ID   PHF8_MOUSE              Reviewed;        1023 AA.
AC   Q80TJ7; A2ABU8; A2ABV0; A2ABV2; Q8BLX8; Q8BLY0; Q8BZ61; Q8CG26;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   27-MAR-2024, entry version 157.
DE   RecName: Full=Histone lysine demethylase PHF8;
DE            EC=1.14.11.27 {ECO:0000250|UniProtKB:Q9UPP1};
DE            EC=1.14.11.65 {ECO:0000250|UniProtKB:Q9UPP1};
DE   AltName: Full=PHD finger protein 8;
DE   AltName: Full=[histone H3]-dimethyl-L-lysine(36) demethylase PHF8 {ECO:0000305};
DE   AltName: Full=[histone H3]-dimethyl-L-lysine(9) demethylase PHF8 {ECO:0000305};
GN   Name=Phf8; Synonyms=Kiaa1111;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND NUCLEOTIDE
RP   SEQUENCE [LARGE SCALE MRNA] OF 1-490 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Bone;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-1023 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-899.
RC   STRAIN=129/Sv;
RX   PubMed=15112104; DOI=10.1007/s00335-003-2329-1;
RA   Abe K., Yuzuriha M., Sugimoto M., Ko M.S., Brathwaite M.E., Waeltz P.,
RA   Nagaraja R.;
RT   "Gene content of the 750-kb critical region for mouse embryonic ectoderm
RT   lethal tcl-w5.";
RL   Mamm. Genome 15:265-276(2004).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615 AND SER-820, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-615; TYR-668; THR-669;
RP   THR-670; SER-790; SER-797 AND SER-820, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   STRUCTURE BY NMR OF 1-66.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of PHD domain in protein AA017385.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone lysine demethylase with selectivity for the di- and
CC       monomethyl states that plays a key role cell cycle progression, rDNA
CC       transcription and brain development. Demethylates mono- and
CC       dimethylated histone H3 'Lys-9' residue (H3K9Me1 and H3K9Me2),
CC       dimethylated H3 'Lys-27' (H3K27Me2) and monomethylated histone H4 'Lys-
CC       20' residue (H4K20Me1). Acts as a transcription activator as H3K9Me1,
CC       H3K9Me2, H3K27Me2 and H4K20Me1 are epigenetic repressive marks.
CC       Involved in cell cycle progression by being required to control G1-S
CC       transition. Acts as a coactivator of rDNA transcription, by activating
CC       polymerase I (pol I) mediated transcription of rRNA genes. Required for
CC       brain development, probably by regulating expression of neuron-specific
CC       genes. Only has activity toward H4K20Me1 when nucleosome is used as a
CC       substrate and when not histone octamer is used as substrate. May also
CC       have weak activity toward dimethylated H3 'Lys-36' (H3K36Me2), however,
CC       the relevance of this result remains unsure in vivo. Specifically binds
CC       trimethylated 'Lys-4' of histone H3 (H3K4me3), affecting histone
CC       demethylase specificity: has weak activity toward H3K9Me2 in absence of
CC       H3K4me3, while it has high activity toward H3K9me2 when binding
CC       H3K4me3. Positively modulates transcription of histone demethylase
CC       KDM5C, acting synergistically with transcription factor ARX; synergy
CC       may be related to enrichment of histone H3K4me3 in regulatory elements.
CC       {ECO:0000250|UniProtKB:Q9UPP1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3]
CC         + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2
CC         succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC         COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:61976; EC=1.14.11.27;
CC         Evidence={ECO:0000250|UniProtKB:Q9UPP1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(9)-[histone H3]
CC         + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(9)-[histone H3] + 2
CC         succinate; Xref=Rhea:RHEA:60188, Rhea:RHEA-COMP:15541, Rhea:RHEA-
CC         COMP:15546, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:61976; EC=1.14.11.65;
CC         Evidence={ECO:0000250|UniProtKB:Q9UPP1};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Interacts with POLR1B, UBTF, SETD1A, HCFC1, E2F1 and ZNF711
CC       (By similarity). Interacts with ZNF263; recruited to the SIX3 promoter
CC       along with other proteins involved in chromatin modification and
CC       transcriptional corepression where it contributes to transcriptional
CC       repression (By similarity). {ECO:0000250|UniProtKB:Q9UPP1}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UPP1}. Nucleus,
CC       nucleolus {ECO:0000250|UniProtKB:Q9UPP1}. Note=Recruited to H3K4me3
CC       sites on chromatin during interphase (By similarity). Dissociates from
CC       chromatin when cells enter mitosis (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UPP1}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q80TJ7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80TJ7-2; Sequence=VSP_014966, VSP_014969, VSP_014970;
CC       Name=3;
CC         IsoId=Q80TJ7-3; Sequence=VSP_014967, VSP_014968;
CC   -!- DOMAIN: The PHD-type zinc finger mediates the binding to H3K4me3.
CC       Binding to H3K4me3 promotes its access to H3K9me2 (By similarity).
CC       {ECO:0000250}.
CC   -!- DOMAIN: The linker region is a critical determinant of demethylase
CC       specificity. It enables the active site of JmjC to reach the target
CC       H3K9me2 when the PHD-type zinc finger binds to H3K4me3 (By similarity).
CC       {ECO:0000250}.
CC   -!- PTM: Phosphorylation at Ser-33 and Ser-84 are required for dissociation
CC       from chromatin and accumulation of H4K20Me1 levels during prophase.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. JHDM1D
CC       subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM17163.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AK036609; BAC29505.1; -; mRNA.
DR   EMBL; AK040943; BAC30755.2; -; mRNA.
DR   EMBL; AK040969; BAC30763.1; -; mRNA.
DR   EMBL; AL662922; CAM17161.1; -; Genomic_DNA.
DR   EMBL; AL840642; CAM15464.1; -; Genomic_DNA.
DR   EMBL; AL662922; CAM15464.1; JOINED; Genomic_DNA.
DR   EMBL; AL662922; CAM17159.1; -; Genomic_DNA.
DR   EMBL; AL840642; CAM17159.1; JOINED; Genomic_DNA.
DR   EMBL; AL662922; CAM17163.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AK122447; BAC65729.1; -; mRNA.
DR   EMBL; AF528164; AAO17385.1; ALT_SEQ; Genomic_DNA.
DR   CCDS; CCDS30470.1; -. [Q80TJ7-2]
DR   CCDS; CCDS53223.1; -. [Q80TJ7-1]
DR   RefSeq; NP_001009544.1; NM_001009544.2.
DR   RefSeq; NP_001106825.1; NM_001113354.1. [Q80TJ7-1]
DR   RefSeq; NP_796175.1; NM_177201.5. [Q80TJ7-2]
DR   RefSeq; XP_006528938.1; XM_006528875.3. [Q80TJ7-1]
DR   RefSeq; XP_006528940.1; XM_006528877.3. [Q80TJ7-1]
DR   RefSeq; XP_006528943.1; XM_006528880.3. [Q80TJ7-1]
DR   PDB; 1WEP; NMR; -; A=1-63.
DR   PDBsum; 1WEP; -.
DR   AlphaFoldDB; Q80TJ7; -.
DR   SMR; Q80TJ7; -.
DR   BioGRID; 236144; 1.
DR   STRING; 10090.ENSMUSP00000127653; -.
DR   ChEMBL; CHEMBL3038497; -.
DR   GlyGen; Q80TJ7; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q80TJ7; -.
DR   PhosphoSitePlus; Q80TJ7; -.
DR   SwissPalm; Q80TJ7; -.
DR   EPD; Q80TJ7; -.
DR   jPOST; Q80TJ7; -.
DR   MaxQB; Q80TJ7; -.
DR   PaxDb; 10090-ENSMUSP00000127653; -.
DR   PeptideAtlas; Q80TJ7; -.
DR   ProteomicsDB; 287706; -. [Q80TJ7-1]
DR   ProteomicsDB; 287707; -. [Q80TJ7-2]
DR   ProteomicsDB; 287708; -. [Q80TJ7-3]
DR   Pumba; Q80TJ7; -.
DR   Antibodypedia; 26685; 174 antibodies from 25 providers.
DR   DNASU; 320595; -.
DR   Ensembl; ENSMUST00000046950.13; ENSMUSP00000040765.7; ENSMUSG00000041229.16. [Q80TJ7-1]
DR   Ensembl; ENSMUST00000046962.11; ENSMUSP00000041312.5; ENSMUSG00000041229.16. [Q80TJ7-2]
DR   Ensembl; ENSMUST00000112662.9; ENSMUSP00000108281.3; ENSMUSG00000041229.16. [Q80TJ7-2]
DR   Ensembl; ENSMUST00000112666.8; ENSMUSP00000108285.2; ENSMUSG00000041229.16. [Q80TJ7-3]
DR   Ensembl; ENSMUST00000168501.8; ENSMUSP00000127653.2; ENSMUSG00000041229.16. [Q80TJ7-1]
DR   GeneID; 320595; -.
DR   KEGG; mmu:320595; -.
DR   UCSC; uc009upd.1; mouse. [Q80TJ7-3]
DR   UCSC; uc012hqt.1; mouse. [Q80TJ7-1]
DR   AGR; MGI:2444341; -.
DR   CTD; 23133; -.
DR   MGI; MGI:2444341; Phf8.
DR   VEuPathDB; HostDB:ENSMUSG00000041229; -.
DR   eggNOG; KOG1633; Eukaryota.
DR   GeneTree; ENSGT00940000157847; -.
DR   HOGENOM; CLU_003540_6_0_1; -.
DR   InParanoid; Q80TJ7; -.
DR   OMA; DIFHQNI; -.
DR   OrthoDB; 2784357at2759; -.
DR   PhylomeDB; Q80TJ7; -.
DR   TreeFam; TF106480; -.
DR   Reactome; R-MMU-3214842; HDMs demethylate histones.
DR   BioGRID-ORCS; 320595; 9 hits in 81 CRISPR screens.
DR   BioGRID-ORCS; 74042; 1 hit in 76 CRISPR screens.
DR   ChiTaRS; Phf8; mouse.
DR   EvolutionaryTrace; Q80TJ7; -.
DR   PRO; PR:Q80TJ7; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q80TJ7; Protein.
DR   Bgee; ENSMUSG00000041229; Expressed in placenta labyrinth and 253 other cell types or tissues.
DR   ExpressionAtlas; Q80TJ7; baseline and differential.
DR   GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR   GO; GO:0032452; F:histone demethylase activity; ISS:UniProtKB.
DR   GO; GO:0071558; F:histone H3K27me2/H3K27me3 demethylase activity; ISS:UniProtKB.
DR   GO; GO:0051864; F:histone H3K36 demethylase activity; ISS:UniProtKB.
DR   GO; GO:0140680; F:histone H3K36me/H3K36me2 demethylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032454; F:histone H3K9 demethylase activity; ISS:UniProtKB.
DR   GO; GO:0140683; F:histone H3K9me/H3K9me2 demethylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0035575; F:histone H4K20 demethylase activity; ISS:UniProtKB.
DR   GO; GO:0005506; F:iron ion binding; ISS:UniProtKB.
DR   GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0061188; P:negative regulation of rDNA heterochromatin formation; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd15642; PHD_PHF8; 1.
DR   Gene3D; 1.20.58.1360; -; 1.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   InterPro; IPR041070; JHD.
DR   InterPro; IPR003347; JmjC_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   PANTHER; PTHR23123:SF11; HISTONE LYSINE DEMETHYLASE PHF8; 1.
DR   PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1.
DR   Pfam; PF17811; JHD; 1.
DR   Pfam; PF02373; JmjC; 1.
DR   Pfam; PF00628; PHD; 1.
DR   SMART; SM00558; JmjC; 1.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
DR   Genevisible; Q80TJ7; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; Cell cycle;
KW   Chromatin regulator; Dioxygenase; Iron; Metal-binding; Nucleus;
KW   Oxidoreductase; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..1023
FT                   /note="Histone lysine demethylase PHF8"
FT                   /id="PRO_0000059296"
FT   DOMAIN          195..351
FT                   /note="JmjC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   ZN_FING         5..56
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          65..79
FT                   /note="Linker"
FT                   /evidence="ECO:0000250"
FT   REGION          472..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          534..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..803
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          815..865
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          877..1009
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..487
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..553
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        732..774
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        821..841
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        908..928
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        961..995
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         244
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         247
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         249
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT   MOD_RES         33
FT                   /note="Phosphoserine; by CDK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPP1"
FT   MOD_RES         84
FT                   /note="Phosphoserine; by CDK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPP1"
FT   MOD_RES         615
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         668
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         669
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         670
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         686
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPP1"
FT   MOD_RES         768
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPP1"
FT   MOD_RES         790
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         797
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         817
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPP1"
FT   MOD_RES         820
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT   MOD_RES         843
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UPP1"
FT   VAR_SEQ         442..542
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014966"
FT   VAR_SEQ         442..464
FT                   /note="DIFQQNVGKTSNIFGLQRIFPAG -> VRSMGEGKAFGKGWRLKWQVRTL
FT                   (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014967"
FT   VAR_SEQ         465..1023
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014968"
FT   VAR_SEQ         883..896
FT                   /note="ELQKAQKKKYIKKK -> VRVDTQLVALLLMT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014969"
FT   VAR_SEQ         897..1023
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014970"
FT   STRAND          16..18
FT                   /evidence="ECO:0007829|PDB:1WEP"
FT   STRAND          20..23
FT                   /evidence="ECO:0007829|PDB:1WEP"
FT   TURN            24..26
FT                   /evidence="ECO:0007829|PDB:1WEP"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:1WEP"
FT   HELIX           32..35
FT                   /evidence="ECO:0007829|PDB:1WEP"
FT   HELIX           39..42
FT                   /evidence="ECO:0007829|PDB:1WEP"
FT   STRAND          46..48
FT                   /evidence="ECO:0007829|PDB:1WEP"
FT   TURN            51..56
FT                   /evidence="ECO:0007829|PDB:1WEP"
SQ   SEQUENCE   1023 AA;  113553 MW;  7B9351944C000487 CRC64;
     MASVPVYCLC RLPYDVTRFM IECDMCQDWF HGSCVGVEEE KAADIDLYHC PNCEVLHGPS
     IMKKRRGSSK GHDNHKGKPL KTGSSMFIRE LRGRTFDSSD EVILKPTGSQ LTVEFLEENS
     FSVPILVLKK DGLGMTLPSP SFTVRDVEHY VGSDKEIDVI DVARQADCKM KLGDFVKYYY
     SGKREKVLNV ISLEFSDTRL SNLVETPRIV RKLSWVENLW PEECVFERPN VQKYCLMSVR
     DSYTDFHIDF GGTSVWYHVL KGEKIFYLIR PTNANLTLFE CWSSSSNQNE MFFGDQVEKC
     YKCSVKQGQT LFIPTGWIHA VLTPVDCLAF GGNFLHSLNI EMQLKAYEIE KRLSTADLFK
     FPNFETICWY VGKHILDIFR GLRENRRHPA SYLVHGGKAL NLAFRAWTKK EALPDHEDEI
     PETVRTVQLI KDLAREIRLV EDIFQQNVGK TSNIFGLQRI FPAGSIPLTK PAHSTSVSMS
     KLSLPSKNGS KKKGLKPKDI FKKAERKGKQ SSALGPAGQL SYNLMDPYSH QALKTGPSQK
     AKFNMSGTSL NDSDDDSADM DLDGSENPLA LLMANGSTKR MKSVSKSRRA KIAKKVDSAR
     LVAEQVMGDE FDLDSDDELQ IDERLGKEKA NLLIRSKFPR KLPRAKPCSD PNRIREPGEV
     EFDIEEDYTT DEDMVEGVES KLGNGSGAGG ILDLLKASRQ VGGPDYAALT EAPASPSTQE
     AIQGMLCMAN LQSSSSSPAT SSLQAWWTGG QERSSGSSSS GLGTVSSSPA SQRTPGKRPI
     KRPAYWKNES EEEENASLDE QDSLGACFKD AEYIYPSLES DDDDPALKSR PKKKKNSDDA
     PWSPKARVTP TLPKQDRPVR EGTRVASIET GLAAAAAKLA QQELQKAQKK KYIKKKPLLK
     EVEQPRPQDS NPIMTMPAPT VATTPQPDTS SSPQPPPEPK QEALSGSLAD HEYTARPNAF
     GMAQANRSTT PMAPGVFLTQ RRPSVGSQSS QAGQGKRPKK GLATAKQRLG RILKIHRNGK
     LLL
//