NAB2_MOUSE
ID NAB2_MOUSE Reviewed; 525 AA.
AC Q61127; Q80VR9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=NGFI-A-binding protein 2;
DE AltName: Full=EGR-1-binding protein 2;
GN Name=Nab2;
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] (ISOFORMS 1 AND 2).
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 [2]
RP PARTIAL NUCLEOTIDE SEQUENCE (ISOFORM 2).
RX PubMed=9126479; DOI=10.1006/geno.1997.4609;
RA Svaren J., Apel E.D., Simburger K.S., Jenkins N.A., Gilbert D.J.,
RA Copeland N.G., Milbrandt J.;
RT "The Nab2 and Stat6 genes share a common transcription termination
RT region.";
RL Genomics 41:33-39(1997).
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 TISSUE=Olfactory epithelium;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157; SER-159; SER-162;
RP SER-171 AND SER-479, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Spleen, and
RC 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. Isoform 2 lacks repression
CC ability.
CC -!- SUBUNIT: Homomultimers may associate with EGR1 bound to DNA.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Isoform 2 is not localized to the
CC nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q61127-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q61127-2; Sequence=VSP_003388, VSP_003389;
CC -!- TISSUE SPECIFICITY: Highly expressed in brain and thymus, and at lower
CC levels in spleen, kidney, heart and testis. Isoform 1 is predominantly
CC expressed in testis, whereas isoform 3 is more abundant in thymus.
CC -!- INDUCTION: By serum stimulation.
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 -!- PTM: Sumoylation by EGR2 represses EGR2 transcriptional activity in
CC hindbrain. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NAB family. {ECO:0000305}.
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DR EMBL; U47543; AAC52650.1; -; mRNA.
DR EMBL; CH466578; EDL24515.1; -; Genomic_DNA.
DR EMBL; BC045139; AAH45139.1; -; mRNA.
DR CCDS; CCDS24247.1; -. [Q61127-1]
DR RefSeq; NP_001116367.1; NM_001122895.1.
DR RefSeq; NP_032694.2; NM_008668.2. [Q61127-1]
DR AlphaFoldDB; Q61127; -.
DR SMR; Q61127; -.
DR BioGRID; 201681; 5.
DR IntAct; Q61127; 5.
DR MINT; Q61127; -.
DR STRING; 10090.ENSMUSP00000026469; -.
DR iPTMnet; Q61127; -.
DR PhosphoSitePlus; Q61127; -.
DR EPD; Q61127; -.
DR jPOST; Q61127; -.
DR MaxQB; Q61127; -.
DR PaxDb; Q61127; -.
DR PeptideAtlas; Q61127; -.
DR PRIDE; Q61127; -.
DR ProteomicsDB; 286139; -. [Q61127-1]
DR ProteomicsDB; 286140; -. [Q61127-2]
DR Antibodypedia; 3858; 413 antibodies from 36 providers.
DR DNASU; 17937; -.
DR Ensembl; ENSMUST00000026469; ENSMUSP00000026469; ENSMUSG00000025402. [Q61127-1]
DR GeneID; 17937; -.
DR KEGG; mmu:17937; -.
DR UCSC; uc011xpt.1; mouse. [Q61127-1]
DR CTD; 4665; -.
DR MGI; MGI:107563; Nab2.
DR VEuPathDB; HostDB:ENSMUSG00000025402; -.
DR eggNOG; KOG3835; Eukaryota.
DR GeneTree; ENSGT00390000006330; -.
DR HOGENOM; CLU_029394_2_0_1; -.
DR InParanoid; Q61127; -.
DR OMA; HARTNAD; -.
DR OrthoDB; 1002244at2759; -.
DR PhylomeDB; Q61127; -.
DR TreeFam; TF315501; -.
DR Reactome; R-MMU-9031628; NGF-stimulated transcription.
DR BioGRID-ORCS; 17937; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Nab2; mouse.
DR PRO; PR:Q61127; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q61127; protein.
DR Bgee; ENSMUSG00000025402; Expressed in cerebellar vermis and 225 other tissues.
DR ExpressionAtlas; Q61127; baseline and differential.
DR Genevisible; Q61127; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
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:0016480; P:negative regulation of transcription by RNA polymerase III; ISO:MGI.
DR GO; GO:1902949; P:positive regulation of tau-protein kinase activity; ISO:MGI.
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; 1.10.150.50; -; 1.
DR Gene3D; 1.20.120.2010; -; 1.
DR InterPro; IPR006989; NAB_co-repressor_dom.
DR InterPro; IPR039040; NAB_fam.
DR InterPro; IPR006988; Nab_N.
DR InterPro; IPR038398; NCD2_sf.
DR InterPro; IPR013761; SAM/pointed_sf.
DR PANTHER; PTHR12623; PTHR12623; 1.
DR Pfam; PF04904; NCD1; 1.
DR Pfam; PF04905; NCD2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..525
FT /note="NGFI-A-binding protein 2"
FT /id="PRO_0000077043"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..113
FT /note="NCD1"
FT REGION 135..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..356
FT /note="NCD2"
FT REGION 353..384
FT /note="Necessary for nuclear localization"
FT /evidence="ECO:0000250"
FT REGION 381..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15742"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 379
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q15742"
FT CROSSLNK 517
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15742"
FT CROSSLNK 517
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15742"
FT VAR_SEQ 320..322
FT /note="LTI -> ASL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8668170"
FT /id="VSP_003388"
FT VAR_SEQ 323..525
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8668170"
FT /id="VSP_003389"
FT CONFLICT 233
FT /note="G -> C (in Ref. 1; AAC52650)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="R -> W (in Ref. 1; AAC52650)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 525 AA; 56577 MW; 4FFA510C8E39DF70 CRC64;
MHRAPSPTAE QPPGRGDNTR RTPQPRFKAS APAMALPRTL GELQLYRVLQ RANLLSYYET
FIQQGGDDVQ QLCEAGEEEF LEIMALVGMA TKPLHVRRLQ KALREWATNP GLFSQPVPAV
PVSSIPLFKI SETAGTRKGS MSNGHGSPGE KAGSARSFSP KSPLELGEKL SPLPGGPGAG
DPRIWPGQST PESDVGAGGE EEAGSPPFSP PAGGGVSEGP GVGGVAAGGA GGGPDRLEPE
MVRMVVESVE RIFRSFPRGD TGEIASLLKL NKKLARSVGH IFEMDDHDAQ KEEEIRKYSV
IYGRLDSKRR EGKQLSLHEL TINEAAAQFC MRDNTLLLRR VELFSLSRQV ARESTYLSSL
KGSRLHSEEL GGPPLKKLKQ EVGEQSHNEI QQPPPGPESY APPYRPSLEE DSASLSGESL
DGHLQAVGSC PRLTPPPADL PLALPAHGLW SRHILQQTLM DEGLRLARLV SHDRVGRLSP
CVPAKPPLAE FEEGLLDRCP APGPHPALVE GRRSSVKVEA EASRQ
