ZN239_PONAB
ID ZN239_PONAB Reviewed; 458 AA.
AC Q5R8G9;
DT 12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Zinc finger protein 239;
GN Name=ZNF239;
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=Heart;
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; CR859783; CAH91941.1; -; mRNA.
DR RefSeq; NP_001126126.1; NM_001132654.1.
DR AlphaFoldDB; Q5R8G9; -.
DR SMR; Q5R8G9; -.
DR STRING; 9601.ENSPPYP00000002589; -.
DR GeneID; 100173082; -.
DR KEGG; pon:100173082; -.
DR CTD; 8187; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q5R8G9; -.
DR OrthoDB; 1318335at2759; -.
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 InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 9.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..458
FT /note="Zinc finger protein 239"
FT /id="PRO_0000290348"
FT ZN_FING 207..229
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 235..257
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 263..285
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 291..313
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 319..341
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 347..369
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 375..397
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 403..425
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 431..453
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q16600"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q16600"
SQ SEQUENCE 458 AA; 51601 MW; 3B76F6B60CB5F78B CRC64;
MASTITGSQD CIVNHRGEVD GEPELDISPC QQWGEASSPI SRNRDSVMTL QSGCFENIES
ETYLPLKVSS QIDTQDSSVK FCKNEPQDHQ ESRRLFVMEE STERKVIKGE SCSENLQVKL
VSDGQELASP LLNGEATCQN GQLKESLDPI DCNCKDIHGW KSQVVSCSQQ RAHTEEKPCD
HNNCGKILNT SPDGHPYEKI HTAEKQYECS QCGKNFSQSS ELLLHQRDHT EEKPYKCEQC
GKGFTRSSSL LIHQAVHTDE KPYKCDKCGK GFTRSSSLLI HHAVHTGEKP YKCDKCGKGF
SQSSKLHIHQ RVHTGEKPYE CEECGMSFSQ RSNLHIHQRV HTGERPYKCG ECGKGFSQSS
NLHIHRCIHT GEKPYQCYEC GKGFSQSPDL RIHLRVHTGE KPYHCGKCGK GFSQSSKLLI
HQRVHTGEKP YECSKCGKGF SQSSNLHIHQ RVHKKDPR