Q9D4H9 · PHF14_MOUSE

  • Protein
    PHD finger protein 14
  • Gene
    Phf14
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Features

Showing features for binding site.

1941100200300400500600700800900
TypeIDPosition(s)Description
Binding site315Zn2+ 1 (UniProtKB | ChEBI)
Binding site318Zn2+ 1 (UniProtKB | ChEBI)
Binding site332Zn2+ 2 (UniProtKB | ChEBI)
Binding site335Zn2+ 2 (UniProtKB | ChEBI)
Binding site340Zn2+ 1 (UniProtKB | ChEBI)
Binding site343Zn2+ 1 (UniProtKB | ChEBI)
Binding site367Zn2+ 2 (UniProtKB | ChEBI)
Binding site370Zn2+ 2 (UniProtKB | ChEBI)
Binding site378Zn2+ 3 (UniProtKB | ChEBI)
Binding site381Zn2+ 3 (UniProtKB | ChEBI)
Binding site398Zn2+ 3 (UniProtKB | ChEBI)
Binding site401Zn2+ 3 (UniProtKB | ChEBI)
Binding site434Zn2+ 4 (UniProtKB | ChEBI)
Binding site437Zn2+ 4 (UniProtKB | ChEBI)
Binding site451Zn2+ 5 (UniProtKB | ChEBI)
Binding site456Zn2+ 5 (UniProtKB | ChEBI)
Binding site461Zn2+ 4 (UniProtKB | ChEBI)
Binding site464Zn2+ 4 (UniProtKB | ChEBI)
Binding site488Zn2+ 5 (UniProtKB | ChEBI)
Binding site491Zn2+ 5 (UniProtKB | ChEBI)
Binding site721Zn2+ 6 (UniProtKB | ChEBI)
Binding site724Zn2+ 6 (UniProtKB | ChEBI)
Binding site736Zn2+ 7 (UniProtKB | ChEBI)
Binding site739Zn2+ 7 (UniProtKB | ChEBI)
Binding site744Zn2+ 6 (UniProtKB | ChEBI)
Binding site747Zn2+ 6 (UniProtKB | ChEBI)
Binding site766Zn2+ 7 (UniProtKB | ChEBI)
Binding site769Zn2+ 7 (UniProtKB | ChEBI)
Binding site864Zn2+ 8 (UniProtKB | ChEBI)
Binding site867Zn2+ 8 (UniProtKB | ChEBI)
Binding site879Zn2+ 9 (UniProtKB | ChEBI)
Binding site882Zn2+ 9 (UniProtKB | ChEBI)
Binding site887Zn2+ 8 (UniProtKB | ChEBI)
Binding site890Zn2+ 8 (UniProtKB | ChEBI)
Binding site908Zn2+ 9 (UniProtKB | ChEBI)
Binding site911Zn2+ 9 (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentchromosome
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular Functionhistone binding
Molecular Functionhistone reader activity
Molecular Functionzinc ion binding
Biological Processgerminal center B cell differentiation
Biological Processlung alveolus development
Biological Processmesenchymal cell proliferation
Biological Processmesenchymal cell proliferation involved in lung development
Biological Processnegative regulation of cell population proliferation
Biological Processnegative regulation of mesenchymal cell proliferation
Biological Processnegative regulation of mesenchymal cell proliferation involved in lung development
Biological Processnegative regulation of platelet-derived growth factor receptor-alpha signaling pathway
Biological Processnegative regulation of transcription by RNA polymerase II
Biological Processregulation of transcription by RNA polymerase II

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    PHD finger protein 14

Gene names

    • Name
      Phf14

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • FVB/N
    • 129S6/SvEvTac
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9D4H9
  • Secondary accessions
    • Q810Z6
    • Q8C284
    • Q8CGF8
    • Q9D1Q8

Proteomes

Organism-specific databases

Subcellular Location

Isoform 1

Nucleus
Chromosome
Note: Mainly localized in the nucleus of interphase cells. In mitotic cells, colocalizes with condensed chromatin during metaphase and anaphase.

Isoform 2

Cytoplasm

Keywords

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).

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00000593071-941PHD finger protein 14
Modified residue26Phosphoserine
Modified residue29Phosphoserine
Modified residue84Phosphoserine
Modified residue189Phosphoserine
Modified residue199Phosphotyrosine
Modified residue201Phosphoserine
Modified residue280Phosphothreonine
Modified residue283Phosphoserine
Modified residue287Phosphoserine
Modified residue291Phosphoserine
Modified residue295Phosphoserine
Modified residue301Phosphoserine
Modified residue352Phosphoserine
Modified residue523Phosphoserine
Modified residue774Phosphoserine
Modified residue775Phosphoserine
Modified residue828Phosphoserine

Keywords

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).

Developmental stage

Expressed throughout embryogenesis and in the adult.

Gene expression databases

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias, zinc finger, coiled coil.

TypeIDPosition(s)Description
Region22-295Disordered
Compositional bias75-133Basic and acidic residues
Compositional bias137-171Polar residues
Compositional bias205-225Basic and acidic residues
Compositional bias226-249Acidic residues
Compositional bias250-278Basic and acidic residues
Compositional bias279-295Polar residues
Zinc finger312-373PHD-type 1
Zinc finger375-408C2HC pre-PHD-type
Zinc finger432-492PHD-type 2
Coiled coil623-671
Zinc finger718-772PHD-type 3
Region804-855Disordered
Compositional bias825-855Basic and acidic residues
Zinc finger861-914PHD-type 4
Region912-941Disordered
Compositional bias913-941Basic and acidic residues

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

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

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.

  • Length
    941
  • Mass (Da)
    105,947
  • Last updated
    2022-10-12 v2
  • Checksum
    C60E58C89C3B6252
MDRSSKRRQVKPLAASLLEALDYDSSDDSDFKVGDASDSEGSGNGSEDPSKDSGEGSCSDSEENILEEELNEDIQVKEEQLKNSTEEIMPSDKQLIKMEKKEEEENGERPRKKKEKEKEKEKEREKDKEKATVSDSAAASAAGTTPATSPPAVTSPSVPTTTTTTTEEQVSEPKKWNLRRNRPLLDFVSMEELNAMDDYDSEDDNDWRPTVVKRKGRSASQKEGSDGDNEDDDDEGSGSEEDENDEGNDEDHSSPASEAGGKKKRSKVLSRNSADDEELTNDSLTLSQSKSNEDSLILEKSQNWSSQKMDHILICCVCLGDNSEDADEIIQCDNCGITVHEGCYGVDGESDSIMSSASENSTEPWFCDACKCGVSPSCELCPNQDGIFKETDAGRWVHIVCALYVPGVAFGDIDKLRPVTLTEMNYSKYGAKECSFCEDPRFARTGVCISCDAGMCRAYFHVTCAQKEGLLSEAAAEEDIADPFFAYCKQHADRLDRKWKRKNYLALQSYCKMSLQEREKQLSPEAQARINARLQQYRAKAELARSTRPQAWVPREKLPRPLTSSASAIRKLMRKAELMGISTDIFPVDNSDTSSSVDGRRKHKQPALTADFVNYYFERNMRMIQIQENMAEQKNIKDKLENEQEKLHVEYNKLCESLEELQNLNGKLRSEGQGIWALLGRITGQKLNVPAILRAPKERKPSKKEGGTQKTSALPTVLYSCGICKKNHDQHLLLLCDTCKLHYHLGCLDPPLTRMPRKTKNSYWQCSECDQAGSSDMEAEMAMETLPDGTKRSRRQIKEPVKFVPQDVPPEPKKIPIRNTRTRGRKRSFVPEEEKHEERVPRERRQRQSVLQKKPKAEDLRTECSTCKGTGDNENLVRCDECRLCYHFGCLDPPLKKSPKQTGYGWICQECDSSSSKEDENEAEKKNASQELSMEQKTPKK

Q9D4H9-1

Q9D4H9-3

Computationally mapped potential isoform sequences

There are 5 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
G5E8S0G5E8S0_MOUSEPhf14881
A0A0N4SV73A0A0N4SV73_MOUSEPhf1490
A0A0N4SWI1A0A0N4SWI1_MOUSEPhf1469
A0A0N4SW36A0A0N4SW36_MOUSEPhf1442
F6TN92F6TN92_MOUSEPhf14243

Sequence caution

The sequence AAO17166.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence BAB22644.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for compositional bias, sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Compositional bias75-133Basic and acidic residues
Sequence conflict133in Ref. 2; AAH40236
Compositional bias137-171Polar residues
Compositional bias205-225Basic and acidic residues
Compositional bias226-249Acidic residues
Compositional bias250-278Basic and acidic residues
Compositional bias279-295Polar residues
Compositional bias825-855Basic and acidic residues
Alternative sequenceVSP_061649879-881in isoform 2
Alternative sequenceVSP_061648879-941in isoform 3
Alternative sequenceVSP_061650882-941in isoform 2
Compositional bias913-941Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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.

Genome annotation databases

Similar Proteins

Disclaimer

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