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Histone H3-like centromeric protein CSE4 (CENP-A homolog) (Chromosome segregation protein 4)

 CENPA_YEAST             Reviewed;         229 AA.
P36012; D6VXN8;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 2.
27-SEP-2017, entry version 151.
RecName: Full=Histone H3-like centromeric protein CSE4;
AltName: Full=CENP-A homolog;
AltName: Full=Chromosome segregation protein 4;
Name=CSE4; Synonyms=CSL2; OrderedLocusNames=YKL049C; ORFNames=YKL262;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
PubMed=7698647; DOI=10.1101/gad.9.5.573;
Stoler S., Keith K.C., Curnick K.E., Fitzgerald-Hayes M.;
"A mutation in CSE4, an essential gene encoding a novel chromatin-
associated protein in yeast, causes chromosome nondisjunction and cell
cycle arrest at mitosis.";
Genes Dev. 9:573-586(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8154189; DOI=10.1002/yea.320091212;
Purnelle B., Tettelin H., van Dyck L., Skala J., Goffeau A.;
"The sequence of a 17.5 kb DNA fragment on the left arm of yeast
chromosome XI identifies the protein kinase gene ELM1, the DNA primase
gene PRI2, a new gene encoding a putative histone and seven new open
reading frames.";
Yeast 9:1379-1384(1993).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=8196765; DOI=10.1038/369371a0;
Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M.,
Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C.,
Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G.,
Zimmermann J., Haasemann M., Becker I., Mewes H.-W.;
"Complete DNA sequence of yeast chromosome XI.";
Nature 369:371-378(1994).
[5]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9741625; DOI=10.1016/S0092-8674(00)81602-5;
Meluh P.B., Yang P., Glowczewski L., Koshland D., Smith M.M.;
"Cse4p is a component of the core centromere of Saccharomyces
cerevisiae.";
Cell 94:607-613(1998).
[6]
FUNCTION.
PubMed=9584087;
Baker R.E., Harris K., Zhang K.;
"Mutations synthetically lethal with cep1 target S. cerevisiae
kinetochore components.";
Genetics 149:73-85(1998).
[7]
SUBCELLULAR LOCATION.
PubMed=10323865; DOI=10.1101/gad.13.9.1140;
Ortiz J., Stemmann O., Rank S., Lechner J.;
"A putative protein complex consisting of Ctf19, Mcm21, and Okp1
represents a missing link in the budding yeast kinetochore.";
Genes Dev. 13:1140-1155(1999).
[8]
FUNCTION.
PubMed=10454560; DOI=10.1128/MCB.19.9.6130;
Keith K.C., Baker R.E., Chen Y., Harris K., Stoler S.,
Fitzgerald-Hayes M.;
"Analysis of primary structural determinants that distinguish the
centromere-specific function of histone variant Cse4p from histone
H3.";
Mol. Cell. Biol. 19:6130-6139(1999).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11063678;
Keith K.C., Fitzgerald-Hayes M.;
"CSE4 genetically interacts with the Saccharomyces cerevisiae
centromere DNA elements CDE I and CDE II but not CDE III. Implications
for the path of the centromere dna around a cse4p variant
nucleosome.";
Genetics 156:973-981(2000).
[10]
FUNCTION, AND MUTAGENESIS OF LEU-176; LEU-194; LEU-197 AND MET-218.
PubMed=10891506; DOI=10.1128/MCB.20.15.5700-5711.2000;
Glowczewski L., Yang P., Kalashnikova T., Santisteban M.S.,
Smith M.M.;
"Histone-histone interactions and centromere function.";
Mol. Cell. Biol. 20:5700-5711(2000).
[11]
FUNCTION.
PubMed=10499801; DOI=10.1016/S0092-8674(00)81518-4;
Tanaka T., Cosma M.P., Wirth K., Nasmyth K.;
"Identification of cohesin association sites at centromeres and along
chromosome arms.";
Cell 98:847-858(1999).
[12]
INTERACTION WITH CTF19.
PubMed=10958698; DOI=10.1128/MCB.20.18.7037-7048.2000;
Chen Y., Baker R.E., Keith K.C., Harris K., Stoler S.,
Fitzgerald-Hayes M.;
"The N-terminus of the centromere H3-like protein Cse4p performs an
essential function distinct from that of the histone fold domain.";
Mol. Cell. Biol. 20:7037-7048(2000).
[13]
FUNCTION.
PubMed=11606525;
Biggins S., Bhalla N., Chang A., Smith D.L., Murray A.W.;
"Genes involved in sister chromatid separation and segregation in the
budding yeast Saccharomyces cerevisiae.";
Genetics 159:453-470(2001).
[14]
SUBCELLULAR LOCATION.
PubMed=11257125; DOI=10.1083/jcb.152.6.1255;
Pearson C.G., Maddox P.S., Salmon E.D., Bloom K.S.;
"Budding yeast chromosome structure and dynamics during mitosis.";
J. Cell Biol. 152:1255-1266(2001).
[15]
IDENTIFICATION IN THE CORE KINETOCHORE.
PubMed=14581449; DOI=10.1083/jcb.200305100;
Westermann S., Cheeseman I.M., Anderson S., Yates J.R. III,
Drubin D.G., Barnes G.;
"Architecture of the budding yeast kinetochore reveals a conserved
molecular core.";
J. Cell Biol. 163:215-222(2003).
[16]
SUBCELLULAR LOCATION, AND UBIQUITIN-MEDIATED PROTEOLYSIS.
PubMed=15530401; DOI=10.1016/j.cub.2004.10.024;
Collins K.A., Furuyama S., Biggins S.;
"Proteolysis contributes to the exclusive centromere localization of
the yeast Cse4/CENP-A histone H3 variant.";
Curr. Biol. 14:1968-1972(2004).
[17]
FUNCTION.
PubMed=15590827; DOI=10.1128/EC.3.6.1533-1543.2004;
Morey L., Barnes K., Chen Y., Fitzgerald-Hayes M., Baker R.E.;
"The histone fold domain of Cse4 is sufficient for CEN targeting and
propagation of active centromeres in budding yeast.";
Eukaryot. Cell 3:1533-1543(2004).
[18]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=16207811; DOI=10.1091/mbc.E05-08-0771;
Collins K.A., Castillo A.R., Tatsutani S.Y., Biggins S.;
"De novo kinetochore assembly requires the centromeric histone H3
variant.";
Mol. Biol. Cell 16:5649-5660(2005).
[19]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16966420; DOI=10.1083/jcb.200603042;
Hajra S., Ghosh S.K., Jayaram M.;
"The centromere-specific histone variant Cse4p (CENP-A) is essential
for functional chromatin architecture at the yeast 2-micrometer circle
partitioning locus and promotes equal plasmid segregation.";
J. Cell Biol. 174:779-790(2006).
[20]
SUBCELLULAR LOCATION.
PubMed=16715078; DOI=10.1038/ncb1414;
Joglekar A.P., Bouck D.C., Molk J.N., Bloom K.S., Salmon E.D.;
"Molecular architecture of a kinetochore-microtubule attachment
site.";
Nat. Cell Biol. 8:581-585(2006).
[21]
3D-STRUCTURE MODELING OF 1-228.
PubMed=16631569; DOI=10.1016/j.cub.2006.03.054;
Bloom K.S., Sharma S., Dokholyan N.V.;
"The path of DNA in the kinetochore.";
Curr. Biol. 16:R276-R278(2006).
-!- FUNCTION: Histone H3-like variant which exclusively replaces
conventional H3 in the nucleosome core of centromeric chromatin at
the inner plate of the kinetochore. Required for recruitment and
assembly of kinetochore proteins, mitotic progression and
chromosome segregation. May serve as an epigenetic mark that
propagates centromere identity through replication and cell
division. Required for functional chromatin architecture at the
yeast 2-micron circle partitioning locus and promotes equal
plasmid segregation. {ECO:0000269|PubMed:10454560,
ECO:0000269|PubMed:10499801, ECO:0000269|PubMed:10891506,
ECO:0000269|PubMed:11063678, ECO:0000269|PubMed:11606525,
ECO:0000269|PubMed:15590827, ECO:0000269|PubMed:16207811,
ECO:0000269|PubMed:16966420, ECO:0000269|PubMed:7698647,
ECO:0000269|PubMed:9584087, ECO:0000269|PubMed:9741625}.
-!- SUBUNIT: Component of the core kinetochore. Interacts with the
central kinetochore protein CTF19. {ECO:0000269|PubMed:10958698,
ECO:0000269|PubMed:14581449}.
-!- INTERACTION:
P53267:DAM1; NbExp=3; IntAct=EBI-5182, EBI-23268;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere,
kinetochore. Note=Localizes exclusively in the kinetochore domain
of centromeres.
-!- PTM: Ubiquitinated (Probable). Is degraded through ubiquitin
mediated proteolysis when not protected by its association to the
kinetochore. This may ensure exclusive localization of CSE4 to the
kinetochore. {ECO:0000305}.
-!- MISCELLANEOUS: Mutation in CSE4 causes chromosome non-disjunction
and cell cycle arrest at mitosis.
-!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA81884.1; Type=Frameshift; Positions=28; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; U20327; AAB60309.1; -; Genomic_DNA.
EMBL; X71621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; Z28049; CAA81884.1; ALT_FRAME; Genomic_DNA.
EMBL; BK006944; DAA09108.1; -; Genomic_DNA.
PIR; S37870; S37870.
RefSeq; NP_012875.2; NM_001179615.1.
PDB; 2FSB; Model; -; E=1-228.
PDB; 2FSC; Model; -; A=1-228.
PDB; 2L5A; NMR; -; A=151-228.
PDB; 2LY8; NMR; -; A=152-225.
PDBsum; 2FSB; -.
PDBsum; 2FSC; -.
PDBsum; 2L5A; -.
PDBsum; 2LY8; -.
ProteinModelPortal; P36012; -.
SMR; P36012; -.
BioGrid; 34084; 397.
DIP; DIP-8048N; -.
IntAct; P36012; 7.
MINT; MINT-4492546; -.
STRING; 4932.YKL049C; -.
MaxQB; P36012; -.
EnsemblFungi; YKL049C; YKL049C; YKL049C.
GeneID; 853817; -.
KEGG; sce:YKL049C; -.
EuPathDB; FungiDB:YKL049C; -.
SGD; S000001532; CSE4.
GeneTree; ENSGT00840000129844; -.
HOGENOM; HOG000155290; -.
InParanoid; P36012; -.
OMA; KRITIMR; -.
OrthoDB; EOG092C5B6S; -.
BioCyc; YEAST:G3O-31850-MONOMER; -.
PRO; PR:P36012; -.
Proteomes; UP000002311; Chromosome XI.
GO; GO:0005729; C:2-micrometer circle DNA; IDA:SGD.
GO; GO:0043505; C:CENP-A containing nucleosome; IDA:SGD.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IDA:SGD.
GO; GO:0000776; C:kinetochore; IDA:SGD.
GO; GO:0019237; F:centromeric DNA binding; IDA:SGD.
GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:SGD.
GO; GO:0030543; P:2-micrometer plasmid partitioning; IMP:SGD.
GO; GO:0051382; P:kinetochore assembly; IMP:SGD.
GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:SGD.
GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
InterPro; IPR009072; Histone-fold.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR000164; Histone_H3/CENP-A.
PANTHER; PTHR11426; PTHR11426; 1.
Pfam; PF00125; Histone; 1.
PRINTS; PR00622; HISTONEH3.
SMART; SM00428; H3; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00959; HISTONE_H3_2; 1.
1: Evidence at protein level;
3D-structure; Centromere; Chromosome; Complete proteome; DNA-binding;
Kinetochore; Nucleus; Reference proteome; Ubl conjugation.
CHAIN 1 229 Histone H3-like centromeric protein CSE4.
/FTId=PRO_0000221376.
REGION 132 229 H3-like.
MOTIF 115 132 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 1 66 Ser-rich.
MUTAGEN 176 176 L->S: In CSE4-102; impairs nuclear
division by disrupting the core
centromere structure; when associated
with T-218.
{ECO:0000269|PubMed:10891506}.
MUTAGEN 194 194 L->Q: In CSE4-111; impairs nuclear
division by disrupting the core
centromere structure.
{ECO:0000269|PubMed:10891506}.
MUTAGEN 197 197 L->S: In CSE4-110; impairs nuclear
division by disrupting the core
centromere structure.
{ECO:0000269|PubMed:10891506}.
MUTAGEN 218 218 M->T: In CSE4-102; impairs nuclear
division by disrupting the core
centromere structure; when associated
with S-176.
{ECO:0000269|PubMed:10891506}.
HELIX 157 169 {ECO:0000244|PDB:2LY8}.
HELIX 180 204 {ECO:0000244|PDB:2LY8}.
TURN 205 207 {ECO:0000244|PDB:2LY8}.
HELIX 214 225 {ECO:0000244|PDB:2LY8}.
SEQUENCE 229 AA; 26841 MW; 0170A10060EEC309 CRC64;
MSSKQQWVSS AIQSDSSGRS LSNVNRLAGD QQSINDRALS LLQRTRATKN LFPRREERRR
YESSKSDLDI ETDYEDQAGN LEIETENEEE AEMETEVPAP VRTHSYALDR YVRQKRREKQ
RKQSLKRVEK KYTPSELALY EIRKYQRSTD LLISKIPFAR LVKEVTDEFT TKDQDLRWQS
MAIMALQEAS EAYLVGLLEH TNLLALHAKR ITIMKKDMQL ARRIRGQFI


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