CENPT_YEAST
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 03-AUG-2022, entry version 152.
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}.
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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 PDBsum; 4GEQ; -.
DR PDBsum; 6WUC; -.
DR PDBsum; 6YPC; -.
DR AlphaFoldDB; P43618; -.
DR SMR; P43618; -.
DR BioGRID; 31204; 135.
DR DIP; DIP-5186N; -.
DR IntAct; P43618; 5.
DR MINT; P43618; -.
DR STRING; 4932.YFR046C; -.
DR iPTMnet; P43618; -.
DR PaxDb; P43618; -.
DR PRIDE; P43618; -.
DR EnsemblFungi; YFR046C_mRNA; YFR046C; YFR046C.
DR GeneID; 850607; -.
DR KEGG; sce:YFR046C; -.
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 BioCyc; YEAST:G3O-30493-MON; -.
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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IPI:SGD.
DR GO; GO:1901720; P:negative regulation of NMS complex 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
