CEBPG_MOUSE
ID CEBPG_MOUSE Reviewed; 150 AA.
AC P53568;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=CCAAT/enhancer-binding protein gamma;
DE Short=C/EBP gamma;
DE AltName: Full=Granulocyte colony-stimulating factor promoter element 1-binding protein;
DE Short=GPE1-BP {ECO:0000303|PubMed:1709121};
DE Short=GPE1-binding protein;
DE AltName: Full=Immunoglobulin enhancer-binding protein 1 {ECO:0000303|PubMed:2121606};
DE Short=IG/EBP-1;
GN Name=Cebpg;
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], FUNCTION, SUBUNIT, INTERACTION WITH CEBPA, AND
RP TISSUE SPECIFICITY.
RX PubMed=2121606; DOI=10.1101/gad.4.8.1404;
RA Roman C., Platero J.S., Shuman J., Calame K.;
RT "Ig/EBP-1: a ubiquitously expressed immunoglobulin enhancer binding protein
RT that is similar to C/EBP and heterodimerizes with C/EBP.";
RL Genes Dev. 4:1404-1415(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Macrophage;
RX PubMed=1709121; DOI=10.1016/0014-5793(91)80452-9;
RA Nishizawa M., Wakabayashi-Ito N., Nagata S.;
RT "Molecular cloning of cDNA and a chromosomal gene encoding GPE1-BP, a
RT nuclear protein which binds to granulocyte colony-stimulating factor
RT promoter element 1.";
RL FEBS Lett. 282:95-97(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [5]
RP FUNCTION, AND INTERACTION WITH ZNF638.
RX PubMed=21602272; DOI=10.1074/jbc.m110.212506;
RA Meruvu S., Hugendubler L., Mueller E.;
RT "Regulation of adipocyte differentiation by the zinc finger protein
RT ZNF638.";
RL J. Biol. Chem. 286:26516-26523(2011).
CC -!- FUNCTION: Transcription factor that binds to the promoter and the
CC enhancer regions of target genes (PubMed:21602272). Binds to the
CC promoter and the enhancer of the immunoglobulin heavy chain
CC (PubMed:2121606). Binds to GPE1, a cis-acting element in the G-CSF gene
CC promoter (PubMed:1709121). Binds to the enhancer element PRE-I
CC (positive regulatory element-I) of the IL-4 gene (By similarity). Binds
CC to the promoter and the enhancer of the alpha-1-fetoprotein gene (By
CC similarity). {ECO:0000250|UniProtKB:P26801,
CC ECO:0000250|UniProtKB:P53567, ECO:0000269|PubMed:1709121,
CC ECO:0000269|PubMed:2121606, ECO:0000269|PubMed:21602272}.
CC -!- SUBUNIT: Binds DNA as a dimer and can form stable heterodimers with
CC CEBPA (PubMed:2121606). Can form stable heterodimers with CEBPB (By
CC similarity). Interacts with ZNF638; this interaction increases
CC transcriptional activation (PubMed:21602272).
CC {ECO:0000250|UniProtKB:P26801, ECO:0000269|PubMed:21602272}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1709121,
CC ECO:0000305|PubMed:2121606}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:1709121,
CC ECO:0000269|PubMed:2121606}.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA39116.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X55499; CAA39116.1; ALT_INIT; mRNA.
DR EMBL; BC011319; AAH11319.1; -; mRNA.
DR CCDS; CCDS21144.1; -.
DR PIR; A36673; A36673.
DR RefSeq; NP_034014.1; NM_009884.3.
DR AlphaFoldDB; P53568; -.
DR SMR; P53568; -.
DR BioGRID; 198671; 4.
DR IntAct; P53568; 2.
DR STRING; 10090.ENSMUSP00000118588; -.
DR iPTMnet; P53568; -.
DR PhosphoSitePlus; P53568; -.
DR EPD; P53568; -.
DR PaxDb; P53568; -.
DR PeptideAtlas; P53568; -.
DR PRIDE; P53568; -.
DR ProteomicsDB; 279996; -.
DR Antibodypedia; 1652; 379 antibodies from 35 providers.
DR DNASU; 12611; -.
DR Ensembl; ENSMUST00000070191; ENSMUSP00000064963; ENSMUSG00000056216.
DR Ensembl; ENSMUST00000130491; ENSMUSP00000118588; ENSMUSG00000056216.
DR GeneID; 12611; -.
DR KEGG; mmu:12611; -.
DR UCSC; uc009gjk.1; mouse.
DR CTD; 1054; -.
DR MGI; MGI:104982; Cebpg.
DR VEuPathDB; HostDB:ENSMUSG00000056216; -.
DR eggNOG; KOG3119; Eukaryota.
DR GeneTree; ENSGT00940000160676; -.
DR HOGENOM; CLU_146813_0_0_1; -.
DR InParanoid; P53568; -.
DR OMA; HAHNFAD; -.
DR OrthoDB; 1008736at2759; -.
DR PhylomeDB; P53568; -.
DR TreeFam; TF105009; -.
DR BioGRID-ORCS; 12611; 5 hits in 111 CRISPR screens.
DR ChiTaRS; Cebpg; mouse.
DR PRO; PR:P53568; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P53568; protein.
DR Bgee; ENSMUSG00000056216; Expressed in olfactory epithelium and 251 other tissues.
DR ExpressionAtlas; P53568; baseline and differential.
DR Genevisible; P53568; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0044377; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding, bending; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0030183; P:B cell differentiation; IEP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; TAS:UniProtKB.
DR GO; GO:0043353; P:enucleate erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0006955; P:immune response; IDA:UniProtKB.
DR GO; GO:0001889; P:liver development; ISS:UniProtKB.
DR GO; GO:0016071; P:mRNA metabolic process; IMP:MGI.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IMP:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0006337; P:nucleosome disassembly; TAS:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISS:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR Pfam; PF07716; bZIP_2; 1.
DR SMART; SM00338; BRLZ; 1.
DR SUPFAM; SSF57959; SSF57959; 1.
DR PROSITE; PS50217; BZIP; 1.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Isopeptide bond; Nucleus; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..150
FT /note="CCAAT/enhancer-binding protein gamma"
FT /id="PRO_0000076629"
FT DOMAIN 62..125
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 27..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..93
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 97..118
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 129..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..94
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 3
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P53567"
SQ SEQUENCE 150 AA; 16400 MW; 697602DA2BD3F8B6 CRC64;
MSKLSQPATT PGVNGISVIH TQAHASGLQQ VPQLVPAGPG GGGKAVPPSK QSKKSSPMDR
NSDEYRQRRE RNNMAVKKSR LKSKQKAQDT LQRVNQLKEE NERLEAKIKL LTKELSVLKD
LFLEHAHSLA DNVQPISTET TATNSDNPGQ
