CENPS_YEAST
ID CENPS_YEAST Reviewed; 90 AA.
AC Q3E835; D6W1Y2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Inner kinetochore subunit MHF1 {ECO:0000305};
DE AltName: Full=CENP-S homolog {ECO:0000303|PubMed:22561346};
DE AltName: Full=Constitutive centromere-associated network protein MHF1 {ECO:0000305};
DE AltName: Full=MHF histone-fold complex subunit 1 {ECO:0000305|PubMed:20347428};
DE AltName: Full=MPH1-associated histone-fold protein 1 {ECO:0000303|PubMed:20347428};
GN Name=MHF1 {ECO:0000303|PubMed:20347428};
GN OrderedLocusNames=YOL086W-A {ECO:0000312|SGD:S000007626};
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=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(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 GENOME REANNOTATION.
RX PubMed=11152879; DOI=10.1016/s0014-5793(00)02275-4;
RA Blandin G., Durrens P., Tekaia F., Aigle M., Bolotin-Fukuhara M., Bon E.,
RA Casaregola S., de Montigny J., Gaillardin C., Lepingle A., Llorente B.,
RA Malpertuy A., Neuveglise C., Ozier-Kalogeropoulos O., Perrin A., Potier S.,
RA Souciet J.-L., Talla E., Toffano-Nioche C., Wesolowski-Louvel M., Marck C.,
RA Dujon B.;
RT "Genomic exploration of the hemiascomycetous yeasts: 4. The genome of
RT Saccharomyces cerevisiae revisited.";
RL FEBS Lett. 487:31-36(2000).
RN [4]
RP FUNCTION, AND INTERACTION WITH MHF2.
RX PubMed=20347428; DOI=10.1016/j.molcel.2010.01.039;
RA Yan Z., Delannoy M., Ling C., Daee D., Osman F., Muniandy P.A., Shen X.,
RA Oostra A.B., Du H., Steltenpool J., Lin T., Schuster B., Decaillet C.,
RA Stasiak A., Stasiak A.Z., Stone S., Hoatlin M.E., Schindler D.,
RA Woodcock C.L., Joenje H., Sen R., de Winter J.P., Li L., Seidman M.M.,
RA Whitby M.C., Myung K., Constantinousend A., Wang W.;
RT "A histone-fold complex and FANCM form a conserved DNA-remodeling complex
RT to maintain genome stability.";
RL Mol. Cell 37:865-878(2010).
RN [5]
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 [6]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF ASP-55;
RP HIS-62 AND 78-ARG-LYS-79.
RX PubMed=22325783; DOI=10.1016/j.str.2011.12.012;
RA Yang H., Zhang T., Tao Y., Wu L., Li H.T., Zhou J.Q., Zhong C., Ding J.;
RT "Saccharomyces cerevisiae MHF complex structurally resembles the histones
RT (H3-H4)(2) heterotetramer and functions as a heterotetramer.";
RL Structure 20:364-370(2012).
CC -!- FUNCTION: dsDNA-binding component of a FANCM-MHF complex involved in
CC DNA damage repair and genome maintenance (PubMed:20347428). FANCM-MHF
CC promotes gene conversion at blocked replication forks, probably by
CC reversal of the stalled fork (By similarity). Component of the
CC kinetochore, a multiprotein complex that assembles on centromeric DNA
CC and attaches chromosomes to spindle microtubules, mediating chromosome
CC segregation and sister chromatid segregation during meiosis and
CC mitosis. Component of the inner kinetochore constitutive centromere-
CC associated network (CCAN), which serves as a structural platform for
CC outer kinetochore assembly (PubMed:22561346).
CC {ECO:0000250|UniProtKB:O74896, ECO:0000269|PubMed:20347428,
CC ECO:0000269|PubMed:22561346}.
CC -!- SUBUNIT: The MHF histone-fold complex is a heterotetramer of 2 MHF1-
CC MHF2 heterodimers. Together with MPH1/FANCM, forms the FANCM-MHF
CC complex. 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 (Probable). {ECO:0000269|PubMed:22325783,
CC ECO:0000305|PubMed:22561346}.
CC -!- INTERACTION:
CC Q3E835; Q3E829: MHF2; NbExp=3; IntAct=EBI-2881690, EBI-15968870;
CC -!- SIMILARITY: Belongs to the TAF9 family. CENP-S/MHF1 subfamily.
CC {ECO:0000305}.
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DR EMBL; Z74828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006948; DAA10698.1; -; Genomic_DNA.
DR RefSeq; NP_076910.1; NM_001184492.1.
DR PDB; 3V9R; X-ray; 2.40 A; A/C=1-90.
DR PDBsum; 3V9R; -.
DR AlphaFoldDB; Q3E835; -.
DR SMR; Q3E835; -.
DR BioGRID; 34316; 19.
DR DIP; DIP-59641N; -.
DR IntAct; Q3E835; 2.
DR STRING; 4932.YOL086W-A; -.
DR MaxQB; Q3E835; -.
DR PaxDb; Q3E835; -.
DR PRIDE; Q3E835; -.
DR EnsemblFungi; YOL086W-A_mRNA; YOL086W-A; YOL086W-A.
DR GeneID; 854067; -.
DR KEGG; sce:YOL086W-A; -.
DR SGD; S000007626; MHF1.
DR VEuPathDB; FungiDB:YOL086W-A; -.
DR eggNOG; ENOG502S7WI; Eukaryota.
DR HOGENOM; CLU_100369_3_1_1; -.
DR InParanoid; Q3E835; -.
DR OMA; MVWAQIE; -.
DR BioCyc; YEAST:G3O-33896-MON; -.
DR PRO; PR:Q3E835; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q3E835; protein.
DR GO; GO:0071821; C:FANCM-MHF complex; IDA:SGD.
DR GO; GO:0043240; C:Fanconi anaemia nuclear complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IGI:SGD.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0031297; P:replication fork processing; IBA:GO_Central.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IBA:GO_Central.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR029003; CENP-S/Mhf1.
DR InterPro; IPR009072; Histone-fold.
DR Pfam; PF15630; CENP-S; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; DNA-binding; Reference proteome.
FT CHAIN 1..90
FT /note="Inner kinetochore subunit MHF1"
FT /id="PRO_0000235928"
FT MUTAGEN 55
FT /note="D->A: Disrupts the heterotetrameric state and
FT becomes hypersensitive to MMS; when associated with A-62."
FT /evidence="ECO:0000269|PubMed:22325783"
FT MUTAGEN 62
FT /note="H->A: Disrupts the heterotetrameric state and
FT becomes hypersensitive to MMS; when associated with A-55 or
FT 78-AA-79."
FT /evidence="ECO:0000269|PubMed:22325783"
FT MUTAGEN 78..79
FT /note="RK->AA: Disrupts the heterotetrameric state and
FT becomes hypersensitive to MMS; when associated with A-62."
FT /evidence="ECO:0000269|PubMed:22325783"
FT HELIX 3..25
FT /evidence="ECO:0007829|PDB:3V9R"
FT HELIX 35..62
FT /evidence="ECO:0007829|PDB:3V9R"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:3V9R"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:3V9R"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:3V9R"
FT HELIX 81..87
FT /evidence="ECO:0007829|PDB:3V9R"
SQ SEQUENCE 90 AA; 10549 MW; A1B7F953FED34C1C CRC64;
MNDDEDRAQL KARLWIRVEE RLQQVLSSED IKYTPRFINS LLELAYLQLG EMGSDLQAFA
RHAGRGVVNK SDLMLYLRKQ PDLQERVTQE
