NDC80_YEAST
ID NDC80_YEAST Reviewed; 691 AA.
AC P40460; D6VVE3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Kinetochore protein NDC80 {ECO:0000303|PubMed:11179222};
DE AltName: Full=80 kDa spindle component protein {ECO:0000303|PubMed:2229181};
DE AltName: Full=Nuclear division cycle protein 80 {ECO:0000303|PubMed:9585415};
DE AltName: Full=Two-hybrid interaction with DMC1 protein 3 {ECO:0000303|PubMed:9335591};
GN Name=NDC80 {ECO:0000303|PubMed:9585415};
GN Synonyms=HEC1 {ECO:0000303|PubMed:10409732},
GN TID3 {ECO:0000303|PubMed:9335591};
GN OrderedLocusNames=YIL144W {ECO:0000312|SGD:S000001406};
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=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(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 SUBCELLULAR LOCATION.
RX PubMed=2229181; DOI=10.1083/jcb.111.5.1913;
RA Rout M.P., Kilmartin J.V.;
RT "Components of the yeast spindle and spindle pole body.";
RL J. Cell Biol. 111:1913-1927(1990).
RN [4]
RP INTERACTION WITH DMC1.
RX PubMed=9335591; DOI=10.1093/genetics/147.2.533;
RA Dresser M.E., Ewing D.J., Conrad M.N., Dominguez A.M., Barstead R.,
RA Jiang H., Kodadek T.;
RT "DMC1 functions in a Saccharomyces cerevisiae meiotic pathway that is
RT largely independent of the RAD51 pathway.";
RL Genetics 147:533-544(1997).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND SUBCELLULAR LOCATION.
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SMC1 AND SMC2.
RX PubMed=10409732; DOI=10.1128/mcb.19.8.5417;
RA Zheng L., Chen Y., Lee W.-H.;
RT "Hec1p, an evolutionarily conserved coiled-coil protein, modulates
RT chromosome segregation through interaction with SMC proteins.";
RL Mol. Cell. Biol. 19:5417-5428(1999).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH SPC24 AND SPC25.
RX PubMed=11179222; DOI=10.1093/emboj/20.4.777;
RA Janke C., Ortiz J., Lechner J., Shevchenko A., Shevchenko A., Magiera M.M.,
RA Schramm C., Schiebel E.;
RT "The budding yeast proteins Spc24p and Spc25p interact with Ndc80p and
RT Nuf2p at the kinetochore and are important for kinetochore clustering and
RT checkpoint control.";
RL EMBO J. 20:777-791(2001).
RN [8]
RP FUNCTION OF THE NDC80 COMPLEX, SUBCELLULAR LOCATION, AND IDENTIFICATION IN
RP THE NDC80 COMPLEX.
RX PubMed=11266451; DOI=10.1083/jcb.152.2.349;
RA Wigge P.A., Kilmartin J.V.;
RT "The Ndc80p complex from Saccharomyces cerevisiae contains conserved
RT centromere components and has a function in chromosome segregation.";
RL J. Cell Biol. 152:349-360(2001).
RN [9]
RP INTERACTION WITH KIN3, AND MUTAGENESIS OF SER-201.
RX PubMed=12386167; DOI=10.1074/jbc.m207069200;
RA Chen Y., Riley D.J., Zheng L., Chen P.-L., Lee W.-H.;
RT "Phosphorylation of the mitotic regulator protein Hec1 by Nek2 kinase is
RT essential for faithful chromosome segregation.";
RL J. Biol. Chem. 277:49408-49416(2002).
RN [10]
RP INTERACTION WITH SPC24 AND SPC25.
RX PubMed=11952896; DOI=10.1046/j.1365-2958.2002.02844.x;
RA Le Masson I., Saveanu C., Chevalier A., Namane A., Gobin R.,
RA Fromont-Racine M., Jacquier A., Mann C.;
RT "Spc24 interacts with Mps2 and is required for chromosome segregation, but
RT is not implicated in spindle pole body duplication.";
RL Mol. Microbiol. 43:1431-1443(2002).
RN [11]
RP FUNCTION OF THE NDC80 COMPLEX.
RX PubMed=12514103; DOI=10.1101/gad.1040903;
RA McCleland M.L., Gardner R.D., Kallio M.J., Daum J.R., Gorbsky G.J.,
RA Burke D.J., Stukenberg P.T.;
RT "The highly conserved Ndc80 complex is required for kinetochore assembly,
RT chromosome congression, and spindle checkpoint activity.";
RL Genes Dev. 17:101-114(2003).
RN [12]
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 [13]
RP IDENTIFICATION IN THE NDC80 COMPLEX.
RX PubMed=15371542; DOI=10.1091/mbc.e04-06-0443;
RA Kerres A., Vietmeier-Decker C., Ortiz J., Karig I., Beuter C., Hegemann J.,
RA Lechner J., Fleig U.;
RT "The fission yeast kinetochore component Spc7 associates with the EB1
RT family member Mal3 and is required for kinetochore-spindle association.";
RL Mol. Biol. Cell 15:5255-5267(2004).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-248, 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).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-38, AND IDENTIFICATION BY
RP 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 [16]
RP 3D-STRUCTURE MODELING OF THE NDC80 COMPLEX.
RX PubMed=15809444; DOI=10.1073/pnas.0501168102;
RA Wei R.R., Sorger P.K., Harrison S.C.;
RT "Molecular organization of the Ndc80 complex, an essential kinetochore
RT component.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:5363-5367(2005).
CC -!- FUNCTION: Acts as a component of the essential kinetochore-associated
CC NDC80 complex, which is involved in chromosome segregation and spindle
CC checkpoint activity. {ECO:0000269|PubMed:10409732,
CC ECO:0000269|PubMed:11266451, ECO:0000269|PubMed:12514103,
CC ECO:0000269|PubMed:9585415}.
CC -!- SUBUNIT: Component of the NDC80 complex, which consists of NDC80, NUF2,
CC SPC24 and SPC25. The NDC80 complex is formed by two subcomplexes,
CC NDC80-NUF2 and SPC24-SPC25, which are joined end-to-end through their
CC coiled-coil domains. It has a rod-like structure with a length of 570
CC Angstroms and globular domains at either end. The NDC80-NUF2 globular
CC domains are probably directed to microtubules, the SPC24-SPC25 globular
CC domains to the centromere. NDC80 probably interacts with SMC1 and SMC2.
CC Also interacts with KIN3. Interacts with DMC1.
CC {ECO:0000269|PubMed:10409732, ECO:0000269|PubMed:11179222,
CC ECO:0000269|PubMed:11266451, ECO:0000269|PubMed:11952896,
CC ECO:0000269|PubMed:12386167, ECO:0000269|PubMed:15371542,
CC ECO:0000269|PubMed:9335591}.
CC -!- INTERACTION:
CC P40460; P53267: DAM1; NbExp=4; IntAct=EBI-25247, EBI-23268;
CC P40460; P54199: MPS1; NbExp=4; IntAct=EBI-25247, EBI-11224;
CC P40460; P40460: NDC80; NbExp=4; IntAct=EBI-25247, EBI-25247;
CC P40460; P33895: NUF2; NbExp=15; IntAct=EBI-25247, EBI-12377;
CC P40460; P53148: SPC105; NbExp=2; IntAct=EBI-25247, EBI-23870;
CC P40460; Q04477: SPC24; NbExp=19; IntAct=EBI-25247, EBI-27228;
CC P40460; P40014: SPC25; NbExp=13; IntAct=EBI-25247, EBI-22458;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore.
CC Note=Associated with kinetochores.
CC -!- MISCELLANEOUS: Present with 1160 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NDC80/HEC1 family. {ECO:0000305}.
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; Z38059; CAA86134.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08409.1; -; Genomic_DNA.
DR PIR; S48390; S48390.
DR RefSeq; NP_012122.3; NM_001179492.3.
DR PDB; 5TCS; X-ray; 2.83 A; A=114-318, A=621-689.
DR PDB; 5TD8; X-ray; 7.53 A; A=114-368, A=621-691.
DR PDB; 7KDF; X-ray; 2.72 A; A=114-689.
DR PDBsum; 5TCS; -.
DR PDBsum; 5TD8; -.
DR PDBsum; 7KDF; -.
DR AlphaFoldDB; P40460; -.
DR SMR; P40460; -.
DR BioGRID; 34848; 308.
DR ComplexPortal; CPX-548; NDC80 complex.
DR DIP; DIP-818N; -.
DR ELM; P40460; -.
DR IntAct; P40460; 42.
DR MINT; P40460; -.
DR STRING; 4932.YIL144W; -.
DR iPTMnet; P40460; -.
DR MaxQB; P40460; -.
DR PaxDb; P40460; -.
DR PRIDE; P40460; -.
DR ABCD; P40460; 1 sequenced antibody.
DR EnsemblFungi; YIL144W_mRNA; YIL144W; YIL144W.
DR GeneID; 854662; -.
DR KEGG; sce:YIL144W; -.
DR SGD; S000001406; NDC80.
DR VEuPathDB; FungiDB:YIL144W; -.
DR eggNOG; KOG0995; Eukaryota.
DR GeneTree; ENSGT00390000018386; -.
DR HOGENOM; CLU_012583_1_2_1; -.
DR InParanoid; P40460; -.
DR OMA; IRFKVHV; -.
DR BioCyc; YEAST:G3O-31394-MON; -.
DR PRO; PR:P40460; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40460; protein.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:SGD.
DR GO; GO:0000776; C:kinetochore; IDA:SGD.
DR GO; GO:0031262; C:Ndc80 complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:SGD.
DR Gene3D; 1.10.418.30; -; 1.
DR InterPro; IPR040967; DUF5595.
DR InterPro; IPR005550; Kinetochore_Ndc80.
DR InterPro; IPR038273; Ndc80_sf.
DR PANTHER; PTHR10643; PTHR10643; 1.
DR Pfam; PF18077; DUF5595; 1.
DR Pfam; PF03801; Ndc80_HEC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW Coiled coil; Kinetochore; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..691
FT /note="Kinetochore protein NDC80"
FT /id="PRO_0000202958"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 376..446
FT /evidence="ECO:0000255"
FT COILED 522..686
FT /evidence="ECO:0000255"
FT COMPBIAS 21..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 38
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 248
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MUTAGEN 201
FT /note="S->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:12386167"
FT HELIX 122..138
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 141..144
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 151..155
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 159..173
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:5TCS"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 215..246
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 249..254
FT /evidence="ECO:0007829|PDB:7KDF"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 267..291
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 298..348
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 351..368
FT /evidence="ECO:0007829|PDB:7KDF"
SQ SEQUENCE 691 AA; 80487 MW; 7DBC492227A80093 CRC64;
MQSSTSTDQH VLHHMDPHRF TSQIPTATSS QLRRRNSTNQ GLTDMINKSI ARNTISGTGI
PTGGINKNKR TRSTVAGGTN GTALALNDKS NSRNSVSRLS INQLGSLQQH LSNRDPRPLR
DKNFQSAIQE EIYDYLKKNK FDIETNHPIS IKFLKQPTQK GFIIIFKWLY LRLDPGYGFT
KSIENEIYQI LKNLRYPFLE SINKSQISAV GGSNWHKFLG MLHWMVRTNI KLDMCLNKVD
RSLINQNTQE ITILSQPLKT LDEQDQRQER YELMVEKLLI DYFTESYKSF LKLEDNYEPS
MQELKLGFEK FVHIINTDIA NLQTQNDNLY EKYQEVMKIS QKIKTTREKW KALKSDSNKY
ENYVNAMKQK SQEWPGKLEK MKSECELKEE EIKALQSNIS ELHKILRKKG ISTEQFELQN
QEREKLTREL DKINIQSDKL TSSIKSRKLE AEGIFKSLLD TLRQYDSSIQ NLTRSRSQLG
HNVNDSSLKI NISENLLDRD FHEGISYEQL FPKGSGINES IKKSILKLND EIQERIKTIE
KDNITLEKDI KNLKHDINEK TQINEKLELE LSEANSKFEL SKQENERLLV AQRIEIEKME
KKINDSNLLM KTKISDAEEL VTSTELKLEE LKVDLNRKRY KLHQQVIHVI DITSKFKINI
QSSLENSENE LGNVIEELRN LEFETEHNVT N
