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 02-SEP-2026, entry version 198. 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}, TID3 GN {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; DOI=10.1038/387s084; 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; P47149: NNF1; NbExp=3; IntAct=EBI-25247, EBI-12098; CC P40460; P33895: NUF2; NbExp=16; IntAct=EBI-25247, EBI-12377; CC P40460; P53148: SPC105; NbExp=2; IntAct=EBI-25247, EBI-23870; CC P40460; Q04477: SPC24; NbExp=20; 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=114-689. DR PDB; 5TD8; X-ray; 7.53 A; A=114-691. DR PDB; 7KDF; X-ray; 2.72 A; A=114-689. DR PDB; 8G0Q; X-ray; 3.22 A; A/C=106-691. DR PDB; 8Q84; EM; 3.15 A; A/F=1-691. DR PDB; 8Q85; EM; 3.97 A; F=1-691. DR PDB; 8QAU; EM; 3.54 A; A=1-691. DR PDB; 8V10; X-ray; 3.02 A; A=114-691. DR PDB; 8V11; X-ray; 3.95 A; A/E=114-684. DR AlphaFoldDB; P40460; -. DR EMDB; EMD-18246; -. DR EMDB; EMD-18247; -. DR EMDB; EMD-18304; -. DR SMR; P40460; -. DR BioGRID; 34848; 333. DR ComplexPortal; CPX-548; NDC80 complex. DR DIP; DIP-818N; -. DR ELM; P40460; -. DR FunCoup; P40460; 400. DR IntAct; P40460; 47. DR MINT; P40460; -. DR STRING; 4932.YIL144W; -. DR iPTMnet; P40460; -. DR PaxDb; 4932-YIL144W; -. DR PeptideAtlas; P40460; -. DR ABCD; P40460; 1 sequenced antibody. DR EnsemblFungi; YIL144W_mRNA; YIL144W; YIL144W. DR GeneID; 854662; -. DR KEGG; sce:YIL144W; -. DR AGR; SGD:S000001406; -. DR SGD; S000001406; NDC80. DR VEuPathDB; FungiDB:YIL144W; -. DR eggNOG; KOG0995; Eukaryota. DR HOGENOM; CLU_012583_1_2_1; -. DR InParanoid; P40460; -. DR OMA; PSHKFQK; -. DR OrthoDB; 7459479at2759; -. DR BioCyc; YEAST:G3O-31394-MONOMER; -. DR BioGRID-ORCS; 854662; 2 hits in 10 CRISPR screens. 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:0000940; C:outer kinetochore; IDA:UniProtKB. 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:0007059; P:chromosome segregation; IMP:SGD. DR GO; GO:1990758; P:mitotic sister chromatid biorientation; IMP:UniProtKB. DR GO; GO:0034501; P:protein localization to kinetochore; IMP:SGD. DR FunFam; 1.10.418.30:FF:000001; Probable kinetochore protein ndc80; 1. DR Gene3D; 6.10.250.1950; -; 1. DR Gene3D; 1.10.418.30; Ncd80 complex, Ncd80 subunit; 1. DR InterPro; IPR040967; DUF5595. DR InterPro; IPR005550; Kinetochore_Ndc80. DR InterPro; IPR055260; Ndc80_CH. DR InterPro; IPR038273; Ndc80_sf. DR PANTHER; PTHR10643; KINETOCHORE PROTEIN NDC80; 1. DR PANTHER; PTHR10643:SF2; KINETOCHORE PROTEIN NDC80 HOMOLOG; 1. DR Pfam; PF18077; DUF5595; 1. DR Pfam; PF03801; Ndc80_HEC; 1. DR PDBsum; 5TCS; -. DR PDBsum; 5TD8; -. DR PDBsum; 7KDF; -. DR PDBsum; 8G0Q; -. DR PDBsum; 8Q84; -. DR PDBsum; 8Q85; -. DR PDBsum; 8QAU; -. DR PDBsum; 8V10; -. DR PDBsum; 8V11; -. 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 10..19 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 20..42 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 54..65 FT /note="Low complexity" 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 HELIX 257..260 FT /evidence="ECO:0007829|PDB:5TCS" 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" FT HELIX 373..392 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 395..408 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 416..478 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 485..488 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 496..498 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 507..510 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 517..521 FT /evidence="ECO:0007829|PDB:8Q84" FT HELIX 632..639 FT /evidence="ECO:0007829|PDB:7KDF" FT HELIX 649..651 FT /evidence="ECO:0007829|PDB:7KDF" FT HELIX 680..683 FT /evidence="ECO:0007829|PDB:8G0Q" 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 //