CENPX_YEAST
ID CENPX_YEAST Reviewed; 80 AA.
AC Q3E829; D6VRI9;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Inner kinetochore subunit MHF2 {ECO:0000305};
DE AltName: Full=CENP-X homolog {ECO:0000303|PubMed:22561346};
DE AltName: Full=Constitutive centromere-associated network protein MHF2 {ECO:0000305};
DE AltName: Full=MHF histone-fold complex subunit 2 {ECO:0000305|PubMed:20347428};
DE AltName: Full=MPH1-associated histone-fold protein 2 {ECO:0000303|PubMed:20347428};
GN Name=MHF2 {ECO:0000303|PubMed:20347428};
GN OrderedLocusNames=YDL160C-A {ECO:0000312|SGD:S000028520};
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=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(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=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [4]
RP FUNCTION, AND INTERACTION WITH MHF1.
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), AND SUBUNIT.
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: DNA-binding component of a FANCM-MHF complex involved in DNA
CC 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 (PubMed:22325783). Component of the inner kinetochore
CC constitutive centromere-associated network (CCAN) (also known as
CC central kinetochore CTF19 complex in yeast), which is composed of at
CC least AME1, CHL4, CNN1, CTF3, CTF19, IML3, MCM16, MCM21, MCM22, MHF1,
CC MHF2, MIF2, NKP1, NKP2, OKP1 and WIP1 (Probable).
CC {ECO:0000269|PubMed:22325783, ECO:0000305|PubMed:22561346}.
CC -!- INTERACTION:
CC Q3E829; Q3E835: MHF1; NbExp=3; IntAct=EBI-15968870, EBI-2881690;
CC -!- SIMILARITY: Belongs to the CENP-X/MHF2 family. {ECO:0000305}.
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DR EMBL; Z74210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BK006938; DAA11699.1; -; Genomic_DNA.
DR RefSeq; NP_878060.1; NM_001184530.1.
DR PDB; 3V9R; X-ray; 2.40 A; B/D=1-80.
DR PDBsum; 3V9R; -.
DR AlphaFoldDB; Q3E829; -.
DR SMR; Q3E829; -.
DR BioGRID; 36973; 32.
DR DIP; DIP-59642N; -.
DR IntAct; Q3E829; 1.
DR STRING; 4932.YDL160C-A; -.
DR MaxQB; Q3E829; -.
DR PaxDb; Q3E829; -.
DR PRIDE; Q3E829; -.
DR EnsemblFungi; YDL160C-A_mRNA; YDL160C-A; YDL160C-A.
DR GeneID; 1466431; -.
DR KEGG; sce:YDL160C-A; -.
DR SGD; S000028520; MHF2.
DR VEuPathDB; FungiDB:YDL160C-A; -.
DR eggNOG; ENOG502S826; Eukaryota.
DR HOGENOM; CLU_113787_0_0_1; -.
DR InParanoid; Q3E829; -.
DR OMA; KYVETYV; -.
DR BioCyc; YEAST:G3O-30114-MON; -.
DR PRO; PR:Q3E829; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q3E829; 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: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:0051382; P:kinetochore assembly; IEA:InterPro.
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; IPR018552; CENP-X.
DR InterPro; IPR009072; Histone-fold.
DR Pfam; PF09415; CENP-X; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; DNA-binding; Reference proteome.
FT CHAIN 1..80
FT /note="Inner kinetochore subunit MHF2"
FT /id="PRO_0000240877"
FT HELIX 5..11
FT /evidence="ECO:0007829|PDB:3V9R"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:3V9R"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:3V9R"
FT HELIX 27..50
FT /evidence="ECO:0007829|PDB:3V9R"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:3V9R"
SQ SEQUENCE 80 AA; 9050 MW; 714F9504D55859BC CRC64;
MLSKEALIKI LSQNEGGNDM KIADEVVPMI QKYLDIFIDE AVLRSLQSHK DINGERGDKS
PLELSHQDLE RIVGLLLMDM
