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Yorodumi- SASDFP7: Complex with all 1H histone acetyltransferase Rtt109 with histone... -
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-Basic information
Entry | Database: SASBDB / ID: SASDFP7 |
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Sample | Complex with all 1H histone acetyltransferase Rtt109 with histones H3 and H4 and histone chaperones Asf1 and Vps75, all full-length, acquired in 100% v/v D2O
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Function / homology | Function and homology information histone H3K23 acetyltransferase activity / histone H3K56 acetyltransferase activity / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / H3 histone acetyltransferase complex / histone H3K14 acetyltransferase activity / regulation of double-strand break repair via nonhomologous end joining / histone H3K9 acetyltransferase activity / maintenance of rDNA / acetyltransferase activator activity / replication-born double-strand break repair via sister chromatid exchange ...histone H3K23 acetyltransferase activity / histone H3K56 acetyltransferase activity / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / H3 histone acetyltransferase complex / histone H3K14 acetyltransferase activity / regulation of double-strand break repair via nonhomologous end joining / histone H3K9 acetyltransferase activity / maintenance of rDNA / acetyltransferase activator activity / replication-born double-strand break repair via sister chromatid exchange / transposable element silencing / histone H3 acetyltransferase activity / DNA replication-dependent chromatin assembly / histone H3K27 acetyltransferase activity / nucleosome disassembly / silent mating-type cassette heterochromatin formation / peptide-lysine-N-acetyltransferase activity / negative regulation of DNA damage checkpoint / subtelomeric heterochromatin formation / regulation of DNA repair / histone acetyltransferase / positive regulation of transcription elongation by RNA polymerase II / regulation of protein phosphorylation / protein modification process / double-strand break repair via nonhomologous end joining / structural constituent of chromatin / nucleosome / protein transport / nucleosome assembly / chromatin organization / histone binding / regulation of gene expression / chromosome, telomeric region / protein heterodimerization activity / DNA damage response / chromatin binding / chromatin / regulation of transcription by RNA polymerase II / DNA binding / identical protein binding / nucleus / cytosol Similarity search - Function |
Biological species | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) Xenopus laevis (African clawed frog) |
Contact author |
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-Structure visualization
-Downloads & links
-Data source
SASBDB page | SASDFP7 |
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-Related structure data
Similar structure data | Similarity search - Function & homologyF&H Search |
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-External links
Related items in Molecule of the Month |
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-Models
-Sample
Sample | Name: Complex with all 1H histone acetyltransferase Rtt109 with histones H3 and H4 and histone chaperones Asf1 and Vps75, all full-length, acquired in 100% v/v D2O Specimen concentration: 2.73 mg/ml / Entity id: 1489 / 1490 / 1492 / 1728 / 1729 |
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Buffer | Name: 50 mM citrate, 150 mM NaCl, 5 mM BME, 100% D2O / pH: 6.5 |
Entity #1489 | Name: Rtt109 / Type: protein / Description: Histone acetyltransferase RTT109 / Formula weight: 50.095 / Num. of mol.: 1 Source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) References: UniProt: Q07794 Sequence: MSLNDFLSSV LPVSEQFEYL SLQSIPLETH AVVTPNKDDK RVPKSTIKTQ HFFSLFHQGK VFFSLEVYVY VTLWDEADAE RLIFVSKADT NGYCNTRVSV RDITKIILEF ILSIDPNYYL QKVKPAIRSY KKISPELISA ASTPARTLRI LARRLKQSGS TVLKEIESPR ...Sequence: MSLNDFLSSV LPVSEQFEYL SLQSIPLETH AVVTPNKDDK RVPKSTIKTQ HFFSLFHQGK VFFSLEVYVY VTLWDEADAE RLIFVSKADT NGYCNTRVSV RDITKIILEF ILSIDPNYYL QKVKPAIRSY KKISPELISA ASTPARTLRI LARRLKQSGS TVLKEIESPR FQQDLYLSFT CPREILTKIC LFTRPASQYL FPDSSKNSKK HILNGEELMK WWGFILDRLL IECFQNDTQA KLRIPGEDPA RVRSYLRGMK YPLWQVGDIF TSKENSLAVY NIPLFPDDPK ARFIHQLAEE DRLLKVSLSS FWIELQERQE FKLSVTSSVM GISGYSLATP SLFPSSADVI VPKSRKQFRA IKKYITGEEY DTEEGAIEAF TNIRDFLLLR MATNLQSLTG KREHRERNQP VPASNINTLA ITMLKPRKKA KALPKT |
Entity #1490 | Name: Asf1 / Type: protein / Description: Histone chaperone ASF1 / Formula weight: 19.125 / Num. of mol.: 1 / References: UniProt: P32447 Sequence: MSIVSLLGIK VLNNPAKFTD PYEFEITFEC LESLKHDLEW KLTYVGSSRS LDHDQELDSI LVGPVPVGVN KFVFSADPPS AELIPASELV SVTVILLSCS YDGREFVRVG YYVNNEYDEE ELRENPPAKV QVDHIVRNIL AEKPRVTRFN IVWDNENEGD LYPPEQPGV |
Entity #1492 | Name: H4 / Type: protein / Description: Histone H4 / Formula weight: 11.367 / Num. of mol.: 1 / Source: Xenopus laevis / References: UniProt: P62799 Sequence: MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVYA LKRQGRTLYG FGG |
Entity #1728 | Name: H3 FL / Type: protein / Description: Histone H3 full-length / Formula weight: 15.328 / Num. of mol.: 1 / Source: Xenopus laevis / References: UniProt: Q6PI79 Sequence: MARTKQTARK STGGKAPRKQ LATKAARKSA PSTGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSAAI GALQEASEAY LVGLFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA |
Entity #1729 | Name: Vps75 (FL) / Type: protein Description: Vacuolar protein sorting-associated protein 75 full-length Formula weight: 30.615 / Num. of mol.: 2 Source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) References: UniProt: P53853 Sequence: MMSDQENENE HAKAFLGLAK CEEEVDAIER EVELYRLNKM KPVYEKRDAY IDEIAEFWKI VLSQHVSFAN YIRASDFKYI DTIDKIKVEW LALESEMYDT RDFSITFHFH GIEGDFKEQQ VTKVFQIKKG KDDQEDGILT SEPVPIEWPQ SYDSINPDLI KDKRSPEGKK ...Sequence: MMSDQENENE HAKAFLGLAK CEEEVDAIER EVELYRLNKM KPVYEKRDAY IDEIAEFWKI VLSQHVSFAN YIRASDFKYI DTIDKIKVEW LALESEMYDT RDFSITFHFH GIEGDFKEQQ VTKVFQIKKG KDDQEDGILT SEPVPIEWPQ SYDSINPDLI KDKRSPEGKK KYRQGMKTIF GWFRWTGLKP GKEFPHGDSL ASLFSEEIYP FCVKYYAEAQ RDLEDEEGES GLSADGDSED DDGSLGEVDL PLSDEEPSSK KRKV |
-Experimental information
Beam | Instrument name: ILL D22 / City: Grenoble / 国: France / Type of source: neutron source / Wavelength: 0.6 Å / Dist. spec. to detc.: 4 mm | |||||||||||||||||||||
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Detector | Name: 128 linear sensitive Reuter-Stokes detector / Type: 3He multidetector / Pixsize x: 0.8 mm | |||||||||||||||||||||
Scan | Title: Complex with all 1H histone acetyltransferase Rtt109 with histones H3 and H4 and histone chaperones Asf1 and Vps75, all full-length, acquired in 100% v/v D2O Measurement date: Jun 9, 2016 / Cell temperature: 25 °C / Exposure time: 7200 sec. / Number of frames: 1 / Unit: 1/A /
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Distance distribution function P(R) | Sofotware P(R): GNOM 4.6 / Number of points: 109 /
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Result | Experimental MW: 157 kDa / Type of curve: single_conc
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