Q9ULD4 · BRPF3_HUMAN
- ProteinBromodomain and PHD finger-containing protein 3
- GeneBRPF3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1205 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Scaffold subunit of various histone acetyltransferase (HAT) complexes, such as the MOZ/MORF and HBO1 complexes, which have a histone H3 acetyltransferase activity (PubMed:16387653, PubMed:26620551, PubMed:26677226).
Plays a role in DNA replication initiation by directing KAT7/HBO1 specificity towards histone H3 'Lys-14' acetylation (H3K14ac), thereby facilitating the activation of replication origins (PubMed:26620551).
Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity (PubMed:16387653).
Plays a role in DNA replication initiation by directing KAT7/HBO1 specificity towards histone H3 'Lys-14' acetylation (H3K14ac), thereby facilitating the activation of replication origins (PubMed:26620551).
Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity (PubMed:16387653).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | extracellular region | |
Cellular Component | histone acetyltransferase complex | |
Cellular Component | MOZ/MORF histone acetyltransferase complex | |
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Biological Process | chromatin remodeling | |
Biological Process | positive regulation of DNA replication | |
Biological Process | regulation of developmental process | |
Biological Process | regulation of DNA-templated transcription | |
Biological Process | regulation of hemopoiesis | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBromodomain and PHD finger-containing protein 3
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9ULD4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_061042 | 177 | in dbSNP:rs45504893 | |||
Sequence: S → G | ||||||
Natural variant | VAR_048431 | 278 | in dbSNP:rs17658935 | |||
Sequence: A → G |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,084 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000211188 | 1-1205 | UniProt | Bromodomain and PHD finger-containing protein 3 | |||
Sequence: MRKPRRKSRQNAEGRRSPSPYSLKCSPTRETLTYAQAQRIVEVDIDGRLHRISIYDPLKIITEDELTAQDITECNSNKENSEQPQFPGKSKKPSSKGKKKESCSKHASGTSFHLPQPSFRMVDSGIQPEAPPLPAAYYRYIEKPPEDLDAEVEYDMDEEDLAWLDMVNEKRRVDGHSLVSADTFELLVDRLEKESYLESRSSGAQQSLIDEDAFCCVCLDDECHNSNVILFCDICNLAVHQECYGVPYIPEGQWLCRCCLQSPSRPVDCILCPNKGGAFKQTSDGHWAHVVCAIWIPEVCFANTVFLEPIEGIDNIPPARWKLTCYICKQKGLGAAIQCHKVNCYTAFHVTCAQRAGLFMKIEPMRETSLNGTIFTVRKTAYCEAHSPPGAATARRKGDSPRSISETGDEEGLKEGDGEEEEEEEVEEEEQEAQGGVSGSLKGVPKKSKMSLKQKIKKEPEEAGQDTPSTLPMLAVPQIPSYRLNKICSGLSFQRKNQFMQRLHNYWLLKRQARNGVPLIRRLHSHLQSQRNAEQREQDEKTSAVKEELKYWQKLRHDLERARLLIELIRKREKLKREQVKVQQAAMELELMPFNVLLRTTLDLLQEKDPAHIFAEPVNLSEVPDYLEFISKPMDFSTMRRKLESHLYRTLEEFEEDFNLIVTNCMKYNAKDTIFHRAAVRLRDLGGAILRHARRQAENIGYDPERGTHLPESPKLEDFYRFSWEDVDNILIPENRAHLSPEVQLKELLEKLDLVSAMRSSGARTRRVRLLRREINALRQKLAQPPPPQPPSLNKTVSNGELPAGPQGDAAVLEQALQEEPEDDGDRDDSKLPPPPTLEPTGPAPSLSEQESPPEPPTLKPINDSKPPSRFLKPRKVEEDELLEKSPLQLGNEPLQRLLSDNGINRLSLMAPDTPAGTPLSGVGRRTSVLFKKAKNGVKLQRSPDRVLENGEDHGVAGSPASPASIEEERHSRKRPRSRSCSESEGERSPQQEEETGMTNGFGKHTESGSDSECSLGLSGGLAFEACSGLTPPKRSRGKPALSRVPFLEGVNGDSDYNGSGRSLLLPFEDRGDLEPLELVWAKCRGYPSYPALIIDPKMPREGLLHNGVPIPVPPLDVLKLGEQKQAEAGEKLFLVLFFDNKRTWQWLPRDKVLPLGVEDTVDKLKMLEGRKTSIRKSVQVAYDRAMIHLSRVRGPHSFVTSSYL | |||||||
Modified residue | 17 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 17 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 19 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 26 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 76 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 400 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 400 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 403 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 403 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 405 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 447 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 449 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 671 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue | 713 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 713 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 740 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 740 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 792 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 852 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 886 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 900 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 900 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 943 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 959 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 962 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 962 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 965 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 965 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Component of some HBO1 complex composed of KAT7/HBO1, MEAF6, ING4 or ING5, and BRPF3 (PubMed:26620551).
Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3 (PubMed:16387653, PubMed:18794358).
Interacts with KAT7/HBO1; the interaction is direct (PubMed:26677226).
Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3 (PubMed:16387653, PubMed:18794358).
Interacts with KAT7/HBO1; the interaction is direct (PubMed:26677226).
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-27 | Disordered | ||||
Sequence: MRKPRRKSRQNAEGRRSPSPYSLKCSP | ||||||
Compositional bias | 75-90 | Polar residues | ||||
Sequence: NSNKENSEQPQFPGKS | ||||||
Region | 75-121 | Disordered | ||||
Sequence: NSNKENSEQPQFPGKSKKPSSKGKKKESCSKHASGTSFHLPQPSFRM | ||||||
Zinc finger | 212-262 | PHD-type 1 | ||||
Sequence: DAFCCVCLDDECHNSNVILFCDICNLAVHQECYGVPYIPEGQWLCRCCLQS | ||||||
Zinc finger | 266-299 | C2HC pre-PHD-type | ||||
Sequence: PVDCILCPNKGGAFKQTSDGHWAHVVCAIWIPEV | ||||||
Zinc finger | 323-387 | PHD-type 2 | ||||
Sequence: LTCYICKQKGLGAAIQCHKVNCYTAFHVTCAQRAGLFMKIEPMRETSLNGTIFTVRKTAYCEAHS | ||||||
Region | 387-472 | Disordered | ||||
Sequence: SPPGAATARRKGDSPRSISETGDEEGLKEGDGEEEEEEEVEEEEQEAQGGVSGSLKGVPKKSKMSLKQKIKKEPEEAGQDTPSTLP | ||||||
Compositional bias | 412-432 | Acidic residues | ||||
Sequence: GLKEGDGEEEEEEEVEEEEQE | ||||||
Domain | 606-676 | Bromo | ||||
Sequence: QEKDPAHIFAEPVNLSEVPDYLEFISKPMDFSTMRRKLESHLYRTLEEFEEDFNLIVTNCMKYNAKDTIFH | ||||||
Region | 779-897 | Disordered | ||||
Sequence: RQKLAQPPPPQPPSLNKTVSNGELPAGPQGDAAVLEQALQEEPEDDGDRDDSKLPPPPTLEPTGPAPSLSEQESPPEPPTLKPINDSKPPSRFLKPRKVEEDELLEKSPLQLGNEPLQR | ||||||
Compositional bias | 834-863 | Pro residues | ||||
Sequence: PPPTLEPTGPAPSLSEQESPPEPPTLKPIN | ||||||
Compositional bias | 869-886 | Basic and acidic residues | ||||
Sequence: SRFLKPRKVEEDELLEKS | ||||||
Region | 907-926 | Disordered | ||||
Sequence: LSLMAPDTPAGTPLSGVGRR | ||||||
Region | 931-1015 | Disordered | ||||
Sequence: FKKAKNGVKLQRSPDRVLENGEDHGVAGSPASPASIEEERHSRKRPRSRSCSESEGERSPQQEEETGMTNGFGKHTESGSDSECS | ||||||
Compositional bias | 938-952 | Basic and acidic residues | ||||
Sequence: VKLQRSPDRVLENGE | ||||||
Compositional bias | 966-992 | Basic and acidic residues | ||||
Sequence: IEEERHSRKRPRSRSCSESEGERSPQQ | ||||||
Compositional bias | 993-1015 | Polar residues | ||||
Sequence: EEETGMTNGFGKHTESGSDSECS | ||||||
Domain | 1076-1159 | PWWP | ||||
Sequence: PLELVWAKCRGYPSYPALIIDPKMPREGLLHNGVPIPVPPLDVLKLGEQKQAEAGEKLFLVLFFDNKRTWQWLPRDKVLPLGVE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9ULD4-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,205
- Mass (Da)135,745
- Last updated2005-07-19 v2
- ChecksumF51DCAB253ED35C7
Q9ULD4-2
- Name2
- Differences from canonical
- 727-996: Missing
Q9ULD4-3
- Name3
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 75-90 | Polar residues | ||||
Sequence: NSNKENSEQPQFPGKS | ||||||
Compositional bias | 412-432 | Acidic residues | ||||
Sequence: GLKEGDGEEEEEEEVEEEEQE | ||||||
Alternative sequence | VSP_055549 | 727-996 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 834-863 | Pro residues | ||||
Sequence: PPPTLEPTGPAPSLSEQESPPEPPTLKPIN | ||||||
Compositional bias | 869-886 | Basic and acidic residues | ||||
Sequence: SRFLKPRKVEEDELLEKS | ||||||
Compositional bias | 938-952 | Basic and acidic residues | ||||
Sequence: VKLQRSPDRVLENGE | ||||||
Compositional bias | 966-992 | Basic and acidic residues | ||||
Sequence: IEEERHSRKRPRSRSCSESEGERSPQQ | ||||||
Compositional bias | 993-1015 | Polar residues | ||||
Sequence: EEETGMTNGFGKHTESGSDSECS | ||||||
Alternative sequence | VSP_055550 | 997-1060 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 1075 | in Ref. 1; BAA86600 | ||||
Sequence: E → K |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB033112 EMBL· GenBank· DDBJ | BAA86600.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
Z84485 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471081 EMBL· GenBank· DDBJ | EAX03878.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC117387 EMBL· GenBank· DDBJ | AAI17388.1 EMBL· GenBank· DDBJ | mRNA | ||
BC143917 EMBL· GenBank· DDBJ | AAI43918.1 EMBL· GenBank· DDBJ | mRNA | ||
BC143918 EMBL· GenBank· DDBJ | AAI43919.1 EMBL· GenBank· DDBJ | mRNA |