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UniProtKB/Swiss-Prot entry P56523


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

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Entry information
Entry name CLR3_SCHPO
Primary accession number P56523
Secondary accession numbers None
Integrated into Swiss-Prot on July 15, 1998
Sequence was last modified on July 15, 1998 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 60)
Name and origin of the protein
Protein name Histone deacetylase clr3
Synonyms EC 3.5.1.98
Cryptic loci regulator 3
Gene name
Name: clr3
ORFNames: SPBC800.03
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]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
DOI=10.1038/nbt1222; PubMed=16823372 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
[4]
FUNCTION, INTERACTION WITH CCQ1; CLR1; CLR2 AND MIT1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-232.
DOI=10.1016/j.cell.2006.12.035; PubMed=17289569 [NCBI, ExPASy, EBI, Israel, Japan]
Sugiyama T., Cam H.P., Sugiyama R., Noma K., Zofall M., Kobayashi R., Grewal S.I.S.;
"SHREC, an effector complex for heterochromatic transcriptional silencing.";
Cell 128:491-504(2007).
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. Required for proper positioning of nucleosomes at heterochromatic loci and for transcriptional gene silencing (TGS) function of the Snf2/Hdac-containing repressor complex (SHREC).
  • CATALYTIC ACTIVITY: Hydrolysis of an N6-acetyl-lysine residue of a histone to yield a deacetylated histone.
  • SUBUNIT: Interacts with ccq1, clr1, clr2 and mit1.
  • SUBCELLULAR LOCATION: Nucleus. Note=Associates with major heterochromatin, centromeres, sub-telomeres, rDNA and the mat locus.
  • SIMILARITY: Belongs to the histone deacetylase family. Type 2 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
AF064207; AAD05212.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329671; CAC01518.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T43797; T43797.
RefSeq NP_595104.1; -.
3D structure databases
ModBase P56523.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-003203-MON; -.
Organism-specific databases
GeneDB_Spombe SPBC800.03; -.
Gene expression databases
ArrayExpress P56523; -.
Ontologies
GO
GO:0005721; Cellular component: centromeric heterochromatin (inferred from direct assay from GeneDB_SPombe).
GO:0031934; Cellular component: mating-type region heterochromatin (inferred from direct assay from GeneDB_SPombe).
GO:0030874; Cellular component: nucleolar chromatin (inferred from direct assay from GeneDB_SPombe).
GO:0016581; Cellular component: NuRD complex (inferred from direct assay from GeneDB_SPombe).
GO:0033553; Cellular component: rDNA heterochromatin (inferred from direct assay from GeneDB_SPombe).
GO:0031933; Cellular component: telomeric heterochromatin (inferred from direct assay from GeneDB_SPombe).
GO:0031078; Molecular function: histone deacetylase activity (H3-K14 specific) (inferred from mutant phenotype from GeneDB_SPombe).
GO:0030702; Biological process: chromatin silencing at centromere (inferred from mutant phenotype from GeneDB_SPombe).
GO:0000183; Biological process: chromatin silencing at rDNA (inferred from mutant phenotype from GeneDB_SPombe).
GO:0030466; Biological process: chromatin silencing at silent mating-type cassette (inferred from mutant phenotype from GeneDB_SPombe).
GO:0006348; Biological process: chromatin silencing at telomere (inferred from mutant phenotype from GeneDB_SPombe).
GO:0016575; Biological process: histone deacetylation (inferred from mutant phenotype from GeneDB_SPombe).
GO:0000122; Biological process: negative regulation of transcription from RNA polymerase II promoter (inferred from mutant phenotype from GeneDB_SPombe).
GO:0016584; Biological process: nucleosome positioning (inferred from mutant phenotype from GeneDB_SPombe).
GO:0031060; Biological process: regulation of histone methylation (inferred from mutant phenotype from GeneDB_SPombe).
GO:0006350; Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR019154; Arb2_domain.
IPR000286; His_deacetylse.
IPR017321; Hist_deAcase_II_yeast.
Graphical view of domain structure.
Gene3D G3DSA:3.40.800.20; His_deacetylse; 1.
PANTHER PTHR10625; His_deacetylse; 1.
Pfam PF09757; Arb2; 1.
PF00850; Hist_deacetyl; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF037919; HDAC_II_yeast; 1.
PRINTS PR01270; HDASUPER.
Genome annotation databases
GeneID 2540821; -.
KEGG spo:SPBC800.03; -.
NMPDR fig|4896.1.peg.970; -.
Phylogenomic databases
OMA P56523; DPHPEDP.
Other
ProtoNet P56523.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chromatin regulator; Complete proteome; Hydrolase; Nucleus; Repressor; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   687  687     Histone deacetylase clr3. PRO_0000114739
REGION   55   385  331     Histone deacetylase. 
ACT_SITE   195   195        By similarity. 
MUTAGEN   232   232        D->N: No activity; weak silencing defect. 
Sequence information
Length: 687 AA [This is the length of the unprocessed precursor] Molecular weight: 76792 Da [This is the MW of the unprocessed precursor] CRC64: 6B0E4184A056D899 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLASNSDGAS TSVKPSDDAV NTVTPWSILL TNNKPMSGSE NTLNNESHEM SQILKKSGLC 

        70         80         90        100        110        120 
YDPRMRFHAT LSEVDDHPED PRRVLRVFEA IKKAGYVSNV PSPSDVFLRI PAREATLEEL 

       130        140        150        160        170        180 
LQVHSQEMYD RVTNTEKMSH EDLANLEKIS DSLYYNNESA FCARLACGSA IETCTAVVTG 

       190        200        210        220        230        240 
QVKNAFAVVR PPGHHAEPHK PGGFCLFNNV SVTARSMLQR FPDKIKRVLI VDWDIHHGNG 

       250        260        270        280        290        300 
TQMAFYDDPN VLYVSLHRYE NGRFYPGTNY GCAENCGEGP GLGRTVNIPW SCAGMGDGDY 

       310        320        330        340        350        360 
IYAFQRVVMP VAYEFDPDLV IVSCGFDAAA GDHIGQFLLT PAAYAHMTQM LMGLADGKVF 

       370        380        390        400        410        420 
ISLEGGYNLD SISTSALAVA QSLLGIPPGR LHTTYACPQA VATINHVTKI QSQYWRCMRP 

       430        440        450        460        470        480 
KHFDANPKDA HVDRLHDVIR TYQAKKLFED WKITNMPILR DSVSNVFNNQ VLCSSNFFQK 

       490        500        510        520        530        540 
DNLLVIVHES PRVLGNGTSE TNVLNLNDSL LVDPVSLYVE WAMQQDWGLI DINIPEVVTD 

       550        560        570        580        590        600 
GENAPVDILS EVKELCLYVW DNYVELSISK NIFFIGGGKA VHGLVNLASS RNVSDRVKCM 

       610        620        630        640        650        660 
VNFLGTEPLV GLKTASEEDL PTWYYRHSLV FVSSSNECWK KAKRAKRRYG RLMQSEHTET 

       670        680 
SDMMEQHYRA VTQYLLHLLQ KARPTSQ 

P56523 in FASTA format

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