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O59702 (CLR6_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase clr6

EC=3.5.1.98
Alternative name(s):
Cryptic loci regulator 6
Gene names
Name:clr6
ORF Names:SPBC36.05c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Has a role in chromatin assembly and chromosome segregation. Ref.3

Catalytic activity

Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

Subunit structure

Heterotetramer of alp13, clr6, prw1 and pst2. Ref.3

Subcellular location

Nucleus Ref.3.

Sequence similarities

Belongs to the histone deacetylase family. HD type 1 subfamily.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Molecular functionChromatin regulator
Hydrolase
Repressor
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin remodeling

Non-traceable author statement. Source: PomBase

chromatin silencing at centromere

Inferred from mutant phenotype Ref.1. Source: PomBase

chromatin silencing at silent mating-type cassette

Inferred from genetic interaction Ref.1. Source: PomBase

chromosome condensation

Inferred from mutant phenotype Ref.3. Source: PomBase

histone H3 deacetylation

Non-traceable author statement. Source: GOC

histone deacetylation

Inferred from mutant phenotype PubMed 11884604. Source: PomBase

mitotic sister chromatid segregation

Traceable author statement PubMed 12526748. Source: PomBase

negative regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 16407326. Source: PomBase

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20404084. Source: PomBase

regulation of histone H3-K9 methylation

Non-traceable author statement. Source: PomBase

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentRpd3L complex

Inferred from direct assay PubMed 17450151. Source: PomBase

Rpd3L-Expanded complex

Inferred from direct assay PubMed 19040720. Source: PomBase

Rpd3S complex

Inferred from direct assay Ref.3PubMed 19040720. Source: PomBase

cytosol

Inferred from direct assay PubMed 16823372. Source: PomBase

nuclear chromatin

Inferred from direct assay PubMed 11884604. Source: PomBase

   Molecular_functionNAD-dependent histone deacetylase activity (H3-K14 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K18 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H3-K9 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

NAD-dependent histone deacetylase activity (H4-K16 specific)

Inferred from electronic annotation. Source: UniProtKB-EC

histone deacetylase activity

Inferred from mutant phenotype PubMed 11884604. Source: PomBase

histone deacetylase activity (H3-K9 specific)

Non-traceable author statement. Source: PomBase

protein binding

Inferred from physical interaction Ref.3. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

pst2O139195EBI-904651,EBI-904686

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 405405Histone deacetylase clr6
PRO_0000114740

Regions

Region6 – 318313Histone deacetylase

Sites

Active site1381 By similarity

Sequences

Sequence LengthMass (Da)Tools
O59702 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 8EDEA43D5839E367

FASTA40546,112
        10         20         30         40         50         60 
MGFGKKKVSY FYDEDVGNYH YGPQHPMKPH RVRMVHNLVV NYNLYEKLNV ITPVRATRND 

        70         80         90        100        110        120 
MTRCHTDEYI EFLWRVTPDT MEKFQPHQLK FNVGDDCPVF DGLYEFCSIS AGGSIGAAQE 

       130        140        150        160        170        180 
LNSGNAEIAI NWAGGLHHAK KREASGFCYV NDIALAALEL LKYHQRVLYI DIDVHHGDGV 

       190        200        210        220        230        240 
EEFFYTTDRV MTCSFHKFGE YFPGTGHIKD TGIGTGKNYA VNVPLRDGID DESYESVFKP 

       250        260        270        280        290        300 
VISHIMQWFR PEAVILQCGT DSLAGDRLGC FNLSMKGHSM CVDFVKSFNL PMICVGGGGY 

       310        320        330        340        350        360 
TVRNVARVWT YETGLLAGEE LDENLPYNDY LQYYGPDYKL NVLSNNMENH NTRQYLDSIT 

       370        380        390        400 
SEIIENLRNL SFAPSVQMHK TPGDFTFENA EKQNIAKEEI MDERV 

« Hide

References

« Hide 'large scale' references
[1]"Histone deacetylase homologs regulate epigenetic inheritance of transcriptional silencing and chromosome segregation in fission yeast."
Grewal S.I.S., Bonaduce M.J., Klar A.J.S.
Genetics 150:563-576(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"Alp13, an MRG family protein, is a component of fission yeast Clr6 histone deacetylase required for genomic integrity."
Nakayama J., Xiao G., Noma K., Malikzay A., Bjerling P., Ekwall K., Kobayashi R., Grewal S.I.S.
EMBO J. 22:2776-2787(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 340-368 AND 381-404, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF064206 Genomic DNA. Translation: AAD05211.1.
CU329671 Genomic DNA. Translation: CAA19053.1.
PIRT40300.
RefSeqNP_595333.1. NM_001021241.2.

3D structure databases

ProteinModelPortalO59702.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid276897. 29 interactions.
DIPDIP-29339N.
IntActO59702. 4 interactions.
MINTMINT-4675495.
STRING4896.SPBC36.05c-1.

Proteomic databases

MaxQBO59702.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC36.05c.1; SPBC36.05c.1:pep; SPBC36.05c.
GeneID2540368.
KEGGspo:SPBC36.05c.

Organism-specific databases

PomBaseSPBC36.05c.

Phylogenomic databases

eggNOGCOG0123.
HOGENOMHOG000225180.
KOK06067.
OMAHAMRDRA.
OrthoDBEOG78M0B2.
PhylomeDBO59702.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR000286. His_deacetylse.
IPR003084. His_deacetylse_1.
IPR023801. His_deacetylse_dom.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037913. His_deacetylse_1. 1 hit.
PRINTSPR01270. HDASUPER.
PR01271. HISDACETLASE.
ProtoNetSearch...

Other

NextBio20801496.

Entry information

Entry nameCLR6_SCHPO
AccessionPrimary (citable) accession number: O59702
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2003
Last sequence update: August 1, 1998
Last modified: June 11, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names