NDD1_YEAST
ID NDD1_YEAST Reviewed; 554 AA.
AC Q08887; D6W365;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Nuclear division defective protein 1;
GN Name=NDD1; OrderedLocusNames=YOR372C;
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., 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., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., 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 [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, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=10207056; DOI=10.1128/mcb.19.5.3312;
RA Loy C.J., Lydall D., Surana U.;
RT "NDD1, a high-dosage suppressor of cdc28-1N, is essential for expression of
RT a subset of late-S-phase-specific genes in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 19:3312-3327(1999).
RN [4]
RP FUNCTION.
RX PubMed=10894549; DOI=10.1038/35017589;
RA Koranda M., Schleiffer A., Endler L., Ammerer G.;
RT "Forkhead-like transcription factors recruit Ndd1 to the chromatin of G2/M-
RT specific promoters.";
RL Nature 406:94-98(2000).
RN [5]
RP FUNCTION.
RX PubMed=11572776; DOI=10.1016/s0092-8674(01)00494-9;
RA Simon I., Barnett J., Hannett N., Harbison C.T., Rinaldi N.J.,
RA Volkert T.L., Wyrick J.J., Zeitlinger J., Gifford D.K., Jaakkola T.S.,
RA Young R.A.;
RT "Serial regulation of transcriptional regulators in the yeast cell cycle.";
RL Cell 106:697-708(2001).
RN [6]
RP RECRUITMENT TO PROMOTER.
RX PubMed=12183363; DOI=10.1101/gad.994902;
RA Sun K., Coic E., Zhou Z., Durrens P., Haber J.E.;
RT "Saccharomyces forkhead protein Fkh1 regulates donor preference during
RT mating-type switching through the recombination enhancer.";
RL Genes Dev. 16:2085-2096(2002).
RN [7]
RP FUNCTION, AND PHOSPHORYLATION.
RX PubMed=14521842; DOI=10.1016/j.cub.2003.08.053;
RA Darieva Z., Pic-Taylor A., Boros J., Spanos A., Geymonat M., Reece R.J.,
RA Sedgwick S.G., Sharrocks A.D., Morgan B.A.;
RT "Cell cycle-regulated transcription through the FHA domain of Fkh2p and the
RT coactivator Ndd1p.";
RL Curr. Biol. 13:1740-1745(2003).
RN [8]
RP FUNCTION, INTERACTION WITH FKH2, PHOSPHORYLATION AT THR-319, AND
RP MUTAGENESIS OF THR-319.
RX PubMed=12865300; DOI=10.1101/gad.1074103;
RA Reynolds D., Shi B.J., McLean C., Katsis F., Kemp B., Dalton S.;
RT "Recruitment of Thr 319-phosphorylated Ndd1p to the FHA domain of Fkh2p
RT requires Clb kinase activity: a mechanism for CLB cluster gene
RT activation.";
RL Genes Dev. 17:1789-1802(2003).
RN [9]
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 [10]
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 [11]
RP FUNCTION.
RX PubMed=15949038; DOI=10.1186/1471-2164-6-90;
RA Yang Y.-L., Suen J., Brynildsen M.P., Galbraith S.J., Liao J.C.;
RT "Inferring yeast cell cycle regulators and interactions using transcription
RT factor activities.";
RL BMC Genomics 6:90-90(2005).
RN [12]
RP FUNCTION, AND INDUCTION.
RX PubMed=16912276; DOI=10.1101/gad.1450606;
RA Pramila T., Wu W., Miles S., Noble W.S., Breeden L.L.;
RT "The Forkhead transcription factor Hcm1 regulates chromosome segregation
RT genes and fills the S-phase gap in the transcriptional circuitry of the
RT cell cycle.";
RL Genes Dev. 20:2266-2278(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-319, AND IDENTIFICATION BY
RP 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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
CC -!- FUNCTION: Transcription activator involved in G2/M transcription
CC through its association with FKH2. {ECO:0000269|PubMed:10207056,
CC ECO:0000269|PubMed:10894549, ECO:0000269|PubMed:11572776,
CC ECO:0000269|PubMed:12865300, ECO:0000269|PubMed:14521842,
CC ECO:0000269|PubMed:15949038, ECO:0000269|PubMed:16912276}.
CC -!- SUBUNIT: Forms an activator complex with FKH2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC {ECO:0000269|PubMed:10207056}.
CC -!- INDUCTION: During S phase of the cell cycle. Expression is cell cycle
CC regulated by HCM1. {ECO:0000269|PubMed:10207056,
CC ECO:0000269|PubMed:16912276}.
CC -!- PTM: Phosphorylation of Thr-319 by CDC28 is required for the
CC interaction with FKH2 and recruitment to promoters.
CC {ECO:0000269|PubMed:12865300, ECO:0000269|PubMed:14521842}.
CC -!- MISCELLANEOUS: Present with 779 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z75280; CAA99703.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11131.1; -; Genomic_DNA.
DR PIR; S67284; S67284.
DR RefSeq; NP_015017.1; NM_001183792.1.
DR AlphaFoldDB; Q08887; -.
DR BioGRID; 34755; 27.
DR DIP; DIP-1806N; -.
DR IntAct; Q08887; 5.
DR MINT; Q08887; -.
DR STRING; 4932.YOR372C; -.
DR iPTMnet; Q08887; -.
DR MaxQB; Q08887; -.
DR PaxDb; Q08887; -.
DR PRIDE; Q08887; -.
DR EnsemblFungi; YOR372C_mRNA; YOR372C; YOR372C.
DR GeneID; 854554; -.
DR KEGG; sce:YOR372C; -.
DR SGD; S000005899; NDD1.
DR VEuPathDB; FungiDB:YOR372C; -.
DR eggNOG; ENOG502RUKY; Eukaryota.
DR HOGENOM; CLU_023935_0_0_1; -.
DR InParanoid; Q08887; -.
DR OMA; TQFPTPY; -.
DR BioCyc; YEAST:G3O-33840-MON; -.
DR PRO; PR:Q08887; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08887; protein.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:SGD.
DR GO; GO:0090282; P:positive regulation of transcription involved in G2/M transition of mitotic cell cycle; IMP:SGD.
PE 1: Evidence at protein level;
KW Activator; Cytoplasm; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..554
FT /note="Nuclear division defective protein 1"
FT /id="PRO_0000268686"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 319
FT /note="Phosphothreonine; by CDC28"
FT /evidence="ECO:0000269|PubMed:12865300,
FT ECO:0007744|PubMed:18407956"
FT MUTAGEN 319
FT /note="T->A: Growth delay."
FT /evidence="ECO:0000269|PubMed:12865300"
SQ SEQUENCE 554 AA; 60523 MW; 1CF99115F2B1F23D CRC64;
MDRDISYQQN YTSTGATATS SRQPSTDNNA DTNFLKVMSE FKYNFNSPLP TTTQFPTPYS
SNQYQQTQDH FANTDAHNSS SNESSLVENS ILPHHQQIQQ QQQQQQQQQQ QQQALGSLVP
PAVTRTDTSE TLDDINVQPS SVLQFGNSLP SEFLVASPEQ FKEFLLDSPS TNFNFFHKTP
AKTPLRFVTD SNGAQQSTTE NPGQQQNVFS NVDLNNLLKS NGKTPSSSCT GAFSRTPLSK
IDMNLMFNQP LPTSPSKRFS SLSLTPYGRK ILNDVGTPYA KALISSNSAL VDFQKARKDI
TTNATSIGLE NANNILQRTP LRSNNKKLFI KTPQDTINST STLTKDNENK QDIYGSSPTT
IQLNSSITKS ISKLDNSRIP LLASRSDNIL DSNVDDQLFD LGLTRLPLSP TPNCNSLHST
TTGTSALQIP ELPKMGSFRS DTGINPISSS NTVSFKSKSG NNNSKGRIKK NGKKPSKFQI
IVANIDQFNQ DTSSSSLSSS LNASSSAGNS NSNVTKKRAS KLKRSQSLLS DSGSKSQARK
SCNSKSNGNL FNSQ
