GMEB2_RAT
ID GMEB2_RAT Reviewed; 529 AA.
AC O88873; Q9JL86; Q9JL87; Q9JL88; Q9QUZ7;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Glucocorticoid modulatory element-binding protein 2;
DE Short=GMEB-2;
GN Name=Gmeb2;
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] (ISOFORMS 1 AND 2), AND PROTEIN SEQUENCE OF
RP 278-294.
RC TISSUE=Hepatoma;
RX PubMed=9651376; DOI=10.1074/jbc.273.28.17756;
RA Zeng H., Jackson D.A., Oshima H., Simons S.S. Jr.;
RT "Cloning and characterization of a novel binding factor (GMEB-2) of the
RT glucocorticoid modulatory element.";
RL J. Biol. Chem. 273:17756-17762(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 4).
RX PubMed=10734202; DOI=10.1093/nar/28.8.1819;
RA Zeng H., Kaul S., Simons S.S. Jr.;
RT "Genomic organization of human GMEB-1 and rat GMEB-2: structural
RT conservation of two multifunctional proteins.";
RL Nucleic Acids Res. 28:1819-1829(2000).
RN [3]
RP PROTEIN SEQUENCE OF 155-168; 242-261 AND 267-275.
RC TISSUE=Hepatoma;
RX PubMed=7665613; DOI=10.1074/jbc.270.37.21893;
RA Oshima H., Szapary D., Simons S.S. Jr.;
RT "The factor binding to the glucocorticoid modulatory element of the
RT tyrosine aminotransferase gene is a novel and ubiquitous heteromeric
RT complex.";
RL J. Biol. Chem. 270:21893-21901(1995).
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 -!- INTERACTION:
CC O88873; Q9Y692-2: GMEB1; Xeno; NbExp=5; IntAct=EBI-25780616, EBI-21554939;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=May be also cytoplasmic.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=O88873-1; Sequence=Displayed;
CC Name=2; Synonyms=2';
CC IsoId=O88873-2; Sequence=VSP_005971, VSP_005976, VSP_005977;
CC Name=3; Synonyms=2a;
CC IsoId=O88873-3; Sequence=VSP_005971, VSP_005974, VSP_005975;
CC Name=4; Synonyms=2b;
CC IsoId=O88873-4; Sequence=VSP_005971, VSP_005972, VSP_005973;
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DR EMBL; AF059273; AAC64001.1; -; mRNA.
DR EMBL; AF205778; AAF65537.1; -; mRNA.
DR EMBL; AF205779; AAF65538.1; -; mRNA.
DR EMBL; AF205780; AAF65539.1; -; mRNA.
DR RefSeq; NP_113991.1; NM_031803.1. [O88873-1]
DR AlphaFoldDB; O88873; -.
DR SMR; O88873; -.
DR IntAct; O88873; 1.
DR STRING; 10116.ENSRNOP00000018237; -.
DR PhosphoSitePlus; O88873; -.
DR PaxDb; O88873; -.
DR PeptideAtlas; O88873; -.
DR GeneID; 83635; -.
DR KEGG; rno:83635; -.
DR UCSC; RGD:620481; rat. [O88873-1]
DR CTD; 26205; -.
DR RGD; 620481; Gmeb2.
DR eggNOG; KOG4333; Eukaryota.
DR InParanoid; O88873; -.
DR OrthoDB; 692814at2759; -.
DR PhylomeDB; O88873; -.
DR PRO; PR:O88873; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
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:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
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; IDA:NTNU_SB.
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 Alternative splicing; Coiled coil; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc.
FT CHAIN 1..529
FT /note="Glucocorticoid modulatory element-binding protein 2"
FT /id="PRO_0000074094"
FT DOMAIN 80..162
FT /note="SAND"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00185"
FT COILED 244..347
FT /evidence="ECO:0000255"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 135
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UKD1"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UKD1"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9UKD1"
FT VAR_SEQ 62..63
FT /note="CA -> AAA (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10734202,
FT ECO:0000303|PubMed:9651376"
FT /id="VSP_005971"
FT VAR_SEQ 317..344
FT /note="ALEQQCDEHRRRAKELKHKSQHLSNVLM -> GPPRPFLAGQRRPNSPICME
FT PSILEEEV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10734202"
FT /id="VSP_005972"
FT VAR_SEQ 345..529
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10734202"
FT /id="VSP_005973"
FT VAR_SEQ 376..379
FT /note="TQSA -> QGRF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10734202"
FT /id="VSP_005974"
FT VAR_SEQ 380..529
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10734202"
FT /id="VSP_005975"
FT VAR_SEQ 471..485
FT /note="VSPLQLLTLPGLGPT -> ITALPRVYTCLSGSS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10734202,
FT ECO:0000303|PubMed:9651376"
FT /id="VSP_005976"
FT VAR_SEQ 486..529
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10734202,
FT ECO:0000303|PubMed:9651376"
FT /id="VSP_005977"
SQ SEQUENCE 529 AA; 56571 MW; 2F24B2C3D511F51E CRC64;
MATPDVSVHM EEVVVVTTPD TAVDGSGVEE VKTVLVTTNL APHGGDLTED NMETENAAAA
ACAFTASSQL KEAVLVKMAE EGENLEAEIV YPITCGDSRA NLIWRKFVCP GINVKCVQYD
EHVISPKEFV HLAGKSTLKD WKRAIRMNGI MLRKIMDSGE LDFYQHDKVC SNTCRSTKID
LSGARVSLSS PTSTEYIPLT PAAADVNGSP ATITIETCED PGDWTTTIGD DTFAFWRGLK
DAGLLDEVIQ EFQQELEETM KGLQQRVQDP PLQLRDAVLL NNIVQNFGML DLVKKVLASH
KCQMDRSREQ YARDLAALEQ QCDEHRRRAK ELKHKSQHLS NVLMTLTPVS LPSPMKRPRL
ARATSGPAAM ASQVLTQSAQ IALGPGMPMS QLTSVPLGKV VSTLPSTVLG KGSPQAAPAS
SPASPLLGGY TVLASSGSTF PSTVEIHPDT SSLTVLSTAA MQDGTTVLKV VSPLQLLTLP
GLGPTLQNVA QASPAGSTIV TMPTAAATGP EEHTATIEVA AVAEDHEQK
