PHF2
entrez
5253
canonical
uniprot
O75151
canonical
ensembl
ENSG00000197724
resolver
ensp
ENSP00000352185
resolver
ensp
ENSP00000521955
resolver
ensp
ENSP00000521956
resolver
enst
ENST00000359246
resolver
genesymbol
PHF2
resolver
genesymbol_syn
CENP-35
resolver
genesymbol_syn
KIAA0662
resolver
hgnc
HGNC:8920
resolver
uniprot
Q4VXG0
resolver
uniprot
Q8N3K2
resolver
uniprot
Q9Y6N4
resolver
uniprot_entry
PHF2_HUMAN
resolver
uniprot_sec
Q4VXG0
resolver
uniprot_sec
Q8N3K2
resolver
uniprot_sec
Q9Y6N4
resolver
activity_regulation
ACTIVITY REGULATION: Enzymatically inactive by itself, and become active following phosphorylation by PKA.
uniprot
proteins
amino_acid_sequence
MATVPVYCVCRLPYDVTRFMIECDACKDWFHGSCVGVEEEEAPDIDIYHCPNCEKTHGKSTLKKKRTWHKHGPGQAPDVKPVQNGSQLFIKELRSRTFPSAEDVVARVPGSQLTLGYMEEHGFTEPILVPKKDGLGLAVPAPTFYVSDVENYVGPERSVDVTDVTKQKDCKMKLKEFVDYYYSTNRKRVLNVTNLEFSDTRMSSFVEPPDIVKKLSWVENYWPDDALLAKPKVTKYCLICVKDSYTDFHIDSGGASAWYHVLKGEKTFYLIRPASANISLYERWRSASNHSEMFFADQVDKCYKCIVKQGQTLFIPSGWIYATLTPVDCLAFAGHFLHSLSVEMQMRAYEVERRLKLGSLTQFPNFETACWYMGKHLLEAFKGSHKSGKQLPPHLVQGAKILNGAFRSWTKKQALAEHEDELPEHFKPSQLIKDLAKEIRLSENASKAVRPEVNTVASSDEVCDGDREKEEPPSPIEATPPQSLLEKVSKKKTPKTVKMPKPSKIPKPPKPPKPPRPPKTLKLKDGGKKKGKKSRESASPTIPNLDLLEAHTKEALTKMEPPKKGKATKSVLSVPNKDVVHMQNDVERLEIREQTKSKSEAKWKYKNSKPDSLLKMEEEQKLEKSPLAGNKDNKFSFSFSNKKLLGSKALRPPTSPGVFGALQNFKEDKPKPVRDEYEYVSDDGELKIDEFPIRRKKNAPKRDLSFLLDKKAVLPTPVTKPKLDSAAYKSDDSSDEGSLHIDTDTKPGRNARVKKESGSSAAGILDLLQASEEVGALEYNPSSQPPASPSTQEAIQGMLSMANLQASDSCLQTTWGAGQAKGSSLAAHGARKNGGGSGKSAGKRLLKRAAKNSVDLDDYEEEQDHLDACFKDSDYVYPSLESDEDNPIFKSRSKKRKGSDDAPYSPTARVGPSVPRQDRPVREGTRVASIETGLAAAAAKLSQQEEQKSKKKKSAKRKLTPNTTSPSTSTSISAGTTSTSTTPASTTPASTTPASTSTASSQASQEGSSPEPPPESHSSSLADHEYTAAGTFTGAQAGRTSQPMAPGVFLTQRRPSASSPNNNTAAKGKRTKKGMATAKQRLGKILKIHRNGKLLL
uniprot
proteins
ec_number
1.14.11.-
uniprot
proteins
function
FUNCTION: Lysine demethylase that demethylates both histones and non-histone proteins (PubMed:20129925, PubMed:21167174, PubMed:21532585). Enzymatically inactive by itself, and becomes active following phosphorylation by PKA: forms a complex with ARID5B and mediates demethylation of methylated ARID5B (PubMed:21532585). Demethylation of ARID5B leads to target the PHF2-ARID5B complex to target promoters, where PHF2 mediates demethylation of dimethylated 'Lys-9' of histone H3 (H3K9me2), followed by transcription activation of target genes (PubMed:21532585). The PHF2-ARID5B complex acts as a coactivator of HNF4A in liver. PHF2 is recruited to trimethylated 'Lys-4' of histone H3 (H3K4me3) at rDNA promoters and promotes expression of rDNA (PubMed:21532585). Involved in the activation of toll-like receptor 4 (TLR4)-target inflammatory genes in macrophages by catalyzing the demethylation of trimethylated histone H4 lysine 20 (H4K20me3) at the gene promoters (By similarity). {ECO:0000250|UniProtKB:Q9WTU0, ECO:0000269|PubMed:20129925, ECO:0000269|PubMed:21167174, ECO:0000269|PubMed:21532585}.
uniprot
proteins
mass_dalton
120775
uniprot
proteins
mutagenesis
MUTAGEN 7; /note="Y->A: Abolishes binding to H3K4me2 and H3K4me3."; /evidence="ECO:0000269|PubMed:20129925"; MUTAGEN 29; /note="W->A: Abolishes binding to H3K4me2 and H3K4me3."; /evidence="ECO:0000269|PubMed:20129925"; MUTAGEN 249; /note="H->A: Abolishes demethylase activity."; /evidence="ECO:0000269|PubMed:21532585"; MUTAGEN 321; /note="Y->H: Does not alter iron-binding nor activates histone demethylase activity."; /evidence="ECO:0000269|PubMed:21167174"; MUTAGEN 757; /note="S->A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-899; A-954 and A-1056."; /evidence="ECO:0000269|PubMed:21532585"; MUTAGEN 899; /note="S->A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-954 and A-1056."; /evidence="ECO:0000269|PubMed:21532585"; MUTAGEN 954; /note="S->A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-899 and A-1056."; /evidence="ECO:0000269|PubMed:21532585"; MUTAGEN 1056; /note="S->A: Abolishes phosphorylation by PKA and activation of demethylase activity; when associated with A-757; A-899 and A-954."; /evidence="ECO:0000269|PubMed:21532585
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PKA on specific serine residues, leading to the formation of an active lysine demethylase complex. {ECO:0000269|PubMed:21532585}.
uniprot
proteins
protein_family
JHDM1 histone demethylase family
uniprot
proteins
protein_family
JHDM1D subfamily
uniprot
proteins
pubmed
10051327
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20129925
uniprot
proteins
pubmed
20813266
uniprot
proteins
pubmed
21167174
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21532585
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
9734811
uniprot
proteins
sequence_length
1096
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:20129925}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:20813266}.
uniprot
proteins