Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone H3-like centromeric protein CSE4

Gene

CSE4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.11 Publications

GO - Molecular functioni

  1. centromeric DNA binding Source: SGD
  2. sequence-specific DNA binding Source: SGD

GO - Biological processi

  1. 2-micrometer plasmid partitioning Source: SGD
  2. mitotic sister chromatid segregation Source: SGD
Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31850-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H3-like centromeric protein CSE4
Alternative name(s):
CENP-A homolog
Chromosome segregation protein 4
Gene namesi
Name:CSE4
Synonyms:CSL2
Ordered Locus Names:YKL049C
ORF Names:YKL262
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XI

Organism-specific databases

CYGDiYKL049c.
SGDiS000001532. CSE4.

Subcellular locationi

Nucleus. Chromosomecentromerekinetochore
Note: Localizes exclusively in the kinetochore domain of centromeres.

GO - Cellular componenti

  1. CENP-A containing nucleosome Source: SGD
  2. chromosome, centromeric region Source: SGD
  3. condensed chromosome kinetochore Source: UniProtKB-SubCell
  4. condensed nuclear chromosome, centromeric region Source: SGD
  5. extrachromosomal circular DNA Source: SGD
  6. kinetochore Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi176 – 1761L → S in CSE4-102; impairs nuclear division by disrupting the core centromere structure; when associated with T-218. 1 Publication
Mutagenesisi194 – 1941L → Q in CSE4-111; impairs nuclear division by disrupting the core centromere structure. 1 Publication
Mutagenesisi197 – 1971L → S in CSE4-110; impairs nuclear division by disrupting the core centromere structure. 1 Publication
Mutagenesisi218 – 2181M → T in CSE4-102; impairs nuclear division by disrupting the core centromere structure; when associated with S-176. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 229229Histone H3-like centromeric protein CSE4PRO_0000221376Add
BLAST

Post-translational modificationi

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.Curated

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiP36012.
PaxDbiP36012.

Expressioni

Gene expression databases

GenevestigatoriP36012.

Interactioni

Subunit structurei

Component of the core kinetochore. Interacts with the central kinetochore protein CTF19.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DAM1P532672EBI-5182,EBI-23268

Protein-protein interaction databases

BioGridi34084. 353 interactions.
DIPiDIP-8048N.
IntActiP36012. 7 interactions.
MINTiMINT-4492546.
STRINGi4932.YKL049C.

Structurei

Secondary structure

1
229
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi157 – 16711Combined sources
Helixi171 – 1733Combined sources
Helixi180 – 20627Combined sources
Turni208 – 2103Combined sources
Helixi212 – 2143Combined sources
Helixi217 – 2226Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FSBmodel-E1-228[»]
2FSCmodel-A1-228[»]
2L5ANMR-A151-228[»]
2LY8NMR-A152-225[»]
ProteinModelPortaliP36012.
SMRiP36012. Positions 152-229.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni132 – 22998H3-likeAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi115 – 13218Nuclear localization signalSequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 6666Ser-richAdd
BLAST

Sequence similaritiesi

Belongs to the histone H3 family.Curated

Phylogenomic databases

eggNOGiCOG2036.
GeneTreeiENSGT00760000119422.
HOGENOMiHOG000155290.
InParanoidiP36012.
OMAiRITIMKK.
OrthoDBiEOG7T4MZ6.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3/CENP-A.
[Graphical view]
PANTHERiPTHR11426. PTHR11426. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00622. HISTONEH3.
SMARTiSM00428. H3. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00959. HISTONE_H3_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36012-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSSKQQWVSS AIQSDSSGRS LSNVNRLAGD QQSINDRALS LLQRTRATKN
60 70 80 90 100
LFPRREERRR YESSKSDLDI ETDYEDQAGN LEIETENEEE AEMETEVPAP
110 120 130 140 150
VRTHSYALDR YVRQKRREKQ RKQSLKRVEK KYTPSELALY EIRKYQRSTD
160 170 180 190 200
LLISKIPFAR LVKEVTDEFT TKDQDLRWQS MAIMALQEAS EAYLVGLLEH
210 220
TNLLALHAKR ITIMKKDMQL ARRIRGQFI
Length:229
Mass (Da):26,841
Last modified:November 1, 1995 - v2
Checksum:i0170A10060EEC309
GO

Sequence cautioni

The sequence CAA81884.1 differs from that shown. Reason: Frameshift at position 28. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20327 Genomic DNA. Translation: AAB60309.1.
X71621 Genomic DNA. No translation available.
Z28049 Genomic DNA. Translation: CAA81884.1. Frameshift.
BK006944 Genomic DNA. Translation: DAA09108.1.
PIRiS37870.
RefSeqiNP_012875.2. NM_001179615.1.

Genome annotation databases

EnsemblFungiiYKL049C; YKL049C; YKL049C.
GeneIDi853817.
KEGGisce:YKL049C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20327 Genomic DNA. Translation: AAB60309.1.
X71621 Genomic DNA. No translation available.
Z28049 Genomic DNA. Translation: CAA81884.1. Frameshift.
BK006944 Genomic DNA. Translation: DAA09108.1.
PIRiS37870.
RefSeqiNP_012875.2. NM_001179615.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FSBmodel-E1-228[»]
2FSCmodel-A1-228[»]
2L5ANMR-A151-228[»]
2LY8NMR-A152-225[»]
ProteinModelPortaliP36012.
SMRiP36012. Positions 152-229.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34084. 353 interactions.
DIPiDIP-8048N.
IntActiP36012. 7 interactions.
MINTiMINT-4492546.
STRINGi4932.YKL049C.

Proteomic databases

MaxQBiP36012.
PaxDbiP36012.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL049C; YKL049C; YKL049C.
GeneIDi853817.
KEGGisce:YKL049C.

Organism-specific databases

CYGDiYKL049c.
SGDiS000001532. CSE4.

Phylogenomic databases

eggNOGiCOG2036.
GeneTreeiENSGT00760000119422.
HOGENOMiHOG000155290.
InParanoidiP36012.
OMAiRITIMKK.
OrthoDBiEOG7T4MZ6.

Enzyme and pathway databases

BioCyciYEAST:G3O-31850-MONOMER.

Miscellaneous databases

NextBioi974993.

Gene expression databases

GenevestigatoriP36012.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3/CENP-A.
[Graphical view]
PANTHERiPTHR11426. PTHR11426. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00622. HISTONEH3.
SMARTiSM00428. H3. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00959. HISTONE_H3_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A mutation in CSE4, an essential gene encoding a novel chromatin-associated protein in yeast, causes chromosome nondisjunction and cell cycle arrest at mitosis."
    Stoler S., Keith K.C., Curnick K.E., Fitzgerald-Hayes M.
    Genes Dev. 9:573-586(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "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."
    Purnelle B., Tettelin H., van Dyck L., Skala J., Goffeau A.
    Yeast 9:1379-1384(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Complete DNA sequence of yeast chromosome XI."
    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.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "Cse4p is a component of the core centromere of Saccharomyces cerevisiae."
    Meluh P.B., Yang P., Glowczewski L., Koshland D., Smith M.M.
    Cell 94:607-613(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "Mutations synthetically lethal with cep1 target S. cerevisiae kinetochore components."
    Baker R.E., Harris K., Zhang K.
    Genetics 149:73-85(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "A putative protein complex consisting of Ctf19, Mcm21, and Okp1 represents a missing link in the budding yeast kinetochore."
    Ortiz J., Stemmann O., Rank S., Lechner J.
    Genes Dev. 13:1140-1155(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "Analysis of primary structural determinants that distinguish the centromere-specific function of histone variant Cse4p from histone H3."
    Keith K.C., Baker R.E., Chen Y., Harris K., Stoler S., Fitzgerald-Hayes M.
    Mol. Cell. Biol. 19:6130-6139(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "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."
    Keith K.C., Fitzgerald-Hayes M.
    Genetics 156:973-981(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. Cited for: FUNCTION, MUTAGENESIS OF LEU-176; LEU-194; LEU-197 AND MET-218.
  11. "Identification of cohesin association sites at centromeres and along chromosome arms."
    Tanaka T., Cosma M.P., Wirth K., Nasmyth K.
    Cell 98:847-858(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "The N-terminus of the centromere H3-like protein Cse4p performs an essential function distinct from that of the histone fold domain."
    Chen Y., Baker R.E., Keith K.C., Harris K., Stoler S., Fitzgerald-Hayes M.
    Mol. Cell. Biol. 20:7037-7048(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTF19.
  13. "Genes involved in sister chromatid separation and segregation in the budding yeast Saccharomyces cerevisiae."
    Biggins S., Bhalla N., Chang A., Smith D.L., Murray A.W.
    Genetics 159:453-470(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Budding yeast chromosome structure and dynamics during mitosis."
    Pearson C.G., Maddox P.S., Salmon E.D., Bloom K.S.
    J. Cell Biol. 152:1255-1266(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  15. "Architecture of the budding yeast kinetochore reveals a conserved molecular core."
    Westermann S., Cheeseman I.M., Anderson S., Yates J.R. III, Drubin D.G., Barnes G.
    J. Cell Biol. 163:215-222(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CORE KINETOCHORE.
  16. "Proteolysis contributes to the exclusive centromere localization of the yeast Cse4/CENP-A histone H3 variant."
    Collins K.A., Furuyama S., Biggins S.
    Curr. Biol. 14:1968-1972(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, UBIQUITIN-MEDIATED PROTEOLYSIS.
  17. "The histone fold domain of Cse4 is sufficient for CEN targeting and propagation of active centromeres in budding yeast."
    Morey L., Barnes K., Chen Y., Fitzgerald-Hayes M., Baker R.E.
    Eukaryot. Cell 3:1533-1543(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "De novo kinetochore assembly requires the centromeric histone H3 variant."
    Collins K.A., Castillo A.R., Tatsutani S.Y., Biggins S.
    Mol. Biol. Cell 16:5649-5660(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION.
  19. "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."
    Hajra S., Ghosh S.K., Jayaram M.
    J. Cell Biol. 174:779-790(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  20. "Molecular architecture of a kinetochore-microtubule attachment site."
    Joglekar A.P., Bouck D.C., Molk J.N., Bloom K.S., Salmon E.D.
    Nat. Cell Biol. 8:581-585(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  21. Cited for: 3D-STRUCTURE MODELING OF 1-228.

Entry informationi

Entry nameiCENPA_YEAST
AccessioniPrimary (citable) accession number: P36012
Secondary accession number(s): D6VXN8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1995
Last modified: January 7, 2015
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Mutation in CSE4 causes chromosome non-disjunction and cell cycle arrest at mitosis.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.