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Protein

CCAAT/enhancer-binding protein delta

Gene

Cebpd

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription activator that recognizes two different DNA motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers (PubMed:7594592, PubMed:19641492). Important transcription factor regulating the expression of genes involved in immune and inflammatory responses. Transcriptional activator that enhances IL6 transcription alone and as heterodimer with CEBPB (By similarity).By similarity2 Publications

GO - Molecular functioni

  • DNA binding Source: MGI
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: MGI
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB
  • transcription regulatory region DNA binding Source: MGI

GO - Biological processi

  • fat cell differentiation Source: MGI
  • hematopoietic progenitor cell differentiation Source: MGI
  • inner ear development Source: MGI
  • negative regulation of transcription, DNA-templated Source: MGI
  • positive regulation of osteoblast differentiation Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  • regulation of transcription from RNA polymerase II promoter Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-381340. Transcriptional regulation of white adipocyte differentiation.
R-MMU-442533. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Names & Taxonomyi

Protein namesi
Recommended name:
CCAAT/enhancer-binding protein delta
Short name:
C/EBP delta
Alternative name(s):
C/EBP-related protein 31 Publication
Gene namesi
Name:Cebpd
Synonyms:Crp31 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:103573. Cebpd.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • nucleoplasm Source: Reactome
  • nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 268267CCAAT/enhancer-binding protein deltaPRO_0000076622Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Cross-linki120 – 120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ00322.
PRIDEiQ00322.

PTM databases

iPTMnetiQ00322.
PhosphoSiteiQ00322.

Expressioni

Gene expression databases

CleanExiMM_CEBPD.

Interactioni

Subunit structurei

Binds DNA as a homodimer and as a heterodimer. Can form stable heterodimers with CEBPA, CEBPB and CEBPE (PubMed:1884998). Interacts with SPI1/PU.1 (PubMed:7594592). Interacts with PRDM16 (PubMed:19641492).3 Publications

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: MGI

Protein-protein interaction databases

BioGridi198670. 6 interactions.
DIPiDIP-41645N.
MINTiMINT-1520790.

Structurei

3D structure databases

ProteinModelPortaliQ00322.
SMRiQ00322. Positions 191-248.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini191 – 25464bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni195 – 22228Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni226 – 25429Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the bZIP family. C/EBP subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG050879.
InParanoidiQ00322.
KOiK10050.
PhylomeDBiQ00322.

Family and domain databases

InterProiIPR004827. bZIP.
IPR031106. C/EBP.
IPR016468. C/EBP_chordates.
[Graphical view]
PANTHERiPTHR23334. PTHR23334. 1 hit.
PfamiPF07716. bZIP_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005879. CCAAT/enhancer-binding. 1 hit.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00322-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAALFSLDS PVRGTPWPTE PAAFYEPGRV DKPGRGPEPG DLGELGSTTP
60 70 80 90 100
AMYDDESAID FSAYIDSMAA VPTLELCHDE LFADLFNSNH KAAGAGGLEL
110 120 130 140 150
LQGGPTRPPG VGSVARGPLK REPDWGDGDA PGSLLPAQVA VCAQTVVSLA
160 170 180 190 200
AAAQPTPPTS PEPPRGSPGP SLAPGTVREK GAGKRGPDRG SPEYRQRRER
210 220 230 240 250
NNIAVRKSRD KAKRRNQEMQ QKLVELSAEN EKLHQRVEQL TRDLAGLRQF
260
FKKLPSPPFL PPTGADCR
Length:268
Mass (Da):28,631
Last modified:November 13, 2007 - v2
Checksum:i151F765946CDB275
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti41 – 411D → E in CAA43905 (PubMed:1840554).Curated
Sequence conflicti255 – 2584PSPP → AQPA in BAC35305 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61800 mRNA. Translation: CAA43905.1.
M85144 Genomic DNA. No translation available.
AK053190 mRNA. Translation: BAC35305.1.
AK151958 mRNA. Translation: BAE30830.1.
PIRiB37279.
RefSeqiNP_031705.3. NM_007679.4.
UniGeneiMm.347407.

Genome annotation databases

GeneIDi12609.
KEGGimmu:12609.
UCSCiuc007yhx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61800 mRNA. Translation: CAA43905.1.
M85144 Genomic DNA. No translation available.
AK053190 mRNA. Translation: BAC35305.1.
AK151958 mRNA. Translation: BAE30830.1.
PIRiB37279.
RefSeqiNP_031705.3. NM_007679.4.
UniGeneiMm.347407.

3D structure databases

ProteinModelPortaliQ00322.
SMRiQ00322. Positions 191-248.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198670. 6 interactions.
DIPiDIP-41645N.
MINTiMINT-1520790.

PTM databases

iPTMnetiQ00322.
PhosphoSiteiQ00322.

Proteomic databases

MaxQBiQ00322.
PRIDEiQ00322.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi12609.
KEGGimmu:12609.
UCSCiuc007yhx.1. mouse.

Organism-specific databases

CTDi1052.
MGIiMGI:103573. Cebpd.

Phylogenomic databases

HOVERGENiHBG050879.
InParanoidiQ00322.
KOiK10050.
PhylomeDBiQ00322.

Enzyme and pathway databases

ReactomeiR-MMU-381340. Transcriptional regulation of white adipocyte differentiation.
R-MMU-442533. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

Miscellaneous databases

PROiQ00322.
SOURCEiSearch...

Gene expression databases

CleanExiMM_CEBPD.

Family and domain databases

InterProiIPR004827. bZIP.
IPR031106. C/EBP.
IPR016468. C/EBP_chordates.
[Graphical view]
PANTHERiPTHR23334. PTHR23334. 1 hit.
PfamiPF07716. bZIP_2. 1 hit.
[Graphical view]
PIRSFiPIRSF005879. CCAAT/enhancer-binding. 1 hit.
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Regulated expression of three C/EBP isoforms during adipose conversion of 3T3-L1 cells."
    Cao Z., Umek R.M., McKnight S.L.
    Genes Dev. 5:1538-1552(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "A family of C/EBP-related proteins capable of forming covalently linked leucine zipper dimers in vitro."
    Williams S.C., Cantwell C.A., Johnson P.F.
    Genes Dev. 5:1553-1567(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT.
    Tissue: Adipose tissue and Lung.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow and Lung.
  4. "Multiple proteins physically interact with PU.1. Transcriptional synergy with NF-IL6 beta (C/EBP delta, CRP3)."
    Nagulapalli S., Pongubala J.M., Atchison M.L.
    J. Immunol. 155:4330-4338(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SPI1, FUNCTION, SUBCELLULAR LOCATION.
  5. "Initiation of myoblast to brown fat switch by a PRDM16-C/EBP-beta transcriptional complex."
    Kajimura S., Seale P., Kubota K., Lunsford E., Frangioni J.V., Gygi S.P., Spiegelman B.M.
    Nature 460:1154-1158(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRDM16.

Entry informationi

Entry nameiCEBPD_MOUSE
AccessioniPrimary (citable) accession number: Q00322
Secondary accession number(s): Q3U937, Q8BW92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 13, 2007
Last modified: July 6, 2016
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.