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P56523 (CLR3_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 99. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone deacetylase clr3

EC=3.5.1.98
Alternative name(s):
Cryptic loci regulator 3
Gene names
Name:clr3
ORF Names:SPBC800.03
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length687 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. Required for proper positioning of nucleosomes at heterochromatic loci and for transcriptional gene silencing (TGS) function of the Snf2/Hdac-containing repressor complex (SHREC). Ref.4

Catalytic activity

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

Subunit structure

Interacts with ccq1, clr1, clr2 and mit1. Ref.4

Subcellular location

Nucleus. Chromosomecentromere. Chromosometelomere. Note: Associates with major heterochromatin, centromeres, sub-telomeres, rDNA and the mat locus. Ref.3 Ref.4

Sequence similarities

Belongs to the histone deacetylase family. HD type 2 subfamily.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCentromere
Chromosome
Nucleus
Telomere
   Molecular functionChromatin regulator
Hydrolase
Repressor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processchromatin silencing at centromere

Inferred from mutant phenotype Ref.1. Source: PomBase

chromatin silencing at rDNA

Inferred from mutant phenotype PubMed 11884604. Source: PomBase

chromatin silencing at silent mating-type cassette

Inferred from mutant phenotype PubMed 8001791PubMed 8138176. Source: PomBase

chromatin silencing at telomere

Inferred from mutant phenotype Ref.1. Source: PomBase

histone H3 deacetylation

Inferred from mutant phenotype PubMed 11884604. Source: GOC

histone deacetylation

Inferred from mutant phenotype PubMed 11884604. Source: PomBase

maintenance of chromatin silencing at silent mating-type cassette

Non-traceable author statement. Source: PomBase

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.4. Source: PomBase

nucleosome positioning

Inferred from mutant phenotype Ref.4. Source: PomBase

regulation of histone methylation

Inferred from mutant phenotype PubMed 11283354. Source: PomBase

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentSHREC complex

Inferred from direct assay Ref.4. Source: PomBase

centromeric heterochromatin

Inferred from direct assay Ref.4. Source: PomBase

mating-type region heterochromatin

Inferred from direct assay Ref.4. Source: PomBase

nuclear chromatin

Inferred from direct assay PubMed 11884604. Source: PomBase

nucleolar chromatin

Inferred from direct assay PubMed 11884604. Source: PomBase

nucleus

Inferred from direct assay Ref.3. Source: PomBase

rDNA heterochromatin

Inferred from direct assay Ref.4. Source: PomBase

telomeric heterochromatin

Inferred from direct assay Ref.4. 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 direct assay PubMed 11884604. Source: PomBase

histone deacetylase activity (H3-K14 specific)

Inferred from mutant phenotype PubMed 11884604. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 687687Histone deacetylase clr3
PRO_0000114739

Regions

Region55 – 385331Histone deacetylase

Sites

Active site1951 By similarity

Experimental info

Mutagenesis2321D → N: No activity; weak silencing defect. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P56523 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 6B0E4184A056D899

FASTA68776,792
        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 

« 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]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]"SHREC, an effector complex for heterochromatic transcriptional silencing."
Sugiyama T., Cam H.P., Sugiyama R., Noma K., Zofall M., Kobayashi R., Grewal S.I.S.
Cell 128:491-504(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CCQ1; CLR1; CLR2 AND MIT1, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-232.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF064207 Genomic DNA. Translation: AAD05212.1.
CU329671 Genomic DNA. Translation: CAC01518.1.
PIRT43797.
RefSeqNP_595104.1. NM_001021011.2.

3D structure databases

ProteinModelPortalP56523.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid277339. 137 interactions.
DIPDIP-59446N.
MINTMINT-4691084.
STRING4896.SPBC800.03-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC800.03.1; SPBC800.03.1:pep; SPBC800.03.
GeneID2540821.
KEGGspo:SPBC800.03.

Organism-specific databases

PomBaseSPBC800.03.

Phylogenomic databases

eggNOGCOG0123.
HOGENOMHOG000161343.
KOK11407.
OMAQGMGDGE.
OrthoDBEOG75B8GB.
PhylomeDBP56523.

Family and domain databases

Gene3D3.40.800.20. 1 hit.
InterProIPR019154. Arb2_domain.
IPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR017321. Hist_deAcase_II_yeast.
[Graphical view]
PANTHERPTHR10625. PTHR10625. 1 hit.
PfamPF09757. Arb2. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFPIRSF037919. HDAC_II_yeast. 1 hit.
PRINTSPR01270. HDASUPER.
ProtoNetSearch...

Other

NextBio20801938.

Entry information

Entry nameCLR3_SCHPO
AccessionPrimary (citable) accession number: P56523
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: April 16, 2014
This is version 99 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