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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=521;
DOI=10.1038/nature05248; PubMed=17080091 [NCBI, ExPASy, EBI, Israel, Japan]
Kaemper J.,
Kahmann R.,
Boelker M.,
Ma L.-J.,
Brefort T.,
Saville B.J.,
Banuett F.,
Kronstad J.W.,
Gold S.E.,
Mueller O.,
Perlin M.H.,
Woesten H.A.B.,
de Vries R.,
Ruiz-Herrera J.,
Reynaga-Pena C.G.,
Snetselaar K.,
McCann M.,
Perez-Martin J.,
Feldbruegge M., ![]()
Basse C.W.,
Steinberg G.,
Ibeas J.I.,
Holloman W.,
Guzman P.,
Farman M.L.,
Stajich J.E.,
Sentandreu R.,
Gonzalez-Prieto J.M.,
Kennell J.C.,
Molina L.,
Schirawski J.,
Mendoza-Mendoza A.,
Greilinger D.,
Muench K.,
Roessel N.,
Scherer M.,
Vranes M.,
Ladendorf O.,
Vincon V.,
Fuchs U.,
Sandrock B.,
Meng S.,
Ho E.C.H.,
Cahill M.J.,
Boyce K.J.,
Klose J.,
Klosterman S.J.,
Deelstra H.J.,
Ortiz-Castellanos L.,
Li W.,
Sanchez-Alonso P.,
Schreier P.H.,
Haeuser-Hahn I.,
Vaupel M.,
Koopmann E.,
Friedrich G.,
Voss H.,
Schlueter T.,
Margolis J.,
Platt D.,
Swimmer C.,
Gnirke A.,
Chen F.,
Vysotskaia V.,
Mannhaupt G.,
Gueldener U.,
Muensterkoetter M.,
Haase D.,
Oesterheld M.,
Mewes H.-W.,
Mauceli E.W.,
DeCaprio D.,
Wade C.M.,
Butler J.,
Young S.K.,
Jaffe D.B.,
Calvo S.E.,
Nusbaum C.,
Galagan J.E.,
Birren B.W.;
"Insights from the genome of the biotrophic fungal plant pathogen Ustilago maydis.";
Nature 444:97-101(2006).
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- FUNCTION: Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me (By similarity).
- CATALYTIC ACTIVITY: Acetyl-CoA + histone = CoA + acetylhistone.
- SUBUNIT: Component of the NuA4 histone acetyltransferase complex (By similarity).
- SUBCELLULAR LOCATION: Nucleus (By similarity).
- DOMAIN: The ESA1-RPD3 motif is common to ESA1 and RPD3 and is required for ESA1 histone acetyl-transferase (HAT) activity and RPD3 histone deacetylase (HDAC) activity.
- SIMILARITY: Belongs to the MYST (SAS/MOZ) family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 565 AA [This is the length of the unprocessed precursor] |
Molecular weight: 63408 Da [This is the MW of the unprocessed precursor] |
CRC64: C35F30CBD96EB754 [This is a checksum on the sequence] |
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10 20 30 40 50 60
MAPRTQKSTS GTPGGSGTPG PDEGPQISPG GTYGLEDVVV GCKAFVQKPD VVTGEMEERK
70 80 90 100 110 120
AEILSIREKP KPRLTKKQQA ELADKPAPTL EETLEYYVHY CEFNKRLDEW VSGTRLITSR
130 140 150 160 170 180
ELEWPKKEVT SDKTKRKVIR AGSGATTPST PLTPTGKGYR GAGASNLLKK AAAQAAKNVQ
190 200 210 220 230 240
GESGLETPQK RKADSGDTST AQSIRADSID ADADGEDDEN GAVVAMEMLG GNDQQEKDDV
250 260 270 280 290 300
ATESNGGLTA SLNANQGQET FSKKQEIEKL RTSGSMTQSV SEVARVKNLN KIQMGKSEVE
310 320 330 340 350 360
TWYFSPYPLE YAHIDTLYIC EMCLSYFPSP FTLKRHRSKC TLLHPPGNEI YRHEDISFFE
370 380 390 400 410 420
IDGRLQRTWC RNLCLLSKCF LDHKTLYYDV DPFLYYCMVK RDDLGCHLLG YFSKEKDSAE
430 440 450 460 470 480
NYNVACILTL PQHQRAGYGK LLIEFSYELT KIEGKLGSPE KPLSDLGLLS YRAYWAEIIV
490 500 510 520 530 540
ELLLKTEDEI SIEEIAQKTA FTHADILHTC MALNMLKQYQ GKHMIVLSDL IISKYTAKRP
550 560
RKRINPQKLH WTAKNWHRSQ LNFGW
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Q4P3S3 in FASTA format |
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ExPASy Home page
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