ZN148_RAT
ID ZN148_RAT Reviewed; 794 AA.
AC Q62806;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Zinc finger protein 148;
DE AltName: Full=Transcription factor ZBP-89;
DE AltName: Full=Zinc finger DNA-binding protein 89;
GN Name=Znf148; Synonyms=Zbp89, Zfp148;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-412 AND SER-784, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(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:8943318}.
CC -!- SUBUNIT: Interacts with HNRNPDL. Interacts with the 5FMC complex; the
CC interaction requires association with CHTOP. Interacts with CAVIN1.
CC {ECO:0000250|UniProtKB:Q61624, ECO:0000250|UniProtKB:Q9UQR1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8943318}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, lung, kidney, skeletal muscle,
CC liver, brain and spleen. {ECO:0000269|PubMed:8943318}.
CC -!- PTM: Sumoylated with SUMO2. Desumoylated by SENP3, resulting in the
CC stimulation of transcription of its target genes (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; U30381; AAC52958.1; -; mRNA.
DR RefSeq; NP_113803.1; NM_031615.2.
DR AlphaFoldDB; Q62806; -.
DR SMR; Q62806; -.
DR STRING; 10116.ENSRNOP00000002435; -.
DR CarbonylDB; Q62806; -.
DR iPTMnet; Q62806; -.
DR PhosphoSitePlus; Q62806; -.
DR jPOST; Q62806; -.
DR PaxDb; Q62806; -.
DR PRIDE; Q62806; -.
DR GeneID; 58820; -.
DR KEGG; rno:58820; -.
DR UCSC; RGD:62063; rat.
DR CTD; 22661; -.
DR RGD; 62063; Zfp148.
DR VEuPathDB; HostDB:ENSRNOG00000001789; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q62806; -.
DR OMA; FEQNFKS; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q62806; -.
DR TreeFam; TF331779; -.
DR PRO; PR:Q62806; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001789; Expressed in Ammon's horn and 19 other tissues.
DR Genevisible; Q62806; RN.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISO:RGD.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:RGD.
DR GO; GO:0007276; P:gamete generation; ISO:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:RGD.
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_0000047429"
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..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61624"
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:0000250|UniProtKB:Q61624"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
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:0007744|PubMed:22673903"
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"
SQ SEQUENCE 794 AA; 88748 MW; 7CAED0E3E79EA756 CRC64;
MNIDDKLEGL FLKCGGIDEM QSSRAMVVMG GVSGQSAVSG ELQESVLQDR SLPHQEILAA
DEVLQESEMR QQDMISHDEL MVHEETVKND EEQTDTHERL PQGLQYALNV PISVKQEITF
TDVSEQLMRD KKQVREPVDL QKKKKRKQRS PAKILTINED GSLGLKTPKS HVCEHCNAAF
RTNYHLQRHV FIHTGEKPFQ CSQCDMRFIQ KYLLQRHEKI HTGEKPFRCD ECGMRFIQKY
HMERHKRTHS GEKPYQCEYC LQYFSRTDRV LKHKRMCHEN HDKKLNRCAI KGGLLTSEED
SGFSTSPKDN SLPKKKRQKP EKKSSGMDKE SVLDKSDTKK DRNDYLPLYS SSTKVKDEYM
VAEYAVEMPH SSVGGSHLED ASGEIHPPKL VLKKINSKRS LKQPLEQSQT ISPLSTYEDS
KVSKYAFELV DKQALLDSEG SADIDQVDNL QEGPSKPVHS STNYDDAMQF LKKKRYLQAA
SNNSREYALN VGTIASQPSV TQAAVASVID ENTTASILDS QALNVEIKSN HDKNVIPDEV
LQTLLDHYSH KANGQHEISF SVADTEVTSS ISINSSDVPE VTQSENVGSS SQASSSDKAN
MLQEYSKFLQ QALDRTSQND AYLNSPSLNF VTDNQTLPNP PAFSSIDKQV YAAMPINSFR
SGMNSPLRTT PDKSHFGLIV GDSQHPFPFS GDETNHASAT STADFLDQVT SQKKAEAQPV
HQAYQMSSFE QPFRAPYHGS RAGIATQFST ANGQVNLRGP GTSAEFSEFP LVNVNDNRAG
MTSSPDATTG QTFG
