ID   NAB1_RAT                Reviewed;         485 AA.
AC   Q62722;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=NGFI-A-binding protein 1;
DE   AltName: Full=EGR-1-binding protein 1;
GN   Name=Nab1;
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].
RC   TISSUE=Brain;
RX   PubMed=7624335; DOI=10.1073/pnas.92.15.6873;
RA   Russo M.W., Sevetson B.R., Milbrandt J.;
RT   "Identification of NAB1, a repressor of NGFI-A- and Krox20-mediated
RT   transcription.";
RL   Proc. Natl. Acad. Sci. U.S.A. 92:6873-6877(1995).
RN   [2]
RP   FUNCTION.
RX   PubMed=9418898; DOI=10.1128/mcb.18.1.512;
RA   Swirnoff A.H., Apel E.D., Svaren J., Sevetson B.R., Zimonjic D.B.,
RA   Popescu N.C., Milbrandt J.;
RT   "Nab1, a corepressor of NGFI-A (Egr-1), contains an active transcriptional
RT   repression domain.";
RL   Mol. Cell. Biol. 18:512-524(1998).
CC   -!- FUNCTION: Acts as a transcriptional repressor for zinc finger
CC       transcription factors EGR1 and EGR2. Also represses multiple types of
CC       non-EGR1 activation domains (in vitro). {ECO:0000269|PubMed:9418898}.
CC   -!- SUBUNIT: Homomultimers may associate with EGR1 bound to DNA.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC52236.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U17253; AAC52236.1; ALT_INIT; mRNA.
DR   PIR; I59402; I59402.
DR   RefSeq; NP_074047.2; NM_022856.5.
DR   RefSeq; XP_006244964.1; XM_006244902.3.
DR   AlphaFoldDB; Q62722; -.
DR   SMR; Q62722; -.
DR   STRING; 10116.ENSRNOP00000017813; -.
DR   iPTMnet; Q62722; -.
DR   PhosphoSitePlus; Q62722; -.
DR   PaxDb; Q62722; -.
DR   PRIDE; Q62722; -.
DR   Ensembl; ENSRNOT00000017813; ENSRNOP00000017813; ENSRNOG00000012959.
DR   GeneID; 64824; -.
DR   KEGG; rno:64824; -.
DR   UCSC; RGD:70882; rat.
DR   CTD; 4664; -.
DR   RGD; 70882; Nab1.
DR   eggNOG; KOG3835; Eukaryota.
DR   GeneTree; ENSGT00390000006330; -.
DR   HOGENOM; CLU_561344_0_0_1; -.
DR   InParanoid; Q62722; -.
DR   OMA; LCMRDTA; -.
DR   OrthoDB; 1002244at2759; -.
DR   PRO; PR:Q62722; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000012959; Expressed in liver and 20 other tissues.
DR   Genevisible; Q62722; RN.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0001958; P:endochondral ossification; ISO:RGD.
DR   GO; GO:0042552; P:myelination; ISO:RGD.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR   GO; GO:0045682; P:regulation of epidermis development; ISO:RGD.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR   GO; GO:0014037; P:Schwann cell differentiation; ISO:RGD.
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_0000077041"
FT   REGION          4..82
FT                   /note="NCD1"
FT   REGION          160..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          220..309
FT                   /note="NCD2"
FT   REGION          391..422
FT                   /note="Necessary for nuclear localization"
FT   REGION          398..431
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         404
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        367
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13506"
FT   CROSSLNK        371
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;  54026 MW;  D77B85B238204677 CRC64;
     MATALPRTLG ELQLYRILQK ANLLSYFDAF IQQGGDDVQQ LCEAGEEEFL EIMALVGMAS
     KPLHVRRLQK ALRDWVTNPG LFNQPLTSLP VSSIPIYKLP EGSPTWLGIS CNSYERSSSA
     REPHLKVPKC AATTCVQSLG QGKSEVGSLA LQSVSESRLW QGHHTTESEH SLSPADLGSP
     ASPKESSEAL DAAAALSVAE CVERMAPTLP KSDLNEVKEL LKNNKKLAKM IGHIFEMSDE
     DPHKEEEIRK YSAIYGRFDS KRKDGKHLTL HELTVNEAAA QLCVKDNALL TRRDELFALA
     RQVSREVTYK YTYRTTRLKC GERDELSPKR IKMEDGFPDF QESVPTLFQQ ARAKSEELAG
     LSSQAEKGMA KQMELLCAQA GYERLQQERR LMAGLYRQSS GEQSPDGGLP SDGSDGQGER
     PLNLRIPSVQ NRQPHHFVVD GELSRLYSNE VKSHSSESLG ILKDYPHSAF TLEKKVIKTE
     PEDSR