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UniProtKB/Swiss-Prot entry O59702


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CLR6_SCHPO
Primary accession number O59702
Secondary accession numbers None
Integrated into Swiss-Prot on July 25, 2003
Sequence was last modified on August 1, 1998 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 64)
Name and origin of the protein
Protein name Histone deacetylase clr6
Synonyms EC 3.5.1.98
Cryptic loci regulator 6
Gene name
Name: clr6
ORFNames: SPBC36.05c
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
PubMed=9755190 [NCBI, ExPASy, EBI, Israel, Japan]
Grewal S.I.S., Bonaduce M.J., Klar A.J.S.;
"Histone deacetylase homologs regulate epigenetic inheritance of transcriptional silencing and chromosome segregation in fission yeast.";
Genetics 150:563-576(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[3]
PROTEIN SEQUENCE OF 340-368 AND 381-404, FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
DOI=10.1093/emboj/cdg248; PubMed=12773392 [NCBI, ExPASy, EBI, Israel, Japan]
Nakayama J., Xiao G., Noma K., Malikzay A., Bjerling P., Ekwall K., Kobayashi R., Grewal S.I.S.;
"Alp13, an MRG family protein, is a component of fission yeast Clr6 histone deacetylase required for genomic integrity.";
EMBO J. 22:2776-2787(2003).
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.
  • CATALYTIC ACTIVITY: Hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone.
  • SUBUNIT: Heterotetramer of alp13, clr6, prw1 and pst2.
  • INTERACTION:
    O13919:pst2; NbExp=1; IntAct=EBI-904651, EBI-904686;
  • SUBCELLULAR LOCATION: Nucleus.
  • SIMILARITY: Belongs to the histone deacetylase family. Type 1 subfamily.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF064206; AAD05211.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329671; CAA19053.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T40300; T40300.
RefSeq NP_595333.1; -.
3D structure databases
HSSP O67135; 1C3P. [HSSP ENTRY / PDB]
ModBase O59702.
Protein-protein interaction databases
IntAct O59702; 4.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-003413-MON; -.
Organism-specific databases
GeneDB_Spombe SPBC36.05c; -.
Gene expression databases
ArrayExpress O59702; -.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0033698; Cellular component: Rpd3/Clr6 histone deacetylase complex I/I' (inferred from direct assay from GeneDB_SPombe).
GO:0032221; Cellular component: Rpd3/Clr6 histone deacetylase complex II' (inferred from direct assay from GeneDB_SPombe).
GO:0070210; Cellular component: Rpd3L-Expanded complex (inferred from direct assay from GeneDB_SPombe).
GO:0032129; Molecular function: histone deacetylase activity (H3-K9 specific) (non-traceable author statement from GeneDB_SPombe).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0030702; Biological process: chromatin silencing at centromere (inferred from mutant phenotype from GeneDB_SPombe).
GO:0030466; Biological process: chromatin silencing at silent mating-type cassette (inferred from genetic interaction from GeneDB_SPombe).
GO:0030261; Biological process: chromosome condensation (inferred from mutant phenotype from GeneDB_SPombe).
GO:0007059; Biological process: chromosome segregation (traceable author statement from GeneDB_SPombe).
GO:0016575; Biological process: histone deacetylation (inferred from mutant phenotype from GeneDB_SPombe).
GO:0006357; Biological process: regulation of transcription from RNA polymerase II promoter (inferred from expression pattern from GeneDB_SPombe).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000286; His_deacetylse.
IPR003084; His_deacetylse_1.
Graphical view of domain structure.
Gene3D G3DSA:3.40.800.20; His_deacetylse; 1.
PANTHER PTHR10625; His_deacetylse; 1.
PTHR10625:SF28; His_deacetylse_1; 1.
Pfam PF00850; Hist_deacetyl; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF037913; His_deacetylse_1; 1.
PRINTS PR01270; HDASUPER.
PR01271; HISDACETLASE.
Genome annotation databases
GeneID 2540368; -.
KEGG spo:SPBC36.05c; -.
NMPDR fig|4896.1.peg.1199; -.
Phylogenomic databases
OMA O59702; IPEDAPH.
Other
ProtoNet O59702.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chromatin regulator; Complete proteome; Direct protein sequencing; Hydrolase; Nucleus; Repressor; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   405  405     Histone deacetylase clr6. PRO_0000114740
REGION   6   318  313     Histone deacetylase. 
ACT_SITE   138   138        By similarity. 
Sequence information
Length: 405 AA [This is the length of the unprocessed precursor] Molecular weight: 46112 Da [This is the MW of the unprocessed precursor] CRC64: 8EDEA43D5839E367 [This is a checksum on the sequence]
        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 

O59702 in FASTA format

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