| UniProt ID | TFCP2_HUMAN | |
|---|---|---|
| UniProt AC | Q12800 | |
| Protein Name | Alpha-globin transcription factor CP2 | |
| Gene Name | TFCP2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 502 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Binds a variety of cellular and viral promoters including fibrinogen, alpha-globin, SV40 and HIV-1 promoters. Activation of the alpha-globin promoter in erythroid cells is via synergistic interaction with UBP1 (By similarity). Functions as part of the SSP (stage selector protein) complex. Facilitates the interaction of the gamma-globin genes with enhancer elements contained in the locus control region in fetal erythroid cells. Interacts by binding to the stage selector element (SSE) in the proximal gamma-globin promoter.. | |
| Protein Sequence | MAWALKLPLADEVIESGLVQDFDASLSGIGQELGAGAYSMSDVLALPIFKQEESSLPPDNENKILPFQYVLCAATSPAVKLHDETLTYLNQGQSYEIRMLDNRKLGELPEINGKLVKSIFRVVFHDRRLQYTEHQQLEGWRWNRPGDRILDIDIPMSVGIIDPRANPTQLNTVEFLWDPAKRTSVFIQVHCISTEFTMRKHGGEKGVPFRVQIDTFKENENGEYTEHLHSASCQIKVFKPKGADRKQKTDREKMEKRTPHEKEKYQPSYETTILTECSPWPEITYVNNSPSPGFNSSHSSFSLGEGNGSPNHQPEPPPPVTDNLLPTTTPQEAQQWLHRNRFSTFTRLFTNFSGADLLKLTRDDVIQICGPADGIRLFNALKGRMVRPRLTIYVCQESLQLREQQQQQQQQQQKHEDGDSNGTFFVYHAIYLEELTAVELTEKIAQLFSISPCQISQIYKQGPTGIHVLISDEMIQNFQEEACFILDTMKAETNDSYHIILK | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 50 | Sumoylation | VLALPIFKQEESSLP HCCCCCCCCCHHCCC | 58.48 | - | |
| 54 | Phosphorylation | PIFKQEESSLPPDNE CCCCCCHHCCCCCCC | 36.10 | 27251275 | |
| 55 | Phosphorylation | IFKQEESSLPPDNEN CCCCCHHCCCCCCCC | 48.45 | 24719451 | |
| 98 | Methylation | QGQSYEIRMLDNRKL CCCCEEEEECCCCCC | 13.99 | - | |
| 104 | Ubiquitination | IRMLDNRKLGELPEI EEECCCCCCCCCCCC | 68.07 | - | |
| 114 | Ubiquitination | ELPEINGKLVKSIFR CCCCCCHHHHHHHHH | 45.69 | - | |
| 131 | Phosphorylation | FHDRRLQYTEHQQLE HCCCCCCCEECHHCC | 20.77 | 20068231 | |
| 132 | Phosphorylation | HDRRLQYTEHQQLEG CCCCCCCEECHHCCC | 17.65 | 20068231 | |
| 181 | Ubiquitination | EFLWDPAKRTSVFIQ EEEECHHHCCEEEEE | 62.69 | - | |
| 194 | Phosphorylation | IQVHCISTEFTMRKH EEEEEEEEEEEEHHC | 18.40 | - | |
| 197 | Phosphorylation | HCISTEFTMRKHGGE EEEEEEEEEHHCCCC | 15.16 | - | |
| 205 | Ubiquitination | MRKHGGEKGVPFRVQ EHHCCCCCCCCEEEE | 69.36 | - | |
| 217 | Ubiquitination | RVQIDTFKENENGEY EEEEECCEECCCCCE | 62.82 | - | |
| 241 | Ubiquitination | QIKVFKPKGADRKQK EEEEECCCCCCCCCC | 68.28 | - | |
| 258 | Phosphorylation | REKMEKRTPHEKEKY HHHHHHCCHHHHHHC | 39.81 | 22817900 | |
| 289 | Phosphorylation | EITYVNNSPSPGFNS EEEEECCCCCCCCCC | 22.88 | 26074081 | |
| 291 | Phosphorylation | TYVNNSPSPGFNSSH EEECCCCCCCCCCCC | 37.16 | 26074081 | |
| 309 | Phosphorylation | SLGEGNGSPNHQPEP CCCCCCCCCCCCCCC | 26.91 | 26657352 | |
| 343 | Phosphorylation | WLHRNRFSTFTRLFT HHHHCCHHHHHHHHH | 21.26 | 22817900 | |
| 344 | Phosphorylation | LHRNRFSTFTRLFTN HHHCCHHHHHHHHHC | 26.72 | 23312004 | |
| 346 | Phosphorylation | RNRFSTFTRLFTNFS HCCHHHHHHHHHCCC | 26.93 | 23312004 | |
| 350 | Phosphorylation | STFTRLFTNFSGADL HHHHHHHHCCCCCHH | 39.69 | 21406692 | |
| 353 | Phosphorylation | TRLFTNFSGADLLKL HHHHHCCCCCHHHHC | 34.83 | 28348404 | |
| 359 | Ubiquitination | FSGADLLKLTRDDVI CCCCHHHHCCCCCEE | 55.92 | - | |
| 382 | Ubiquitination | IRLFNALKGRMVRPR HHHHHHHCCCCCCCC | 41.90 | - | |
| 391 | Phosphorylation | RMVRPRLTIYVCQES CCCCCCEEEEEEHHH | 16.13 | 20860994 | |
| 398 | Phosphorylation | TIYVCQESLQLREQQ EEEEEHHHHHHHHHH | 8.78 | 24505115 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 258 | T | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
| 289 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
| 289 | S | Phosphorylation | Kinase | ERK-SUBFAMILY | - | GPS |
| 289 | S | Phosphorylation | Kinase | JNK-SUBFAMILY | - | GPS |
| 291 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
| 291 | S | Phosphorylation | Kinase | ERK-SUBFAMILY | - | GPS |
| 291 | S | Phosphorylation | Kinase | JNK-SUBFAMILY | - | GPS |
| 309 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
| 309 | S | Phosphorylation | Kinase | CDK3 | Q00526 | PSP |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TFCP2_HUMAN !! | ||||||
* 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 TFCP2_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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