UniProt ID | E2F1_HUMAN | |
---|---|---|
UniProt AC | Q01094 | |
Protein Name | Transcription factor E2F1 | |
Gene Name | E2F1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 437 | |
Subcellular Localization | Nucleus . | |
Protein Description | Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle progression from G1 to S phase. E2F1 binds preferentially RB1 in a cell-cycle dependent manner. It can mediate both cell proliferation and TP53/p53-dependent apoptosis. Blocks adipocyte differentiation by binding to specific promoters repressing CEBPA binding to its target gene promoters. [PubMed: 20176812 Positively regulates transcription of RRP1B] | |
Protein Sequence | MALAGAPAGGPCAPALEALLGAGALRLLDSSQIVIISAAQDASAPPAPTGPAAPAAGPCDPDLLLFATPQAPRPTPSAPRPALGRPPVKRRLDLETDHQYLAESSGPARGRGRHPGKGVKSPGEKSRYETSLNLTTKRFLELLSHSADGVVDLNWAAEVLKVQKRRIYDITNVLEGIQLIAKKSKNHIQWLGSHTTVGVGGRLEGLTQDLRQLQESEQQLDHLMNICTTQLRLLSEDTDSQRLAYVTCQDLRSIADPAEQMVMVIKAPPETQLQAVDSSENFQISLKSKQGPIDVFLCPEETVGGISPGKTPSQEVTSEEENRATDSATIVSPPPSSPPSSLTTDPSQSLLSLEQEPLLSRMGSLRAPVDEDRLSPLVAADSLLEHVREDFSGLLPEEFISLSPPHEALDYHFGLEEGEGIRDLFDCDFGDLTPLDF | |
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 |
---|---|---|---|---|---|
31 | Phosphorylation | ALRLLDSSQIVIISA HHHHCCCCCEEEEEE | 24.48 | 11459832 | |
96 | Phosphorylation | KRRLDLETDHQYLAE CCCCCCCCCHHHHHH | 46.18 | - | |
109 | Methylation | AESSGPARGRGRHPG HHCCCCCCCCCCCCC | 38.17 | - | |
111 | Methylation | SSGPARGRGRHPGKG CCCCCCCCCCCCCCC | 33.16 | - | |
113 | Methylation | GPARGRGRHPGKGVK CCCCCCCCCCCCCCC | 31.31 | - | |
117 | Acetylation | GRGRHPGKGVKSPGE CCCCCCCCCCCCCCC | 66.05 | 10675335 | |
117 | Neddylation | GRGRHPGKGVKSPGE CCCCCCCCCCCCCCC | 66.05 | - | |
120 | Acetylation | RHPGKGVKSPGEKSR CCCCCCCCCCCCCHH | 60.65 | 10675335 | |
120 | Neddylation | RHPGKGVKSPGEKSR CCCCCCCCCCCCCHH | 60.65 | - | |
121 | Phosphorylation | HPGKGVKSPGEKSRY CCCCCCCCCCCCHHC | 35.41 | 24719451 | |
125 | Acetylation | GVKSPGEKSRYETSL CCCCCCCCHHCHHHC | 46.26 | 10675335 | |
125 | Neddylation | GVKSPGEKSRYETSL CCCCCCCCHHCHHHC | 46.26 | - | |
131 | Phosphorylation | EKSRYETSLNLTTKR CCHHCHHHCCHHHHH | 11.88 | 22210691 | |
135 | Phosphorylation | YETSLNLTTKRFLEL CHHHCCHHHHHHHHH | 29.24 | 22210691 | |
136 | Phosphorylation | ETSLNLTTKRFLELL HHHCCHHHHHHHHHH | 24.32 | - | |
161 | Ubiquitination | NWAAEVLKVQKRRIY HHHHHHHHHHHHHHH | 48.04 | - | |
164 | Ubiquitination | AEVLKVQKRRIYDIT HHHHHHHHHHHHHHH | 46.78 | - | |
185 | Neddylation | QLIAKKSKNHIQWLG HHHHHHCCCCEEECC | 62.52 | - | |
185 | Methylation | QLIAKKSKNHIQWLG HHHHHHCCCCEEECC | 62.52 | 20603083 | |
302 | Phosphorylation | VFLCPEETVGGISPG EEECCHHCCCCCCCC | 23.84 | 23663014 | |
307 | Phosphorylation | EETVGGISPGKTPSQ HHCCCCCCCCCCCCC | 30.76 | 23663014 | |
311 | Phosphorylation | GGISPGKTPSQEVTS CCCCCCCCCCCCCCC | 33.80 | 23663014 | |
313 | Phosphorylation | ISPGKTPSQEVTSEE CCCCCCCCCCCCCHH | 44.18 | 23663014 | |
317 | Phosphorylation | KTPSQEVTSEEENRA CCCCCCCCCHHHHCC | 29.66 | 23663014 | |
318 | Phosphorylation | TPSQEVTSEEENRAT CCCCCCCCHHHHCCC | 48.46 | 23663014 | |
325 | Phosphorylation | SEEENRATDSATIVS CHHHHCCCCCCEEEC | 27.52 | 28176443 | |
327 | Phosphorylation | EENRATDSATIVSPP HHHCCCCCCEEECCC | 23.98 | 28176443 | |
329 | Phosphorylation | NRATDSATIVSPPPS HCCCCCCEEECCCCC | 26.34 | 28176443 | |
332 | Phosphorylation | TDSATIVSPPPSSPP CCCCEEECCCCCCCC | 28.04 | 20616879 | |
336 | Phosphorylation | TIVSPPPSSPPSSLT EEECCCCCCCCHHCC | 62.34 | 30108239 | |
337 | Phosphorylation | IVSPPPSSPPSSLTT EECCCCCCCCHHCCC | 46.75 | 20616879 | |
340 | Phosphorylation | PPPSSPPSSLTTDPS CCCCCCCHHCCCCCC | 41.17 | 30108239 | |
341 | Phosphorylation | PPSSPPSSLTTDPSQ CCCCCCHHCCCCCCH | 35.19 | 30108239 | |
343 | Phosphorylation | SSPPSSLTTDPSQSL CCCCHHCCCCCCHHH | 30.97 | 28176443 | |
344 | Phosphorylation | SPPSSLTTDPSQSLL CCCHHCCCCCCHHHH | 51.73 | 28176443 | |
347 | Phosphorylation | SSLTTDPSQSLLSLE HHCCCCCCHHHHCCC | 34.90 | 28176443 | |
349 | Phosphorylation | LTTDPSQSLLSLEQE CCCCCCHHHHCCCHH | 35.30 | 28176443 | |
352 | Phosphorylation | DPSQSLLSLEQEPLL CCCHHHHCCCHHHHH | 34.84 | 28176443 | |
364 | Phosphorylation | PLLSRMGSLRAPVDE HHHHHHCCCCCCCCH | 12.82 | 22496350 | |
375 | Phosphorylation | PVDEDRLSPLVAADS CCCHHHCHHHHHHHH | 19.65 | 30266825 | |
382 | Phosphorylation | SPLVAADSLLEHVRE HHHHHHHHHHHHHHH | 30.08 | 30266825 | |
403 | Phosphorylation | PEEFISLSPPHEALD CHHHHCCCCCHHHHH | 29.60 | 20616879 | |
433 | Phosphorylation | DCDFGDLTPLDF--- CCCCCCCCCCCC--- | 26.92 | 10428966 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
31 | S | Phosphorylation | Kinase | ATM | Q13315 | PSP |
31 | S | Phosphorylation | Kinase | ATR | Q13535 | PSP |
332 | S | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
332 | S | Phosphorylation | Kinase | TBK1 | Q9UHD2 | PSP |
337 | S | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
337 | S | Phosphorylation | Kinase | MAP3K7 | O43318 | GPS |
364 | S | Phosphorylation | Kinase | CHK2 | O96017 | PSP |
375 | S | Phosphorylation | Kinase | CDK8 | P49336 | PSP |
403 | S | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
403 | S | Phosphorylation | Kinase | GSK3B | P49841 | PSP |
403 | S | Phosphorylation | Kinase | P38B | Q15759 | PSP |
403 | S | Phosphorylation | Kinase | MAPK11 | Q9WUI1 | GPS |
433 | T | Phosphorylation | Kinase | CDK7 | P50613 | PSP |
433 | T | Phosphorylation | Kinase | GSK3B | P49841 | PSP |
433 | T | Phosphorylation | Kinase | P38B | Q15759 | PSP |
433 | T | Phosphorylation | Kinase | MAPK11 | Q9WUI1 | GPS |
- | K | Ubiquitination | E3 ubiquitin ligase | MDM2 | Q00987 | PMID:22199232 |
- | K | Ubiquitination | E3 ubiquitin ligase | SKP2 | Q13309 | PMID:10559858 |
- | K | Ubiquitination | E3 ubiquitin ligase | EP300 | Q09472 | PMID:15917652 |
- | K | Ubiquitination | E3 ubiquitin ligase | FZR1 | Q9UM11 | PMID:22580462 |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
364 | S | Phosphorylation |
| 12717439 |
* 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 E2F1_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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Acetylation | |
Reference | PubMed |
"Regulation of E2F1 activity by acetylation."; Martinez-Balbas M.A., Bauer U.M., Nielsen S.J., Brehm A.,Kouzarides T.; EMBO J. 19:662-671(2000). Cited for: ACETYLATION AT LYS-117; LYS-120 AND LYS-125, DNA-BINDING, INTERACTIONWITH KAT2B, FUNCTION, AND MUTAGENESIS OF LYS-117; LYS-120 AND LYS-125. | |
Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND MASSSPECTROMETRY. | |
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND MASSSPECTROMETRY. | |
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-375, AND MASSSPECTROMETRY. |