ID   GMEB1_MOUSE             Reviewed;         562 AA.
AC   Q9JL60; Q80Y88;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Glucocorticoid modulatory element-binding protein 1;
DE            Short=GMEB-1;
GN   Name=Gmeb1;
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=Embryo;
RX   PubMed=10692587; DOI=10.1016/s0014-5793(00)01209-6;
RA   Jimenez-Lara A.M., Heine M.J.S., Gronemeyer H.;
RT   "Cloning of a mouse glucocorticoid modulatory element binding protein, a
RT   new member of the KDWK family.";
RL   FEBS Lett. 468:203-210(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Colon;
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Spleen;
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: Trans-acting factor that binds to glucocorticoid modulatory
CC       elements (GME) present in the TAT (tyrosine aminotransferase) promoter
CC       and increases sensitivity to low concentrations of glucocorticoids.
CC       Binds also to the transferrin receptor promoter (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer, and heterodimer of GMEB1 and GMEB2. Interacts with
CC       TRIM63 (By similarity). Interacts with the glucocorticoid receptor
CC       (NR3C1) and NCOA2/TIF2. May interact with HSP27 and CREB-binding
CC       protein (CBP). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=May be also cytoplasmic.
CC   -!- TISSUE SPECIFICITY: Ubiquitous. Low levels were detected in heart,
CC       brain, spleen, lung, liver, skeletal muscle, kidney and testis.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF210433; AAF72874.1; -; mRNA.
DR   EMBL; BX537301; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466552; EDL30116.1; -; Genomic_DNA.
DR   EMBL; BC046983; AAH46983.1; -; mRNA.
DR   CCDS; CCDS18720.1; -.
DR   RefSeq; NP_001116464.1; NM_001122992.1.
DR   RefSeq; NP_064669.2; NM_020273.2.
DR   RefSeq; XP_006539141.1; XM_006539078.3.
DR   RefSeq; XP_006539142.1; XM_006539079.3.
DR   RefSeq; XP_006539143.1; XM_006539080.3.
DR   RefSeq; XP_017175821.1; XM_017320332.1.
DR   AlphaFoldDB; Q9JL60; -.
DR   SMR; Q9JL60; -.
DR   BioGRID; 208184; 7.
DR   IntAct; Q9JL60; 4.
DR   STRING; 10090.ENSMUSP00000131331; -.
DR   PhosphoSitePlus; Q9JL60; -.
DR   EPD; Q9JL60; -.
DR   MaxQB; Q9JL60; -.
DR   PaxDb; Q9JL60; -.
DR   PeptideAtlas; Q9JL60; -.
DR   PRIDE; Q9JL60; -.
DR   ProteomicsDB; 263379; -.
DR   Antibodypedia; 30978; 170 antibodies from 25 providers.
DR   DNASU; 56809; -.
DR   Ensembl; ENSMUST00000030733; ENSMUSP00000030733; ENSMUSG00000028901.
DR   Ensembl; ENSMUST00000105964; ENSMUSP00000101584; ENSMUSG00000028901.
DR   Ensembl; ENSMUST00000105965; ENSMUSP00000101585; ENSMUSG00000028901.
DR   Ensembl; ENSMUST00000168553; ENSMUSP00000131331; ENSMUSG00000028901.
DR   GeneID; 56809; -.
DR   KEGG; mmu:56809; -.
DR   UCSC; uc008vat.2; mouse.
DR   CTD; 10691; -.
DR   MGI; MGI:2135604; Gmeb1.
DR   VEuPathDB; HostDB:ENSMUSG00000028901; -.
DR   eggNOG; KOG4333; Eukaryota.
DR   GeneTree; ENSGT00410000025596; -.
DR   HOGENOM; CLU_030344_1_0_1; -.
DR   InParanoid; Q9JL60; -.
DR   OMA; MVNPVEL; -.
DR   OrthoDB; 692814at2759; -.
DR   PhylomeDB; Q9JL60; -.
DR   TreeFam; TF317090; -.
DR   BioGRID-ORCS; 56809; 3 hits in 74 CRISPR screens.
DR   ChiTaRS; Gmeb1; mouse.
DR   PRO; PR:Q9JL60; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q9JL60; protein.
DR   Bgee; ENSMUSG00000028901; Expressed in animal zygote and 238 other tissues.
DR   Genevisible; Q9JL60; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR   GO; GO:0051008; F:Hsp27 protein binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.10.390.10; -; 1.
DR   InterPro; IPR024830; GMEB1/2.
DR   InterPro; IPR010919; SAND-like_dom_sf.
DR   InterPro; IPR000770; SAND_dom.
DR   PANTHER; PTHR10417; PTHR10417; 1.
DR   Pfam; PF01342; SAND; 1.
DR   SMART; SM00258; SAND; 1.
DR   SUPFAM; SSF63763; SSF63763; 1.
DR   PROSITE; PS50864; SAND; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Coiled coil; Cytoplasm; DNA-binding; Metal-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y692"
FT   CHAIN           2..562
FT                   /note="Glucocorticoid modulatory element-binding protein 1"
FT                   /id="PRO_0000074090"
FT   DOMAIN          72..156
FT                   /note="SAND"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00185"
FT   REGION          360..384
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          311..355
FT                   /evidence="ECO:0000255"
FT   BINDING         103
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         129
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         164
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         168
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y692"
FT   CONFLICT        263
FT                   /note="V -> I (in Ref. 1; AAF72874)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   562 AA;  61058 MW;  733C8A0D50DD477E CRC64;
     MANAEVSVPV GDVVVVPTEG NEGENPEDTK TQVILQLQPV QQGIYEAGSE NSAAVVAVET
     HSIHKIEEGI DASSIEGNED MEIAYPITCG ESKAVLLWKK FVCPGINVKC VKFNDQLISP
     KHFVHLAGKS TLKDWKRAIR LGGIMLRKMM DSGQIDFYQH DKVCSNTCRS TKFDLLISSA
     RAPVPGQQTS VVQTPTSADG NITQIAISEE SMEEAGLEWN SALTAAVTMA TEEGIKKESE
     EISEDTLMFW KGIADVGLME EVVCNIQKEM EELLRGVQQR LIQAPFQVTD AAVLNNVANT
     FGLMDAVKRV LDNRRKQVEQ GEEQFLYTLA DLERQLEEQK KQAQDPRLKS QTVQNVVLMP
     VSTPKPPKRP RLQRPASTTV LSPSPVQQPQ FTVISPITIT PVGQSFSMGN IPVATLSQGS
     SPVTVHTLPS GPQLFRYATV VSSAKSNSPD TVTIHPSSSL ALLSSTSMQD GSSLGNMATM
     VSPMELVAME SGLTSAIQAV ESTSEDGQTI IEIDPAPDSE ADDTEGKAVI LETGLRTEEK
     VVAEMEEHQH QVHNVEIVVL ED