PHF8_MOUSE
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 03-AUG-2022, entry version 148.
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. Has activity toward H4K20Me1 only 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. {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 iPTMnet; Q80TJ7; -.
DR PhosphoSitePlus; Q80TJ7; -.
DR SwissPalm; Q80TJ7; -.
DR EPD; Q80TJ7; -.
DR jPOST; Q80TJ7; -.
DR MaxQB; Q80TJ7; -.
DR PaxDb; Q80TJ7; -.
DR PeptideAtlas; Q80TJ7; -.
DR PRIDE; Q80TJ7; -.
DR ProteomicsDB; 287706; -. [Q80TJ7-1]
DR ProteomicsDB; 287707; -. [Q80TJ7-2]
DR ProteomicsDB; 287708; -. [Q80TJ7-3]
DR Antibodypedia; 26685; 130 antibodies from 25 providers.
DR DNASU; 320595; -.
DR Ensembl; ENSMUST00000046950; ENSMUSP00000040765; ENSMUSG00000041229. [Q80TJ7-1]
DR Ensembl; ENSMUST00000046962; ENSMUSP00000041312; ENSMUSG00000041229. [Q80TJ7-2]
DR Ensembl; ENSMUST00000112662; ENSMUSP00000108281; ENSMUSG00000041229. [Q80TJ7-2]
DR Ensembl; ENSMUST00000112666; ENSMUSP00000108285; ENSMUSG00000041229. [Q80TJ7-3]
DR Ensembl; ENSMUST00000168501; ENSMUSP00000127653; ENSMUSG00000041229. [Q80TJ7-1]
DR GeneID; 320595; -.
DR KEGG; mmu:320595; -.
DR UCSC; uc009upd.1; mouse. [Q80TJ7-3]
DR UCSC; uc012hqt.1; mouse. [Q80TJ7-1]
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; 1384737at2759; -.
DR PhylomeDB; Q80TJ7; -.
DR TreeFam; TF106480; -.
DR Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-MMU-3214842; HDMs demethylate histones.
DR BioGRID-ORCS; 320595; 9 hits in 75 CRISPR screens.
DR BioGRID-ORCS; 74042; 1 hit in 71 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 250 other tissues.
DR ExpressionAtlas; Q80TJ7; baseline and differential.
DR Genevisible; Q80TJ7; MM.
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:0140680; F:histone H3-di/monomethyl-lysine-36 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0140683; F:histone H3-di/monomethyl-lysine-9 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; ISS:UniProtKB.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; ISS:UniProtKB.
DR GO; GO:0071558; F:histone H3-tri/di-methyl-lysine-27 demethylase activity; ISS:UniProtKB.
DR GO; GO:0035575; F:histone H4-methyl-lysine-20 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:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0071557; P:histone H3-K27 demethylation; ISS:UniProtKB.
DR GO; GO:0070544; P:histone H3-K36 demethylation; ISS:UniProtKB.
DR GO; GO:0033169; P:histone H3-K9 demethylation; ISS:UniProtKB.
DR GO; GO:0035574; P:histone H4-K20 demethylation; ISS:UniProtKB.
DR GO; GO:0061188; P:negative regulation of ribosomal DNA heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 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; SSF57903; SSF57903; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
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
