ID   GMEB2_MOUSE             Reviewed;         530 AA.
AC   P58929; Q6PCY0;
DT   26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 2.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Glucocorticoid modulatory element-binding protein 2;
DE            Short=GMEB-2;
GN   Name=Gmeb2;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, 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).
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       the glucocorticoid receptor (NR3C1). May interact with CREB-binding
CC       protein (CBP) (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00185}.
CC       Cytoplasm {ECO:0000250}. Note=May be also cytoplasmic. {ECO:0000250}.
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DR   EMBL; BC029763; AAH29763.1; -; mRNA.
DR   EMBL; BC059066; AAH59066.1; -; mRNA.
DR   CCDS; CCDS17206.1; -.
DR   RefSeq; NP_937812.1; NM_198169.2.
DR   RefSeq; XP_006500665.1; XM_006500602.2.
DR   RefSeq; XP_006500666.1; XM_006500603.1.
DR   RefSeq; XP_006500667.1; XM_006500604.1.
DR   RefSeq; XP_006500668.1; XM_006500605.2.
DR   AlphaFoldDB; P58929; -.
DR   SMR; P58929; -.
DR   BioGRID; 230807; 11.
DR   IntAct; P58929; 11.
DR   STRING; 10090.ENSMUSP00000037075; -.
DR   iPTMnet; P58929; -.
DR   PhosphoSitePlus; P58929; -.
DR   EPD; P58929; -.
DR   jPOST; P58929; -.
DR   MaxQB; P58929; -.
DR   PaxDb; P58929; -.
DR   PeptideAtlas; P58929; -.
DR   PRIDE; P58929; -.
DR   ProteomicsDB; 266820; -.
DR   Antibodypedia; 1759; 111 antibodies from 24 providers.
DR   DNASU; 229004; -.
DR   Ensembl; ENSMUST00000049032; ENSMUSP00000037075; ENSMUSG00000038705.
DR   GeneID; 229004; -.
DR   KEGG; mmu:229004; -.
DR   UCSC; uc008olq.1; mouse.
DR   CTD; 26205; -.
DR   MGI; MGI:2652836; Gmeb2.
DR   VEuPathDB; HostDB:ENSMUSG00000038705; -.
DR   eggNOG; KOG4333; Eukaryota.
DR   GeneTree; ENSGT00410000025596; -.
DR   HOGENOM; CLU_030344_2_0_1; -.
DR   InParanoid; P58929; -.
DR   OMA; PGTVEIH; -.
DR   OrthoDB; 692814at2759; -.
DR   PhylomeDB; P58929; -.
DR   TreeFam; TF317090; -.
DR   BioGRID-ORCS; 229004; 12 hits in 80 CRISPR screens.
DR   ChiTaRS; Gmeb2; mouse.
DR   PRO; PR:P58929; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; P58929; protein.
DR   Bgee; ENSMUSG00000038705; Expressed in granulocyte and 217 other tissues.
DR   ExpressionAtlas; P58929; baseline and differential.
DR   Genevisible; P58929; MM.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
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; IBA:GO_Central.
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   2: Evidence at transcript level;
KW   Coiled coil; Cytoplasm; DNA-binding; Isopeptide bond; Metal-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc.
FT   CHAIN           1..530
FT                   /note="Glucocorticoid modulatory element-binding protein 2"
FT                   /id="PRO_0000074093"
FT   DOMAIN          81..163
FT                   /note="SAND"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00185"
FT   COILED          245..270
FT                   /evidence="ECO:0000255"
FT   COILED          304..344
FT                   /evidence="ECO:0000255"
FT   BINDING         110
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         136
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         154
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         373
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKD1"
FT   CROSSLNK        155
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKD1"
FT   CROSSLNK        155
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UKD1"
SQ   SEQUENCE   530 AA;  56631 MW;  9CFF4660A1CB97ED CRC64;
     MATPDVSVHM EEVVVVTTPD TAVDGSGVEE VKTVLVTTNL APHGGDLTED NMETENAAAA
     AAAAFTASSQ LKEAVLVKMA EEGENLEAEI VYPITCGDSR ANLIWRKFVC PGINVKCVQY
     DEHVISPKEF VHLAGKSTLK DWKRAIRMNG IMLRKIMDSG ELDFYQHDKV CSNTCRSTKI
     DLSGARVSLS SPTSTEYIPL TPAAADVNGS PATITIETCE DPGDWTTTIG DDTFAFWRGL
     KDAGLLDEVI QEFQQELEET MKGLQQRVQD PPLQLRDAVL LNNIVQNFGM LDLVKKVLAS
     HKCQMDRSRE QYARDLAALE QQCDEHRRRA KELKHKSQHL SNVLMTLTPV PLPSPMKRPR
     LARATSGPAA MASQVLTQSA QIALSPGMPV SQLTSVPLGK VVSTLPSTVL GKGSPQAAPA
     SSPASPLLGG YTVLASSGST FPNAVEIHPD TSSLTVLSTA AMQDGSTVLK VVSPLQLLTL
     PGLGPTLQNV AQASPAGSTI VTMPTATATG PEEHTATIEV AAVAEDHEQK