CEBPE_MOUSE
ID CEBPE_MOUSE Reviewed; 281 AA.
AC Q6PZD9; Q32MW9;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=CCAAT/enhancer-binding protein epsilon;
DE Short=C/EBP epsilon;
GN Name=Cebpe; Synonyms=Gm294;
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 STRAIN=C57BL/6J; TISSUE=Spleen;
RA Zhuang D., Zhang P., Dong F.;
RT "Characterization of the macrophage differentiation induced by mutated G-
RT CSF receptors.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, AND IDENTIFICATION BY
RP 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: Transcriptional activator. C/EBP are DNA-binding proteins
CC that recognize two different motifs: the CCAAT homology common to many
CC promoters and the enhanced core homology common to many enhancers.
CC Required for the promyelocyte-myelocyte transition in myeloid
CC differentiation. {ECO:0000250|UniProtKB:Q15744}.
CC -!- SUBUNIT: Binds DNA as a homodimer and as a heterodimer. Can form stable
CC heterodimers with CEBPA, CEBPB and CEBPD (By similarity). Interacts
CC with GATA1 AND SPI1 (By similarity). Interacts with SMARCD2 (By
CC similarity). {ECO:0000250|UniProtKB:P56261,
CC ECO:0000250|UniProtKB:Q15744}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
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DR EMBL; AY570294; AAS78198.1; -; mRNA.
DR EMBL; BC108953; AAI08954.1; -; mRNA.
DR CCDS; CCDS27100.1; -.
DR RefSeq; NP_997014.1; NM_207131.1.
DR AlphaFoldDB; Q6PZD9; -.
DR SMR; Q6PZD9; -.
DR BioGRID; 225912; 1.
DR STRING; 10090.ENSMUSP00000068927; -.
DR iPTMnet; Q6PZD9; -.
DR PhosphoSitePlus; Q6PZD9; -.
DR MaxQB; Q6PZD9; -.
DR PaxDb; Q6PZD9; -.
DR PRIDE; Q6PZD9; -.
DR ProteomicsDB; 281526; -.
DR Antibodypedia; 150; 392 antibodies from 31 providers.
DR DNASU; 110794; -.
DR Ensembl; ENSMUST00000064290; ENSMUSP00000068927; ENSMUSG00000052435.
DR GeneID; 110794; -.
DR KEGG; mmu:110794; -.
DR UCSC; uc007twz.1; mouse.
DR CTD; 1053; -.
DR MGI; MGI:103572; Cebpe.
DR VEuPathDB; HostDB:ENSMUSG00000052435; -.
DR eggNOG; KOG3119; Eukaryota.
DR GeneTree; ENSGT00940000161681; -.
DR HOGENOM; CLU_043327_0_0_1; -.
DR InParanoid; Q6PZD9; -.
DR OMA; CDHEASI; -.
DR OrthoDB; 1284308at2759; -.
DR PhylomeDB; Q6PZD9; -.
DR TreeFam; TF105008; -.
DR BioGRID-ORCS; 110794; 0 hits in 73 CRISPR screens.
DR PRO; PR:Q6PZD9; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q6PZD9; protein.
DR Bgee; ENSMUSG00000052435; Expressed in granulocyte and 12 other tissues.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
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:0042802; F:identical protein 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; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
DR GO; GO:0030851; P:granulocyte differentiation; ISO:MGI.
DR GO; GO:0030225; P:macrophage differentiation; IMP:MGI.
DR GO; GO:0030099; P:myeloid cell differentiation; IBA:GO_Central.
DR GO; GO:0006909; P:phagocytosis; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
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; IBA:GO_Central.
DR InterPro; IPR004827; bZIP.
DR InterPro; IPR046347; bZIP_sf.
DR InterPro; IPR016468; C/EBP_chordates.
DR Pfam; PF07716; bZIP_2; 1.
DR PIRSF; PIRSF005879; CCAAT/enhancer-binding; 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; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..281
FT /note="CCAAT/enhancer-binding protein epsilon"
FT /id="PRO_0000076625"
FT DOMAIN 204..267
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 208..245
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 246..267
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15744"
SQ SEQUENCE 281 AA; 30617 MW; 864F3FABA54E939A CRC64;
MSHGTYYECE PRGGQQPLEF SGGRAGPGEL GDMCEHEASI DLSAYIESGE EQLLSDLFAM
KPTPEARSLK GPGAPSFPHY LPADPRPFAY PSHTFGPDRK ALGPGIYSNP GSYDPRAVAV
KEEPRGPEGN RGTSRGSYNP LQYQVAHCGQ TAVHLPPTLA APGQPLRVLK APVAAAAPPC
SPLLKAPSPA GPSHKGKKAV NKDSLEYRLR RERNNIAVRK SRDKAKRRIM ETQQKVLEYM
AENERLRNRV DQLTQELDTL RNLFRQIPEA ASLIKGVGGC S
