ZN148_PONAB
ID ZN148_PONAB Reviewed; 794 AA.
AC Q5R782;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Zinc finger protein 148;
GN Name=ZNF148;
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=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
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:0000250}.
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; CR860236; CAH92378.1; -; mRNA.
DR RefSeq; NP_001126401.1; NM_001132929.1.
DR AlphaFoldDB; Q5R782; -.
DR SMR; Q5R782; -.
DR STRING; 9601.ENSPPYP00000015057; -.
DR GeneID; 100447276; -.
DR KEGG; pon:100447276; -.
DR CTD; 7707; -.
DR eggNOG; KOG1721; Eukaryota.
DR InParanoid; Q5R782; -.
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; 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 2: Evidence at transcript 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_0000354689"
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: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:0000250|UniProtKB:Q9UQR1"
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"
SQ SEQUENCE 794 AA; 88879 MW; 213020192A29F37A CRC64;
MNIDDKLEGL FLKCGGIDEM QSSRTMVVMG GVSGQSTVSG ELQDSVLQDR SMPHQEILAA
DEVLQESEMR QQDMISHDEL MVHEETVKND EEQMETHERL PQGLQYALNV PISVKQEITF
TDVSEQLMRD KKQIREPVDL QKKKKRKQRS PAKILTINED GSLGLKTPKS HVCEHCNAAF
RTNYHLQRHV FIHTGEKPFQ CSQCDMRFIQ KYLLQRHEKI HTGEKPFRCD ECGMRFIQKY
HMERHKRTHS GEKPYQCEYC LQYFSRTDRV LKHKRMCHEN HDKKLNRCAI KGGLLTSEED
SGFSTSPKDN SLPKKKRQKT EKKSSGMDKE SALDKSDLKK DKNDYLPLYS SSTKVKDGYM
VAEYAVEMPH SSVGGSHLED ASGEIHPPKL VLKKINSKRS LKQPLEQNQT ISPLTTYEES
KVSKYAFELV DKQALLDSEG NADIDQVDNL QEGPSKPVHS STNYDDAMQF LKKKRYLQAA
SNNSREYALN VGTIASQPSV TQAAVASVID ESTTASILES QALNVEIKSN HDKNVIPDEV
LQTLLDHYSH KANGQHEISF SVADTEVTSS ISINSSEVPE VTPSENVGSS SQASSSDKAN
MLQEYSKFLQ QALDRTSQND AYLNSPSLNF VTDNQTLPNQ PAFSSTDKQV YATMPINSFR
SGMNSPLRTT PDKSHFGLIV GDSQHSFPFS GDETNHASAT STQDFLDQVT SQKKAEAQPV
HQAYQMSSFE QPFRAPYHGS RAGIATQFST ANGQVNLRGP GTSAEFSEFP LVNVNDSRAG
MTSSPDATTG QTFG
