UniProt functional annotation for Q92785



	UniProt functional annotation for Q92785

UniProt code: Q92785.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Plays an active role in transcriptional regulation by binding modified histones H3 and H4 (PubMed:28533407, PubMed:27775714). Is a negative regulator of myeloid differentiation of hematopoietic progenitor cells (PubMed:28533407). Might also have a role in the development and maturation of lymphoid cells (By similarity). Involved in the regulation of non-canonical NF-kappa-B pathway (PubMed:20460684). {ECO:0000250|UniProtKB:Q61103, ECO:0000269|PubMed:20460684, ECO:0000269|PubMed:27775714, ECO:0000269|PubMed:28533407}.

Subunit: Interacts with the nucleosomes, in particular nucleosomes bearing histone H3 crotonylated at 'Lys-14' (H3K14cr) for which DPF2 has high affinity (PubMed:27775714). Also interacts (via PHD-type zinc finger domains) with histone H3 butyrylated at 'Lys-14' (H3K14bu), histone H3 propionylated at 'Lys-14' (H3K14pr), and histone H3 acetylated at 'Lys-14' (H3K14ac) (PubMed:29429572, PubMed:28533407, PubMed:27775714). Interacts with histone H3 acetylated at 'Lys-9' (H3K9ac), histone H3 di-methylated at 'Lys-9' (H3K9me2), and histone H3 tri-methylated at 'Lys-9' (H3K9me3) (PubMed:29429572). Interacts with histone H4 acetylated at 'Lys-12' (H4K12ac) (PubMed:29429572). Interacts with histone H4 acetylated at 'Lys-16' (H4K16ac) (PubMed:28533407). Interacts with SWI/SNF complex components (PubMed:20460684, PubMed:28533407). Interacts with SMARCA2, SMARCA4, SMARCB1 and SMARCD1 (PubMed:20460684). Interacts with SMARCC1, SMARCC2 and ACTL6A (PubMed:28533407). Interacts with RUNX1 (PubMed:28533407). {ECO:0000269|PubMed:20460684, ECO:0000269|PubMed:28533407, ECO:0000269|PubMed:29429572}.

Subcellular location: Nucleus {ECO:0000269|PubMed:28533407, ECO:0000269|PubMed:29429572}. Cytoplasm {ECO:0000269|PubMed:28533407}.

Tissue specificity: Ubiquitous.

Disease: Coffin-Siris syndrome 7 (CSS7) [MIM:618027]: A form of Coffin- Siris syndrome, a congenital multiple malformation syndrome with broad phenotypic and genetic variability. Cardinal features are intellectual disability, coarse facial features, hypertrichosis, and hypoplastic or absent fifth digit nails or phalanges. Additional features include malformations of the cardiac, gastrointestinal, genitourinary, and/or central nervous systems. Sucking/feeding difficulties, poor growth, ophthalmologic abnormalities, hearing impairment, and spinal anomalies are common findings. Both autosomal dominant and autosomal recessive inheritance patterns have been reported. CSS7 inheritance is autosomal dominant. {ECO:0000269|PubMed:29429572}. Note=The disease is caused by variants affecting the gene represented in this entry.

Similarity: Belongs to the requiem/DPF family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Plays an active role in transcriptional regulation by binding modified histones H3 and H4 (PubMed:28533407, PubMed:27775714). Is a negative regulator of myeloid differentiation of hematopoietic progenitor cells (PubMed:28533407). Might also have a role in the development and maturation of lymphoid cells (By similarity). Involved in the regulation of non-canonical NF-kappa-B pathway (PubMed:20460684). {ECO:0000250\|UniProtKB:Q61103, ECO:0000269\|PubMed:20460684, ECO:0000269\|PubMed:27775714, ECO:0000269\|PubMed:28533407}.


Subunit:		Interacts with the nucleosomes, in particular nucleosomes bearing histone H3 crotonylated at 'Lys-14' (H3K14cr) for which DPF2 has high affinity (PubMed:27775714). Also interacts (via PHD-type zinc finger domains) with histone H3 butyrylated at 'Lys-14' (H3K14bu), histone H3 propionylated at 'Lys-14' (H3K14pr), and histone H3 acetylated at 'Lys-14' (H3K14ac) (PubMed:29429572, PubMed:28533407, PubMed:27775714). Interacts with histone H3 acetylated at 'Lys-9' (H3K9ac), histone H3 di-methylated at 'Lys-9' (H3K9me2), and histone H3 tri-methylated at 'Lys-9' (H3K9me3) (PubMed:29429572). Interacts with histone H4 acetylated at 'Lys-12' (H4K12ac) (PubMed:29429572). Interacts with histone H4 acetylated at 'Lys-16' (H4K16ac) (PubMed:28533407). Interacts with SWI/SNF complex components (PubMed:20460684, PubMed:28533407). Interacts with SMARCA2, SMARCA4, SMARCB1 and SMARCD1 (PubMed:20460684). Interacts with SMARCC1, SMARCC2 and ACTL6A (PubMed:28533407). Interacts with RUNX1 (PubMed:28533407). {ECO:0000269\|PubMed:20460684, ECO:0000269\|PubMed:28533407, ECO:0000269\|PubMed:29429572}.
Subcellular location:		Nucleus {ECO:0000269\|PubMed:28533407, ECO:0000269\|PubMed:29429572}. Cytoplasm {ECO:0000269\|PubMed:28533407}.
Tissue specificity:		Ubiquitous.
Disease:		Coffin-Siris syndrome 7 (CSS7) [MIM:618027]: A form of Coffin- Siris syndrome, a congenital multiple malformation syndrome with broad phenotypic and genetic variability. Cardinal features are intellectual disability, coarse facial features, hypertrichosis, and hypoplastic or absent fifth digit nails or phalanges. Additional features include malformations of the cardiac, gastrointestinal, genitourinary, and/or central nervous systems. Sucking/feeding difficulties, poor growth, ophthalmologic abnormalities, hearing impairment, and spinal anomalies are common findings. Both autosomal dominant and autosomal recessive inheritance patterns have been reported. CSS7 inheritance is autosomal dominant. {ECO:0000269\|PubMed:29429572}. Note=The disease is caused by variants affecting the gene represented in this entry.
Similarity:		Belongs to the requiem/DPF family. {ECO:0000305}.