    602       LRR 5.
FT   REPEAT      616    637       LRR 6.
FT   REPEAT      645    669       LRR 7.
FT   MOD_RES     393    393       Phosphoserine.
FT                                {ECO:0000244|PubMed:18407956}.
SQ   SEQUENCE   732 AA;  85070 MW;  98B610994BA2F803 CRC64;
     MSSPGNSGVA IDSTVLKAIE LGTRLFKSGE YLQAKRIFTN ALRVCDSYSQ EQIMRIRNAY
     QLDTARPDNK RLYHPRYIKI LDNICACYEK LNDLKSCLDV SQRLLKLEPG NIKCYIRCTR
     TLIKLKDWKR AYKTCSRGLQ LCNNDSNHLR QQKQFIKNNM VQKQDGKRSY IDPLEETKIA
     KKKKNNNVLE SLPKKKIKGS TKKTDLVGNL PIEILPIIFQ RFTTKELVTL SLVCNKWRDK
     ILYHLDCFQE FNLAPINFKN FVKFMDFLQQ NFTRTYRKYI LSQVKVSSRI TSEELRITQL
     LFSKMPKCIN IERLILSMPT LTTTQIFKLM VRGGTDFFTR LLELSLMITY RPDKQHELEI
     LQTCPLLKKI ELIFVNSLVP IFDGNNSVGR DGSFNVMARH TNMQISTADN DEQGIVEEKV
     IYSELEKITL ICDKKKIKNF PLCRALLRGQ FPLLQKLTIT GVTFPMNNQD IMNFQWLLNF
     PDLKELWIED NDNCELSKFL QLLKFSNVWK NLEKLTFREN KLYPIVNLDE DQPVTNDDEV
     PSMLFYKENL QNLEKLDLMG TSISGSALTR LCEQEYLDGR KLRSLNIGNC PNIQFPNNHA
     HTARMILDVN AVLKRLSKLE EINLSHLSSL NDSTMKSFII NVPFLENLKR LDISHNFEIT
     GISIYEFLKK FQMDHDNEAG GQPLAYLNID GCSQVSHITV NMIRAQNLVT QVDCVYERDV
     WRKFGINSYS YS
//
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