ID B4DFE2_HUMAN Unreviewed; 986 AA.
AC B4DFE2;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=cDNA FLJ58454, highly similar to PHD finger protein 12 {ECO:0000313|EMBL:BAG57403.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAG57403.1};
RN [1] {ECO:0000313|EMBL:BAG57403.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cerebellum {ECO:0000313|EMBL:BAG57403.1};
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project focused on splicing variants.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; AK294056; BAG57403.1; -; mRNA.
DR AlphaFoldDB; B4DFE2; -.
DR PeptideAtlas; B4DFE2; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd22703; FHA_PHF12; 1.
DR CDD; cd15533; PHD1_PHF12; 1.
DR CDD; cd15534; PHD2_PHF12_Rco1; 1.
DR Gene3D; 6.10.20.60; PHD finger protein 12; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR031966; PHF12_MRG-bd.
DR InterPro; IPR038098; PHF12_MRG-bd_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
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 PANTHER; PTHR46309; PHD FINGER PROTEIN 12; 1.
DR PANTHER; PTHR46309:SF1; PHD FINGER PROTEIN 12; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF16737; PHF12_MRG_bd; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 38..87
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 253..303
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 797..851
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT REGION 10..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 136..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 512..546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 986 AA; 107600 MW; 138BDC86925305FD CRC64;
MCVQQIQALL APPKTDEAEK RSRKPEKEPR RSGRATNHDS CDSCKEGGDL LCCDHCPAAF
HLQCCNPPLS EEMLPPGEWM CHRCTVRRKK REQKKELGHV NGLVDKSGKR TTSPSSDTDL
LDRSASKTEL KAIAHARILE RRASRPGTPT SSASTETPTS EQNDVDEDII DVDEEPVAAE
PDYVQPQLRR PFELLIAAAM ERNPTQFQLP NELTCTTALP GSSKRRRKEE TTGKNVKKTQ
HELDHNGLVP LPVKVCFTCN RSCRVAPLIQ CDYCPLLFHM DCLEPPLTAM PLGRWMCPNH
IEHVVLNQKN MTLSNRCQVF DRFQDTVSQH VVKVDFLNRI HKKHPPNRRV LQSVKRRSLK
VPDAIKSQYQ FPPPLIAPAA IRDGELICNG IPEESQMHLL NSEHLATQAE QQEWLCSVVA
LQCSILKHLS AKQMPSHWDS EQTEKADIKP VIVTDSSVTT SLQTADKTPT PSHYPLSCPS
GISTQNSLSC SPPHQSPALE DIGCSSCAEK SKKTPCGTAN GPVNTEVKAN GPHLYSSPTD
STDPRRLPGA NTPLPGLSHR QGWPRPLTPP AAGGLQNHTV GIIVKTENAT GPSSCPQRSL
VPVPSLPPSI PSSCASIENT STLQRKTVQS QIGPPLTDSR PLGSPPNATR VLTPPQAAGD
GILATTANQR FSSPAPSSDG KVSPGTLSIG SALTVPSFPA NSTAMVDLTN SLRAFMDVNG
EIEINMLDEK LIKFLALQRI HQLFPSRVQP SPGSVGTHQL ASGGHHIEVQ RKEVQARAVF
YPLLGLGGAV NMCYRTLYIG TGADMDVCLT NYGHCNYVSG KHACIFYDEN TKHYELLNYS
EHGTTVDNVL YSCDFSEKTP PTPPSSIVAK VQSVIRRRRH QKQDEEPSEE AAMMSSQAQG
PQRRPCNCKA SSSSLIGGSG AGWEGTALLH HGSYIKLGCL QFVFSITEFA TKQPKGDASL
LQDGVLAEKL SLKPHQGPVL RSNSVP
//
