Q06205 · FKBP4_YEAST
- ProteinFK506-binding protein 4
- GeneFPR4
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids392 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
PPIase that acts as a histone chaperone (PubMed:14981505, PubMed:16846601).
Histone proline isomerase that increases the rate of cis-trans isomerization at 'Pro-17' (H3P16), 'Pro-31' (H3P30) and 'Pro-39 (H3P38) on the histone H3 N-terminal tail (PubMed:16959570, PubMed:23888048).
H3P16 and H3P30 are the major proline targets with little activity shown against H3P38 (PubMed:23888048).
H3P38 isomerization influences SET2-mediated H3K36 methylation thereby regulating gene expression (PubMed:16959570).
Histone proline isomerase that increases the rate of cis-trans isomerization at 'Pro-17' (H3P16), 'Pro-31' (H3P30) and 'Pro-39 (H3P38) on the histone H3 N-terminal tail (PubMed:16959570, PubMed:23888048).
H3P16 and H3P30 are the major proline targets with little activity shown against H3P38 (PubMed:23888048).
H3P38 isomerization influences SET2-mediated H3K36 methylation thereby regulating gene expression (PubMed:16959570).
Miscellaneous
Present with 14100 molecules/cell in log phase SD medium.
Catalytic activity
- [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
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 | chromatin | |
Cellular Component | nucleolus | |
Cellular Component | nucleus | |
Molecular Function | macrolide binding | |
Molecular Function | peptidyl-prolyl cis-trans isomerase activity | |
Biological Process | epigenetic regulation of gene expression | |
Biological Process | maintenance of rDNA | |
Biological Process | nucleosome assembly |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameFK506-binding protein 4
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ06205
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000075314 | 1-392 | FK506-binding protein 4 | |||
Sequence: MSDMLPLATYSLNVEPYSPTPALNFKIPVTIRITMAAIDPEPFDDDKKPSTLRIIKRNPELTRGEYYNQDNNDGLEEDESESEQEADVPKRSVKSKKGKAVEQSESEDSEDENEIDDEFEECVLLTLSPKGQYQQALDITIAPEEDVQFVVTGSYTISLTGNYVKHPFDNSSDSDEDEEDYYSDEESSNGEEEEEEEEEDDEELSSGDDDLDDLVDASDIESRLDELVKKDEKKKNNKKDSKRKHEEDEEESAKPAEKKQTTKKDKKAEKVKDSEESKPKPKTKLLEGGIIIEDRVTGKGPHAKKGTRVGMRYVGKLKNGKVFDKNTKGKPFVFKLGQGEVIKGWDIGVAGMAVGGERRIVIPAPYAYGKQALPGIPANSELTFDVKLVSMK | ||||||
Modified residue | 80 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 82 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Binds to histones H3 and H4 (PubMed:16959570).
Interacts with NOP53
Interacts with NOP53
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q06205 | EBP2 P36049 | 3 | EBI-6956, EBI-6289 | |
BINARY | Q06205 | FPR3 P38911 | 5 | EBI-6956, EBI-6951 | |
BINARY | Q06205 | HHF2 P02309 | 5 | EBI-6956, EBI-8113 | |
BINARY | Q06205 | HHT2 P61830 | 7 | EBI-6956, EBI-8098 | |
BINARY | Q06205 | LOC1 P43586 | 4 | EBI-6956, EBI-22906 | |
BINARY | Q06205 | NOC2 P39744 | 3 | EBI-6956, EBI-29259 | |
BINARY | Q06205 | NOP53 Q12080 | 3 | EBI-6956, EBI-29395 | |
BINARY | Q06205 | SPB1 P25582 | 3 | EBI-6956, EBI-17814 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 58-116 | Disordered | ||||
Sequence: NPELTRGEYYNQDNNDGLEEDESESEQEADVPKRSVKSKKGKAVEQSESEDSEDENEID | ||||||
Compositional bias | 84-104 | Basic and acidic residues | ||||
Sequence: QEADVPKRSVKSKKGKAVEQS | ||||||
Region | 161-284 | Disordered | ||||
Sequence: GNYVKHPFDNSSDSDEDEEDYYSDEESSNGEEEEEEEEEDDEELSSGDDDLDDLVDASDIESRLDELVKKDEKKKNNKKDSKRKHEEDEEESAKPAEKKQTTKKDKKAEKVKDSEESKPKPKTK | ||||||
Compositional bias | 173-216 | Acidic residues | ||||
Sequence: DSDEDEEDYYSDEESSNGEEEEEEEEEDDEELSSGDDDLDDLVD | ||||||
Compositional bias | 217-284 | Basic and acidic residues | ||||
Sequence: ASDIESRLDELVKKDEKKKNNKKDSKRKHEEDEEESAKPAEKKQTTKKDKKAEKVKDSEESKPKPKTK | ||||||
Domain | 306-392 | PPIase FKBP-type | ||||
Sequence: GTRVGMRYVGKLKNGKVFDKNTKGKPFVFKLGQGEVIKGWDIGVAGMAVGGERRIVIPAPYAYGKQALPGIPANSELTFDVKLVSMK |
Sequence similarities
Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length392
- Mass (Da)43,903
- Last updated1996-11-01 v1
- ChecksumCF90C6714F04572E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 84-104 | Basic and acidic residues | ||||
Sequence: QEADVPKRSVKSKKGKAVEQS | ||||||
Compositional bias | 173-216 | Acidic residues | ||||
Sequence: DSDEDEEDYYSDEESSNGEEEEEEEEEDDEELSSGDDDLDDLVD | ||||||
Compositional bias | 217-284 | Basic and acidic residues | ||||
Sequence: ASDIESRLDELVKKDEKKKNNKKDSKRKHEEDEEESAKPAEKKQTTKKDKKAEKVKDSEESKPKPKTK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U22382 EMBL· GenBank· DDBJ | AAB67528.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006945 EMBL· GenBank· DDBJ | DAA09749.1 EMBL· GenBank· DDBJ | Genomic DNA |