Q9D4H9 · PHF14_MOUSE
- ProteinPHD finger protein 14
- GenePhf14
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids941 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Histone-binding protein (By similarity).
Binds preferentially to unmodified histone H3 but can also bind to a lesser extent to histone H3 trimethylated at 'Lys-9' (H3K9me3) as well as to histone H3 monomethylated at 'Lys-27' (H3K27ac) and trimethylated at 'Lys-27' (H3K27me3) (By similarity).
Represses PDGFRA expression, thus playing a role in regulation of mesenchymal cell proliferation (PubMed:22730381).
Suppresses the expression of CDKN1A/p21 by reducing the level of trimethylation of histone H3 'Lys-4', leading to enhanced proliferation of germinal center B cells (PubMed:33035772).
Binds preferentially to unmodified histone H3 but can also bind to a lesser extent to histone H3 trimethylated at 'Lys-9' (H3K9me3) as well as to histone H3 monomethylated at 'Lys-27' (H3K27ac) and trimethylated at 'Lys-27' (H3K27me3) (By similarity).
Represses PDGFRA expression, thus playing a role in regulation of mesenchymal cell proliferation (PubMed:22730381).
Suppresses the expression of CDKN1A/p21 by reducing the level of trimethylation of histone H3 'Lys-4', leading to enhanced proliferation of germinal center B cells (PubMed:33035772).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 315 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 318 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 332 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 335 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 340 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 343 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 367 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 370 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 378 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 381 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 398 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 401 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 434 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 437 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 451 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 456 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 461 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 464 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 488 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 491 | Zn2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 721 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 724 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 736 | Zn2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 739 | Zn2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 744 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 747 | Zn2+ 6 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 766 | Zn2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 769 | Zn2+ 7 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 864 | Zn2+ 8 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 867 | Zn2+ 8 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 879 | Zn2+ 9 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 882 | Zn2+ 9 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 887 | Zn2+ 8 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 890 | Zn2+ 8 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 908 | Zn2+ 9 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 911 | Zn2+ 9 (UniProtKB | ChEBI) | ||||
Sequence: C |
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 | chromosome | |
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | histone binding | |
Molecular Function | histone reader activity | |
Molecular Function | zinc ion binding | |
Biological Process | germinal center B cell differentiation | |
Biological Process | lung alveolus development | |
Biological Process | mesenchymal cell proliferation | |
Biological Process | mesenchymal cell proliferation involved in lung development | |
Biological Process | negative regulation of cell population proliferation | |
Biological Process | negative regulation of mesenchymal cell proliferation | |
Biological Process | negative regulation of mesenchymal cell proliferation involved in lung development | |
Biological Process | negative regulation of platelet-derived growth factor receptor-alpha signaling pathway | |
Biological Process | negative regulation of transcription by RNA polymerase II | |
Biological Process | regulation of transcription by RNA polymerase II |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended namePHD finger protein 14
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ9D4H9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Isoform 1
Note: Mainly localized in the nucleus of interphase cells. In mitotic cells, colocalizes with condensed chromatin during metaphase and anaphase.
Isoform 2
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Death just after birth due to respiratory failure with lungs showing interstitial hyperplasia (PubMed:22730381, PubMed:23688586).
Abnormalities are also observed in other organs such as kidney and lung (PubMed:23688586).
Mesenchymal fibroblasts exhibit increased proliferation and increased PDGFRA expression (PubMed:22730381).
Conditional knockout in germinal center (GC) B cells results in reduced GC response in the spleen following immune challenge, with fewer and smaller GCs observed (PubMed:33035772).
Abnormalities are also observed in other organs such as kidney and lung (PubMed:23688586).
Mesenchymal fibroblasts exhibit increased proliferation and increased PDGFRA expression (PubMed:22730381).
Conditional knockout in germinal center (GC) B cells results in reduced GC response in the spleen following immune challenge, with fewer and smaller GCs observed (PubMed:33035772).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 41 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000059307 | 1-941 | PHD finger protein 14 | |||
Sequence: MDRSSKRRQVKPLAASLLEALDYDSSDDSDFKVGDASDSEGSGNGSEDPSKDSGEGSCSDSEENILEEELNEDIQVKEEQLKNSTEEIMPSDKQLIKMEKKEEEENGERPRKKKEKEKEKEKEREKDKEKATVSDSAAASAAGTTPATSPPAVTSPSVPTTTTTTTEEQVSEPKKWNLRRNRPLLDFVSMEELNAMDDYDSEDDNDWRPTVVKRKGRSASQKEGSDGDNEDDDDEGSGSEEDENDEGNDEDHSSPASEAGGKKKRSKVLSRNSADDEELTNDSLTLSQSKSNEDSLILEKSQNWSSQKMDHILICCVCLGDNSEDADEIIQCDNCGITVHEGCYGVDGESDSIMSSASENSTEPWFCDACKCGVSPSCELCPNQDGIFKETDAGRWVHIVCALYVPGVAFGDIDKLRPVTLTEMNYSKYGAKECSFCEDPRFARTGVCISCDAGMCRAYFHVTCAQKEGLLSEAAAEEDIADPFFAYCKQHADRLDRKWKRKNYLALQSYCKMSLQEREKQLSPEAQARINARLQQYRAKAELARSTRPQAWVPREKLPRPLTSSASAIRKLMRKAELMGISTDIFPVDNSDTSSSVDGRRKHKQPALTADFVNYYFERNMRMIQIQENMAEQKNIKDKLENEQEKLHVEYNKLCESLEELQNLNGKLRSEGQGIWALLGRITGQKLNVPAILRAPKERKPSKKEGGTQKTSALPTVLYSCGICKKNHDQHLLLLCDTCKLHYHLGCLDPPLTRMPRKTKNSYWQCSECDQAGSSDMEAEMAMETLPDGTKRSRRQIKEPVKFVPQDVPPEPKKIPIRNTRTRGRKRSFVPEEEKHEERVPRERRQRQSVLQKKPKAEDLRTECSTCKGTGDNENLVRCDECRLCYHFGCLDPPLKKSPKQTGYGWICQECDSSSSKEDENEAEKKNASQELSMEQKTPKK | ||||||
Modified residue | 26 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 29 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 84 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 189 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 199 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 201 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 280 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 283 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 287 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 291 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 295 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 301 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 352 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 523 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 774 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 775 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 828 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
High levels detected in testis, lung and spleen and low levels in muscle, heart, intestine and kidney (at protein level) (PubMed:23688586).
Widely expressed in adult with increased levels in intestine, colon and lung (PubMed:22730381).
Widely expressed in adult with increased levels in intestine, colon and lung (PubMed:22730381).
Developmental stage
Expressed throughout embryogenesis and in the adult.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 22-295 | Disordered | ||||
Sequence: DYDSSDDSDFKVGDASDSEGSGNGSEDPSKDSGEGSCSDSEENILEEELNEDIQVKEEQLKNSTEEIMPSDKQLIKMEKKEEEENGERPRKKKEKEKEKEKEREKDKEKATVSDSAAASAAGTTPATSPPAVTSPSVPTTTTTTTEEQVSEPKKWNLRRNRPLLDFVSMEELNAMDDYDSEDDNDWRPTVVKRKGRSASQKEGSDGDNEDDDDEGSGSEEDENDEGNDEDHSSPASEAGGKKKRSKVLSRNSADDEELTNDSLTLSQSKSNEDS | ||||||
Compositional bias | 75-133 | Basic and acidic residues | ||||
Sequence: QVKEEQLKNSTEEIMPSDKQLIKMEKKEEEENGERPRKKKEKEKEKEKEREKDKEKATV | ||||||
Compositional bias | 137-171 | Polar residues | ||||
Sequence: AAASAAGTTPATSPPAVTSPSVPTTTTTTTEEQVS | ||||||
Compositional bias | 205-225 | Basic and acidic residues | ||||
Sequence: NDWRPTVVKRKGRSASQKEGS | ||||||
Compositional bias | 226-249 | Acidic residues | ||||
Sequence: DGDNEDDDDEGSGSEEDENDEGND | ||||||
Compositional bias | 250-278 | Basic and acidic residues | ||||
Sequence: EDHSSPASEAGGKKKRSKVLSRNSADDEE | ||||||
Compositional bias | 279-295 | Polar residues | ||||
Sequence: LTNDSLTLSQSKSNEDS | ||||||
Zinc finger | 312-373 | PHD-type 1 | ||||
Sequence: ILICCVCLGDNSEDADEIIQCDNCGITVHEGCYGVDGESDSIMSSASENSTEPWFCDACKCG | ||||||
Zinc finger | 375-408 | C2HC pre-PHD-type | ||||
Sequence: SPSCELCPNQDGIFKETDAGRWVHIVCALYVPGV | ||||||
Zinc finger | 432-492 | PHD-type 2 | ||||
Sequence: KECSFCEDPRFARTGVCISCDAGMCRAYFHVTCAQKEGLLSEAAAEEDIADPFFAYCKQHA | ||||||
Coiled coil | 623-671 | |||||
Sequence: MIQIQENMAEQKNIKDKLENEQEKLHVEYNKLCESLEELQNLNGKLRSE | ||||||
Zinc finger | 718-772 | PHD-type 3 | ||||
Sequence: LYSCGICKKNHDQHLLLLCDTCKLHYHLGCLDPPLTRMPRKTKNSYWQCSECDQA | ||||||
Region | 804-855 | Disordered | ||||
Sequence: VPQDVPPEPKKIPIRNTRTRGRKRSFVPEEEKHEERVPRERRQRQSVLQKKP | ||||||
Compositional bias | 825-855 | Basic and acidic residues | ||||
Sequence: RKRSFVPEEEKHEERVPRERRQRQSVLQKKP | ||||||
Zinc finger | 861-914 | PHD-type 4 | ||||
Sequence: RTECSTCKGTGDNENLVRCDECRLCYHFGCLDPPLKKSPKQTGYGWICQECDSS | ||||||
Region | 912-941 | Disordered | ||||
Sequence: DSSSSKEDENEAEKKNASQELSMEQKTPKK | ||||||
Compositional bias | 913-941 | Basic and acidic residues | ||||
Sequence: SSSSKEDENEAEKKNASQELSMEQKTPKK |
Domain
The N-terminal region, including the PHD-type 1 and 2 zinc fingers and the C2HC pre-PHD-type zinc finger, is required for binding to histone H3.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9D4H9-2
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
- Length941
- Mass (Da)105,947
- Last updated2022-10-12 v2
- ChecksumC60E58C89C3B6252
Q9D4H9-1
- Name2
Q9D4H9-3
- Name3
- Differences from canonical
- 879-941: Missing
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
G5E8S0 | G5E8S0_MOUSE | Phf14 | 881 | ||
A0A0N4SV73 | A0A0N4SV73_MOUSE | Phf14 | 90 | ||
A0A0N4SWI1 | A0A0N4SWI1_MOUSE | Phf14 | 69 | ||
A0A0N4SW36 | A0A0N4SW36_MOUSE | Phf14 | 42 | ||
F6TN92 | F6TN92_MOUSE | Phf14 | 243 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 75-133 | Basic and acidic residues | ||||
Sequence: QVKEEQLKNSTEEIMPSDKQLIKMEKKEEEENGERPRKKKEKEKEKEKEREKDKEKATV | ||||||
Sequence conflict | 133 | in Ref. 2; AAH40236 | ||||
Sequence: V → I | ||||||
Compositional bias | 137-171 | Polar residues | ||||
Sequence: AAASAAGTTPATSPPAVTSPSVPTTTTTTTEEQVS | ||||||
Compositional bias | 205-225 | Basic and acidic residues | ||||
Sequence: NDWRPTVVKRKGRSASQKEGS | ||||||
Compositional bias | 226-249 | Acidic residues | ||||
Sequence: DGDNEDDDDEGSGSEEDENDEGND | ||||||
Compositional bias | 250-278 | Basic and acidic residues | ||||
Sequence: EDHSSPASEAGGKKKRSKVLSRNSADDEE | ||||||
Compositional bias | 279-295 | Polar residues | ||||
Sequence: LTNDSLTLSQSKSNEDS | ||||||
Compositional bias | 825-855 | Basic and acidic residues | ||||
Sequence: RKRSFVPEEEKHEERVPRERRQRQSVLQKKP | ||||||
Alternative sequence | VSP_061649 | 879-881 | in isoform 2 | |||
Sequence: CDE → NLT | ||||||
Alternative sequence | VSP_061648 | 879-941 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_061650 | 882-941 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 913-941 | Basic and acidic residues | ||||
Sequence: SSSSKEDENEAEKKNASQELSMEQKTPKK |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK003209 EMBL· GenBank· DDBJ | BAB22644.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK016517 EMBL· GenBank· DDBJ | BAB30282.1 EMBL· GenBank· DDBJ | mRNA | ||
AK089073 EMBL· GenBank· DDBJ | BAC40735.1 EMBL· GenBank· DDBJ | mRNA | ||
BC040236 EMBL· GenBank· DDBJ | AAH40236.1 EMBL· GenBank· DDBJ | mRNA | ||
AY162410 EMBL· GenBank· DDBJ | AAO17166.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. |