GenomeNet

Database: UniProt
Entry: M3YKN8_MUSPF
LinkDB: M3YKN8_MUSPF
Original site: M3YKN8_MUSPF 
ID   M3YKN8_MUSPF            Unreviewed;       405 AA.
AC   M3YKN8;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Double PHD fingers 2 {ECO:0000313|Ensembl:ENSMPUP00000011895.1};
DE   SubName: Full=Zinc finger protein ubi-d4 isoform X1 {ECO:0000313|RefSeq:XP_004770123.1};
GN   Name=DPF2 {ECO:0000313|Ensembl:ENSMPUP00000011895.1,
GN   ECO:0000313|RefSeq:XP_004770123.1};
OS   Mustela putorius furo (European domestic ferret) (Mustela furo).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC   Mustelinae; Mustela.
OX   NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000011895.1};
RN   [1] {ECO:0000313|Ensembl:ENSMPUP00000011895.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2023) to UniProtKB.
RN   [2] {ECO:0000313|RefSeq:XP_004770123.1}
RP   IDENTIFICATION.
RC   TISSUE=Brain {ECO:0000313|RefSeq:XP_004770123.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; AEYP01074211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_004770123.1; XM_004770066.3.
DR   STRING; 9669.ENSMPUP00000011895; -.
DR   Ensembl; ENSMPUT00000012090.1; ENSMPUP00000011895.1; ENSMPUG00000011987.1.
DR   GeneID; 101686153; -.
DR   KEGG; mpuf:101686153; -.
DR   CTD; 5977; -.
DR   eggNOG; KOG1244; Eukaryota.
DR   GeneTree; ENSGT00940000155070; -.
DR   HOGENOM; CLU_038980_0_1_1; -.
DR   OMA; EHSKDAW; -.
DR   OrthoDB; 5490909at2759; -.
DR   Proteomes; UP000000715; Unplaced.
DR   GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0062072; F:H3K9me3 modified histone binding; IEA:Ensembl.
DR   GO; GO:0070577; F:lysine-acetylated histone binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1905454; P:negative regulation of myeloid progenitor cell differentiation; IEA:Ensembl.
DR   CDD; cd15691; PHD1_DPF2_like; 1.
DR   CDD; cd15530; PHD2_d4; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR025750; DPF1-3_N.
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   PANTHER; PTHR45888; HL01030P-RELATED; 1.
DR   PANTHER; PTHR45888:SF13; ZINC FINGER PROTEIN UBI-D4; 1.
DR   Pfam; PF14051; DPF1-3_N; 1.
DR   Pfam; PF00628; PHD; 2.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00146}.
FT   DOMAIN          284..344
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   DOMAIN          341..391
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          79..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..213
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   405 AA;  45794 MW;  5FFC5A781BDA98C9 CRC64;
     MAAVVENVVK LLGEQYYKDA MEQCHNYNAR LCAERSVRLP FLDSQTGVAQ SNCYIWMEKR
     HRGPGLASGQ LYSYPARRWR KKRRAHPPED PRLSFPSIKP DTDQTLKKEG LISQDGSSLE
     ALLRTDPLEK RGAPDPRVDD DSLGEFPVTN SRARKRILEP EDFLDDLDDE DYEEDTPKRR
     GKGKSKGKGV GSARKKLDAS ILEDRDKPYA CDNSFKQKHT SKAPQRVCGK RYKNRPGLSY
     HYAHSHLAEE EGEDKEDSQP PTPVSQRSEE QKSKKGPDGL ALPNNYCDFC LGDSKINKKT
     GQPEELVSCS DCGRSGHPSC LQFTPVMMAA VKTYRWQCIE CKCCNICGTS ENDDQLLFCD
     DCDRGYHMYC LTPSMSEPPE GSWSCHLCLD LLKEKASIYQ NQNSS
//
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