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   27-MAR-2024, entry version 175.
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; 6.
DR   IntAct; P53568; 2.
DR   STRING; 10090.ENSMUSP00000118588; -.
DR   iPTMnet; P53568; -.
DR   PhosphoSitePlus; P53568; -.
DR   EPD; P53568; -.
DR   PaxDb; 10090-ENSMUSP00000118588; -.
DR   PeptideAtlas; P53568; -.
DR   ProteomicsDB; 279996; -.
DR   Pumba; P53568; -.
DR   Antibodypedia; 1652; 400 antibodies from 35 providers.
DR   DNASU; 12611; -.
DR   Ensembl; ENSMUST00000070191.10; ENSMUSP00000064963.9; ENSMUSG00000056216.10.
DR   Ensembl; ENSMUST00000130491.3; ENSMUSP00000118588.2; ENSMUSG00000056216.10.
DR   GeneID; 12611; -.
DR   KEGG; mmu:12611; -.
DR   UCSC; uc009gjk.1; mouse.
DR   AGR; MGI:104982; -.
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; 2966182at2759; -.
DR   PhylomeDB; P53568; -.
DR   TreeFam; TF105009; -.
DR   BioGRID-ORCS; 12611; 5 hits in 116 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 254 other cell types or tissues.
DR   ExpressionAtlas; P53568; baseline and differential.
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:0006351; P:DNA-templated transcription; IEA:InterPro.
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:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0032729; P:positive regulation of type II interferon production; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR   CDD; cd14713; bZIP_CEBPG; 1.
DR   Gene3D; 1.20.5.170; -; 1.
DR   InterPro; IPR004827; bZIP.
DR   InterPro; IPR046347; bZIP_sf.
DR   InterPro; IPR031106; C/EBP.
DR   PANTHER; PTHR23334; CCAAT/ENHANCER BINDING PROTEIN; 1.
DR   PANTHER; PTHR23334:SF69; CCAAT_ENHANCER-BINDING PROTEIN GAMMA; 1.
DR   Pfam; PF07716; bZIP_2; 1.
DR   SMART; SM00338; BRLZ; 1.
DR   SUPFAM; SSF57959; Leucine zipper domain; 1.
DR   PROSITE; PS50217; BZIP; 1.
DR   Genevisible; P53568; MM.
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
//