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P56523

- CLR3_SCHPO

UniProt

P56523 - CLR3_SCHPO

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Protein
Histone deacetylase clr3
Gene
clr3, SPBC800.03
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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).1 Publication

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei195 – 1951 By similarity

GO - Molecular functioni

  1. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
  2. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
  3. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
  4. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
  5. histone deacetylase activity Source: PomBase
  6. histone deacetylase activity (H3-K14 specific) Source: PomBase

GO - Biological processi

  1. chromatin silencing at centromere Source: PomBase
  2. chromatin silencing at rDNA Source: PomBase
  3. chromatin silencing at silent mating-type cassette Source: PomBase
  4. chromatin silencing at telomere Source: PomBase
  5. histone H3 deacetylation Source: GOC
  6. histone deacetylation Source: PomBase
  7. maintenance of chromatin silencing at silent mating-type cassette Source: PomBase
  8. negative regulation of transcription from RNA polymerase II promoter Source: PomBase
  9. nucleosome positioning Source: PomBase
  10. regulation of histone methylation Source: PomBase
  11. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Hydrolase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase clr3 (EC:3.5.1.98)
Alternative name(s):
Cryptic loci regulator 3
Gene namesi
Name:clr3
ORF Names:SPBC800.03
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC800.03.

Subcellular locationi

Nucleus. Chromosomecentromere. Chromosometelomere
Note: Associates with major heterochromatin, centromeres, sub-telomeres, rDNA and the mat locus.2 Publications

GO - Cellular componenti

  1. SHREC complex Source: PomBase
  2. centromeric heterochromatin Source: PomBase
  3. mating-type region heterochromatin Source: PomBase
  4. nuclear chromatin Source: PomBase
  5. nucleolar chromatin Source: PomBase
  6. nucleus Source: PomBase
  7. rDNA heterochromatin Source: PomBase
  8. telomeric heterochromatin Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus, Telomere

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi232 – 2321D → N: No activity; weak silencing defect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 687687Histone deacetylase clr3
PRO_0000114739Add
BLAST

Proteomic databases

MaxQBiP56523.

Interactioni

Subunit structurei

Interacts with ccq1, clr1, clr2 and mit1.1 Publication

Protein-protein interaction databases

BioGridi277339. 137 interactions.
DIPiDIP-59446N.
MINTiMINT-4691084.
STRINGi4896.SPBC800.03-1.

Structurei

3D structure databases

ProteinModelPortaliP56523.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni55 – 385331Histone deacetylase
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0123.
HOGENOMiHOG000161343.
KOiK11407.
OMAiCYDDRMK.
OrthoDBiEOG75B8GB.
PhylomeDBiP56523.

Family and domain databases

Gene3Di3.40.800.20. 1 hit.
InterProiIPR019154. Arb2_domain.
IPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR017321. Hist_deAcase_II_yeast.
[Graphical view]
PANTHERiPTHR10625. PTHR10625. 1 hit.
PfamiPF09757. Arb2. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view]
PIRSFiPIRSF037919. HDAC_II_yeast. 1 hit.
PRINTSiPR01270. HDASUPER.

Sequencei

Sequence statusi: Complete.

P56523-1 [UniParc]FASTAAdd to Basket

« Hide

MLASNSDGAS TSVKPSDDAV NTVTPWSILL TNNKPMSGSE NTLNNESHEM    50
SQILKKSGLC YDPRMRFHAT LSEVDDHPED PRRVLRVFEA IKKAGYVSNV 100
PSPSDVFLRI PAREATLEEL LQVHSQEMYD RVTNTEKMSH EDLANLEKIS 150
DSLYYNNESA FCARLACGSA IETCTAVVTG QVKNAFAVVR PPGHHAEPHK 200
PGGFCLFNNV SVTARSMLQR FPDKIKRVLI VDWDIHHGNG TQMAFYDDPN 250
VLYVSLHRYE NGRFYPGTNY GCAENCGEGP GLGRTVNIPW SCAGMGDGDY 300
IYAFQRVVMP VAYEFDPDLV IVSCGFDAAA GDHIGQFLLT PAAYAHMTQM 350
LMGLADGKVF ISLEGGYNLD SISTSALAVA QSLLGIPPGR LHTTYACPQA 400
VATINHVTKI QSQYWRCMRP KHFDANPKDA HVDRLHDVIR TYQAKKLFED 450
WKITNMPILR DSVSNVFNNQ VLCSSNFFQK DNLLVIVHES PRVLGNGTSE 500
TNVLNLNDSL LVDPVSLYVE WAMQQDWGLI DINIPEVVTD GENAPVDILS 550
EVKELCLYVW DNYVELSISK NIFFIGGGKA VHGLVNLASS RNVSDRVKCM 600
VNFLGTEPLV GLKTASEEDL PTWYYRHSLV FVSSSNECWK KAKRAKRRYG 650
RLMQSEHTET SDMMEQHYRA VTQYLLHLLQ KARPTSQ 687
Length:687
Mass (Da):76,792
Last modified:July 15, 1998 - v1
Checksum:i6B0E4184A056D899
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF064207 Genomic DNA. Translation: AAD05212.1.
CU329671 Genomic DNA. Translation: CAC01518.1.
PIRiT43797.
RefSeqiNP_595104.1. NM_001021011.2.

Genome annotation databases

EnsemblFungiiSPBC800.03.1; SPBC800.03.1:pep; SPBC800.03.
GeneIDi2540821.
KEGGispo:SPBC800.03.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF064207 Genomic DNA. Translation: AAD05212.1 .
CU329671 Genomic DNA. Translation: CAC01518.1 .
PIRi T43797.
RefSeqi NP_595104.1. NM_001021011.2.

3D structure databases

ProteinModelPortali P56523.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 277339. 137 interactions.
DIPi DIP-59446N.
MINTi MINT-4691084.
STRINGi 4896.SPBC800.03-1.

Proteomic databases

MaxQBi P56523.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPBC800.03.1 ; SPBC800.03.1:pep ; SPBC800.03 .
GeneIDi 2540821.
KEGGi spo:SPBC800.03.

Organism-specific databases

PomBasei SPBC800.03.

Phylogenomic databases

eggNOGi COG0123.
HOGENOMi HOG000161343.
KOi K11407.
OMAi CYDDRMK.
OrthoDBi EOG75B8GB.
PhylomeDBi P56523.

Miscellaneous databases

NextBioi 20801938.

Family and domain databases

Gene3Di 3.40.800.20. 1 hit.
InterProi IPR019154. Arb2_domain.
IPR000286. His_deacetylse.
IPR023801. His_deacetylse_dom.
IPR017321. Hist_deAcase_II_yeast.
[Graphical view ]
PANTHERi PTHR10625. PTHR10625. 1 hit.
Pfami PF09757. Arb2. 1 hit.
PF00850. Hist_deacetyl. 1 hit.
[Graphical view ]
PIRSFi PIRSF037919. HDAC_II_yeast. 1 hit.
PRINTSi PR01270. HDASUPER.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiCLR3_SCHPO
AccessioniPrimary (citable) accession number: P56523
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: May 14, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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