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bromodomain-containing protein 4; protein HUNK1 (BRD4, HUNK1)
Function:
1) chromosomal dynamics during mitosis
2) associated with chromosomes during mitosis
2) recognizes acetylated residues on histones
Pharmacology:
- anti-tubulin drugs disrupt BRD4 chromosomal interactions
Pathology:
- interacts with bovine papillomavirus type 1 regulatory protein E2
- chromosomal translocation t(15;19)(q14;p13) involving BRD4 with NUT is found in a rare, aggressive, & lethal carcinoma arising in midline organs of young people
- t(15;19)(q14;p13) produces a BRD4-NUT fusion protein
General
Bromodomain-containing protein
phosphoprotein
Properties
SIZE: entity length = 1362 aa
MW = 152 kD
COMPARTMENT: cell nucleus
MOTIF: bromodomain {75-147}
bromodomain {368-440}
Ser phosphorylation site {S469}
Ser phosphorylation site {S470}
lysine-rich region {535-594}
MOTIF: lysine residue (SEVERAL)
Thr phosphorylation site {T598}
Ser phosphorylation site {S601}
serine-rich region {692-717}
MOTIF: serine residue (SEVERAL)
serine-rich region {703-714}
MOTIF: serine residue (SEVERAL)
breakpoint {719-720}
histidine-rich region {738-743}
MOTIF: histidine residue (SEVERAL)
proline-rich region
SITE: 757-761
MOTIF: proline residue (SEVERAL)
proline-rich region
SITE: 764-770
MOTIF: proline residue (SEVERAL)
glutamine-rich region {771-775}
MOTIF: glutamine residue (SEVERAL)
proline-rich region
SITE: 776-783
MOTIF: proline residue (SEVERAL)
proline-rich region
SITE: 954-964
MOTIF: proline residue (SEVERAL)
proline-rich region
SITE: 974-986
MOTIF: proline residue (SEVERAL)
proline-rich region
SITE: 1011-1014
MOTIF: proline residue (SEVERAL)
proline-rich region
SITE: 1028-1033
MOTIF: proline residue (SEVERAL)
Ser phosphorylation site {S1045}
Ser phosphorylation site {S1117}
glutamine-rich region {1283-1300}
MOTIF: glutamine residue (SEVERAL)
alanine-rich region {1301-1308}
MOTIF: alanine residue (SEVERAL)
arginine-rich region {1335-1338}
MOTIF: arginine residue (SEVERAL)
Database Correlations
OMIM 608749
UniProt O60885
Pfam PF00439
Entrez Gene 23476
Kegg hsa:23476
References
UniProt :accession O60885