PHF2_DICLA
ID PHF2_DICLA Reviewed; 1081 AA.
AC E6ZGB4;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Lysine-specific demethylase phf2;
DE EC=1.14.11.-;
DE AltName: Full=PHD finger protein 2;
GN Name=phf2; ORFNames=DLA_It00560;
OS Dicentrarchus labrax (European seabass) (Morone labrax).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Moronidae; Dicentrarchus.
OX NCBI_TaxID=13489;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kuhl H., Tine M., Beck A., Timmermann B., Reinhardt R.;
RT "Chromosome directed sequencing of European seabass (Dicentrarchus labrax
RT L.) by comparatively mapped BAC clones.";
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Lysine demethylase that demethylates both histones and non-
CC histone proteins. Mediates demethylation of dimethylated 'Lys-9' of
CC histone H3 (H3K9me2). Recruited to trimethylated 'Lys-4' of histone H3
CC (H3K4me3) at rDNA promoters and promotes expression of rDNA (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:O75151}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:O75151}.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family. JHDM1D
CC subfamily. {ECO:0000305}.
CC -!- CAUTION: In contrast to the related histone demethylases jhdm1d and
CC phf8, the conserved active His in position 321 is replaced by an Asn.
CC However, the presence of an Asn residue neither affects binding to the
CC catalytic iron nor abolishes demethylase activity. {ECO:0000305}.
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DR EMBL; FQ310506; CBN80631.1; -; Genomic_DNA.
DR AlphaFoldDB; E6ZGB4; -.
DR SMR; E6ZGB4; -.
DR PRIDE; E6ZGB4; -.
DR Ensembl; ENSDLAT00005070186; ENSDLAP00005077504; ENSDLAG00005028696.
DR Proteomes; UP000694389; Unassembled WGS sequence.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 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:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006482; P:protein demethylation; ISS:UniProtKB.
DR Gene3D; 3.30.40.10; -; 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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
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 3: Inferred from homology;
KW Activator; Centromere; Chromatin regulator; Chromosome; Dioxygenase; Iron;
KW Kinetochore; Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1081
FT /note="Lysine-specific demethylase phf2"
FT /id="PRO_0000410902"
FT DOMAIN 197..353
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 450..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..1062
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..510
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..747
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..840
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 972..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1018..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
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 251
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 259
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 266
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 321
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT MOD_RES 1022
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1081 AA; 120753 MW; F02DE03919A9484C CRC64;
MATVPVYCIC RLPYDVTQFM IECDACKDWF HGSCVGVDED DAPDIDIYHC PNCEKTHGKS
TLKKKKNWSK HDTGQSTDIK AVQNGSQVFI KELRSRTFPS ADDVVVKLSG SQLTMDYLEE
NGFNEPILAQ KKDGLGLSMP APTFYISDVE NYVGPDVGVD VVDVTKQTDS KMKLKEFVDY
YYSTNRKKVL NVINLEFSDT RMNSIVESPQ IVRRLSWVEN YWPDDALLGK PKVTKYCLIC
VKDSYTDFHI ECGGASVWYH VLKGEKIFFL IKPTSANLSL YERWRSSSNH SEMFFADQVD
KCYKCTLKQG QTLFIPSGWI NAILTPVDCL AFSGHFVHNL SVEMQMRAYE IEKRLKVKTL
TPFPNFETAC WYVGRHLLER FKGLHKANKQ PAPYLIHGAK IINGAFRAWT KKQALLEHED
ELPENMKPSQ LIKDLAKEIR LSENATKAIK SEPSIKVPVE EPPSTHSEPE EPVSPAHVPS
PSREKARKKA SKPPKPPKPP KPPKMPKAPK PPKVPKVKEG GKKKAKKVKE SSPPPKPSSF
AALESHAKDI LSKMDQPKKT KAVKNVLSMS EKEISKQNNL EKFEIREQNK NKTEAKWKYK
NSKPDSLLKM EEECKFDRTL LSGNKDKFSF TMSHKKMLGS KTLKPQTNSS VFGSLQNLKE
DKTKPVRDEY EYVSDEGELK IDEFPIRRKK NTVKRDQSFL SDIREPIQPA KKPKFQPLVT
KNVDSSDEET LHIDTEAKPE VKSRNSKVKK KGGSAAGILD LLQASKQVGG IDYSTNSQPP
ASPSTQEAIQ GMLSMANLSS SDSLQQPWSN SQSKNNSQSK SNSHGAQGGK KGSGGGGNNS
KRPTKRLPKK PRKSSSIESL DYDDDQDHMD ACFKDSDYVY PSLESEEDNP VFKSRSKKRK
SSDDTPYSPT ARVGPSVPRQ ERPARDGARV ASIETGLAAA AAKLSHQEEQ QKTKKKKKST
KKKAIVIEEP PKISQDSSSP EHNLDSQDGS LTDHEFNTGT VKSPGGPQPM APGVFLSQRR
PSMSSPNNST NSTSTNSSSM AKGDRVGSAD AKAKRLKKGM ATAKQRLGKI LKIHRNGKLL
L
