[English] 日本語
![](img/lk-miru.gif)
- SASDFL7: Complex with 1H histone chaperone Asf1, histones H3 and H4, 2H ac... -
+
Open data
-
Basic information
Entry | Database: SASBDB / ID: SASDFL7 |
---|---|
![]() | Complex with 1H histone chaperone Asf1, histones H3 and H4, 2H acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) in 42% v/v D2O
|
Function / homology | ![]() histone H3K23 acetyltransferase activity / histone H3K56 acetyltransferase activity / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / H3 histone acetyltransferase complex / histone H3K14 acetyltransferase activity / negative regulation of DNA damage checkpoint / regulation of double-strand break repair via nonhomologous end joining / histone H3K9 acetyltransferase activity / maintenance of rDNA / acetyltransferase activator activity ...histone H3K23 acetyltransferase activity / histone H3K56 acetyltransferase activity / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / H3 histone acetyltransferase complex / histone H3K14 acetyltransferase activity / negative regulation of DNA damage checkpoint / 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 / retrotransposon silencing / DNA replication-dependent chromatin assembly / histone H3 acetyltransferase activity / histone H3K27 acetyltransferase activity / nucleosome disassembly / silent mating-type cassette heterochromatin formation / peptide-lysine-N-acetyltransferase activity / subtelomeric heterochromatin formation / regulation of DNA repair / positive regulation of transcription elongation by RNA polymerase II / histone acetyltransferase / 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 / regulation of gene expression / histone binding / chromosome, telomeric region / protein heterodimerization activity / chromatin binding / DNA damage response / regulation of transcription by RNA polymerase II / chromatin / DNA binding / identical protein binding / nucleus / cytosol Similarity search - Function |
Biological species | ![]() ![]() ![]() |
![]() |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-Data source
SASBDB page | ![]() |
---|
-Related structure data
Similar structure data |
---|
-
External links
Related items in Molecule of the Month |
---|
-Models
Model #3176 | ![]() Type: atomic / Chi-square value: 0.941 / P-value: 0.000001 ![]() |
---|---|
Model #3177 | ![]() Type: atomic / Chi-square value: 2.848 / P-value: 0.000001 ![]() |
-
Sample
![]() | Name: Complex with 1H histone chaperone Asf1, histones H3 and H4, 2H acetyltransferase Rtt109 and histone chaperone Vps75 (1-225aa) in 42% v/v D2O Specimen concentration: 4 mg/ml / Entity id: 1488 / 1489 / 1490 / 1492 / 1728 |
---|---|
Buffer | Name: 50 mM citrate, 150 mM NaCl, 5 mM BME, 42% D2O / pH: 6.5 |
Entity #1488 | Name: Vps75 1-225 / Type: protein Description: Vacuolar protein sorting-associated protein 75 (1-225 aa) Formula weight: 26.554 / 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 RDLED |
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 |
-Experimental information
Beam | Instrument name: ILL D22 / City: Grenoble / 国: France ![]() | |||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Detector | Name: 128 linear sensitive Reuter-Stokes detector / Type: 3He multidetector / Pixsize x: 0.8 mm | |||||||||||||||||||||
Scan | Measurement date: Nov 14, 2016 / Cell temperature: 25.2 °C / Exposure time: 3600 sec. / Number of frames: 1 / Unit: 1/A /
| |||||||||||||||||||||
Distance distribution function P(R) |
| |||||||||||||||||||||
Result |
|