SPC24_YEAST
ID SPC24_YEAST Reviewed; 213 AA.
AC Q04477; D6VZU0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Kinetochore protein SPC24;
GN Name=SPC24; OrderedLocusNames=YMR117C; ORFNames=YM9718.16C;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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, AND INTERACTION WITH TID3 AND NUF2.
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 [4]
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 [5]
RP FUNCTION, INTERACTION WITH MPS2; NDC80 AND SPC25, AND SUBCELLULAR LOCATION.
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 [6]
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 [7]
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 [8]
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 [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
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:11266451,
CC ECO:0000269|PubMed:11952896, ECO:0000269|PubMed:12514103}.
CC -!- SUBUNIT: Component of the NDC80 complex, which consists of TID3/NDC80,
CC NUF2, SPC24 and SPC25. The NDC80 complex is formed by two subcomplexes,
CC TID3/NDC80-NUF2 and SPC24-SPC25, which are joined end-to-end through
CC their coiled-coil domains. It has a rod-like structure with a length of
CC 570 Angstroms and globular domains at either end. The TID3/NDC80-NUF2
CC globular domains are probably directed to microtubules, the SPC24-SPC25
CC globular domains to the centromere. Can also interact with MPS2.
CC {ECO:0000269|PubMed:11266451, ECO:0000269|PubMed:15371542}.
CC -!- INTERACTION:
CC Q04477; P32468: CDC12; NbExp=3; IntAct=EBI-27228, EBI-4182;
CC Q04477; Q06324: MMR1; NbExp=3; IntAct=EBI-27228, EBI-37386;
CC Q04477; P53159: MPS2; NbExp=8; IntAct=EBI-27228, EBI-23834;
CC Q04477; P40460: NDC80; NbExp=19; IntAct=EBI-27228, EBI-25247;
CC Q04477; P33895: NUF2; NbExp=8; IntAct=EBI-27228, EBI-12377;
CC Q04477; Q04477: SPC24; NbExp=3; IntAct=EBI-27228, EBI-27228;
CC Q04477; P40014: SPC25; NbExp=23; IntAct=EBI-27228, EBI-22458;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11179222,
CC ECO:0000269|PubMed:11266451, ECO:0000269|PubMed:11952896}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:11179222,
CC ECO:0000269|PubMed:11266451, ECO:0000269|PubMed:11952896}.
CC Note=Associated with kinetochores. {ECO:0000269|PubMed:11179222,
CC ECO:0000269|PubMed:11266451, ECO:0000269|PubMed:11952896}.
CC -!- MISCELLANEOUS: Present with 1750 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the SPC24 family. {ECO:0000305}.
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DR EMBL; Z49702; CAA89755.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10014.1; -; Genomic_DNA.
DR PIR; S54579; S54579.
DR RefSeq; NP_013835.1; NM_001182617.1.
DR PDB; 2FTX; X-ray; 1.90 A; B=154-213.
DR PDB; 2FV4; NMR; -; B=138-213.
DR PDB; 4GEQ; X-ray; 2.01 A; B/D=155-213.
DR PDB; 5T6J; X-ray; 1.75 A; A=155-213.
DR PDB; 5TCS; X-ray; 2.83 A; C=1-213.
DR PDB; 5TD8; X-ray; 7.53 A; C=1-213.
DR PDB; 7KDF; X-ray; 2.72 A; C=1-213.
DR PDBsum; 2FTX; -.
DR PDBsum; 2FV4; -.
DR PDBsum; 4GEQ; -.
DR PDBsum; 5T6J; -.
DR PDBsum; 5TCS; -.
DR PDBsum; 5TD8; -.
DR PDBsum; 7KDF; -.
DR AlphaFoldDB; Q04477; -.
DR SMR; Q04477; -.
DR BioGRID; 35293; 549.
DR ComplexPortal; CPX-548; NDC80 complex.
DR DIP; DIP-893N; -.
DR IntAct; Q04477; 83.
DR MINT; Q04477; -.
DR STRING; 4932.YMR117C; -.
DR iPTMnet; Q04477; -.
DR MaxQB; Q04477; -.
DR PaxDb; Q04477; -.
DR PRIDE; Q04477; -.
DR EnsemblFungi; YMR117C_mRNA; YMR117C; YMR117C.
DR GeneID; 855144; -.
DR KEGG; sce:YMR117C; -.
DR SGD; S000004723; SPC24.
DR VEuPathDB; FungiDB:YMR117C; -.
DR eggNOG; ENOG502S3GS; Eukaryota.
DR HOGENOM; CLU_095757_0_0_1; -.
DR InParanoid; Q04477; -.
DR OMA; FKTKYIW; -.
DR BioCyc; YEAST:G3O-32812-MON; -.
DR EvolutionaryTrace; Q04477; -.
DR PRO; PR:Q04477; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04477; protein.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0098653; P:centromere clustering; IMP:SGD.
DR GO; GO:0007059; P:chromosome segregation; IMP:SGD.
DR Gene3D; 3.30.160.430; -; 1.
DR InterPro; IPR013252; Ndc80_Spc24.
DR InterPro; IPR038066; Spc24_Fungi_globular_sf.
DR PANTHER; PTHR22142; PTHR22142; 1.
DR Pfam; PF08286; Spc24; 1.
DR SUPFAM; SSF143026; SSF143026; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell cycle; Cell division; Centromere;
KW Chromosome; Coiled coil; Kinetochore; Mitosis; Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..213
FT /note="Kinetochore protein SPC24"
FT /id="PRO_0000203294"
FT COILED 54..123
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 11..20
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 24..48
FT /evidence="ECO:0007829|PDB:7KDF"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:5T6J"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:5T6J"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:5T6J"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:5T6J"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:7KDF"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:5T6J"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:2FV4"
FT HELIX 200..211
FT /evidence="ECO:0007829|PDB:5T6J"
SQ SEQUENCE 213 AA; 24604 MW; 8BE4B8619DD4C8FB CRC64;
MSQKDNLLDN PVEFLKEVRE SFDIQQDVDA MKRIRHDLDV IKEESEARIS KEHSKVSESN
KKLNAERINV AKLEGDLEYT NEESNEFGSK DELVKLLKDL DGLERNIVSL RSELDEKMKL
YLKDSEIIST PNGSKIKAKV IEPELEEQSA VTPEANENIL KLKLYRSLGV ILDLENDQVL
INRKNDGNID ILPLDNNLSD FYKTKYIWER LGK
