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Q00322

- CEBPD_MOUSE

UniProt

Q00322 - CEBPD_MOUSE

Protein

CCAAT/enhancer-binding protein delta

Gene

Cebpd

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 2 (13 Nov 2007)
      Previous versions | rss
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    Functioni

    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.By similarity

    GO - Molecular functioni

    1. DNA binding Source: MGI
    2. protein binding Source: UniProtKB
    3. protein heterodimerization activity Source: UniProtKB
    4. protein homodimerization activity Source: MGI
    5. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
    6. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: NTNU_SB
    7. transcription regulatory region DNA binding Source: MGI

    GO - Biological processi

    1. fat cell differentiation Source: MGI
    2. hematopoietic progenitor cell differentiation Source: MGI
    3. inner ear development Source: MGI
    4. negative regulation of transcription, DNA-templated Source: MGI
    5. positive regulation of osteoblast differentiation Source: MGI
    6. positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
    7. regulation of transcription from RNA polymerase II promoter Source: MGI

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_27166. 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 3
    Gene namesi
    Name:Cebpd
    Synonyms:Crp3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:103573. Cebpd.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy 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

    PRIDEiQ00322.

    PTM databases

    PhosphoSiteiQ00322.

    Expressioni

    Gene expression databases

    CleanExiMM_CEBPD.
    GenevestigatoriQ00322.

    Interactioni

    Subunit structurei

    Binds DNA as a dimer and can form stable heterodimers with C/EBP alpha. Interacts with SPI1/PU.1. Interacts with PRDM16.2 Publications

    Protein-protein interaction databases

    BioGridi198670. 6 interactions.
    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.
    KOiK10050.
    PhylomeDBiQ00322.

    Family and domain databases

    InterProiIPR004827. bZIP.
    IPR016468. CCAAT/enhancer-binding.
    [Graphical view]
    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

    MSAALFSLDS PVRGTPWPTE PAAFYEPGRV DKPGRGPEPG DLGELGSTTP    50
    AMYDDESAID FSAYIDSMAA VPTLELCHDE LFADLFNSNH KAAGAGGLEL 100
    LQGGPTRPPG VGSVARGPLK REPDWGDGDA PGSLLPAQVA VCAQTVVSLA 150
    AAAQPTPPTS PEPPRGSPGP SLAPGTVREK GAGKRGPDRG SPEYRQRRER 200
    NNIAVRKSRD KAKRRNQEMQ QKLVELSAEN EKLHQRVEQL TRDLAGLRQF 250
    FKKLPSPPFL PPTGADCR 268
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X61800 mRNA. Translation: CAA43905.1 .
    M85144 Genomic DNA. No translation available.
    AK053190 mRNA. Translation: BAC35305.1 .
    AK151958 mRNA. Translation: BAE30830.1 .
    PIRi B37279.
    RefSeqi NP_031705.3. NM_007679.4.
    UniGenei Mm.347407.

    3D structure databases

    ProteinModelPortali Q00322.
    SMRi Q00322. Positions 191-248.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198670. 6 interactions.
    MINTi MINT-1520790.

    PTM databases

    PhosphoSitei Q00322.

    Proteomic databases

    PRIDEi Q00322.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 12609.
    KEGGi mmu:12609.
    UCSCi uc007yhx.1. mouse.

    Organism-specific databases

    CTDi 1052.
    MGIi MGI:103573. Cebpd.

    Phylogenomic databases

    HOVERGENi HBG050879.
    KOi K10050.
    PhylomeDBi Q00322.

    Enzyme and pathway databases

    Reactomei REACT_27166. Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.

    Miscellaneous databases

    NextBioi 281762.
    PROi Q00322.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_CEBPD.
    Genevestigatori Q00322.

    Family and domain databases

    InterProi IPR004827. bZIP.
    IPR016468. CCAAT/enhancer-binding.
    [Graphical view ]
    Pfami PF07716. bZIP_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005879. CCAAT/enhancer-binding. 1 hit.
    SMARTi SM00338. BRLZ. 1 hit.
    [Graphical view ]
    PROSITEi PS50217. BZIP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    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: October 1, 2014
    This is version 107 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

    External Data

    Dasty 3