PHF6_BOVIN
ID PHF6_BOVIN Reviewed; 365 AA.
AC Q08DR0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=PHD finger protein 6;
GN Name=PHF6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Placenta;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional regulator that associates with ribosomal RNA
CC promoters and suppresses ribosomal RNA (rRNA) transcription.
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with UBTF. Interacts with the NuRD complex component
CC RBBP4 (via the nucleolar localization motif), the interaction mediates
CC transcriptional repression activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Nucleus, nucleolus
CC {ECO:0000250}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q8IWS0}. Note=Nuclear, it particularly localizes
CC to the nucleolus. {ECO:0000250}.
CC -!- DOMAIN: The PHD-type zinc finger 1 mediates both nucleolar localization
CC and interaction with UBTF. {ECO:0000250}.
CC -!- DOMAIN: The ePHD2 domain folds as an integrated structural module
CC comprizing the C2HC pre-PHD-type 2 zinc finger and the PHD-type 2 zinc
CC finger. It mediates non-specific binding to dsDNA, but doesn't bind
CC histones in contrast to many PHD-type zinc fingers.
CC {ECO:0000250|UniProtKB:Q8IWS0}.
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DR EMBL; BC123609; AAI23610.1; -; mRNA.
DR RefSeq; NP_001069237.1; NM_001075769.1.
DR RefSeq; XP_010819737.1; XM_010821435.1.
DR RefSeq; XP_015325676.1; XM_015470190.1.
DR AlphaFoldDB; Q08DR0; -.
DR SMR; Q08DR0; -.
DR STRING; 9913.ENSBTAP00000020218; -.
DR Ensembl; ENSBTAT00000020218; ENSBTAP00000020218; ENSBTAG00000015196.
DR GeneID; 518186; -.
DR KEGG; bta:518186; -.
DR CTD; 84295; -.
DR VEuPathDB; HostDB:ENSBTAG00000015196; -.
DR VGNC; VGNC:97297; PHF6.
DR GeneTree; ENSGT00950000182865; -.
DR InParanoid; Q08DR0; -.
DR OMA; RRTYHYH; -.
DR OrthoDB; 783078at2759; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000015196; Expressed in nasopharynx and 112 other tissues.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051219; F:phosphoprotein binding; IEA:Ensembl.
DR GO; GO:0043021; F:ribonucleoprotein complex binding; IEA:Ensembl.
DR GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR GO; GO:0015631; F:tubulin binding; IEA:Ensembl.
DR GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR SMART; SM00249; PHD; 2.
DR PROSITE; PS51805; EPHD; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Centromere; Chromosome; DNA-binding; Isopeptide bond;
KW Kinetochore; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q8IWS0"
FT CHAIN 2..365
FT /note="PHD finger protein 6"
FT /id="PRO_0000288798"
FT ZN_FING 14..52
FT /note="C2HC pre-PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 80..132
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 209..249
FT /note="C2HC pre-PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 278..330
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 14..132
FT /note="Extended PHD1 domain (ePHD1)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 139..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..330
FT /note="Extended PHD2 domain (ePHD2)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 330..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 13..16
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 129..133
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 157..169
FT /note="Nucleolar localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 139..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..350
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWS0"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWS0"
FT MOD_RES 145
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWS0"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWS0"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D4J7"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWS0"
FT MOD_RES 358
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWS0"
FT CROSSLNK 173
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWS0"
FT CROSSLNK 227
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IWS0"
SQ SEQUENCE 365 AA; 41289 MW; 463F47908423BB83 CRC64;
MSSSVEQKKG PTRQRKCGFC KSNRDKECGQ LLISENQKVA AHHKCMLFSS ALVSSHSDNE
SLGGFSIEDV QKEIKRGTKL MCSLCHCPGA TIGCDVKTCH RTYHYHCALH DKAQIREKPS
QGIYMVYCRK HKKTAHNSEA DLEESFNEHE LEPSSPKSKK KSRKGRPRKT NFKGLSEDTR
STSSHGTDEM ESSSYRDRSP HRSSPSDTRP KCGFCHVGEE ENQARGKLHI FNAKKAAAHY
KCMLFSSGTV QLTTTSRAEF GDFDIKTVLQ EIKRGKRMKC TLCSQPGATI GCEIKACVKT
YHYHCGVQDK AKYIENMSRG IYKLYCKNHS GNDERDEEDE ERESKSRGKV EIDQQQLTQQ
QLNGN
