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UniProt functional annotation for Q9UNL4 | ||
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| UniProt code: Q9UNL4. |
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| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
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| Function: | |
Component of HBO1 complexes, which specifically mediate acetylation of histone H3 at 'Lys-14' (H3K14ac), and have reduced activity toward histone H4 (PubMed:16387653). Through chromatin acetylation it may function in DNA replication (PubMed:16387653). May inhibit tumor progression by modulating the transcriptional output of signaling pathways which regulate cell proliferation (PubMed:15251430, PubMed:15528276). Can suppress brain tumor angiogenesis through transcriptional repression of RELA/NFKB3 target genes when complexed with RELA (PubMed:15029197). May also specifically suppress loss of contact inhibition elicited by activated oncogenes such as MYC (PubMed:15029197). Represses hypoxia inducible factor's (HIF) activity by interacting with HIF prolyl hydroxylase 2 (EGLN1) (PubMed:15897452). Can enhance apoptosis induced by serum starvation in mammary epithelial cell line HC11 (By similarity). {ECO:0000250|UniProtKB:Q8C0D7, ECO:0000269|PubMed:15029197, ECO:0000269|PubMed:15251430, ECO:0000269|PubMed:15528276, ECO:0000269|PubMed:15897452, ECO:0000269|PubMed:16387653}. |
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| Subunit: | |
Homodimer (PubMed:19187765, PubMed:22334692). Component of the HBO1 complex composed of KAT7/HBO1, MEAF6, ING4 or ING5, and one scaffold subunit: complexes containing BRPF scaffold (BRPF1, BRD1/BRPF2 or BRPF3) direct KAT7/HBO1 specificity towards H3K14ac, while complexes containing JADE scaffold (JADE1, JADE2 and JADE3) mediate acetylation of histone H4 (PubMed:16387653). Interacts with H3K4me3 and to a lesser extent with H3K4me2, the interaction augments KAT7/HBO1 acetylation activity on H3 tails (PubMed:16728974, PubMed:18381289). Interacts with EP300, RELA and TP53; these interactions may be indirect (PubMed:12750254, PubMed:15029197). Interacts with EGLN1 (PubMed:15897452). Interacts with BCL2A1 (By similarity). {ECO:0000250|UniProtKB:Q8C0D7, ECO:0000269|PubMed:12750254, ECO:0000269|PubMed:15029197, ECO:0000269|PubMed:15897452, ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:16728974, ECO:0000269|PubMed:18381289, ECO:0000269|PubMed:19187765, ECO:0000269|PubMed:22334692}. |
| Subcellular location: | |
Nucleus {ECO:0000269|PubMed:15029197, ECO:0000269|PubMed:16973615}. |
| Domain: | |
The PHD-type zinc finger mediates the binding to H3K4me3. {ECO:0000269|PubMed:16728974, ECO:0000269|PubMed:18381289}. |
| Domain: | |
The N-terminal coiled-coil domain mediates homodimerization. {ECO:0000269|PubMed:22334692}. |
| Ptm: | |
Citrullination by PADI4 within the nuclear localization signal disrupts the interaction with p53 and increases susceptibility to degradation. {ECO:0000269|PubMed:21454715}. |
| Miscellaneous: | |
[Isoform 2]: May be due to a competing donor splice site. {ECO:0000305}. |
| Miscellaneous: | |
[Isoform 4]: Lacks the nuclear localization signal (NLS), resulting in increased cytoplasmic localization. {ECO:0000305}. |
| Miscellaneous: | |
[Isoform 6]: Lacks the nuclear localization signal (NLS), resulting in increased cytoplasmic localization. {ECO:0000305}. |
| Miscellaneous: | |
[Isoform 7]: Lacks the nuclear localization signal (NLS), resulting in increased cytoplasmic localization. {ECO:0000305}. |
| Similarity: | |
Belongs to the ING family. {ECO:0000305}. |
| Sequence caution: | |
Sequence=AAG43153.1; Type=Frameshift; Evidence={ECO:0000305}; |
Annotations taken from UniProtKB at the EBI.