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Protein

CCAAT/enhancer-binding protein alpha

Gene

Cebpa

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription factor that coordinates proliferation arrest and the differentiation of myeloid progenitors, adipocytes, hepatocytes, and cells of the lung and the placenta (PubMed:8367486, PubMed:11672531, PubMed:16735515, PubMed:20176812). Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes. During early embryogenesis, plays essential and redundant functions with CEBPB (By similarity). Essential for the transition from common myeloid progenitors (CMP) to granulocyte/monocyte progenitors (GMP) (PubMed:11672531). Critical for the proper development of the liver and the lung (By similarity). Necessary for terminal adipocyte differentiation, is required for postnatal maintenance of systemic energy homeostasis and lipid storage (PubMed:11672531). To regulate these different processes at the proper moment and tissue, interplays with other transcription factors and modulators. Downregulates the expression of genes that maintain cells in an undifferentiated and proliferative state through E2F1 repression, which is critical for its ability to induce adipocyte and granulocyte terminal differentiation. Reciprocally E2F1 blocks adipocyte differentiation by binding to specific promoters and repressing CEBPA binding to its target gene promoters (PubMed:11672531). Proliferation arrest also depends on a functional binding to SWI/SNF complex (By similarity). In liver, regulates gluconeogenesis and lipogenesis through different mechanisms. To regulate gluconeogenesis, functionally cooperates with FOXO1 binding to IRE-controlled promoters and regulating the expression of target genes such as PCK1 or G6PC. To modulate lipogenesis, interacts and transcriptionally synergizes with SREBF1 in promoter activation of specific lipogenic target genes such as ACAS2. In adipose tissue, seems to act as FOXO1 coactivator accessing to ADIPOQ promoter through FOXO1 binding sites (By similarity).By similarity4 Publications
Isoform 3: Can act as dominant-negative. Binds DNA and have transctivation activity, even if much less efficiently than isoform 2. Does not inhibit cell proliferation.By similarity1 Publication
Isoform 4: Directly and specifically enhances ribosomal DNA transcription interacting with RNA polymerase I-specific cofactors and inducing histone acetylation.By similarity

GO - Molecular functioni

  • DNA binding Source: UniProtKB
  • histone deacetylase binding Source: RGD
  • HMG box domain binding Source: UniProtKB
  • protein complex binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: NTNU_SB
  • RNA polymerase I regulatory region DNA binding Source: UniProtKB
  • sequence-specific DNA binding Source: UniProtKB
  • transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding Source: NTNU_SB
  • transcription coactivator activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • acute-phase response Source: RGD
  • cell differentiation Source: RGD
  • cellular response to drug Source: RGD
  • fat cell differentiation Source: UniProtKB
  • glucose homeostasis Source: UniProtKB
  • granulocyte differentiation Source: UniProtKB
  • lipid homeostasis Source: UniProtKB
  • liver development Source: UniProtKB
  • lung development Source: UniProtKB
  • memory Source: RGD
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • organ regeneration Source: RGD
  • osteoblast development Source: RGD
  • positive regulation of fat cell differentiation Source: RGD
  • positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • response to dexamethasone Source: RGD
  • response to nutrient Source: RGD
  • response to phenylpropanoid Source: RGD
  • response to vitamin B2 Source: RGD
  • transcription from RNA polymerase II promoter Source: GOC
  • transcription from RNA polymerase I promoter Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
CCAAT/enhancer-binding protein alphaImported
Short name:
C/EBP alpha
Gene namesi
Name:CebpaImported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2326. Cebpa.

Subcellular locationi

  • Nucleus 1 Publication
Isoform 4 :
  • Nucleusnucleolus 1 Publication

GO - Cellular componenti

  • CHOP-C/EBP complex Source: ParkinsonsUK-UCL
  • nuclear matrix Source: RGD
  • nucleolus Source: UniProtKB
  • nucleus Source: UniProtKB
  • protein complex Source: RGD
  • Rb-E2F complex Source: RGD
  • transcription factor complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi159 – 1591K → A or R: Not sumoylated. No effect of sumoylation on cell cycle inhibition. 1 Publication
Mutagenesisi285 – 2851Y → A: Increases interaction with TFDP1 and TFDP2, reduces DNA-binding, transactivation activity and represses E2F1:TFDP1-mediated transcription, loss of cell cycle inhibition and adipogenesis induction. 2 Publications
Mutagenesisi287 – 2871V → A: No effect on repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-290. 1 Publication
Mutagenesisi290 – 2901E → A: No effect on repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-287. 1 Publication
Mutagenesisi294 – 2941I → A: Increases interaction with TFDP1 and TFDP2, reduces transactivation activity and represses E2F1:TFDP1-mediated transcription, loss of cell cycle inhibition and adipogenesis induction, no effect on DNA-binding; when associated with A-297. 2 Publications
Mutagenesisi297 – 2971R → A: Increases interaction with TFDP1 and TFDP2, reduces transactivation activity and represses E2F1:TFDP1-mediated transcription, loss of cell cycle inhibition and adipogenesis induction, no effect on DNA-binding; when associated with A-294. 2 Publications
Mutagenesisi299 – 2991S → D: Isoform-4: Stimulates nucleolar retention of isoform-4. No effect on interaction with NPM1, TAF1A and UBTF. 1 Publication
Mutagenesisi301 – 3011D → A: No effect neither on interaction with TFDP1 or TFDP2 nor on transactivation activity or repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-304. 2 Publications
Mutagenesisi304 – 3041K → A: No effect neither on interaction with TFDP1 or TFDP2 nor on transactivation activity or repression of E2F1:TFDP1-mediated transcription, no effect on cell cycle inhibition or adipogenesis; when associated with A-301. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358CCAAT/enhancer-binding protein alphaPRO_0000076615Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei159 – 1591N6-acetyllysine; alternateBy similarity
Cross-linki159 – 159Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate1 Publication
Cross-linki159 – 159Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei193 – 1931PhosphoserineBy similarity
Modified residuei222 – 2221Phosphothreonine; by GSK3By similarity
Modified residuei226 – 2261Phosphothreonine; by GSK3By similarity
Modified residuei230 – 2301Phosphoserine; by GSK3By similarity

Post-translational modificationi

Sumoylated, sumoylation blocks the inhibitory effect on cell proliferation by disrupting the interaction with SMARCA2.1 Publication
Phosphorylation at Ser-193 is required for interaction with CDK2, CDK4 and SWI/SNF complex leading to cell cycle inhibiton. Dephosphorylated at Ser-193 by protein phosphatase 2A (PP2A) through PI3K/AKT signaling pathway regulation. Phosphorylation at Thr-222 and Thr-226 by GSK3 is constitutive in adipose tissue and lung. In liver, both Thr-222 and Thr-226 are phosphorylated only during feeding but not during fasting. Phosphorylation of the GSK3 consensus sites selectively decreases transactivation activity on IRE-controlled promoters.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP05554.

PTM databases

iPTMnetiP05554.
PhosphoSiteiP05554.

Expressioni

Tissue specificityi

Isoform 2 and isoform 3 are expressed in liver (at protein level).1 Publication

Developmental stagei

Isoform 2 and isoform 3 are not expressed at 1 day before birth, relative concentration of both isoforms increases with the age of the animal, reaching maximal levels in the adulthood.1 Publication

Gene expression databases

GenevisibleiP05554. RN.

Interactioni

Subunit structurei

Binds DNA as a homodimer and as a heterodimer (PubMed:1884998, PubMed:8367486). Can form stable heterodimers with CEBPB, CEBPD, CEBPE and CEBPG (PubMed:1884998, PubMed:1377818). Can form stable homodimers (also isoform 2 and isoform 3 dimers) and heterodimers with CEBPB (with isoform 2 and isoform 3) and CEBPG (PubMed:1377818, PubMed:8367486). Interacts with PRDM16 (By similarity). Interacts with UBN1 (By similarity). Interacts with ZNF638; this interaction increases transcriptional activation (By similarity). Interacts with the complex TFDP2:E2F1; the interaction prevents CEBPA binding to target gene promoters and represses its transcriptional activity (By similarity). Interacts with RB1 (By similarity). Interacts (when phosphorylated at SER-193) with CDK2, CDK4, E2F4 and SMARCA2 (By similarity). Interacts with SREBPF1 (By similarity). Interacts with FOXO1 (via the Fork-head domain); the interaction increases when FOXO1 is deacetylated (By similarity). Isoform 1 and Isoform 4 interact with TAF1A and UBTF (PubMed:20075868). Isoform 4 interacts with NPM1 (PubMed:20075868).By similarity4 Publications

GO - Molecular functioni

  • histone deacetylase binding Source: RGD
  • HMG box domain binding Source: UniProtKB
  • protein complex binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein heterodimerization activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi246437. 3 interactions.
DIPiDIP-28138N.
IntActiP05554. 5 interactions.
STRINGi10116.ENSRNOP00000063123.

Structurei

Secondary structure

1
358
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi282 – 33857Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NWQX-ray2.80A/C281-340[»]
ProteinModelPortaliP05554.
SMRiP05554. Positions 281-340.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP05554.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini282 – 34564bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 7070Required to repress E2F1:TFDP1-mediated transcription, to inhibit cell cycle and to induce adipocyte differentiation1 PublicationAdd
BLAST
Regioni126 – 20075Required to induce adipocyte differentiation1 PublicationAdd
BLAST
Regioni180 – 19415Required to functionally cooperate with SREBF1 in promoter activationBy similarityAdd
BLAST
Regioni240 – 358119Interaction with FOXO1By similarityAdd
BLAST
Regioni286 – 31328Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni317 – 34529Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi181 – 19010Poly-Pro
Compositional biasi262 – 27211Poly-GlyAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG3119. Eukaryota.
ENOG410YJ8G. LUCA.
HOGENOMiHOG000013112.
HOVERGENiHBG050879.
InParanoidiP05554.
KOiK09055.
OMAiFDYPGAP.
OrthoDBiEOG7R56TQ.
PhylomeDBiP05554.
TreeFamiTF105008.

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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P05554-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MESADFYEAE PRPPMSSHLQ SPPHAPSNAA FGFPRGAGPA PPPAPPAAPE
60 70 80 90 100
PLGGICEHET SIDISAYIDP AAFNDEFLAD LFQHSRQQEK AKAAAGPAGG
110 120 130 140 150
GGDFDYPGAP AGPGGAVMSA GAHGPPPGYG CAAAGYLDGR LEPLYERVGA
160 170 180 190 200
PALRPLVIKQ EPREEDEAKQ LALAGLFPYQ PPPPPPPPHP HASPAHLAAP
210 220 230 240 250
HLQFQIAHCG QTTMHLQPGH PTPPPTPVPS PHPAPAMGAA GLPGPGGSLK
260 270 280 290 300
GLAGPHPDLR TGGGGGGGAG AGKAKKSVDK NSNEYRVRRE RNNIAVRKSR
310 320 330 340 350
DKAKQRNVET QQKVLELTSD NDRLRKRVEQ LSRELDTLRG IFRQLPESSL

VKAMGNCA
Length:358
Mass (Da):37,371
Last modified:February 1, 1996 - v3
Checksum:i4DA8F112F6EA95D0
GO
Isoform 2 (identifier: P05554-2) [UniParc]FASTAAdd to basket

Also known as: CEBPalpha-p421 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: Missing.

Show »
Length:344
Mass (Da):35,750
Checksum:i530FA6D51C5E7BDA
GO
Isoform 3 (identifier: P05554-3) [UniParc]FASTAAdd to basket

Also known as: C/EBPalpha-p301 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-117: Missing.

Show »
Length:241
Mass (Da):25,526
Checksum:i16713D706888AA35
GO
Isoform 4 (identifier: P05554-4) [UniParc]FASTAAdd to basket

Also known as: extended-C/EBPalpha1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRGRGRVGVLGGRRRQRRHAQAGGRRGSPCRENSNSPM

Note: Mutagenesis in position: 14: RRQR -> AAAA abolishes nucleolar localization and prevents induction of 45S pre-RNA.1 Publication
Show »
Length:395
Mass (Da):41,440
Checksum:i01D1DA74BD4A48C8
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 117117Missing in isoform 3. 1 PublicationVSP_057551Add
BLAST
Alternative sequencei1 – 1414Missing in isoform 2. 1 PublicationVSP_057552Add
BLAST
Alternative sequencei1 – 11M → MRGRGRVGVLGGRRRQRRHA QAGGRRGSPCRENSNSPM in isoform 4. VSP_057609

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12752 Genomic DNA. Translation: CAA31242.1.
AC109741 Genomic DNA. No translation available.
PIRiS06890. A54265.
RefSeqiNP_001274506.1. NM_001287577.1. [P05554-4]
NP_001274507.1. NM_001287578.1. [P05554-2]
NP_001274508.1. NM_001287579.1. [P05554-3]
NP_036656.1. NM_012524.3. [P05554-1]

Genome annotation databases

GeneIDi24252.
KEGGirno:24252.
UCSCiRGD:2326. rat. [P05554-1]

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12752 Genomic DNA. Translation: CAA31242.1.
AC109741 Genomic DNA. No translation available.
PIRiS06890. A54265.
RefSeqiNP_001274506.1. NM_001287577.1. [P05554-4]
NP_001274507.1. NM_001287578.1. [P05554-2]
NP_001274508.1. NM_001287579.1. [P05554-3]
NP_036656.1. NM_012524.3. [P05554-1]

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NWQX-ray2.80A/C281-340[»]
ProteinModelPortaliP05554.
SMRiP05554. Positions 281-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi246437. 3 interactions.
DIPiDIP-28138N.
IntActiP05554. 5 interactions.
STRINGi10116.ENSRNOP00000063123.

PTM databases

iPTMnetiP05554.
PhosphoSiteiP05554.

Proteomic databases

PaxDbiP05554.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24252.
KEGGirno:24252.
UCSCiRGD:2326. rat. [P05554-1]

Organism-specific databases

CTDi1050.
RGDi2326. Cebpa.

Phylogenomic databases

eggNOGiKOG3119. Eukaryota.
ENOG410YJ8G. LUCA.
HOGENOMiHOG000013112.
HOVERGENiHBG050879.
InParanoidiP05554.
KOiK09055.
OMAiFDYPGAP.
OrthoDBiEOG7R56TQ.
PhylomeDBiP05554.
TreeFamiTF105008.

Miscellaneous databases

EvolutionaryTraceiP05554.
PROiP05554.

Gene expression databases

GenevisibleiP05554. RN.

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. "Isolation of a recombinant copy of the gene encoding C/EBP."
    Landschulz W.H., Johnson P.F., Adashi E.Y., Graves B.J., McKnight S.L.
    Genes Dev. 2:786-800(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 253-269.
    Strain: Sprague-Dawley.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION.
    Strain: Sprague-Dawley.
    Tissue: Liver.
  3. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  4. "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: FUNCTION, SUBUNIT.
  5. "Molecular cloning of two C/EBP-related proteins that bind to the promoter and the enhancer of the alpha 1-fetoprotein gene. Further analysis of C/EBP beta and C/EBP gamma."
    Thomassin H., Hamel D., Bernier D., Guertin M., Belanger L.
    Nucleic Acids Res. 20:3091-3098(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  6. "CCAAT/enhancer-binding protein mRNA is translated into multiple proteins with different transcription activation potentials."
    Ossipow V., Descombes P., Schibler U.
    Proc. Natl. Acad. Sci. U.S.A. 90:8219-8223(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ALTERNATIVE TRANSLATIONAL INITIATION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY, SUBUNIT, DNA-BINDING.
  7. "E2F repression by C/EBPalpha is required for adipogenesis and granulopoiesis in vivo."
    Porse B.T., Pedersen T.A., Xu X., Lindberg B., Wewer U.M., Friis-Hansen L., Nerlov C.
    Cell 107:247-258(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF TYR-285; VAL-287; GLU-290; ILE-294; ARG-297; ASP-301 AND LYS-304.
  8. "Sumoylation of CCAAT/enhancer-binding protein alpha and its functional roles in hepatocyte differentiation."
    Sato Y., Miyake K., Kaneoka H., Iijima S.
    J. Biol. Chem. 281:21629-21639(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SMARCA2, SUMOYLATION AT LYS-159, MUTAGENESIS OF LYS-159.
  9. "Nucleolar retention of a translational C/EBPalpha isoform stimulates rDNA transcription and cell size."
    Muller C., Bremer A., Schreiber S., Eichwald S., Calkhoven C.F.
    EMBO J. 29:897-909(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE INITIATION, IDENTIFICATION OF NON-CANONICAL INITIATION CODON, SUBCELLULAR LOCATION (ISOFORM 4), MUTAGENESIS (ISOFORM 4), MUTAGENESIS OF SER-299, INTERACTION WITH NPM1; TAF1A AND UBTF.
  10. "Repression of transcriptional activity of C/EBPalpha by E2F-dimerization partner complexes."
    Zaragoza K., Begay V., Schuetz A., Heinemann U., Leutz A.
    Mol. Cell. Biol. 30:2293-2304(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TFDP1; TFDP2 AND E2F1, MUTAGENESIS OF GLU-290; ILE-294; ARG-297; ASP-301 AND LYS-304.

Entry informationi

Entry nameiCEBPA_RAT
AccessioniPrimary (citable) accession number: P05554
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: February 1, 1996
Last modified: June 8, 2016
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.