CEBPD_HUMAN
ID CEBPD_HUMAN Reviewed; 269 AA.
AC P49716; Q14937; Q2M2X9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=CCAAT/enhancer-binding protein delta;
DE Short=C/EBP delta;
DE AltName: Full=Nuclear factor NF-IL6-beta {ECO:0000303|PubMed:1741402};
DE Short=NF-IL6-beta {ECO:0000303|PubMed:1741402};
GN Name=CEBPD;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, AND INTERACTION WITH CEBPB.
RC TISSUE=Placenta;
RX PubMed=1741402; DOI=10.1073/pnas.89.4.1473;
RA Kinoshita S., Akira S., Kishimoto T.;
RT "A member of the C/EBP family, NF-IL6 beta, forms a heterodimer and
RT transcriptionally synergizes with NF-IL6.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:1473-1476(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8314590; DOI=10.1006/geno.1993.1220;
RA Cleutjens C.B., van Eekelen C.C., van Dekken H., Smit E.M., Hagemeijer A.,
RA Wagner M.J., Wells D.E., Trapman J.;
RT "The human C/EBP delta (CRP3/CELF) gene: structure and chromosomal
RT localization.";
RL Genomics 16:520-523(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, SUMOYLATION AT LYS-120, AND MUTAGENESIS OF
RP LYS-120.
RX PubMed=16397300; DOI=10.1093/nar/gkj422;
RA Wang J.-M., Ko C.-Y., Chen L.-C., Wang W.-L., Chang W.-C.;
RT "Functional role of NF-IL6beta and its sumoylation and acetylation
RT modifications in promoter activation of cyclooxygenase 2 gene.";
RL Nucleic Acids Res. 34:217-231(2006).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Transcription activator that recognizes two different DNA
CC motifs: the CCAAT homology common to many promoters and the enhanced
CC core homology common to many enhancers (PubMed:16397300). Important
CC transcription factor regulating the expression of genes involved in
CC immune and inflammatory responses (PubMed:1741402, PubMed:16397300).
CC Transcriptional activator that enhances IL6 transcription alone and as
CC heterodimer with CEBPB (PubMed:1741402). {ECO:0000269|PubMed:1741402}.
CC -!- SUBUNIT: Binds DNA as a homodimer and as a heterodimer
CC (PubMed:1741402). Can form stable heterodimers with CEBPB
CC (PubMed:1741402). Can form stable heterodimers with CEBPA and CEBPE.
CC Interacts with SPI1/PU.1. Interacts with PRDM16.
CC {ECO:0000250|UniProtKB:Q00322, ECO:0000269|PubMed:1741402}.
CC -!- INTERACTION:
CC P49716; P18848: ATF4; NbExp=2; IntAct=EBI-7962058, EBI-492498;
CC P49716; P49715: CEBPA; NbExp=2; IntAct=EBI-7962058, EBI-1172054;
CC P49716; P53567: CEBPG; NbExp=2; IntAct=EBI-7962058, EBI-740209;
CC P49716; P35638: DDIT3; NbExp=2; IntAct=EBI-7962058, EBI-742651;
CC P49716; Q9BXW9: FANCD2; NbExp=8; IntAct=EBI-7962058, EBI-359343;
CC P49716; Q8TEX9: IPO4; NbExp=5; IntAct=EBI-7962058, EBI-395967;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:16397300}.
CC -!- SIMILARITY: Belongs to the bZIP family. C/EBP subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M83667; AAA59927.1; -; mRNA.
DR EMBL; S63168; AAB27293.1; -; Genomic_DNA.
DR EMBL; CH471068; EAW86679.1; -; Genomic_DNA.
DR EMBL; BC105109; AAI05110.1; -; mRNA.
DR CCDS; CCDS6142.1; -.
DR PIR; A47008; A47008.
DR RefSeq; NP_005186.2; NM_005195.3.
DR AlphaFoldDB; P49716; -.
DR SMR; P49716; -.
DR BioGRID; 107481; 46.
DR ComplexPortal; CPX-617; bZIP transcription factor complex, CEBPD-CEBPD.
DR ComplexPortal; CPX-6528; bZIP transcription factor complex, ATF4-CEBPD.
DR ComplexPortal; CPX-7009; bZIP transcription factor complex, BATF-CEBPD.
DR ComplexPortal; CPX-7098; bZIP transcription factor complex, BATF3-CEBPD.
DR DIP; DIP-146N; -.
DR ELM; P49716; -.
DR IntAct; P49716; 26.
DR MINT; P49716; -.
DR STRING; 9606.ENSP00000386165; -.
DR iPTMnet; P49716; -.
DR PhosphoSitePlus; P49716; -.
DR BioMuta; CEBPD; -.
DR DMDM; 160332350; -.
DR EPD; P49716; -.
DR jPOST; P49716; -.
DR MassIVE; P49716; -.
DR MaxQB; P49716; -.
DR PaxDb; P49716; -.
DR PeptideAtlas; P49716; -.
DR PRIDE; P49716; -.
DR ProteomicsDB; 56055; -.
DR Antibodypedia; 24255; 266 antibodies from 29 providers.
DR DNASU; 1052; -.
DR Ensembl; ENST00000408965.4; ENSP00000386165.3; ENSG00000221869.5.
DR GeneID; 1052; -.
DR KEGG; hsa:1052; -.
DR MANE-Select; ENST00000408965.4; ENSP00000386165.3; NM_005195.4; NP_005186.2.
DR UCSC; uc003xqh.2; human.
DR CTD; 1052; -.
DR DisGeNET; 1052; -.
DR GeneCards; CEBPD; -.
DR HGNC; HGNC:1835; CEBPD.
DR HPA; ENSG00000221869; Low tissue specificity.
DR MIM; 116898; gene.
DR neXtProt; NX_P49716; -.
DR OpenTargets; ENSG00000221869; -.
DR PharmGKB; PA26378; -.
DR VEuPathDB; HostDB:ENSG00000221869; -.
DR eggNOG; KOG3119; Eukaryota.
DR GeneTree; ENSGT00940000163032; -.
DR HOGENOM; CLU_043327_2_1_1; -.
DR InParanoid; P49716; -.
DR OMA; QIATCAQ; -.
DR OrthoDB; 1284308at2759; -.
DR PhylomeDB; P49716; -.
DR TreeFam; TF105008; -.
DR PathwayCommons; P49716; -.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR SignaLink; P49716; -.
DR SIGNOR; P49716; -.
DR BioGRID-ORCS; 1052; 23 hits in 1104 CRISPR screens.
DR ChiTaRS; CEBPD; human.
DR GeneWiki; CEBPD; -.
DR GenomeRNAi; 1052; -.
DR Pharos; P49716; Tbio.
DR PRO; PR:P49716; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; P49716; protein.
DR Bgee; ENSG00000221869; Expressed in pericardium and 207 other tissues.
DR Genevisible; P49716; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IPI:ComplexPortal.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0045444; P:fat cell differentiation; IEA:Ensembl.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0048839; P:inner ear development; IEA:Ensembl.
DR GO; GO:0140467; P:integrated stress response signaling; IC:ComplexPortal.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
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 Acetylation; Activator; DNA-binding; Isopeptide bond; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..269
FT /note="CCAAT/enhancer-binding protein delta"
FT /id="PRO_0000076621"
FT DOMAIN 191..254
FT /note="bZIP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..222
FT /note="Basic motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT REGION 226..254
FT /note="Leucine-zipper"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00978"
FT COMPBIAS 156..171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:16397300"
FT VARIANT 248
FT /note="R -> W (in dbSNP:rs34948549)"
FT /id="VAR_037087"
FT MUTAGEN 120
FT /note="K->A: Loss of sumoylation."
FT /evidence="ECO:0000269|PubMed:16397300"
FT CONFLICT 2
FT /note="S -> T (in Ref. 1; AAA59927)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="R -> G (in Ref. 1; AAA59927)"
FT /evidence="ECO:0000305"
FT CONFLICT 140..141
FT /note="AA -> GP (in Ref. 1; AAA59927 and 2; AAB27293)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 28467 MW; AFDE9E2244BDF84A CRC64;
MSAALFSLDG PARGAPWPAE PAPFYEPGRA GKPGRGAEPG ALGEPGAAAP AMYDDESAID
FSAYIDSMAA VPTLELCHDE LFADLFNSNH KAGGAGPLEL LPGGPARPLG PGPAAPRLLK
REPDWGDGDA PGSLLPAQVA ACAQTVVSLA AAGQPTPPTS PEPPRSSPRQ TPAPGPAREK
SAGKRGPDRG SPEYRQRRER NNIAVRKSRD KAKRRNQEMQ QKLVELSAEN EKLHQRVEQL
TRDLAGLRQF FKQLPSPPFL PAAGTADCR
