UniProt ID | ETS1_MOUSE | |
---|---|---|
UniProt AC | P27577 | |
Protein Name | Protein C-ets-1 | |
Gene Name | Ets1 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 440 | |
Subcellular Localization | Cytoplasm . Nucleus . Delocalizes from nucleus to cytoplasm when coexpressed with isoform Ets-1 p27. | |
Protein Description | Transcription factor. Directly controls the expression of cytokine and chemokine genes in a wide variety of different cellular contexts. May control the differentiation, survival and proliferation of lymphoid cells. May also regulate angiogenesis through regulation of expression of genes controlling endothelial cell migration and invasion (By similarity).. | |
Protein Sequence | MKAAVDLKPTLTIIKTEKVDLELFPSPDMECADVPLLTPSSKEMMSQALKATFSGFTKEQQRLGIPKDPRQWTETHVRDWVMWAVNEFSLKGVDFQKFCMSGAALCALGKECFLELAPDFVGDILWEHLEILQKEDVKPYQVNGANPTYPESCYTSDYFISYGIEHAQCVPPSEFSEPSFITESYQTLHPISSEELLSLKYENDYPSVILQDPLQTDTLQTDYFAIKQEVLTPDNMCLGRASRGKLGGQDSFESVESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDYEDYPAALPNHKPKGTFKDYVRDRADLNKDKPVIPAAALAGYTGSGPIQLWQFLLELLTDKSCQSFISWTGDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVYRFVCDLQSLLGYTPEELHAMLDVKPDAD | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MKAAVDLKP ------CCCCCCCCC | 45.08 | 22826441 | |
8 | Acetylation | MKAAVDLKPTLTIIK CCCCCCCCCEEEEEE | 31.34 | - | |
15 | Acetylation | KPTLTIIKTEKVDLE CCEEEEEEECCCCCC | 46.94 | 23236377 | |
15 | Sumoylation | KPTLTIIKTEKVDLE CCEEEEEEECCCCCC | 46.94 | - | |
15 | Sumoylation | KPTLTIIKTEKVDLE CCEEEEEEECCCCCC | 46.94 | - | |
26 | Phosphorylation | VDLELFPSPDMECAD CCCCCCCCCCCCCCC | 26.63 | 25338131 | |
38 | Phosphorylation | CADVPLLTPSSKEMM CCCCCCCCCCHHHHH | 28.89 | 9770451 | |
41 | Phosphorylation | VPLLTPSSKEMMSQA CCCCCCCHHHHHHHH | 33.56 | 20534573 | |
58 | Ubiquitination | ATFSGFTKEQQRLGI HHHCCCCHHHHHHCC | 51.79 | 22790023 | |
223 | Phosphorylation | TDTLQTDYFAIKQEV CCCCCCCCEEEECCE | 9.78 | - | |
227 | Sumoylation | QTDYFAIKQEVLTPD CCCCEEEECCEECCC | 36.66 | 16862185 | |
227 | Sumoylation | QTDYFAIKQEVLTPD CCCCEEEECCEECCC | 36.66 | - | |
245 | Acetylation | LGRASRGKLGGQDSF CCCCCCCCCCCCCCC | 42.73 | 23236377 | |
251 | Phosphorylation | GKLGGQDSFESVESY CCCCCCCCCCCHHHH | 24.03 | 28833060 | |
254 | Phosphorylation | GGQDSFESVESYDSC CCCCCCCCHHHHHCC | 29.22 | 28833060 | |
257 | Phosphorylation | DSFESVESYDSCDRL CCCCCHHHHHCCCHH | 31.89 | - | |
265 | Phosphorylation | YDSCDRLTQSWSSQS HHCCCHHCHHCCCCC | 22.81 | - | |
267 | Phosphorylation | SCDRLTQSWSSQSSF CCCHHCHHCCCCCCC | 24.56 | 27566939 | |
269 | Phosphorylation | DRLTQSWSSQSSFNS CHHCHHCCCCCCCCC | 24.60 | 27566939 | |
270 | Phosphorylation | RLTQSWSSQSSFNSL HHCHHCCCCCCCCCC | 28.02 | - | |
282 | Phosphorylation | NSLQRVPSYDSFDYE CCCCCCCCCCCCCCC | 38.42 | 27742792 | |
283 | Phosphorylation | SLQRVPSYDSFDYED CCCCCCCCCCCCCCC | 14.99 | 25619855 | |
285 | Phosphorylation | QRVPSYDSFDYEDYP CCCCCCCCCCCCCCC | 16.28 | 25619855 | |
288 | Phosphorylation | PSYDSFDYEDYPAAL CCCCCCCCCCCCCCC | 14.53 | 25619855 | |
291 | Phosphorylation | DSFDYEDYPAALPNH CCCCCCCCCCCCCCC | 5.26 | 29472430 | |
305 | Acetylation | HKPKGTFKDYVRDRA CCCCCCHHHHHHHHH | 48.24 | - | |
377 | Ubiquitination | EVARRWGKRKNKPKM HHHHHHHHCCCCCCC | 53.92 | - | |
379 | Ubiquitination | ARRWGKRKNKPKMNY HHHHHHCCCCCCCCH | 73.19 | - | |
381 | Ubiquitination | RWGKRKNKPKMNYEK HHHHCCCCCCCCHHH | 49.39 | - | |
405 | Phosphorylation | DKNIIHKTAGKRYVY HCCCEECCCCCHHHH | 26.87 | - | |
410 | Phosphorylation | HKTAGKRYVYRFVCD ECCCCCHHHHHHHHH | 12.81 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
38 | T | Phosphorylation | Kinase | MAPK1 | P28482 | GPS |
38 | T | Phosphorylation | Kinase | ERK2 | P63085 | PSP |
38 | T | Phosphorylation | Kinase | MAPK3 | P27361 | GPS |
38 | T | Phosphorylation | Kinase | MAPK-FAMILY | - | GPS |
38 | T | Phosphorylation | Kinase | MAPK | - | Uniprot |
41 | S | Phosphorylation | Kinase | ERK2 | P63085 | PSP |
* 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 ETS1_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ETS1_MOUSE | Ets1 | physical | 20211142 | |
HDAC1_MOUSE | Hdac1 | physical | 22266280 | |
PRDM1_MOUSE | Prdm1 | physical | 17977828 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Structure of the ets-1 pointed domain and mitogen-activated proteinkinase phosphorylation site."; Slupsky C.M., Gentile L.N., Donaldson L.W., Mackereth C.D.,Seidel J.J., Graves B.J., McIntosh L.P.; Proc. Natl. Acad. Sci. U.S.A. 95:12129-12134(1998). Cited for: STRUCTURE BY NMR OF 29-138, AND PHOSPHORYLATION AT THR-38. | |
Sumoylation | |
Reference | PubMed |
"Regulation of the Ets-1 transcription factor by sumoylation andubiquitinylation."; Ji Z., Degerny C., Vintonenko N., Deheuninck J., Foveau B., Leroy C.,Coll J., Tulasne D., Baert J.-L., Fafeur V.; Oncogene 26:395-406(2007). Cited for: SUMOYLATION AT LYS-15 AND LYS-227, AND UBIQUITINATION. |