ZN184_BOVIN
ID ZN184_BOVIN Reviewed; 752 AA.
AC A6QLU5;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Zinc finger protein 184;
GN Name=ZNF184;
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=Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in transcriptional regulation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; BC148089; AAI48090.1; -; mRNA.
DR RefSeq; NP_001093842.1; NM_001100372.1.
DR RefSeq; XP_005223780.1; XM_005223723.3.
DR RefSeq; XP_005223781.1; XM_005223724.3.
DR RefSeq; XP_005223782.1; XM_005223725.3.
DR AlphaFoldDB; A6QLU5; -.
DR SMR; A6QLU5; -.
DR STRING; 9913.ENSBTAP00000015283; -.
DR PaxDb; A6QLU5; -.
DR PRIDE; A6QLU5; -.
DR GeneID; 515674; -.
DR KEGG; bta:515674; -.
DR CTD; 7738; -.
DR eggNOG; KOG1721; Eukaryota.
DR HOGENOM; CLU_002678_44_5_1; -.
DR InParanoid; A6QLU5; -.
DR OrthoDB; 1318335at2759; -.
DR TreeFam; TF350822; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; 18.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 19.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 10.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 19.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 19.
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..752
FT /note="Zinc finger protein 184"
FT /id="PRO_0000347242"
FT DOMAIN 28..99
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 223..245
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 251..273
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 279..301
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 307..329
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 335..357
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 363..385
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 391..413
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 419..441
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 447..469
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 475..497
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 503..525
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 531..553
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 559..581
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 587..609
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 615..637
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 643..665
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 671..693
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 699..721
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 727..749
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99676"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99676"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99676"
FT CROSSLNK 207
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99676"
SQ SEQUENCE 752 AA; 86023 MW; F5B7470CC12525F6 CRC64;
MEDLSAPESA LFQGGHTLLP SASFQESVTF KDVIVDFTQE EWKQLDPVQR GLFRDVTLEN
YTHLVSIGLQ VSKPDVISQL EQGTEPWIVE PSIPVGTPGD WVTRPENSIT ASELDISGEE
PSPGAVAEKH KRDDPWSTNF LETCESKGSP ERQQANKQTL PREIKITEKT IPTLEQAHVN
NDFEKSISVS LDLLTHKQIS PKQTSTKTNV KQNLNPVKKE KSCKCNECGK AFTYCSALIR
HQRTHTGEKP YKCNECEKAF SRSENLINHQ RIHTGDKPYK CDQCGKGFIE GPSLTQHQRI
HTGEKPYKCD ECGKAFSQRT HLVQHQRIHT GEKPYTCNEC GKAFSQRGHF MEHQKIHTGE
KPFKCDECDK TFTRSTHLTQ HQKIHTGEKT YKCNECGKAF NGPSTFIRHH MIHTGEKPYE
CNECGKAFSQ HSNLTQHQKT HTGEKPYDCA ECGKSFSYWS SLAQHLKIHT GEKPYKCNEC
GKAFSYCSSL TQHRRIHTRE KPFECSECGK AFSYLSNLNQ HQKTHTQEKA YECKECGKAF
IRSSSLAKHE RIHTGEKPYQ CHECGKTFSY GSSLIQHRKI HTGERPYKCN ECGRAFNQNI
HLTQHKRIHT GAKPYECAEC GKAFRHCSSL AQHQKTHTEE KPYHCNKCEK AFSQSSHLAQ
HQRIHTGEKP YKCNECDKTF SRSTHLTEHQ NTHTGEKPYN CNECRKTFSQ STYLIQHQRI
HSAEKPFGCN DCGKAFRYRS ALNKHQRLHP GI
