NAB1_MESAU
ID NAB1_MESAU Reviewed; 485 AA.
AC O35589;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=NGFI-A-binding protein 1;
DE AltName: Full=EGR-1-binding protein 1;
DE AltName: Full=Transcriptional repressor TA16;
GN Name=NAB1;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Leiomyosarcoma;
RX PubMed=9259324; DOI=10.1210/mend.11.9.9969;
RA Fan W., Ma J.-X., Cheng L., Norris J.S.;
RT "Molecular cloning of TA16, a transcriptional repressor that may mediate
RT glucocorticoid-induced growth arrest of leiomyosarcoma cells.";
RL Mol. Endocrinol. 11:1342-1352(1997).
CC -!- FUNCTION: Acts as a transcriptional repressor for zinc finger
CC transcription factors EGR1 and EGR2. {ECO:0000250}.
CC -!- SUBUNIT: Homomultimers may associate with EGR1 bound to DNA.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- INDUCTION: By glucocorticoids.
CC -!- DOMAIN: The NAB conserved domain 1 (NCD1) interacts with EGR1
CC inhibitory domain and mediates multimerization.
CC -!- DOMAIN: The NAB conserved domain 2 (NCD2) is necessary for
CC transcriptional repression.
CC -!- SIMILARITY: Belongs to the NAB family. {ECO:0000305}.
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DR EMBL; U88975; AAC53313.1; -; mRNA.
DR RefSeq; NP_001268536.1; NM_001281607.1.
DR AlphaFoldDB; O35589; -.
DR SMR; O35589; -.
DR STRING; 10036.XP_005084551.1; -.
DR PRIDE; O35589; -.
DR GeneID; 101827193; -.
DR CTD; 4664; -.
DR eggNOG; KOG3835; Eukaryota.
DR OrthoDB; 1002244at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.20.120.2010; -; 1.
DR InterPro; IPR006986; Nab1_C.
DR InterPro; IPR006989; NAB_co-repressor_dom.
DR InterPro; IPR039040; NAB_fam.
DR InterPro; IPR006988; Nab_N.
DR InterPro; IPR038398; NCD2_sf.
DR PANTHER; PTHR12623; PTHR12623; 1.
DR Pfam; PF04902; Nab1; 1.
DR Pfam; PF04904; NCD1; 1.
DR Pfam; PF04905; NCD2; 1.
PE 2: Evidence at transcript level;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..485
FT /note="NGFI-A-binding protein 1"
FT /id="PRO_0000077039"
FT REGION 4..82
FT /note="NCD1"
FT REGION 160..187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..309
FT /note="NCD2"
FT REGION 306..337
FT /note="Necessary for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 398..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61122"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61122"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61122"
FT CROSSLNK 126
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT CROSSLNK 129
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT CROSSLNK 143
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT CROSSLNK 211
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT CROSSLNK 332
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT CROSSLNK 332
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT CROSSLNK 354
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT CROSSLNK 368
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT CROSSLNK 372
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT CROSSLNK 452
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT CROSSLNK 463
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT CROSSLNK 475
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT CROSSLNK 478
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT CROSSLNK 478
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
SQ SEQUENCE 485 AA; 54062 MW; AD8EFC04D1460F62 CRC64;
MATALPRTLG ELQLYRILQK ANLLSYFGAF IQQGGDDVQQ LCEAGEEEFL EIMALVGMAS
KPLHVRRLQK ALRDWVTNPG LFNQPLTSLP VSSIPIYKLP KGSPTWLGIS CNSYERNSSA
REPHLKIPKC AATTCVQSLG QGKSEVGSLA VQSVSESRLW QGHHATESEH SLSPADVGSP
ASPKESSEAL DAAAALSVAE CVERMASTLP KSDLNEVKEL LKNNKKLAKM IGHIFEMSDE
DPHKEEEIRK YSAIYGRFDS KRKDGKHLTL HELTVNEAAA QLCVKDNALL TRRDELFALA
RQVSREVTYK YTYRTTRLKC GERDELSPKR IKVEDGFPDF QEPVQTLFQQ ARAKSEELAA
LSSQQTEKGM AKQMELLCAQ ASYERLQQER RLTAGLYRQS SGEHSPDGLP SDGSDGQGER
PLNLRMPNVQ NRQPHHFVAD GELSRLYSSE AKSHSSENLG ILKDYPHSAF TLEKKVIKTE
PEDSR
