NUD1_YEAST
ID NUD1_YEAST Reviewed; 851 AA.
AC P32336; D6W366; Q08895;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Protein NUD1;
GN Name=NUD1; OrderedLocusNames=YOR373W;
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].
RA Dulic V., Zanolari B., Riezman H.;
RT "NUD1, a cell-cycle regulated gene required for nuclear division in
RT Saccharomyces cerevisiae.";
RL Submitted (SEP-1991) to the EMBL/GenBank/DDBJ databases.
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., 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 [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 IDENTIFICATION BY MASS SPECTROMETRY IN SPINDLE POLE BODY.
RX PubMed=9585415; DOI=10.1083/jcb.141.4.967;
RA Wigge P.A., Jensen O.N., Holmes S., Soues S., Mann M., Kilmartin J.V.;
RT "Analysis of the Saccharomyces spindle pole by matrix-assisted laser
RT desorption/ionization (MALDI) mass spectrometry.";
RL J. Cell Biol. 141:967-977(1998).
RN [5]
RP INTERACTION WITH CNM67.
RX PubMed=9571234; DOI=10.1091/mbc.9.5.977;
RA Brachat A., Kilmartin J.V., Wach A., Philippsen P.;
RT "Saccharomyces cerevisiae cells with defective spindle pole body outer
RT plaques accomplish nuclear migration via half-bridge-organized
RT microtubules.";
RL Mol. Biol. Cell 9:977-991(1998).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=10330408; DOI=10.1083/jcb.145.4.809;
RA Adams I.R., Kilmartin J.V.;
RT "Localization of core spindle pole body (SPB) components during SPB
RT duplication in Saccharomyces cerevisiae.";
RL J. Cell Biol. 145:809-823(1999).
RN [7]
RP FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH SPC72.
RX PubMed=11101520; DOI=10.1093/emboj/19.23.6475;
RA Gruneberg U., Campbell K., Simpson C., Grindlay J., Schiebel E.;
RT "Nud1p links astral microtubule organization and the control of exit from
RT mitosis.";
RL EMBO J. 19:6475-6488(2000).
RN [8]
RP ERRATUM OF PUBMED:11101520.
RA Gruneberg U., Campbell K., Simpson C., Grindlay J., Schiebel E.;
RL EMBO J. 20:305-305(2001).
RN [9]
RP INTERACTION WITH MPC54 AND SPO21.
RX PubMed=10899120; DOI=10.1093/emboj/19.14.3657;
RA Knop M., Strasser K.;
RT "Role of the spindle pole body of yeast in mediating assembly of the
RT prospore membrane during meiosis.";
RL EMBO J. 19:3657-3667(2000).
RN [10]
RP COMPOSITION OF A SPB COMPLEX, AND INTERACTION WITH ADY3.
RX PubMed=11742972; DOI=10.1093/emboj/20.24.6946;
RA Moreno-Borchart A.C., Strasser K., Finkbeiner M.G., Shevchenko A.,
RA Shevchenko A., Knop M.;
RT "Prospore membrane formation linked to the leading edge protein (LEP) coat
RT assembly.";
RL EMBO J. 20:6946-6957(2001).
RN [11]
RP INTERACTION WITH ADY3.
RX PubMed=11973299; DOI=10.1093/genetics/160.4.1439;
RA Nickas M.E., Neiman A.M.;
RT "Ady3p links spindle pole body function to spore wall synthesis in
RT Saccharomyces cerevisiae.";
RL Genetics 160:1439-1450(2002).
RN [12]
RP INTERACTION WITH ADY4.
RX PubMed=12796288; DOI=10.1128/ec.2.3.431-445.2003;
RA Nickas M.E., Schwartz C., Neiman A.M.;
RT "Ady4p and Spo74p are components of the meiotic spindle pole body that
RT promote growth of the prospore membrane in Saccharomyces cerevisiae.";
RL Eukaryot. Cell 2:431-445(2003).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-417 AND SER-419, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [15]
RP IDENTIFICATION 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 phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-388 AND THR-392, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [17]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-357, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Involved in astral microtubule organization by binding SCP72
CC to the outer plaque in a cell-cycle dependent manner. Required for the
CC mitotic exit by facilitating the binding of TEMP1 to CDC15. Also
CC involved in the pathway that organizes the shaping and sizing of the
CC prospore membrane (PSM) during sporulation.
CC {ECO:0000269|PubMed:11101520}.
CC -!- SUBUNIT: Interacts directly with MPC54, CNM67, SPO21/MPC70, ADY3 and
CC ADY4. Probable component of a spindle pole boby (SPB) complex composed
CC of ADY3, SSP1, DON1, MPC54, SPO21/MPC70, NUD1 and CNM67.
CC {ECO:0000269|PubMed:10899120, ECO:0000269|PubMed:11101520,
CC ECO:0000269|PubMed:11742972, ECO:0000269|PubMed:11973299,
CC ECO:0000269|PubMed:12796288, ECO:0000269|PubMed:9571234}.
CC -!- INTERACTION:
CC P32336; Q08550: MPC54; NbExp=2; IntAct=EBI-12361, EBI-34513;
CC P32336; Q12411: SPO21; NbExp=3; IntAct=EBI-12361, EBI-36275;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body {ECO:0000269|PubMed:10330408}. Nucleus
CC envelope {ECO:0000269|PubMed:10330408}. Note=Localizes to the meiotic
CC outer plaque of the SPB, at the end of the meiotic spindles.
CC -!- PTM: Phosphorylated from S/G2 phase until the end of mitosis.
CC {ECO:0000269|PubMed:11101520}.
CC -!- MISCELLANEOUS: Present with 892 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X62147; CAA44073.1; -; Genomic_DNA.
DR EMBL; Z75281; CAA99704.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11132.1; -; Genomic_DNA.
DR PIR; S67285; S67285.
DR RefSeq; NP_015018.3; NM_001183793.3.
DR AlphaFoldDB; P32336; -.
DR SMR; P32336; -.
DR BioGRID; 34756; 47.
DR DIP; DIP-2448N; -.
DR IntAct; P32336; 20.
DR MINT; P32336; -.
DR STRING; 4932.YOR373W; -.
DR iPTMnet; P32336; -.
DR MaxQB; P32336; -.
DR PaxDb; P32336; -.
DR PRIDE; P32336; -.
DR EnsemblFungi; YOR373W_mRNA; YOR373W; YOR373W.
DR GeneID; 854555; -.
DR KEGG; sce:YOR373W; -.
DR SGD; S000005900; NUD1.
DR VEuPathDB; FungiDB:YOR373W; -.
DR eggNOG; KOG0531; Eukaryota.
DR HOGENOM; CLU_340727_0_0_1; -.
DR InParanoid; P32336; -.
DR OMA; TNTFKRH; -.
DR BioCyc; YEAST:G3O-33841-MON; -.
DR PRO; PR:P32336; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; P32336; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0061499; C:outer plaque of mitotic spindle pole body; IDA:SGD.
DR GO; GO:0043014; F:alpha-tubulin binding; IBA:GO_Central.
DR GO; GO:0045504; F:dynein heavy chain binding; IBA:GO_Central.
DR GO; GO:0035591; F:signaling adaptor activity; IMP:SGD.
DR GO; GO:0030953; P:astral microtubule organization; IMP:SGD.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051293; P:establishment of spindle localization; IMP:SGD.
DR GO; GO:0000073; P:initial mitotic spindle pole body separation; IMP:SGD.
DR GO; GO:0045132; P:meiotic chromosome segregation; IMP:SGD.
DR GO; GO:0031536; P:positive regulation of exit from mitosis; IMP:SGD.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR PROSITE; PS51450; LRR; 9.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Isopeptide bond;
KW Leucine-rich repeat; Meiosis; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..851
FT /note="Protein NUD1"
FT /id="PRO_0000057981"
FT REPEAT 544..566
FT /note="LRR 1"
FT REPEAT 567..588
FT /note="LRR 2"
FT REPEAT 589..609
FT /note="LRR 3"
FT REPEAT 621..642
FT /note="LRR 4"
FT REPEAT 643..664
FT /note="LRR 5"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 388
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 392
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CROSSLNK 357
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 5..6
FT /note="TQ -> SE (in Ref. 2; CAA44073)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 851 AA; 94104 MW; CB9F0408633C1315 CRC64;
MDMDTQEAEL SSQLENLTIN SPRKLRSNAH SNSGKVFKEY ESNHDFQDSN FTSQVVEPAI
SDSVKKPPTM TVLNNYSTVH QKVPSGFSGT TATSHQEAQW KQYFPGIGSG GGTNFGGAVG
TANKVPESDL IVSDLVKDLS GVLETNTFKR HLDMKNKTTT MQTHENHDTI SISHSKDFFN
AEKVSSSFSD DSDSGPAAEA HDVFDGILQK QKSNYLVGSY PSNSNNKNNN NNNNNNNNNS
ININNKDNAR TKEEDEEDTS NSFEFSSSSS MSSSQTQSGR KSKVLKKPPL NTISPGQLGY
QFNHTHGAWD PPLNQGLDVS SSHSLDNTSS NQSQFATMVP TGDNHTNGKA PSILDKKAYE
LTSTKPGDVG YRQKKIQEEE NLANSDDTPL DTPKFNDLFT KNGTRAKVKG QMRTSRSISN
SNLLEAHKKL KTFPAERVED ITSISEVNTS FNETEKQLIS ILTSKLSGSP SYDSDWEKIL
KVDLSRGKLK NMFGMQRLLP NVLVLNLSDN EMNTLEGIPS NVVQLFCSNN KITSAHCSLA
GFHDLECLDL SYNLLNTSLK FLSLCHHLQE VNLSYNSIQS LEGIGSSRMK KLNLSNNEIN
GIIDFEQLIL TNNSVVGGWL TVEVLDLSNN NIIGVRNINC LPRLKVLNLN GNPLVSIVES
SKMENGTLRA LSIKNTGGAL SKLQNYKLDD QFTFPYQNLK ILKLDGFAQL SKWQKWPATL
QILEINGGLA SSLPRFSSLK STNLYSLTIA NVRDFTHLPV DLSKELPFLQ ELHLPGNNLQ
NAHKLTKTLP RQSVKFLDLR NNPITTPRHD RASTSLHYRQ LLQLAGLCQQ QCPALATLWL
DDTPAPTATN L
