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Q00322 (CEBPD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
CCAAT/enhancer-binding protein delta

Short name=C/EBP delta
Alternative name(s):
C/EBP-related protein 3
Gene names
Name:Cebpd
Synonyms:Crp3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length268 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

C/EBP is a DNA-binding protein that recognizes two different motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers. Important transcriptional activator in the regulation of genes involved in immune and inflammatory responses, may play an important role in the regulation of the several genes associated with activation and/or differentiation of macrophages By similarity.

Subunit structure

Binds DNA as a dimer and can form stable heterodimers with C/EBP alpha. Interacts with SPI1/PU.1. Interacts with PRDM16. Ref.4 Ref.5

Subcellular location

Nucleus.

Sequence similarities

Belongs to the bZIP family. C/EBP subfamily.

Contains 1 bZIP (basic-leucine zipper) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfat cell differentiation

Inferred from direct assay PubMed 17888405. Source: MGI

hematopoietic progenitor cell differentiation

Inferred from genetic interaction PubMed 24029230. Source: MGI

inner ear development

Inferred from direct assay PubMed 21795542. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15175325. Source: MGI

positive regulation of osteoblast differentiation

Inferred from direct assay PubMed 15175325. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 18632661. Source: MGI

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 18632661. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 11940593PubMed 12821655. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 12821655. Source: MGI

protein binding

Inferred from physical interaction PubMed 12177065Ref.5. Source: UniProtKB

protein heterodimerization activity

Inferred from direct assay PubMed 12177065. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay PubMed 12821655. Source: MGI

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

transcription regulatory region DNA binding

Inferred from direct assay PubMed 18632661. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 268267CCAAT/enhancer-binding protein delta
PRO_0000076622

Regions

Domain191 – 25464bZIP
Region195 – 22228Basic motif By similarity
Region226 – 25429Leucine-zipper By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Cross-link120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Experimental info

Sequence conflict411D → E in CAA43905. Ref.1
Sequence conflict255 – 2584PSPP → AQPA in BAC35305. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q00322 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: 151F765946CDB275

FASTA26828,631
        10         20         30         40         50         60 
MSAALFSLDS PVRGTPWPTE PAAFYEPGRV DKPGRGPEPG DLGELGSTTP AMYDDESAID 

        70         80         90        100        110        120 
FSAYIDSMAA VPTLELCHDE LFADLFNSNH KAAGAGGLEL LQGGPTRPPG VGSVARGPLK 

       130        140        150        160        170        180 
REPDWGDGDA PGSLLPAQVA VCAQTVVSLA AAAQPTPPTS PEPPRGSPGP SLAPGTVREK 

       190        200        210        220        230        240 
GAGKRGPDRG SPEYRQRRER NNIAVRKSRD KAKRRNQEMQ QKLVELSAEN EKLHQRVEQL 

       250        260 
TRDLAGLRQF FKKLPSPPFL PPTGADCR 

« Hide

References

« Hide 'large scale' references
[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].
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. expand/collapse author list , 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.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61800 mRNA. Translation: CAA43905.1.
M85144 Genomic DNA. No translation available.
AK053190 mRNA. Translation: BAC35305.1.
AK151958 mRNA. Translation: BAE30830.1.
PIRB37279.
RefSeqNP_031705.3. NM_007679.4.
UniGeneMm.347407.

3D structure databases

ProteinModelPortalQ00322.
SMRQ00322. Positions 191-248.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198670. 6 interactions.
MINTMINT-1520790.

PTM databases

PhosphoSiteQ00322.

Proteomic databases

PRIDEQ00322.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID12609.
KEGGmmu:12609.
UCSCuc007yhx.1. mouse.

Organism-specific databases

CTD1052.
MGIMGI:103573. Cebpd.

Phylogenomic databases

HOVERGENHBG050879.
KOK10050.
PhylomeDBQ00322.

Enzyme and pathway databases

ReactomeREACT_188576. Developmental Biology.
REACT_200794. Mus musculus biological processes.

Gene expression databases

CleanExMM_CEBPD.
GenevestigatorQ00322.

Family and domain databases

InterProIPR004827. bZIP.
IPR016468. CCAAT/enhancer-binding.
[Graphical view]
PfamPF07716. bZIP_2. 1 hit.
[Graphical view]
PIRSFPIRSF005879. CCAAT/enhancer-binding. 1 hit.
SMARTSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEPS50217. BZIP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio281762.
PROQ00322.
SOURCESearch...

Entry information

Entry nameCEBPD_MOUSE
AccessionPrimary (citable) accession number: Q00322
Secondary accession number(s): Q3U937, Q8BW92
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: November 13, 2007
Last modified: July 9, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot