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Protein

CCAAT/enhancer-binding protein alpha

Gene

CEBPA

Organism
Homo sapiens (Human)
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. Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes (PubMed:11242107). During early embryogenesis, plays essential and redundant functions with CEBPB. Essential for the transition from common myeloid progenitors (CMP) to granulocyte/monocyte progenitors (GMP). 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 (By similarity). 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. Proliferation arrest also depends on a functional binding to SWI/SNF complex (PubMed:14660596). 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 similarity2 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 (PubMed:14660596).By similarity1 Publication

GO - Molecular functioni

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

GO - Biological processi

  1. acute-phase response Source: Ensembl
  2. brown fat cell differentiation Source: Ensembl
  3. cell maturation Source: Ensembl
  4. cellular response to lithium ion Source: Ensembl
  5. cellular response to organic cyclic compound Source: Ensembl
  6. cholesterol metabolic process Source: Ensembl
  7. cytokine-mediated signaling pathway Source: UniProtKB
  8. embryonic placenta development Source: Ensembl
  9. fat cell differentiation Source: UniProtKB
  10. generation of precursor metabolites and energy Source: ProtInc
  11. glucose homeostasis Source: UniProtKB
  12. granulocyte differentiation Source: UniProtKB
  13. inner ear development Source: Ensembl
  14. liver development Source: UniProtKB
  15. lung development Source: UniProtKB
  16. macrophage differentiation Source: Ensembl
  17. mitochondrion organization Source: Ensembl
  18. myeloid cell differentiation Source: UniProtKB
  19. negative regulation of cell proliferation Source: UniProtKB
  20. negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: ParkinsonsUK-UCL
  21. negative regulation of transcription, DNA-templated Source: UniProtKB
  22. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  23. organ regeneration Source: Ensembl
  24. positive regulation of fat cell differentiation Source: Ensembl
  25. positive regulation of osteoblast differentiation Source: Ensembl
  26. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
  27. positive regulation of transcription from RNA polymerase III promoter Source: UniProtKB
  28. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  29. response to glucocorticoid Source: Ensembl
  30. response to vitamin B2 Source: Ensembl
  31. transcription, DNA-templated Source: UniProtKB
  32. transcription from RNA polymerase II promoter Source: ProtInc
  33. urea cycle Source: Ensembl
  34. viral process Source: UniProtKB-KW
  35. white fat cell differentiation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Host-virus interaction, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiP49715.

Names & Taxonomyi

Protein namesi
Recommended name:
CCAAT/enhancer-binding protein alphaImported
Short name:
C/EBP alphaImported
Gene namesi
Name:CEBPAImported
Synonyms:CEBPImported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:1833. CEBPA.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nuclear matrix Source: Ensembl
  2. nucleus Source: UniProtKB
  3. Rb-E2F complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Leukemia, acute myelogenous (AML)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA subtype of acute leukemia, a cancer of the white blood cells. AML is a malignant disease of bone marrow characterized by maturational arrest of hematopoietic precursors at an early stage of development. Clonal expansion of myeloid blasts occurs in bone marrow, blood, and other tissue. Myelogenous leukemias develop from changes in cells that normally produce neutrophils, basophils, eosinophils and monocytes.

See also OMIM:601626
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti84 – 841H → L in AML; no effect on expression; no effect on DNA-binding or transactivation activity. 1 Publication
VAR_072677
Natural varianti312 – 3121Q → QK in AML; nuclear; no effect on expression; loss of DNA-binding and transactivation activity. 1 Publication
VAR_072678

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi601626. phenotype.
Orphaneti102724. 'Acute myeloid leukemia with t(8;21)(q22;q22) translocation'.
319480. Acute myeloid leukemia with CEBPA somatic mutations.
319465. Inherited acute myeloid leukemia.
PharmGKBiPA26376.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 358358CCAAT/enhancer-binding protein alphaPRO_0000076613Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei161 – 1611N6-acetyllysine1 Publication
Cross-linki161 – 161Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei190 – 1901Phosphoserine1 Publication
Modified residuei226 – 2261Phosphothreonine; by GSK3By similarity
Modified residuei230 – 2301Phosphothreonine; by GSK3By similarity
Modified residuei234 – 2341Phosphoserine; by GSK3By similarity

Post-translational modificationi

Phosphorylation at Ser-190 is required for interaction with CDK2, CDK4 and SWI/SNF complex leading to cell cycle inhibiton. Dephosphorylated at Ser-190 by protein phosphatase 2A (PP2A) through PI3K/AKT signaling pathway regulation (PubMed:15107404). Phosphorylation at Thr-226 and Thr-230 by GSK3 is constitutive in adipose tissue and lung. In liver, both Thr-226 and Thr-230 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
Sumoylated, sumoylation blocks the inhibitory effect on cell proliferation by disrupting the interaction with SMARCA2.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP49715.
PRIDEiP49715.

PTM databases

PhosphoSiteiP49715.

Expressioni

Gene expression databases

BgeeiP49715.
CleanExiHS_CEBPA.
ExpressionAtlasiP49715. baseline and differential.
GenevestigatoriP49715.

Organism-specific databases

HPAiHPA065037.

Interactioni

Subunit structurei

Binds DNA as a dimer and can form stable heterodimers with CEBPB and CEBPG (By similarity). Interacts with PRDM16 (By similarity). Interacts with UBN1 (PubMed:10725330). 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 (PubMed:20176812). Interacts with RB1 (PubMed:15107404). Interacts (when phosphorylated at SER-190) with CDK2, CDK4, E2F4 and SMARCA2 (PubMed:15107404). Interacts with SREBPF1 (By similarity). Interacts with FOXO1 (via the Fork-head domain); the interaction increases when FOXO1 is deacetylated (By similarity). Interacts with HBV protein X (PubMed:9915821).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDX1P479023EBI-1172054,EBI-8514176
E2P031222EBI-1172054,EBI-7028618From a different organism.
E2P064224EBI-1172054,EBI-7136851From a different organism.
PARP1P098742EBI-1172054,EBI-355676

Protein-protein interaction databases

BioGridi107479. 98 interactions.
IntActiP49715. 14 interactions.
MINTiMINT-264048.

Structurei

3D structure databases

ProteinModelPortaliP49715.
SMRiP49715. Positions 281-340.
ModBaseiSearch...
MobiDBiSearch...

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 differentiationBy similarityAdd
BLAST
Regioni128 – 20477Required to induce adipocyte differentiationBy similarityAdd
BLAST
Regioni182 – 19817Required to functionally cooperate with SREBF1 in promoter activationBy similarityAdd
BLAST
Regioni244 – 358115Interaction 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 biasi99 – 1046Poly-Gly
Compositional biasi183 – 1897Poly-Pro

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00530000063192.
HOGENOMiHOG000013112.
HOVERGENiHBG050879.
InParanoidiP49715.
KOiK09055.
OMAiPPPGYGC.
OrthoDBiEOG7R56TQ.
PhylomeDBiP49715.
TreeFamiTF105008.

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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative initiation. AlignAdd to basket

Isoform 1 (identifier: P49715-1) [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 SPPHAPSSAA FGFPRGAGPA QPPAPPAAPE
60 70 80 90 100
PLGGICEHET SIDISAYIDP AAFNDEFLAD LFQHSRQQEK AKAAVGPTGG
110 120 130 140 150
GGGGDFDYPG APAGPGGAVM PGGAHGPPPG YGCAAAGYLD GRLEPLYERV
160 170 180 190 200
GAPALRPLVI KQEPREEDEA KQLALAGLFP YQPPPPPPPS HPHPHPPPAH
210 220 230 240 250
LAAPHLQFQI AHCGQTTMHL QPGHPTPPPT PVPSPHPAPA LGAAGLPGPG
260 270 280 290 300
SALKGLGAAH PDLRASGGSG AGKAKKSVDK NSNEYRVRRE RNNIAVRKSR
310 320 330 340 350
DKAKQRNVET QQKVLELTSD NDRLRKRVEQ LSRELDTLRG IFRQLPESSL

VKAMGNCA
Length:358
Mass (Da):37,561
Last modified:February 4, 2008 - v3
Checksum:i574C0A049E25BCAC
GO
Isoform 2 (identifier: P49715-2) [UniParc]FASTAAdd to basket

Also known as: C/EBPalpha-p421 Publication

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

Show »
Length:344
Mass (Da):35,940
Checksum:i49EB5DC3749152A6
GO
Isoform 3 (identifier: P49715-3) [UniParc]FASTAAdd to basket

Also known as: C/EBPalpha-p301 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-119: Missing.

Show »
Length:239
Mass (Da):25,540
Checksum:i4A9F7812303016A0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti40 – 412AQ → PK in AAC50235 (PubMed:7575576).Curated
Sequence conflicti95 – 984VGPT → WAH in CAA72289 (Ref. 2) Curated
Sequence conflicti241 – 2411L → V in CAA72289 (Ref. 2) Curated
Sequence conflicti248 – 2503GPG → ALA in CAA72289 (Ref. 2) Curated
Sequence conflicti269 – 2691S → T in AAC50235 (PubMed:7575576).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti84 – 841H → L in AML; no effect on expression; no effect on DNA-binding or transactivation activity. 1 Publication
VAR_072677
Natural varianti312 – 3121Q → QK in AML; nuclear; no effect on expression; loss of DNA-binding and transactivation activity. 1 Publication
VAR_072678

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 119119Missing in isoform 3. VSP_057547Add
BLAST
Alternative sequencei1 – 1414Missing in isoform 2. VSP_057548Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34070 Genomic DNA. Translation: AAC50235.1.
Y11525 mRNA. Translation: CAA72289.1.
EU048234 Genomic DNA. Translation: ABS82765.1.
BC027902 mRNA. Translation: AAH27902.1.
CCDSiCCDS54243.1.
PIRiJC4311.
RefSeqiNP_004355.2. NM_004364.4.
UniGeneiHs.76171.

Genome annotation databases

EnsembliENST00000498907; ENSP00000427514; ENSG00000245848.
GeneIDi1050.
KEGGihsa:1050.
UCSCiuc002nun.3. human.

Polymorphism databases

DMDMi166898082.

Keywords - Coding sequence diversityi

Alternative initiation

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34070 Genomic DNA. Translation: AAC50235.1.
Y11525 mRNA. Translation: CAA72289.1.
EU048234 Genomic DNA. Translation: ABS82765.1.
BC027902 mRNA. Translation: AAH27902.1.
CCDSiCCDS54243.1.
PIRiJC4311.
RefSeqiNP_004355.2. NM_004364.4.
UniGeneiHs.76171.

3D structure databases

ProteinModelPortaliP49715.
SMRiP49715. Positions 281-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107479. 98 interactions.
IntActiP49715. 14 interactions.
MINTiMINT-264048.

PTM databases

PhosphoSiteiP49715.

Polymorphism databases

DMDMi166898082.

Proteomic databases

MaxQBiP49715.
PRIDEiP49715.

Protocols and materials databases

DNASUi1050.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000498907; ENSP00000427514; ENSG00000245848.
GeneIDi1050.
KEGGihsa:1050.
UCSCiuc002nun.3. human.

Organism-specific databases

CTDi1050.
GeneCardsiGC19M033790.
GeneReviewsiCEBPA.
H-InvDBHIX0040095.
HGNCiHGNC:1833. CEBPA.
HPAiHPA065037.
MIMi116897. gene.
601626. phenotype.
neXtProtiNX_P49715.
Orphaneti102724. 'Acute myeloid leukemia with t(8;21)(q22;q22) translocation'.
319480. Acute myeloid leukemia with CEBPA somatic mutations.
319465. Inherited acute myeloid leukemia.
PharmGKBiPA26376.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00530000063192.
HOGENOMiHOG000013112.
HOVERGENiHBG050879.
InParanoidiP49715.
KOiK09055.
OMAiPPPGYGC.
OrthoDBiEOG7R56TQ.
PhylomeDBiP49715.
TreeFamiTF105008.

Enzyme and pathway databases

ReactomeiREACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiP49715.

Miscellaneous databases

ChiTaRSiCEBPA. human.
GeneWikiiCEBPA.
GenomeRNAii1050.
NextBioi4397.
PROiP49715.
SOURCEiSearch...

Gene expression databases

BgeeiP49715.
CleanExiHS_CEBPA.
ExpressionAtlasiP49715. baseline and differential.
GenevestigatoriP49715.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, sequence, and expression patterns of the human gene encoding CCAAT/enhancer binding protein alpha (C/EBP alpha)."
    Antonson P., Xanthopoulos K.G.
    Biochem. Biophys. Res. Commun. 215:106-113(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Umbilical cord.
  2. "Transcription factor C/EBP-alpha: novel sites of expression and cloning of the human gene."
    Swart G.W.M., van Groningen J.J.M., van Ruissen F., Bergers M., Schalwijk J.
    Biol. Chem. Hoppe-Seyler 378:373-379(1996)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. SeattleSNPs variation discovery resource
    Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-133.
    Tissue: Pancreas.
  5. "Interaction of hepatitis B viral X protein and CCAAT/enhancer-binding protein alpha synergistically activates the hepatitis B viral enhancer II/pregenomic promoter."
    Choi B.H., Park G.T., Rho H.M.
    J. Biol. Chem. 274:2858-2865(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HBV PROTEIN X.
  6. "Ubinuclein, a novel nuclear protein interacting with cellular and viral transcription factors."
    Aho S., Buisson M., Pajunen T., Ryoo Y.W., Giot J.-F., Gruffat H., Sergeant A., Uitto J.
    J. Cell Biol. 148:1165-1176(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UBN1.
  7. Cited for: INVOLVEMENT IN AML.
  8. "Liver tumors escape negative control of proliferation via PI3K/Akt-mediated block of C/EBP alpha growth inhibitory activity."
    Wang G.L., Iakova P., Wilde M., Awad S., Timchenko N.A.
    Genes Dev. 18:912-925(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDK2; CDK4; E2F4; RB1 AND SMARCA2, PHOSPHORYLATION AT SER-190.
  9. "The CCAAT enhancer-binding protein alpha (C/EBPalpha) requires a SWI/SNF complex for proliferation arrest."
    Muller C., Calkhoven C.F., Sha X., Leutz A.
    J. Biol. Chem. 279:7353-7358(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORMS 1 AND 3).
  10. Cited for: INVOLVEMENT IN AML.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-161, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TFDP1; TFDP2 AND E2F1.
  13. "Dominant-negative mutations of CEBPA, encoding CCAAT/enhancer binding protein-alpha (C/EBPalpha), in acute myeloid leukemia."
    Pabst T., Mueller B.U., Zhang P., Radomska H.S., Narravula S., Schnittger S., Behre G., Hiddemann W., Tenen D.G.
    Nat. Genet. 27:263-270(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS AML LEU-84 AND LYS-312 INS, CHARACTERIZATION OF VARIANTS AML LEU-84 AND LYS-312 INS, INVOLVEMENT IN AML, FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE TRANSLATIONAL INITIATION, DNA-BINDING.

Entry informationi

Entry nameiCEBPA_HUMAN
AccessioniPrimary (citable) accession number: P49715
Secondary accession number(s): A7LNP2, P78319, Q05CA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1996
Last sequence update: February 4, 2008
Last modified: March 31, 2015
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.