ZN148_MOUSE
ID ZN148_MOUSE Reviewed; 794 AA.
AC Q61624; P97475;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Zinc finger protein 148;
DE AltName: Full=Beta enolase repressor factor 1;
DE AltName: Full=G-rich box-binding protein;
DE AltName: Full=Transcription factor BFCOL1;
DE AltName: Full=Transcription factor ZBP-89;
DE AltName: Full=Zinc finger DNA-binding protein 89;
GN Name=Znf148; Synonyms=Zbp89, Zfp148;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=CD-1; TISSUE=Limb;
RX PubMed=9417107; DOI=10.1074/jbc.273.1.484;
RA Passantino R., Antona V., Barbieri G., Rubino P., Melchionna R., Cossu G.,
RA Feo S., Giallongo A.;
RT "Negative regulation of beta enolase gene transcription in embryonic muscle
RT is dependent upon a zinc finger factor that binds to the G-rich box within
RT the muscle-specific enhancer.";
RL J. Biol. Chem. 273:484-494(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland;
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 26-794.
RX PubMed=9030551; DOI=10.1074/jbc.272.8.4915;
RA Hasegawa T., Takeuchi A., Miyaishi O., Isobe K., de Crombrugghe B.;
RT "Cloning and characterization of a transcription factor that binds to the
RT proximal promoters of the two mouse type I collagen genes.";
RL J. Biol. Chem. 272:4915-4923(1997).
RN [4]
RP DEVELOPMENTAL STAGE.
RC TISSUE=Pituitary adenoma;
RX PubMed=8943318; DOI=10.1128/mcb.16.12.6644;
RA Merchant J.L., Iyer G.R., Taylor B.R., Kitchen J.R., Mortensen E.R.,
RA Wang Z., Flintoft R.J., Michel J., Bassel-Duby R.;
RT "ZBP-89, a Kruppel-like zinc finger protein, inhibits epidermal growth
RT factor induction of the gastrin promoter.";
RL Mol. Cell. Biol. 16:6644-6653(1996).
RN [5]
RP INTERACTION WITH CAVIN1.
RX PubMed=10727401; DOI=10.1042/bj3470055;
RA Hasegawa T., Takeuchi A., Miyaishi O., Xiao H., Mao J., Isobe K.;
RT "PTRF (polymerase I and transcript-release factor) is tissue-specific and
RT interacts with the BFCOL1 (binding factor of a type-I collagen promoter)
RT zinc-finger transcription factor which binds to the two mouse type-I
RT collagen gene promoters.";
RL Biochem. J. 347:55-59(2000).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-301 AND SER-306, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH THE 5FMC COMPLEX AND CHTOP, SUMOYLATION, AND DESUMOYLATION
RP BY SENP3.
RX PubMed=22872859; DOI=10.1074/mcp.m112.017194;
RA Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
RA Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.;
RT "Five friends of methylated chromatin target of protein-arginine-
RT methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation
RT to desumoylation.";
RL Mol. Cell. Proteomics 11:1263-1273(2012).
CC -!- FUNCTION: Involved in transcriptional regulation. Represses the
CC transcription of a number of genes including gastrin, stromelysin and
CC enolase. Binds to the G-rich box in the enhancer region of these genes.
CC {ECO:0000269|PubMed:9417107}.
CC -!- SUBUNIT: Interacts with HNRNPDL (By similarity). Interacts with the
CC 5FMC complex; the interaction requires association with CHTOP
CC (PubMed:22872859). Interacts with CAVIN1 (PubMed:10727401).
CC {ECO:0000250|UniProtKB:Q9UQR1, ECO:0000269|PubMed:10727401,
CC ECO:0000269|PubMed:22872859}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Strong expression detected in brain, lung, liver
CC and kidney, with lower levels detected in spleen, skeletal muscle,
CC testis and heart. {ECO:0000269|PubMed:9417107}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryos from 7 dpc to 17 dpc.
CC Expression decreases in developing skeletal muscles.
CC {ECO:0000269|PubMed:8943318, ECO:0000269|PubMed:9417107}.
CC -!- PTM: Sumoylated with SUMO2. Desumoylated by SENP3, resulting in the
CC stimulation of transcription of its target genes.
CC {ECO:0000269|PubMed:22872859}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; X98096; CAA66725.1; -; mRNA.
DR EMBL; BC026144; AAH26144.1; -; mRNA.
DR EMBL; U80078; AAB38507.1; -; mRNA.
DR CCDS; CCDS28130.1; -.
DR RefSeq; NP_035879.1; NM_011749.4.
DR RefSeq; XP_006522165.1; XM_006522102.3.
DR RefSeq; XP_017172469.1; XM_017316980.1.
DR AlphaFoldDB; Q61624; -.
DR SMR; Q61624; -.
DR BioGRID; 204640; 3.
DR IntAct; Q61624; 1.
DR MINT; Q61624; -.
DR STRING; 10090.ENSMUSP00000126338; -.
DR iPTMnet; Q61624; -.
DR PhosphoSitePlus; Q61624; -.
DR EPD; Q61624; -.
DR jPOST; Q61624; -.
DR MaxQB; Q61624; -.
DR PaxDb; Q61624; -.
DR PRIDE; Q61624; -.
DR ProteomicsDB; 302076; -.
DR Antibodypedia; 901; 258 antibodies from 29 providers.
DR DNASU; 22661; -.
DR Ensembl; ENSMUST00000089677; ENSMUSP00000087106; ENSMUSG00000022811.
DR Ensembl; ENSMUST00000165418; ENSMUSP00000126338; ENSMUSG00000022811.
DR GeneID; 22661; -.
DR KEGG; mmu:22661; -.
DR UCSC; uc007zab.1; mouse.
DR CTD; 22661; -.
DR MGI; MGI:1332234; Zfp148.
DR VEuPathDB; HostDB:ENSMUSG00000022811; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000157406; -.
DR HOGENOM; CLU_025987_1_0_1; -.
DR InParanoid; Q61624; -.
DR OMA; FEQNFKS; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q61624; -.
DR TreeFam; TF331779; -.
DR BioGRID-ORCS; 22661; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Zfp148; mouse.
DR PRO; PR:Q61624; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q61624; protein.
DR Bgee; ENSMUSG00000022811; Expressed in rostral migratory stream and 251 other tissues.
DR ExpressionAtlas; Q61624; baseline and differential.
DR Genevisible; Q61624; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0007276; P:gamete generation; IMP:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0065003; P:protein-containing complex assembly; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 4.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE 1: Evidence at protein level;
KW Acetylation; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..794
FT /note="Zinc finger protein 148"
FT /id="PRO_0000047428"
FT ZN_FING 171..193
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 199..221
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 227..249
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 255..278
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 298..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..599
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 194
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT MOD_RES 301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT MOD_RES 607
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT MOD_RES 665
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT MOD_RES 784
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT CROSSLNK 88
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT CROSSLNK 132
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT CROSSLNK 291
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT CROSSLNK 308
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT CROSSLNK 356
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT CROSSLNK 356
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT CROSSLNK 402
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT CROSSLNK 421
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT CROSSLNK 424
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9UQR1"
FT CONFLICT 283
FT /note="K -> N (in Ref. 3; AAB38507)"
FT /evidence="ECO:0000305"
FT CONFLICT 314
FT /note="K -> P (in Ref. 3; AAB38507)"
FT /evidence="ECO:0000305"
FT CONFLICT 319
FT /note="K -> Q (in Ref. 3; AAB38507)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 794 AA; 88751 MW; 4CB1C2A1822703FD CRC64;
MNIDDKLEGL FLKCGGIDEM QSSRAMVVMG GVSGQSAVSG ELQESVLQDR SLPHQEILAA
DEVLQESEMR QQDMISHDEL MVHEETVKND EEQMDTHERL PQGLQYALNV PISVKQEITF
TDVSEQLMRD KKQVREPVDL QKKKKRKQRS PAKILTINED GSLGLKTPKS HVCEHCNAAF
RTNYHLQRHV FIHTGEKPFQ CSQCDMRFIQ KYLLQRHEKI HTGEKPFRCD ECGMRFIQKY
HMERHKRTHS GEKPYQCEYC LQYFSRTDRV LKHKRMCHEN HDKKLNRCAI KGGLLTSEED
SGFSTSPKDN SLPKKKRQKT EKKSSGMDKE SVLDKSDLKK DKNDYLPLYS SSTKVKDEYM
VAEYAVEMPH SSVGGSHLED ASGEIHPPKL VLKKINSKRS LKQPLEQSQT ISPLSSYEDS
KVSKYAFELV DKQALLDSEG SADIDQVDNL QEGPSKPVHS STNYDDAMQF LKKKRYLQAA
SNNSREYALN VGTIASQPSV TQAAVASVID ESTTASILDS QALNVEIKSN HDKNVIPDEV
LQTLLDHYSH KPNGQHEISF SVADTEVTSS ISINSSDVPE VTQSENVGSS SQASSSDKAN
MLQEYSKFLQ QALDRTSQND AYLNSPSLNF VTDNQTLPNP PAFSSIDKQV YAAMPINSFR
SGMNSPLRTT PDKSHFGLIV GDSQHPFPFS GDETNHASAT STADFLDQVT SQKKAEAQPV
HQAYQMSSFE QPFRAPYHGS RAGIATQFST ANGQVNLRGP GTSAEFSEFP LVNVNDNRAG
MTSSPDATTG QTFG
