CENPC_YEAST
ID CENPC_YEAST Reviewed; 549 AA.
AC P35201; D6VXJ9;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Inner kinetochore subunit MIF2 {ECO:0000305};
DE AltName: Full=CENP-C homolog {ECO:0000303|PubMed:22561346};
DE AltName: Full=Constitutive centromere-associated network protein MIF2 {ECO:0000305};
DE AltName: Full=Mitotic fidelity of chromosome transmission protein 2 {ECO:0000303|PubMed:8408221};
GN Name=MIF2; OrderedLocusNames=YKL089W;
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], AND FUNCTION.
RX PubMed=8408221; DOI=10.1083/jcb.123.2.387;
RA Brown M.T., Goetsch L., Hartwell L.H.;
RT "MIF2 is required for mitotic spindle integrity during anaphase spindle
RT elongation in Saccharomyces cerevisiae.";
RL J. Cell Biol. 123:387-403(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
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 CHARACTERIZATION.
RX PubMed=7579695; DOI=10.1091/mbc.6.7.793;
RA Meluh P.B., Koshland D.;
RT "Evidence that the MIF2 gene of Saccharomyces cerevisiae encodes a
RT centromere protein with homology to the mammalian centromere protein CENP-
RT C.";
RL Mol. Biol. Cell 6:793-807(1995).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325, 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 [9]
RP IDENTIFICATION IN CCAN, AND SUBUNIT.
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 IDENTIFICATION BY MASS SPECTROMETRY [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 X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 365-530.
RX PubMed=18701705; DOI=10.1091/mbc.e08-03-0297;
RA Cohen R.L., Espelin C.W., De Wulf P., Sorger P.K., Harrison S.C.,
RA Simons K.T.;
RT "Structural and functional dissection of Mif2p, a conserved DNA-binding
RT kinetochore protein.";
RL Mol. Biol. Cell 19:4480-4491(2008).
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:8408221, PubMed:7579695, PubMed:22561346).
CC {ECO:0000269|PubMed:22561346, ECO:0000269|PubMed:7579695,
CC ECO:0000269|PubMed:8408221}.
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:22561346). Interacts with CBF1 (PubMed:7579695).
CC {ECO:0000269|PubMed:22561346, ECO:0000269|PubMed:7579695}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere. Chromosome,
CC centromere, kinetochore {ECO:0000305|PubMed:22561346}.
CC -!- MISCELLANEOUS: Present with 465 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CENP-C/MIF2 family. {ECO:0000305}.
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DR EMBL; Z18294; CAA79163.1; -; Genomic_DNA.
DR EMBL; Z28089; CAA81927.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09069.1; -; Genomic_DNA.
DR PIR; S37914; S37914.
DR RefSeq; NP_012834.1; NM_001179655.1.
DR PDB; 2VPV; X-ray; 2.70 A; A/B=365-530.
DR PDB; 6QLD; EM; 4.15 A; C=284-305.
DR PDB; 7ON1; EM; 3.35 A; C/D=1-549.
DR PDBsum; 2VPV; -.
DR PDBsum; 6QLD; -.
DR PDBsum; 7ON1; -.
DR AlphaFoldDB; P35201; -.
DR SMR; P35201; -.
DR BioGRID; 34044; 296.
DR DIP; DIP-7297N; -.
DR IntAct; P35201; 4.
DR MINT; P35201; -.
DR STRING; 4932.YKL089W; -.
DR iPTMnet; P35201; -.
DR MaxQB; P35201; -.
DR PaxDb; P35201; -.
DR PRIDE; P35201; -.
DR EnsemblFungi; YKL089W_mRNA; YKL089W; YKL089W.
DR GeneID; 853773; -.
DR KEGG; sce:YKL089W; -.
DR SGD; S000001572; MIF2.
DR VEuPathDB; FungiDB:YKL089W; -.
DR eggNOG; ENOG502S47H; Eukaryota.
DR GeneTree; ENSGT00390000016737; -.
DR HOGENOM; CLU_038087_0_0_1; -.
DR InParanoid; P35201; -.
DR OMA; AKMFFVQ; -.
DR BioCyc; YEAST:G3O-31880-MON; -.
DR EvolutionaryTrace; P35201; -.
DR PRO; PR:P35201; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P35201; protein.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:SGD.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019237; F:centromeric DNA binding; IDA:SGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
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:0051382; P:kinetochore assembly; IMP:SGD.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:SGD.
DR GO; GO:0051455; P:monopolar spindle attachment to meiosis I kinetochore; IBA:GO_Central.
DR DisProt; DP02395; -.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR028386; CENP-C/Mif2/cnp3.
DR InterPro; IPR025974; Mif2/CENP-C_cupin.
DR InterPro; IPR028929; Mif2_N.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR16684; PTHR16684; 1.
DR Pfam; PF11699; CENP-C_C; 1.
DR Pfam; PF15624; Mif2_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
KW DNA-binding; Kinetochore; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..549
FT /note="Inner kinetochore subunit MIF2"
FT /id="PRO_0000096486"
FT DNA_BIND 356..364
FT /note="A.T hook"
FT REGION 47..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..110
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..226
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..243
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..258
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 325
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:7ON1"
FT TURN 447..449
FT /evidence="ECO:0007829|PDB:2VPV"
FT STRAND 453..459
FT /evidence="ECO:0007829|PDB:2VPV"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:2VPV"
FT STRAND 467..470
FT /evidence="ECO:0007829|PDB:2VPV"
FT STRAND 473..489
FT /evidence="ECO:0007829|PDB:2VPV"
FT STRAND 492..497
FT /evidence="ECO:0007829|PDB:2VPV"
FT STRAND 501..504
FT /evidence="ECO:0007829|PDB:2VPV"
FT STRAND 509..514
FT /evidence="ECO:0007829|PDB:2VPV"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:2VPV"
FT STRAND 520..528
FT /evidence="ECO:0007829|PDB:2VPV"
SQ SEQUENCE 549 AA; 62473 MW; A6A4FAC9F6B66EB1 CRC64;
MDYMKLGLKS RKTGIDVKQD IPKDEYSMEN IDDFFKDDET SLISMRRKSR RKSSLFLPST
LNGDTKNVLP PFLQSYKSQD DEVVQSPSGK GDGSRRSSLL SHQSNFLSPA NDFEPIEEEP
EQEENDIRGN DFATPITQKL SKPTYKRKYS TRYSLDTSES PSVRLTPDRI TNKNVYSDVP
DLVADEDDDD RVNTSLNTSD NALLEDELED DGFIPESEED GDYIESDSSL DSGSDSASDS
DGDNTYQEVE EEAEVNTNDN EDDYIRRQAS DVVRTDSIID RNGLRKSTRV KVAPLQYWRN
EKIVYKRKSN KPVLDIDKIV TYDESEDEEE ILAAQRRKKQ KKKPTPTRPY NYVPTGRPRG
RPKKDPNAKE NLIPEDPNED IIERIESGGI ENGEWLKHGI LEANVKISDT KEETKDEIIA
FAPNLSQTEQ VKDTKDENFA LEIMFDKHKE YFASGILKLP AISGQKKLSN SFRTYITFHV
IQGIVEVTVC KNKFLSVKGS TFQIPAFNEY AIANRGNDEA KMFFVQVTVS EDANDDNDKE
LDSTFDTFG
