ZN184_MOUSE
ID ZN184_MOUSE Reviewed; 737 AA.
AC Q7TSH9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Zinc finger protein 184;
GN Name=Zfp184;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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; BC053084; AAH53084.1; -; mRNA.
DR CCDS; CCDS26302.1; -.
DR RefSeq; NP_898835.1; NM_183014.1.
DR RefSeq; XP_006516659.1; XM_006516596.3.
DR RefSeq; XP_006516660.1; XM_006516597.3.
DR AlphaFoldDB; Q7TSH9; -.
DR SMR; Q7TSH9; -.
DR STRING; 10090.ENSMUSP00000100043; -.
DR iPTMnet; Q7TSH9; -.
DR PhosphoSitePlus; Q7TSH9; -.
DR jPOST; Q7TSH9; -.
DR MaxQB; Q7TSH9; -.
DR PaxDb; Q7TSH9; -.
DR PRIDE; Q7TSH9; -.
DR ProteomicsDB; 275003; -.
DR DNASU; 193452; -.
DR Ensembl; ENSMUST00000006903; ENSMUSP00000006903; ENSMUSG00000006720.
DR Ensembl; ENSMUST00000102978; ENSMUSP00000100043; ENSMUSG00000006720.
DR Ensembl; ENSMUST00000176511; ENSMUSP00000135173; ENSMUSG00000006720.
DR GeneID; 193452; -.
DR KEGG; mmu:193452; -.
DR UCSC; uc007pry.1; mouse.
DR CTD; 193452; -.
DR MGI; MGI:1922244; Zfp184.
DR VEuPathDB; HostDB:ENSMUSG00000006720; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000164849; -.
DR HOGENOM; CLU_002678_0_9_1; -.
DR InParanoid; Q7TSH9; -.
DR OMA; KEKTCKC; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q7TSH9; -.
DR TreeFam; TF350822; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR BioGRID-ORCS; 193452; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Zfp184; mouse.
DR PRO; PR:Q7TSH9; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q7TSH9; protein.
DR Bgee; ENSMUSG00000006720; Expressed in undifferentiated genital tubercle and 120 other tissues.
DR ExpressionAtlas; Q7TSH9; baseline and differential.
DR Genevisible; Q7TSH9; MM.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; 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; 15.
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; 18.
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..737
FT /note="Zinc finger protein 184"
FT /id="PRO_0000348469"
FT DOMAIN 28..99
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 201..223
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 229..251
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 257..279
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 285..307
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 313..335
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 341..363
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 369..391
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 397..419
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 425..447
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 453..475
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 481..503
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 509..531
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 537..559
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 565..587
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 593..615
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 621..643
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 649..671
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 677..698
FT /note="C2H2-type 18; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 704..726
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 CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q99676"
SQ SEQUENCE 737 AA; 84027 MW; 8846AE11B55D040A CRC64;
MAGLSFADSA SLHEGRPLLL PSSFRESVTF KDVVVNFTQE EWKHLDPIQR DLFRDVTLEN
YTHLVSIGLQ VSKPDMISQL EQGTEPWTED SCIPVGPLED WKKRAGNSVS SLELDISEEH
LFSETVVTNS KRDDGSLEKL QANQQMLPRE VQITEKTAPT CESNLSVSSS FITQTEVALD
QPSTKTRAKQ NSHPVKKEKL CKCNECGKAF TYCSALIRHQ RTHTGEKPYK CNECNKAFSR
SENLINHQRI HTGDKPYKCD QCGKGFIEGP SLTQHQRIHT GEKPYKCDEC GKAFSQRTHL
VQHQRIHTGE KPYTCTECGK SFSQRGHFME HQKIHTGEKP FKCEECEKTF TRSTHLTQHQ
KIHTGEKTYK CNECGKAFNG PSTFIRHHMI HTGEKPYECN ECGKAFSQHS NLTQHQKTHT
GEKPYDCAEC GKAFSYWSSL AQHLKIHTGE KPYKCSDCGK AFSYCSSLTQ HRRIHTREKP
FECSECGKAF SYLSNLNQHQ KTHTQEKAYE CKECGKAFIR SSSLAKHERI HTGEKPYQCH
ECGKTFSYGS SLIQHKKIHT GERPYKCNEC GRAFNQKIHL TQHKRIHTGA KPYACPKCGK
TFRHCSSLAQ HQKTHTEEKP YQCNKCEKTF SQNSRLTQHQ RIHTGEKPYK CSECDKCFTG
SVHLTEHRST HTGEKPYNSE CPQTFSQSTY LTQHQKIHSG EKLLGCEDCE KAFQCHSALT
KHQRLHPAVA AVGTSLT
