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| Gene ID | At1g16710 |
| Gene name | HAC12 (histone acetyltransferase of the CBP family 12) |
| Functional description | Encodes an enzyme with histone acetyltransferase activity that can use both H3 and H4 histones as substrates. No single prior lysine acetylation is sufficient to block HAC12 acetylation of the H3 or H4 peptides, suggesting that HAC12 can acetylate any of several lysines present in the peptides. |
| HF | Ev | BS | Gene ID | Repr. ID | Gene Name | Functional Description | O.I. | C.G. | S.X. | Other DB |
|---|---|---|---|---|---|---|---|---|---|---|
| 0.67 | 0 | 2424 | At1g79000 | 844241 | HAC1 (HISTONE ACETYLTRANSFERASE OF THE CBP FAMILY 1) | Homologous to CREB-binding protein, a co-activator of transcription with histone acetyl-transferase activity. No single prior lysine acetylation is sufficient to block HAC1 acetylation of the H3 or H4 peptides, suggesting that HAC1, HAC5, and HAC12 can acetylate any of several lysines present in the peptides. HAM2 acetylates histone H4 lysine 5. A plant line expressing an RNAi construct targeted against HAC1 has reduced rates of agrobacterium-mediated root transformation. | O.I. | C.G. | S.X. | |
| 0.17 | 2e-25 | 119 | At3g12980 | 820484 | HAC5 | Encodes an enzyme with histone acetyltransferase activity that can use both H3 and H4 histones as substrates. No single prior lysine acetylation is sufficient to block HAC5 acetylation of the H3 or H4 peptides, suggesting that HAC5 can acetylate any of several lysines present in the peptides. Di-acetylation of both lysines 9 and 14 on the H3 peptide significantly reduces the level of incorporated radioactive acetylation catalyzed by HAC5, indicating that HAC5 may acetylate either lysine 9 or lysine 14. | O.I. | C.G. | S.X. | |
| 0.14 | 3e-21 | 105 | At1g55970 | 842048 | HAC4 (HISTONE ACETYLTRANSFERASE OF THE CBP FAMILY 4) | HAC4 is most likely to be an expressed pseudogene that lacks HAT function. there is a single nucleotide deletion in both the HAC4 genomic and cDNA sequences relative to its homologs. The resulting frameshift within the open reading frame causes a stop codon to occur within the predicted acetyltransferase catalytic domain. | O.I. | C.G. | S.X. | |
| 0.05 | 5e-17 | 91 | At1g16705 | 838241 | p300/CBP acetyltransferase-related protein-related | F:molecular_function unknown;P:biological_process unknown;C:cellular_component unknown;P | O.I. | C.G. | S.X. | |
| 0.01 | 1e-2 | 44 | At4g01050 | 827921 | hydroxyproline-rich glycoprotein family protein | hydroxyproline-rich glycoprotein family protein, contains a rhodanese homology domain. | O.I. | C.G. | S.X. | |
| 0.01 | 4e-2 | 42 | At5g07600 | 830653 | oleosin / glycine-rich protein | F:unknown;P:lipid storage;C:monolayer-surrounded lipid storage body, endomembrane system, integral to membrane, membrane;BMOPFVA | O.I. | C.G. | S.X. |
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