NAB1_MOUSE
ID NAB1_MOUSE Reviewed; 486 AA.
AC Q61122; Q99J24;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=NGFI-A-binding protein 1;
DE AltName: Full=EGR-1-binding protein 1;
GN Name=Nab1;
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].
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 NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8668170; DOI=10.1128/mcb.16.7.3545;
RA Svaren J., Sevetson B.R., Apel E.D., Zimonjic D.B., Popescu N.C.,
RA Milbrandt J.;
RT "NAB2, a corepressor of NGFI-A (Egr-1) and Krox20, is induced by
RT proliferative and differentiative stimuli.";
RL Mol. Cell. Biol. 16:3545-3553(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129, and FVB/N; TISSUE=Kidney, and Mammary tumor;
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 [5]
RP FUNCTION, AND MUTAGENESIS.
RX PubMed=9774344; DOI=10.1093/emboj/17.20.6010;
RA Svaren J., Sevetson B.R., Golda T., Stanton J.J., Swirnoff A.H.,
RA Milbrandt J.;
RT "Novel mutants of NAB corepressors enhance activation by Egr
RT transactivators.";
RL EMBO J. 17:6010-6019(1998).
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-171; SER-182 AND SER-405, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Testis;
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).
CC -!- FUNCTION: Acts as a transcriptional repressor for zinc finger
CC transcription factors EGR1 and EGR2. {ECO:0000250,
CC ECO:0000269|PubMed:9774344}.
CC -!- SUBUNIT: Homomultimers may associate with EGR1 bound to DNA.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Widely expressed in adult. In day 16 embryo highest
CC levels in forebrain, thymus, salivary gland and cartilage.
CC -!- DEVELOPMENTAL STAGE: In day 16 embryo highest levels in forebrain,
CC thymus, salivary gland and cartilage.
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; U47008; AAC52649.1; -; mRNA.
DR EMBL; CH466548; EDK99971.1; -; Genomic_DNA.
DR EMBL; BC005627; AAH05627.1; -; mRNA.
DR EMBL; BC016886; AAH16886.1; -; mRNA.
DR CCDS; CCDS14944.1; -.
DR RefSeq; NP_032693.2; NM_008667.3.
DR RefSeq; XP_006495833.1; XM_006495770.2.
DR AlphaFoldDB; Q61122; -.
DR SMR; Q61122; -.
DR IntAct; Q61122; 1.
DR MINT; Q61122; -.
DR STRING; 10090.ENSMUSP00000066696; -.
DR iPTMnet; Q61122; -.
DR PhosphoSitePlus; Q61122; -.
DR EPD; Q61122; -.
DR MaxQB; Q61122; -.
DR PaxDb; Q61122; -.
DR PRIDE; Q61122; -.
DR ProteomicsDB; 252643; -.
DR Antibodypedia; 1209; 327 antibodies from 26 providers.
DR DNASU; 17936; -.
DR Ensembl; ENSMUST00000069792; ENSMUSP00000066696; ENSMUSG00000002881.
DR GeneID; 17936; -.
DR KEGG; mmu:17936; -.
DR UCSC; uc007ayh.2; mouse.
DR CTD; 4664; -.
DR MGI; MGI:107564; Nab1.
DR VEuPathDB; HostDB:ENSMUSG00000002881; -.
DR eggNOG; KOG3835; Eukaryota.
DR GeneTree; ENSGT00390000006330; -.
DR InParanoid; Q61122; -.
DR OMA; LCMRDTA; -.
DR OrthoDB; 1002244at2759; -.
DR PhylomeDB; Q61122; -.
DR TreeFam; TF315501; -.
DR BioGRID-ORCS; 17936; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Nab1; mouse.
DR PRO; PR:Q61122; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q61122; protein.
DR Bgee; ENSMUSG00000002881; Expressed in carotid body and 262 other tissues.
DR ExpressionAtlas; Q61122; baseline and differential.
DR Genevisible; Q61122; MM.
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; IGI:MGI.
DR GO; GO:0042552; P:myelination; IGI:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0045682; P:regulation of epidermis development; IGI:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IGI:MGI.
DR GO; GO:0014037; P:Schwann cell differentiation; IGI:MGI.
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 1: Evidence at protein level;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..486
FT /note="NGFI-A-binding protein 1"
FT /id="PRO_0000077040"
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..438
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 COMPBIAS 398..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT MOD_RES 405
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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 453
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT CROSSLNK 464
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT CROSSLNK 476
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT CROSSLNK 479
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT CROSSLNK 479
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13506"
FT MUTAGEN 33
FT /note="Q->R: Loss of transcriptional repression; when
FT associated with Q-64."
FT /evidence="ECO:0000269|PubMed:9774344"
FT MUTAGEN 51
FT /note="E->K: Loss of transcriptional repression."
FT /evidence="ECO:0000269|PubMed:9774344"
FT MUTAGEN 64
FT /note="H->Q: Loss of transcriptional repression; when
FT associated with R-33."
FT /evidence="ECO:0000269|PubMed:9774344"
FT CONFLICT 181
FT /note="A -> V (in Ref. 2; AAC52649)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 54010 MW; 535CC2ADD604219C CRC64;
MATALPRTLG ELQLYRILQK ANLLSYFDAF IQQGGDDVQQ LCEAGEEEFL EIMALVGMAS
KPLHVRRLQK ALRDWVTNPG LFNQPLTSLP VSSIPIYKLP EGSPTWLGIS CNSYERSSSS
REPHLKIPKC AATTCVQSLG QGKSEVGSLA LQSVSDSRLW QGHHATESEH SLSPADLGSP
ASPKESSEAL DAAAALSVAE CVERMAPTLP KSDLSEVKEL LKNNKKLAKM IGHIFEMSDE
DPHKEEEIRK YSAIYGRFDS KRKDGKHLTL HELTVNEAAA QLCVKDNALL TRRDELFALA
RQVSREVTYK YTYRTTRLKC GERDELSPKR IKIEDGFPDF QESVPTLFQQ ARAKSEELAG
LGSQQAEKGM AKQMELLCAQ AGYERLQQER RLTAGLYRQS SGEQSPDGGL PSDSSDGQGE
RPLNLRIPSV QNRQPHHFVV DGELSRLYSS EAKSHSSESL GILKDYPHSA FTLEKKVIKT
EPEDSR
