| UniProt ID | CEBPA_HUMAN | |
|---|---|---|
| UniProt AC | P49715 | |
| Protein Name | CCAAT/enhancer-binding protein alpha {ECO:0000312|HGNC:HGNC:1833} | |
| Gene Name | CEBPA {ECO:0000312|HGNC:HGNC:1833} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 358 | |
| Subcellular Localization |
Nucleus . Isoform 4: Nucleus, nucleolus . |
|
| Protein Description | 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] | |
| Protein Sequence | MESADFYEAEPRPPMSSHLQSPPHAPSSAAFGFPRGAGPAQPPAPPAAPEPLGGICEHETSIDISAYIDPAAFNDEFLADLFQHSRQQEKAKAAVGPTGGGGGGDFDYPGAPAGPGGAVMPGGAHGPPPGYGCAAAGYLDGRLEPLYERVGAPALRPLVIKQEPREEDEAKQLALAGLFPYQPPPPPPPSHPHPHPPPAHLAAPHLQFQIAHCGQTTMHLQPGHPTPPPTPVPSPHPAPALGAAGLPGPGSALKGLGAAHPDLRASGGSGAGKAKKSVDKNSNEYRVRRERNNIAVRKSRDKAKQRNVETQQKVLELTSDNDRLRKRVEQLSRELDTLRGIFRQLPESSLVKAMGNCA | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MESADFYEAE -----CCCCCCCCCC | 31.66 | 28450419 | |
| 7 | Phosphorylation | -MESADFYEAEPRPP -CCCCCCCCCCCCCC | 18.12 | 28450419 | |
| 16 | Phosphorylation | AEPRPPMSSHLQSPP CCCCCCCCHHCCCCC | 22.00 | 23401153 | |
| 17 | Phosphorylation | EPRPPMSSHLQSPPH CCCCCCCHHCCCCCC | 23.20 | 28450419 | |
| 21 | Phosphorylation | PMSSHLQSPPHAPSS CCCHHCCCCCCCCCC | 46.92 | 23401153 | |
| 42 | Ubiquitination | RGAGPAQPPAPPAAP CCCCCCCCCCCCCCC | 29.18 | 21890473 | |
| 42 | Acetylation | RGAGPAQPPAPPAAP CCCCCCCCCCCCCCC | 29.18 | 19608861 | |
| 147 | Ubiquitination | DGRLEPLYERVGAPA CCCCHHHHHHHCCCC | 16.65 | 21890473 | |
| 147 | Acetylation | DGRLEPLYERVGAPA CCCCHHHHHHHCCCC | 16.65 | 19608861 | |
| 147 | Phosphorylation | DGRLEPLYERVGAPA CCCCHHHHHHHCCCC | 16.65 | 28674151 | |
| 161 | Acetylation | ALRPLVIKQEPREED CHHEEEECCCCCCHH | 40.92 | 19608861 | |
| 161 | Ubiquitination | ALRPLVIKQEPREED CHHEEEECCCCCCHH | 40.92 | 21890473 | |
| 161 | Sumoylation | ALRPLVIKQEPREED CHHEEEECCCCCCHH | 40.92 | 28112733 | |
| 161 | Sumoylation | ALRPLVIKQEPREED CHHEEEECCCCCCHH | 40.92 | - | |
| 190 | Phosphorylation | PPPPPPPSHPHPHPP CCCCCCCCCCCCCCC | 56.26 | 15107404 | |
| 194 | Ubiquitination | PPPSHPHPHPPPAHL CCCCCCCCCCCCHHH | 46.24 | 21890473 | |
| 196 | Acetylation | PSHPHPHPPPAHLAA CCCCCCCCCCHHHCC | 40.81 | 19608861 | |
| 196 | Ubiquitination | PSHPHPHPPPAHLAA CCCCCCCCCCHHHCC | 40.81 | 21890473 | |
| 226 | Phosphorylation | HLQPGHPTPPPTPVP ECCCCCCCCCCCCCC | 42.63 | 10567568 | |
| 230 | Phosphorylation | GHPTPPPTPVPSPHP CCCCCCCCCCCCCCC | 42.57 | 10567568 | |
| 234 | Phosphorylation | PPPTPVPSPHPAPAL CCCCCCCCCCCCCCC | 35.75 | 20101026 | |
| 266 | Phosphorylation | AHPDLRASGGSGAGK CCCCHHHCCCCCCCC | 36.93 | 25159151 | |
| 298 | Acetylation | RNNIAVRKSRDKAKQ HHCCCHHHHHHHHHH | 43.15 | 112788007 | |
| 299 | Ubiquitination | NNIAVRKSRDKAKQR HCCCHHHHHHHHHHC | 34.84 | 21890473 | |
| 302 | Acetylation | AVRKSRDKAKQRNVE CHHHHHHHHHHCCHH | 57.27 | 112788009 | |
| 313 | Ubiquitination | RNVETQQKVLELTSD CCHHHHHHHHHHCCC | 38.68 | 21890473 | |
| 326 | Acetylation | SDNDRLRKRVEQLSR CCHHHHHHHHHHHHH | 66.44 | 112788011 | |
| 332 | Phosphorylation | RKRVEQLSRELDTLR HHHHHHHHHHHHHHH | 24.33 | - | |
| 348 | Ubiquitination | IFRQLPESSLVKAMG HHHHCCHHHHHHHHC | 27.34 | 21890473 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 21 | S | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
| 21 | S | Phosphorylation | Kinase | MAPK3 | P27361 | GPS |
| 226 | T | Phosphorylation | Kinase | GSK3 | - | Uniprot |
| 230 | T | Phosphorylation | Kinase | GSK3 | - | Uniprot |
| 234 | S | Phosphorylation | Kinase | GSK3 | - | Uniprot |
| - | K | Ubiquitination | E3 ubiquitin ligase | FBXW7 | Q969H0 | PMID:24658274 |
| - | K | Ubiquitination | E3 ubiquitin ligase | UBE3A | Q05086 | PMID:23598402 |
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CEBPA_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 601626 | Leukemia, acute myelogenous (AML) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| Acetylation | |
| Reference | PubMed |
| "Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-161, AND MASS SPECTROMETRY. | |
