PHF8
entrez
23133
canonical
uniprot
Q9UPP1
canonical
ensembl
ENSG00000172943
resolver
ensp
ENSP00000319473
resolver
ensp
ENSP00000338868
resolver
ensp
ENSP00000350676
resolver
ensp
ENSP00000379578
resolver
enst
ENST00000396282
resolver
genesymbol
PHF8
resolver
genesymbol_syn
KDM7B
resolver
genesymbol_syn
KIAA1111
resolver
genesymbol_syn
ZNF422
resolver
hgnc
HGNC:20672
resolver
uniprot
B3KMV4
resolver
uniprot
B7Z911
resolver
uniprot
H0Y3N9
resolver
uniprot
O95327
resolver
uniprot
Q5H9U5
resolver
uniprot
Q5JPR9
resolver
uniprot
Q5JPS0
resolver
uniprot
Q5JPS2
resolver
uniprot
Q5JPS3
resolver
uniprot
Q5VUJ4
resolver
uniprot
Q7Z6D4
resolver
uniprot
Q9HAH2
resolver
uniprot_entry
H0Y3N9_HUMAN
resolver
uniprot_entry
O95327_HUMAN
resolver
uniprot_entry
PHF8_HUMAN
resolver
uniprot_sec
B3KMV4
resolver
uniprot_sec
B7Z911
resolver
uniprot_sec
Q5H9U5
resolver
uniprot_sec
Q5JPR9
resolver
uniprot_sec
Q5JPS0
resolver
uniprot_sec
Q5JPS2
resolver
uniprot_sec
Q5JPS3
resolver
uniprot_sec
Q5VUJ4
resolver
uniprot_sec
Q7Z6D4
resolver
uniprot_sec
Q9HAH2
resolver
amino_acid_sequence
MNRSRAIVQRGRVLPPPAPLDTTNLAGRRTLQGRAKMASVPVYCLCRLPYDVTRFMIECDMCQDWFHGSCVGVEEEKAADIDLYHCPNCEVLHGPSIMKKRRGSSKGHDTHKGKPVKTGSPTFVRELRSRTFDSSDEVILKPTGNQLTVEFLEENSFSVPILVLKKDGLGMTLPSPSFTVRDVEHYVGSDKEIDVIDVTRQADCKMKLGDFVKYYYSGKREKVLNVISLEFSDTRLSNLVETPKIVRKLSWVENLWPEECVFERPNVQKYCLMSVRDSYTDFHIDFGGTSVWYHVLKGEKIFYLIRPTNANLTLFECWSSSSNQNEMFFGDQVDKCYKCSVKQGQTLFIPTGWIHAVLTPVDCLAFGGNFLHSLNIEMQLKAYEIEKRLSTADLFRFPNFETICWYVGKHILDIFRGLRENRRHPASYLVHGGKALNLAFRAWTRKEALPDHEDEIPETVRTVQLIKDLAREIRLVEDIFQQNVGKTSNIFGLQRIFPAGSIPLTRPAHSTSVSMSRLSLPSKNGSKKKGLKPKELFKKAERKGKESSALGPAGQLSYNLMDTYSHQALKTGSFQKAKFNITGACLNDSDDDSPDLDLDGNESPLALLMSNGSTKRVKSLSKSRRTKIAKKVDKARLMAEQVMEDEFDLDSDDELQIDERLGKEKATLIIRPKFPRKLPRAKPCSDPNRVREPGEVEFDIEEDYTTDEDMVEGVEGKLGNGSGAGGILDLLKASRQVGGPDYAALTEAPASPSTQEAIQGMLCMANLQSSSSSPATSSLQAWWTGGQDRSSGSSSSGLGTVSNSPASQRTPGKRPIKRPAYWRTESEEEEENASLDEQDSLGACFKDAEYIYPSLESDDDDPALKSRPKKKKNSDDAPWSPKARVTPTLPKQDRPVREGTRVASIETGLAAAAAKLAQQELQKAQKKKYIKKKPLLKEVEQPRPQDSNLSLTVPAPTVAATPQLVTSSSPLPPPEPKQEALSGSLADHEYTARPNAFGMAQANRSTTPMAPGVFLTQRRPSVGSQSNQAGQGKRPKKGLATAKQRLGRILKIHRNGKLLL
uniprot
proteins
disease_involvement
DISEASE: Intellectual developmental disorder, X-linked, syndromic, Siderius type (MRXSSD) [MIM:300263]: A syndrome characterized by mild to borderline intellectual disability with or without cleft lip/cleft palate. {ECO:0000269|PubMed:16199551, ECO:0000269|PubMed:17661819, ECO:0000269|PubMed:20101266, ECO:0000269|PubMed:20208542, ECO:0000269|PubMed:20346720, ECO:0000269|PubMed:20421419, ECO:0000269|PubMed:20548336, ECO:0000269|PubMed:20622853, ECO:0000269|PubMed:20622854, ECO:0000269|PubMed:31691806}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
1.14.11.-
uniprot
proteins
ec_number
1.14.11.65
uniprot
proteins
function
FUNCTION: Histone lysine demethylase with selectivity for mono- and dimethylated residues. It plays an essential role in cell cycle progression and rDNA transcription (PubMed:19843542, PubMed:20531378, PubMed:20548336, PubMed:20622854). Demethylates mono- and dimethylated histone H3 'Lys-9' residue (H3K9Me1 and H3K9Me2) and monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1 are epigenetic repressive marks (PubMed:20101266, PubMed:20208542, PubMed:20346720, PubMed:20622853, PubMed:20622854). Displays a very low intrinsic activity toward dimethylated H3 'Lys-27' (H3K27Me2) (PubMed:20346720). May also have weak activity toward dimethylated H3 'Lys-36' (H3K36Me2), however, the relevance of this result remains unsure in vivo (PubMed:19843542, PubMed:20023638, PubMed:20346720). Involved in cell cycle progression by being required to control G1-S transition (PubMed:20622854). Acts as a coactivator of rDNA transcription, by activating polymerase I (pol I) mediated transcription of rRNA genes (PubMed:20531378). Specifically binds trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone demethylase specificity: has weak activity toward H3K9Me2 in absence of H3K4me3, while it has high activity toward H3K9me2 when binding H3K4me3 (PubMed:20023638, PubMed:20346720, PubMed:20421419). Positively modulates transcription of histone demethylase KDM5C, acting synergistically with transcription factor ARX; synergy may be related to enrichment of histone H3K4me3 in regulatory elements (PubMed:31691806). Required for brain development, probably by regulating expression of neuron-specific genes (By similarity). {ECO:0000250|UniProtKB:P0CH95, ECO:0000269|PubMed:19843542, ECO:0000269|PubMed:20023638, ECO:0000269|PubMed:20101266, ECO:0000269|PubMed:20208542, ECO:0000269|PubMed:20346720, ECO:0000269|PubMed:20421419, ECO:0000269|PubMed:20531378, ECO:0000269|PubMed:20548336, ECO:0000269|PubMed:20622853, ECO:0000269|PubMed:20622854, ECO:0000269|PubMed:31691806}.
uniprot
proteins
mass_dalton
117864
uniprot
proteins
mutagenesis
MUTAGEN 43; /note="Y->A: Abolishes binding to H3K4me3; when associated with A-50."; /evidence="ECO:0000269|PubMed:20208542, ECO:0000269|PubMed:20622853"; MUTAGEN 50; /note="Y->A: Abolishes binding to H3K4me3; when associated with A-43. Abolishes binding to H3K4me3; when associated with A-65."; /evidence="ECO:0000269|PubMed:20622853"; MUTAGEN 65; /note="W->A: Abolishes binding to H3K4me3; when associated with A-50."; /evidence="ECO:0000269|PubMed:20622853"; MUTAGEN 69; /note="S->A: Impairs phosphorylation by CDK1 and dissociation from chromatin when cells enter mitosis; when associated with A-120."; /evidence="ECO:0000269|PubMed:20622854"; MUTAGEN 120; /note="S->A: Impairs phosphorylation by CDK1 and dissociation from chromatin when cells enter mitosis; when associated with A-69."; /evidence="ECO:0000269|PubMed:20622854"; MUTAGEN 283..285; /note="HID->AAA: Abolishes histone methyltransferase activity."; /evidence="ECO:0000269|PubMed:20208542"; MUTAGEN 283; /note="H->A: Abolishes histone methyltransferase activity."; /evidence="ECO:0000269|PubMed:20346720, ECO:0000269|PubMed:20531378, ECO:0000269|PubMed:20622854"; MUTAGEN 943; /note="R->H: Reduces transcriptional activation activity."; /evidence="ECO:0000269|PubMed:31691806
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-69 and Ser-120 are required for dissociation from chromatin and accumulation of H4K20Me1 levels during prophase. {ECO:0000269|PubMed:20622854}.
uniprot
proteins
protein_family
JHDM1 histone demethylase family
uniprot
proteins
protein_family
JHDM1D subfamily
uniprot
proteins
pubmed
10470851
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
16199551
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17661819
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19843542
uniprot
proteins
pubmed
20023638
uniprot
proteins
pubmed
20067792
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20101266
uniprot
proteins
pubmed
20208542
uniprot
proteins
pubmed
20346720
uniprot
proteins
pubmed
20421419
uniprot
proteins
pubmed
20531378
uniprot
proteins
pubmed
20548336
uniprot
proteins
pubmed
20622853
uniprot
proteins
pubmed
20622854
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23092983
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
31691806
uniprot
proteins
pubmed
32051553
uniprot
proteins
sequence_length
1060
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19843542, ECO:0000269|PubMed:20622854}. Nucleus, nucleolus {ECO:0000269|PubMed:20208542, ECO:0000269|PubMed:20531378}. Note=Recruited to H3K4me3 sites on chromatin during interphase (PubMed:20622854). Dissociates from chromatin when cells enter mitosis (PubMed:20622854). {ECO:0000269|PubMed:20622854}.
uniprot
proteins