ETS1_MOUSE - dbPTM
ETS1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MKAAVDLKP
------CCCCCCCCC
45.0822826441
8AcetylationMKAAVDLKPTLTIIK
CCCCCCCCCEEEEEE
31.34-
15AcetylationKPTLTIIKTEKVDLE
CCEEEEEEECCCCCC
46.9423236377
15SumoylationKPTLTIIKTEKVDLE
CCEEEEEEECCCCCC
46.94-
15SumoylationKPTLTIIKTEKVDLE
CCEEEEEEECCCCCC
46.94-
26PhosphorylationVDLELFPSPDMECAD
CCCCCCCCCCCCCCC
26.6325338131
38PhosphorylationCADVPLLTPSSKEMM
CCCCCCCCCCHHHHH
28.899770451
41PhosphorylationVPLLTPSSKEMMSQA
CCCCCCCHHHHHHHH
33.5620534573
58UbiquitinationATFSGFTKEQQRLGI
HHHCCCCHHHHHHCC
51.7922790023
223PhosphorylationTDTLQTDYFAIKQEV
CCCCCCCCEEEECCE
9.78-
227SumoylationQTDYFAIKQEVLTPD
CCCCEEEECCEECCC
36.6616862185
227SumoylationQTDYFAIKQEVLTPD
CCCCEEEECCEECCC
36.66-
245AcetylationLGRASRGKLGGQDSF
CCCCCCCCCCCCCCC
42.7323236377
251PhosphorylationGKLGGQDSFESVESY
CCCCCCCCCCCHHHH
24.0328833060
254PhosphorylationGGQDSFESVESYDSC
CCCCCCCCHHHHHCC
29.2228833060
257PhosphorylationDSFESVESYDSCDRL
CCCCCHHHHHCCCHH
31.89-
265PhosphorylationYDSCDRLTQSWSSQS
HHCCCHHCHHCCCCC
22.81-
267PhosphorylationSCDRLTQSWSSQSSF
CCCHHCHHCCCCCCC
24.5627566939
269PhosphorylationDRLTQSWSSQSSFNS
CHHCHHCCCCCCCCC
24.6027566939
270PhosphorylationRLTQSWSSQSSFNSL
HHCHHCCCCCCCCCC
28.02-
282PhosphorylationNSLQRVPSYDSFDYE
CCCCCCCCCCCCCCC
38.4227742792
283PhosphorylationSLQRVPSYDSFDYED
CCCCCCCCCCCCCCC
14.9925619855
285PhosphorylationQRVPSYDSFDYEDYP
CCCCCCCCCCCCCCC
16.2825619855
288PhosphorylationPSYDSFDYEDYPAAL
CCCCCCCCCCCCCCC
14.5325619855
291PhosphorylationDSFDYEDYPAALPNH
CCCCCCCCCCCCCCC
5.2629472430
305AcetylationHKPKGTFKDYVRDRA
CCCCCCHHHHHHHHH
48.24-
377UbiquitinationEVARRWGKRKNKPKM
HHHHHHHHCCCCCCC
53.92-
379UbiquitinationARRWGKRKNKPKMNY
HHHHHHCCCCCCCCH
73.19-
381UbiquitinationRWGKRKNKPKMNYEK
HHHHCCCCCCCCHHH
49.39-
405PhosphorylationDKNIIHKTAGKRYVY
HCCCEECCCCCHHHH
26.87-
410PhosphorylationHKTAGKRYVYRFVCD
ECCCCCHHHHHHHHH
12.81-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
38TPhosphorylationKinaseMAPK1P28482
GPS
38TPhosphorylationKinaseERK2P63085
PSP
38TPhosphorylationKinaseMAPK3P27361
GPS
38TPhosphorylationKinaseMAPK-FAMILY-GPS
38TPhosphorylationKinaseMAPK-Uniprot
41SPhosphorylationKinaseERK2P63085
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
15KSumoylation

16862185
227KSumoylation

16862185

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ETS1_MOUSEEts1physical
20211142
HDAC1_MOUSEHdac1physical
22266280
PRDM1_MOUSEPrdm1physical
17977828

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ETS1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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
ReferencePubMed
"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.

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