ID CENPT_YEAST Reviewed; 361 AA. AC P43618; D6VTS9; Q6B2K8; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 159. DE RecName: Full=Inner kinetochore subunit CNN1 {ECO:0000305}; DE AltName: Full=CENP-T homolog {ECO:0000303|PubMed:22561346}; DE AltName: Full=Co-purified with NNF1 protein 1; DE AltName: Full=Constitutive centromere-associated network protein CNN1 {ECO:0000305}; GN Name=CNN1; OrderedLocusNames=YFR046C; 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]. RC STRAIN=ATCC 204511 / S288c / AB972; RX PubMed=8686379; RX DOI=10.1002/(sici)1097-0061(199602)12:2<149::aid-yea893>3.0.co;2-g; RA Eki T., Naitou M., Hagiwara H., Ozawa M., Sasanuma S., Sasanuma M., RA Tsuchiya Y., Shibata T., Hanaoka F., Murakami Y.; RT "Analysis of a 36.2 kb DNA sequence including the right telomere of RT chromosome VI from Saccharomyces cerevisiae."; RL Yeast 12:149-167(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7670463; DOI=10.1038/ng0795-261; RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., RA Eki T.; RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces RT cerevisiae."; RL Nat. Genet. 10:261-268(1995). 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [5] RP INTERACTION WITH NNF1, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=14633972; DOI=10.1101/gad.1144403; RA De Wulf P., McAinsh A.D., Sorger P.K.; RT "Hierarchical assembly of the budding yeast kinetochore from multiple RT subcomplexes."; RL Genes Dev. 17:2902-2921(2003). RN [6] 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 [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 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 [9] RP IDENTIFICATION IN CCAN, SUBUNIT, AND INTERACTION WITH SPC24 AND SPC25. RX PubMed=22561346; DOI=10.1038/ncb2493; RA Schleiffer A., Maier M., Litos G., Lampert F., Hornung P., Mechtler K., RA Westermann S.; RT "CENP-T proteins are conserved centromere receptors of the Ndc80 complex."; RL Nat. Cell Biol. 14:604-613(2012). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 60-84 IN COMPLEX WITH SPC24 AND RP SPC25, PHOSPHORYLATION AT SER-2; THR-14; SER-17; THR-21; THR-42; SER-50; RP SER-52; THR-53; SER-55; SER-74; THR-86; THR-88; THR-91; SER-115; THR-129; RP THR-134; SER-135; THR-139; SER-153; THR-174; SER-177; THR-191; SER-192 AND RP SER-268, AND MUTAGENESIS OF SER-74. RX PubMed=23334295; DOI=10.1038/emboj.2012.356; RA Malvezzi F., Litos G., Schleiffer A., Heuck A., Mechtler K., Clausen T., RA Westermann S.; RT "A structural basis for kinetochore recruitment of the Ndc80 complex via RT two distinct centromere receptors."; RL EMBO J. 32:409-423(2013). CC -!- FUNCTION: Component of the kinetochore, a multiprotein complex that CC assembles on centromeric DNA and attaches chromosomes to spindle CC microtubules, mediating chromosome segregation and sister chromatid CC segregation during meiosis and mitosis. Component of the inner CC kinetochore constitutive centromere-associated network (CCAN), which CC serves as a structural platform for outer kinetochore assembly CC (PubMed:22561346). CNN1 is important for the recruitment of the outer CC kinetochore Ndc80 complex (PubMed:23334295). CC {ECO:0000269|PubMed:22561346, ECO:0000269|PubMed:23334295}. CC -!- SUBUNIT: Component of the inner kinetochore constitutive centromere- CC associated network (CCAN) (also known as central kinetochore CTF19 CC complex in yeast), which is composed of at least AME1, CHL4, CNN1, CC CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1, MHF2, MIF2, NKP1, NKP2, CC OKP1 and WIP1 (PubMed:14633972, PubMed:22561346). Interacts with outer CC kinetochore MIND complex subunit NNF1 (PubMed:14633972). Interacts with CC outer kinetochore Ndc80 complex subunits SPC24 and SPC25 CC (PubMed:22561346, PubMed:23334295). {ECO:0000269|PubMed:14633972, CC ECO:0000269|PubMed:22561346, ECO:0000269|PubMed:23334295}. CC -!- INTERACTION: CC P43618; P33895: NUF2; NbExp=2; IntAct=EBI-23036, EBI-12377; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. CC Chromosome, centromere, kinetochore {ECO:0000305|PubMed:22561346}. CC -!- PTM: Phosphorylation of the C-ter by MPS1 kinase regulates interaction CC with the outer kinetochore Ndc80 complex. CC {ECO:0000269|PubMed:23334295}. CC -!- MISCELLANEOUS: Present with 1300 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the CENP-T/CNN1 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; D50617; BAA09285.1; -; Genomic_DNA. DR EMBL; AY692722; AAT92741.1; -; Genomic_DNA. DR EMBL; BK006940; DAA12489.1; -; Genomic_DNA. DR PIR; S56301; S56301. DR RefSeq; NP_116704.1; NM_001180011.1. DR PDB; 4GEQ; X-ray; 2.01 A; E/F=60-84. DR PDB; 6WUC; EM; 3.23 A; T=1-361. DR PDB; 6YPC; X-ray; 2.90 A; T=1-361. DR PDB; 8OVW; EM; 3.40 A; T=1-361. DR PDB; 8OW0; EM; 3.40 A; T=1-361. DR PDB; 8OW1; EM; 3.70 A; T/TT=1-361. DR PDBsum; 4GEQ; -. DR PDBsum; 6WUC; -. DR PDBsum; 6YPC; -. DR PDBsum; 8OVW; -. DR PDBsum; 8OW0; -. DR PDBsum; 8OW1; -. DR AlphaFoldDB; P43618; -. DR EMDB; EMD-17224; -. DR EMDB; EMD-17226; -. DR EMDB; EMD-17227; -. DR EMDB; EMD-21910; -. DR SMR; P43618; -. DR BioGRID; 31204; 140. DR ComplexPortal; CPX-2533; Kinetochore CCAN complex. DR DIP; DIP-5186N; -. DR IntAct; P43618; 5. DR MINT; P43618; -. DR STRING; 4932.YFR046C; -. DR iPTMnet; P43618; -. DR PaxDb; 4932-YFR046C; -. DR PeptideAtlas; P43618; -. DR EnsemblFungi; YFR046C_mRNA; YFR046C; YFR046C. DR GeneID; 850607; -. DR KEGG; sce:YFR046C; -. DR AGR; SGD:S000001942; -. DR SGD; S000001942; CNN1. DR VEuPathDB; FungiDB:YFR046C; -. DR eggNOG; ENOG502S7KF; Eukaryota. DR HOGENOM; CLU_070156_0_0_1; -. DR InParanoid; P43618; -. DR OMA; XTEVSEI; -. DR OrthoDB; 2036976at2759; -. DR BioCyc; YEAST:G3O-30493-MONOMER; -. DR BioGRID-ORCS; 850607; 7 hits in 10 CRISPR screens. DR PRO; PR:P43618; -. DR Proteomes; UP000002311; Chromosome VI. DR RNAct; P43618; Protein. DR GO; GO:0000776; C:kinetochore; IDA:SGD. DR GO; GO:0005634; C:nucleus; HDA:SGD. DR GO; GO:0019237; F:centromeric DNA binding; IDA:SGD. DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0007059; P:chromosome segregation; IPI:SGD. DR GO; GO:1905560; P:negative regulation of kinetochore assembly; IMP:SGD. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome; KW Kinetochore; Mitosis; Nucleus; Phosphoprotein; Reference proteome. FT CHAIN 1..361 FT /note="Inner kinetochore subunit CNN1" FT /id="PRO_0000202697" FT REGION 1..22 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 65..79 FT /note="Required for interaction with SPC24-SPC25" FT /evidence="ECO:0000269|PubMed:22561346" FT REGION 103..132 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 193..255 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..17 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 221..250 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 14 FT /note="Phosphothreonine; by CDK1 and MPS1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 17 FT /note="Phosphoserine; by CDK1 and MPS1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 21 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 42 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 50 FT /note="Phosphoserine; by CDK1 and MPS1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 52 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 53 FT /note="Phosphothreonine; by MPS1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 55 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 74 FT /note="Phosphoserine; by CDK1 and MPS1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 86 FT /note="Phosphothreonine; by MPS1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 88 FT /note="Phosphothreonine; by MPS1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 91 FT /note="Phosphothreonine; by CDK1 and MPS1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 115 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 129 FT /note="Phosphothreonine; by CDK1 and MPS1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 134 FT /note="Phosphothreonine; by MPS1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 135 FT /note="Phosphoserine; by MPS1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 139 FT /note="Phosphothreonine; by CDK1 and MPS1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 153 FT /note="Phosphoserine; by MPS1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 174 FT /note="Phosphothreonine; by MPS1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 177 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 191 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 192 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:23334295" FT MOD_RES 268 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:23334295" FT MUTAGEN 74 FT /note="S->A: Increases interaction with SPC24-SPC25." FT /evidence="ECO:0000269|PubMed:23334295" FT MUTAGEN 74 FT /note="S->D: Abolishes interaction with SPC24-SPC25." FT /evidence="ECO:0000269|PubMed:23334295" FT CONFLICT 8 FT /note="A -> T (in Ref. 2; AAT92741)" FT /evidence="ECO:0000305" FT HELIX 63..78 FT /evidence="ECO:0007829|PDB:4GEQ" FT HELIX 275..281 FT /evidence="ECO:0007829|PDB:6YPC" FT HELIX 283..288 FT /evidence="ECO:0007829|PDB:6YPC" FT HELIX 295..315 FT /evidence="ECO:0007829|PDB:6YPC" FT HELIX 323..330 FT /evidence="ECO:0007829|PDB:6YPC" FT HELIX 337..347 FT /evidence="ECO:0007829|PDB:6YPC" FT HELIX 350..359 FT /evidence="ECO:0007829|PDB:6YPC" SQ SEQUENCE 361 AA; 41313 MW; 48CEEC087A056D42 CRC64; MSTPRKAAGN NENTEVSEIR TPFRERALEE QRLKDEVLIR NTPGYRKLLS ASTKSHDILN KDPNEVRSFL QDLSQVLARK SQGNDTTTNK TQARNLIDEL AYEESQPEEN ELLRSRSEKL TDNNIGNETQ PDYTSLSQTV FAKLQERDKG LKSRKIDPII IQDVPTTGHE DELTVHSPDK ANSISMEVLR TSPSIGMDQV DEPPVRDPVP ISITQQEEPL SEDLPSDDKE ETEEAENEDY SFENTSDENL DDIGNDPIRL NVPAVRRSSI KPLQIMDLKH LTRQFLNENR IILPKQTWST IQEESLNIMD FLKQKIGTLQ KQELVDSFID MGIINNVDDM FELAHELLPL ELQSRIESYL F //