ZN248_PONAB
ID ZN248_PONAB Reviewed; 578 AA.
AC Q5REN4;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Zinc finger protein 248;
GN Name=ZNF248;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; CR857488; CAH89773.1; -; mRNA.
DR RefSeq; NP_001124811.1; NM_001131339.1.
DR AlphaFoldDB; Q5REN4; -.
DR SMR; Q5REN4; -.
DR STRING; 9601.ENSPPYP00000002572; -.
DR GeneID; 100436044; -.
DR KEGG; pon:100436044; -.
DR CTD; 57209; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q5REN4; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 7.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..578
FT /note="Zinc finger protein 248"
FT /id="PRO_0000290349"
FT DOMAIN 8..78
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 239..263
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 379..401
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 407..429
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 435..457
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 463..485
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 491..513
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 519..542
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 547..569
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 340
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NDW4"
SQ SEQUENCE 578 AA; 66986 MW; CBB60CF48696C7CC CRC64;
MNKSQEQVSF KDVCVDFTQE EWYLLDPAQK ILYRDVILEN YSNLVSVGYC ITKPEVIFKI
EQGEEPWILE KGFPSQDPER KWKVDDMLES SQENEDDHFW ELLFHNNKTV SVENGDRGSK
TFNLGTDPVS LRNYPYKICD SCEMSLKNIS GLIISKKSCS RKKPDEFNVC EKLLLDIRHE
KIPIGEKSYK YDQKRNAINY HQDLSQPSFG QSFEYSKNGQ GFHDEAAFFT NKRSQIGETV
CKYNECGRTF IESLKLNISQ RPHLEMEPYG CSICGKSFCM NLRFGHQRAL TKDNPYEYNE
YGEIFCDNSA FIIHQGAYTR KILREYKVSD KTWEKSTVLK HQIVHMGGKS YDYNENGSNF
SKKSHLTQLR RAHTGEKTFE CGECGKTFWE KSNLTQHQRT HTGEKPYECT ECGKAFCQKP
HLTNHQRTHT GEKPYECKQC GKTFCVKSNL TEHQRTHTGE KPYECNACGK SFCHRSALTV
HQRTHTGEKP FICNECGKSF CVKSNLIVHQ RTHTGEKPYK CNECGKTFCE KSALTKHQRT
HTGEKPYECN ACGKTFSQRS VLTKHQRIHM RVKALSTS