Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00310
Entry Name
UniProt Accession
Theoretical PI
8.69
Molecular Weight
113553.04
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Histone lysine demethylase PHF8
Protein Synonyms/Alias
1.14.11.27; PHD finger protein 8;
Gene Name
Phf8
Gene Synonyms/Alias
Kiaa1111;
Created Date
19-JUL-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
8
Canonical
MASVPVYCLCRLPYD
[1]
S-Palmitoylation
10
Canonical
SVPVYCLCRLPYDVT
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Predicted from GPS-Lipid
Functional Description
Histone lysine demethylase with selectivity for the di- and monomethyl states that plays a key role cell cycle progression, rDNA transcription and brain development. Demethylates mono- and dimethylated histone H3 'Lys-9' residue (H3K9Me1 and H3K9Me2), dimethylated H3 'Lys-27' (H3K27Me2) and monomethylated histone H4 'Lys-20' residue (H4K20Me1). Acts as a transcription activator as H3K9Me1, H3K9Me2, H3K27Me2 and H4K20Me1 are epigenetic repressive marks. Involved in cell cycle progression by being required to control G1-S transition. Acts as a coactivator of rDNA transcription, by activating polymerase I (pol I) mediated transcription of rRNA genes. Required for brain development, probably by regulating expression of neuron-specific genes. Has activity toward H4K20Me1 only when nucleosome is used as a substrate and when not histone octamer is used as substrate. May also have weak activity toward dimethylated H3 'Lys-36' (H3K36Me2), however, the relevance of this result remains unsure in vivo. 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 (By similarity).
Sequence Annotation
Domain: 195 351 JmjC.
Region: 65 79 Linker.
Metal binding site: 247 247 Iron; catalytic.
Metal binding site: 249 249 Iron; catalytic.
Metal binding site: 319 319 Iron; catalytic.
Binding site: 244 244 Substrate.
Binding site: 264 264 Substrate.
Modified residue: 33 33 Phosphoserine; by CDK1.
Modified residue: 84 84 Phosphoserine; by CDK1.
Modified residue: 615 615 Phosphoserine.
Modified residue: 669 669 Phosphothreonine.
Modified residue: 670 670 Phosphothreonine.
Modified residue: 768 768 Phosphoserine.
Modified residue: 817 817 Phosphoserine.
Modified residue: 820 820 Phosphoserine.
Modified residue: 843 843 Phosphoserine.
Protein Length
1023 AA.
Protein Sequence
(Canonical)
MASVPVYCLC RLPYDVTRFM IECDMCQDWF HGSCVGVEEE KAADIDLYHC PNCEVLHGPS  60
IMKKRRGSSK GHDNHKGKPL KTGSSMFIRE LRGRTFDSSD EVILKPTGSQ LTVEFLEENS  120
FSVPILVLKK DGLGMTLPSP SFTVRDVEHY VGSDKEIDVI DVARQADCKM KLGDFVKYYY  180
SGKREKVLNV ISLEFSDTRL SNLVETPRIV RKLSWVENLW PEECVFERPN VQKYCLMSVR  240
DSYTDFHIDF GGTSVWYHVL KGEKIFYLIR PTNANLTLFE CWSSSSNQNE MFFGDQVEKC  300
YKCSVKQGQT LFIPTGWIHA VLTPVDCLAF GGNFLHSLNI EMQLKAYEIE KRLSTADLFK  360
FPNFETICWY VGKHILDIFR GLRENRRHPA SYLVHGGKAL NLAFRAWTKK EALPDHEDEI  420
PETVRTVQLI KDLAREIRLV EDIFQQNVGK TSNIFGLQRI FPAGSIPLTK PAHSTSVSMS  480
KLSLPSKNGS KKKGLKPKDI FKKAERKGKQ SSALGPAGQL SYNLMDPYSH QALKTGPSQK  540
AKFNMSGTSL NDSDDDSADM DLDGSENPLA LLMANGSTKR MKSVSKSRRA KIAKKVDSAR  600
LVAEQVMGDE FDLDSDDELQ IDERLGKEKA NLLIRSKFPR KLPRAKPCSD PNRIREPGEV  660
EFDIEEDYTT DEDMVEGVES KLGNGSGAGG ILDLLKASRQ VGGPDYAALT EAPASPSTQE  720
AIQGMLCMAN LQSSSSSPAT SSLQAWWTGG QERSSGSSSS GLGTVSSSPA SQRTPGKRPI  780
KRPAYWKNES EEEENASLDE QDSLGACFKD AEYIYPSLES DDDDPALKSR PKKKKNSDDA  840
PWSPKARVTP TLPKQDRPVR EGTRVASIET GLAAAAAKLA QQELQKAQKK KYIKKKPLLK  900
EVEQPRPQDS NPIMTMPAPT VATTPQPDTS SSPQPPPEPK QEALSGSLAD HEYTARPNAF  960
GMAQANRSTT PMAPGVFLTQ RRPSVGSQSS QAGQGKRPKK GLATAKQRLG RILKIHRNGK  1020
LLL                                                                1023
FASTA
(Canonical)
>LipidDB-10090-00310|Q80TJ7
MASVPVYCLCRLPYDVTRFMIECDMCQDWFHGSCVGVEEEKAADIDLYHCPNCEVLHGPS
IMKKRRGSSKGHDNHKGKPLKTGSSMFIRELRGRTFDSSDEVILKPTGSQLTVEFLEENS
FSVPILVLKKDGLGMTLPSPSFTVRDVEHYVGSDKEIDVIDVARQADCKMKLGDFVKYYY
SGKREKVLNVISLEFSDTRLSNLVETPRIVRKLSWVENLWPEECVFERPNVQKYCLMSVR
DSYTDFHIDFGGTSVWYHVLKGEKIFYLIRPTNANLTLFECWSSSSNQNEMFFGDQVEKC
YKCSVKQGQTLFIPTGWIHAVLTPVDCLAFGGNFLHSLNIEMQLKAYEIEKRLSTADLFK
FPNFETICWYVGKHILDIFRGLRENRRHPASYLVHGGKALNLAFRAWTKKEALPDHEDEI
PETVRTVQLIKDLAREIRLVEDIFQQNVGKTSNIFGLQRIFPAGSIPLTKPAHSTSVSMS
KLSLPSKNGSKKKGLKPKDIFKKAERKGKQSSALGPAGQLSYNLMDPYSHQALKTGPSQK
AKFNMSGTSLNDSDDDSADMDLDGSENPLALLMANGSTKRMKSVSKSRRAKIAKKVDSAR
LVAEQVMGDEFDLDSDDELQIDERLGKEKANLLIRSKFPRKLPRAKPCSDPNRIREPGEV
EFDIEEDYTTDEDMVEGVESKLGNGSGAGGILDLLKASRQVGGPDYAALTEAPASPSTQE
AIQGMLCMANLQSSSSSPATSSLQAWWTGGQERSSGSSSSGLGTVSSSPASQRTPGKRPI
KRPAYWKNESEEEENASLDEQDSLGACFKDAEYIYPSLESDDDDPALKSRPKKKKNSDDA
PWSPKARVTPTLPKQDRPVREGTRVASIETGLAAAAAKLAQQELQKAQKKKYIKKKPLLK
EVEQPRPQDSNPIMTMPAPTVATTPQPDTSSSPQPPPEPKQEALSGSLADHEYTARPNAF
GMAQANRSTTPMAPGVFLTQRRPSVGSQSSQAGQGKRPKKGLATAKQRLGRILKIHRNGK
LLL
Gene Ontology
GO:0005730; C:nucleolus; ISS:UniProtKB
GO:0005634; C:nucleus; ISS:UniProtKB
GO:0003682; F:chromatin binding; ISS:UniProtKB
GO:0032452; F:histone demethylase activity; ISS:UniProtKB
GO:0071558; F:histone demethylase activity (H3-K27 specific); ISS:UniProtKB
GO:0051864; F:histone demethylase activity (H3-K36 specific); ISS:UniProtKB
GO:0032454; F:histone demethylase activity (H3-K9 specific); ISS:UniProtKB
GO:0035575; F:histone demethylase activity (H4-K20 specific); ISS:UniProtKB
GO:0005506; F:iron ion binding; ISS:UniProtKB
GO:0035064; F:methylated histone binding; ISS:UniProtKB
GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; ISS:UniProtKB
GO:0008270; F:zinc ion binding; ISS:UniProtKB
GO:0007420; P:brain development; ISS:UniProtKB
GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB
GO:0071557; P:histone H3-K27 demethylation; ISS:UniProtKB
GO:0070544; P:histone H3-K36 demethylation; ISS:UniProtKB
GO:0033169; P:histone H3-K9 demethylation; ISS:UniProtKB
GO:0035574; P:histone H4-K20 demethylation; ISS:UniProtKB
GO:0061188; P:negative regulation of chromatin silencing at rDNA; ISS:UniProtKB
GO:0045943; P:positive regulation of transcription from RNA polymerase I promoter; ISS:UniProtKB
GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB
GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW
Interpro
InterPro; IPR003347; JmjC_dom
InterPro; IPR019786; Zinc_finger_PHD-type_CS
InterPro; IPR011011; Znf_FYVE_PHD
InterPro; IPR001965; Znf_PHD
InterPro; IPR019787; Znf_PHD-finger
InterPro; IPR013083; Znf_RING/FYVE/PHD
Pfam
Pfam; PF02373; JmjC;
Pfam; PF00628; PHD;
SMART
SMART; SM00558; JmjC;
SMART; SM00249; PHD;
PROSITE
PROSITE; PS51184; JMJC;
PROSITE; PS01359; ZF_PHD_1;
PROSITE; PS50016; ZF_PHD_2;
PRINTS