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P56523

- CLR3_SCHPO

UniProt

P56523 - CLR3_SCHPO

Protein

Histone deacetylase clr3

Gene

clr3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (15 Jul 1998)
      Previous versions | rss
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    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 – 1951By similarity

    GO - Molecular functioni

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

    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 deacetylation Source: PomBase
    6. histone H3 deacetylation Source: GOC
    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

    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.

    GO - Cellular componenti

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

    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 clr3PRO_0000114739Add
    BLAST

    Proteomic databases

    MaxQBiP56523.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi277339. 138 interactions.
    DIPiDIP-59446N.
    MINTiMINT-4691084.
    STRINGi4896.SPBC800.03-1.

    Structurei

    3D structure databases

    ProteinModelPortaliP56523.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni55 – 385331Histone deacetylaseAdd
    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. 138 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

    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: October 1, 2014
    This is version 101 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