ETS1_HUMAN - dbPTM
ETS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ETS1_HUMAN
UniProt AC P14921
Protein Name Protein C-ets-1
Gene Name ETS1
Organism Homo sapiens (Human).
Sequence Length 441
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..
Protein Sequence MKAAVDLKPTLTIIKTEKVDLELFPSPDMECADVPLLTPSSKEMMSQALKATFSGFTKEQQRLGIPKDPRQWTETHVRDWVMWAVNEFSLKGVDFQKFCMNGAALCALGKDCFLELAPDFVGDILWEHLEILQKEDVKPYQVNGVNPAYPESRYTSDYFISYGIEHAQCVPPSEFSEPSFITESYQTLHPISSEELLSLKYENDYPSVILRDPLQTDTLQNDYFAIKQEVVTPDNMCMGRTSRGKLGGQDSFESIESYDSCDRLTQSWSSQSSFNSLQRVPSYDSFDSEDYPAALPNHKPKGTFKDYVRDRADLNKDKPVIPAAALAGYTGSGPIQLWQFLLELLTDKSCQSFISWTGDGWEFKLSDPDEVARRWGKRKNKPKMNYEKLSRGLRYYYDKNIIHKTAGKRYVYRFVCDLQSLLGYTPEELHAMLDVKPDADE
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
1Acetylation-------MKAAVDLK
-------CCCCCCCC		6.34-
2Acetylation------MKAAVDLKP
------CCCCCCCCC		45.0819608861
2 (in isoform 3)Phosphorylation-45.0821712546
2Ubiquitination------MKAAVDLKP
------CCCCCCCCC		45.08-
3 (in isoform 3)Phosphorylation-16.0628985074
7 (in isoform 3)Phosphorylation-6.0221712546
8UbiquitinationMKAAVDLKPTLTIIK
CCCCCCCCCEEEEEE		31.34-
8SumoylationMKAAVDLKPTLTIIK
CCCCCCCCCEEEEEE		31.3428112733
8AcetylationMKAAVDLKPTLTIIK
CCCCCCCCCEEEEEE		31.3419608861
15 (in isoform 3)Phosphorylation-46.9421712546
15SumoylationKPTLTIIKTEKVDLE
CCEEEEEEECCCCCC		46.9428112733
15UbiquitinationKPTLTIIKTEKVDLE
CCEEEEEEECCCCCC		46.94-
15SumoylationKPTLTIIKTEKVDLE
CCEEEEEEECCCCCC		46.94-
15AcetylationKPTLTIIKTEKVDLE
CCEEEEEEECCCCCC		46.9419608861
16PhosphorylationPTLTIIKTEKVDLEL
CEEEEEEECCCCCCC		30.5429978859
18UbiquitinationLTIIKTEKVDLELFP
EEEEEECCCCCCCCC		46.40-
26PhosphorylationVDLELFPSPDMECAD
CCCCCCCCCCCCCCC		26.6326657352
31 (in isoform 3)Phosphorylation-2.9228985074
38PhosphorylationCADVPLLTPSSKEMM
CCCCCCCCCCHHHHH		28.8928102081
40PhosphorylationDVPLLTPSSKEMMSQ
CCCCCCCCHHHHHHH		49.1322199227
41PhosphorylationVPLLTPSSKEMMSQA
CCCCCCCHHHHHHHH		33.5629116813
42UbiquitinationPLLTPSSKEMMSQAL
CCCCCCHHHHHHHHH		54.70-
46PhosphorylationPSSKEMMSQALKATF
CCHHHHHHHHHHHHH		15.81-
50UbiquitinationEMMSQALKATFSGFT
HHHHHHHHHHHCCCC		48.69-
54PhosphorylationQALKATFSGFTKEQQ
HHHHHHHCCCCHHHH		28.74-
58UbiquitinationATFSGFTKEQQRLGI
HHHCCCCHHHHHHCC		51.79-
67UbiquitinationQQRLGIPKDPRQWTE
HHHHCCCCCHHHCHH		77.70-
89PhosphorylationMWAVNEFSLKGVDFQ
HHHHHCCCCCCCCHH		24.0024719451
97UbiquitinationLKGVDFQKFCMNGAA
CCCCCHHHHHHCHHH		40.29-
138 (in isoform 1)Ubiquitination-50.7821906983
138 (in isoform 2)Ubiquitination-50.7821906983
138SumoylationILQKEDVKPYQVNGV
HHCCCCCCCCCCCCC		50.7828112733
138UbiquitinationILQKEDVKPYQVNGV
HHCCCCCCCCCCCCC		50.7821906983
138SumoylationILQKEDVKPYQVNGV
HHCCCCCCCCCCCCC		50.78-
138UbiquitinationILQKEDVKPYQVNGV
HHCCCCCCCCCCCCC		50.782190698
140PhosphorylationQKEDVKPYQVNGVNP
CCCCCCCCCCCCCCC		21.26-
158PhosphorylationESRYTSDYFISYGIE
CHHHCCCCEEEECCC		11.54-
184 (in isoform 3)Phosphorylation-17.5627642862
192PhosphorylationYQTLHPISSEELLSL
EECCCCCCHHHHHCC		35.8326074081
193PhosphorylationQTLHPISSEELLSLK
ECCCCCCHHHHHCCC		35.4926074081
198PhosphorylationISSEELLSLKYENDY
CCHHHHHCCCCCCCC		35.1324719451
200SumoylationSEELLSLKYENDYPS
HHHHHCCCCCCCCCC		47.33-
205PhosphorylationSLKYENDYPSVILRD
CCCCCCCCCCEEECC		14.6919060867
207PhosphorylationKYENDYPSVILRDPL
CCCCCCCCEEECCCC		18.63-
223PhosphorylationTDTLQNDYFAIKQEV
CCCCCCCEEEEEEEE		11.4928796482
227UbiquitinationQNDYFAIKQEVVTPD
CCCEEEEEEEEECCC		36.66-
227SumoylationQNDYFAIKQEVVTPD
CCCEEEEEEEEECCC		36.66-
232PhosphorylationAIKQEVVTPDNMCMG
EEEEEEECCCCCCCC		30.0522199227
241PhosphorylationDNMCMGRTSRGKLGG
CCCCCCCCCCCCCCC		19.6226074081
242PhosphorylationNMCMGRTSRGKLGGQ
CCCCCCCCCCCCCCC		37.3626074081
245UbiquitinationMGRTSRGKLGGQDSF
CCCCCCCCCCCCCCC		42.73-
245AcetylationMGRTSRGKLGGQDSF
CCCCCCCCCCCCCCC		42.7323749302
249 (in isoform 3)Phosphorylation-41.1827642862
251PhosphorylationGKLGGQDSFESIESY
CCCCCCCCCCCHHHH		24.0323401153
251 (in isoform 3)Phosphorylation-24.0327642862
254PhosphorylationGGQDSFESIESYDSC
CCCCCCCCHHHHHCC		29.6428102081
257PhosphorylationDSFESIESYDSCDRL
CCCCCHHHHHCCCHH		32.3528796482
258PhosphorylationSFESIESYDSCDRLT
CCCCHHHHHCCCHHH		10.0928796482
260PhosphorylationESIESYDSCDRLTQS
CCHHHHHCCCHHHHH		15.0828796482
265PhosphorylationYDSCDRLTQSWSSQS
HHCCCHHHHHCCCCC		22.8123403867
267 (in isoform 3)Phosphorylation-24.5627642862
267PhosphorylationSCDRLTQSWSSQSSF
CCCHHHHHCCCCCCC		24.5619690332
269PhosphorylationDRLTQSWSSQSSFNS
CHHHHHCCCCCCCCC		24.6023403867
270PhosphorylationRLTQSWSSQSSFNSL
HHHHHCCCCCCCCCC		28.0223403867
272PhosphorylationTQSWSSQSSFNSLQR
HHHCCCCCCCCCCCC		38.5523403867
273PhosphorylationQSWSSQSSFNSLQRV
HHCCCCCCCCCCCCC		22.3223403867
276PhosphorylationSSQSSFNSLQRVPSY
CCCCCCCCCCCCCCC		24.7026074081
282PhosphorylationNSLQRVPSYDSFDSE
CCCCCCCCCCCCCCC		38.4223401153
283PhosphorylationSLQRVPSYDSFDSED
CCCCCCCCCCCCCCC		14.9925159151
285PhosphorylationQRVPSYDSFDSEDYP
CCCCCCCCCCCCCCC		23.7923401153
288PhosphorylationPSYDSFDSEDYPAAL
CCCCCCCCCCCCCCC		30.2922617229
291PhosphorylationDSFDSEDYPAALPNH
CCCCCCCCCCCCCCC		7.2428102081
295 (in isoform 3)Phosphorylation-4.7924719451
299UbiquitinationPAALPNHKPKGTFKD
CCCCCCCCCCCCHHH		55.88-
299AcetylationPAALPNHKPKGTFKD
CCCCCCCCCCCCHHH		55.8825953088
301UbiquitinationALPNHKPKGTFKDYV
CCCCCCCCCCHHHHH		75.32-
302 (in isoform 3)Phosphorylation-44.9327642862
305UbiquitinationHKPKGTFKDYVRDRA
CCCCCCHHHHHHHHH		48.24-
305AcetylationHKPKGTFKDYVRDRA
CCCCCCHHHHHHHHH		48.2419608861
311 (in isoform 3)Phosphorylation-21.3127251275
313 (in isoform 3)Phosphorylation-52.2324719451
326 (in isoform 3)Phosphorylation-3.0524719451
327 (in isoform 3)Phosphorylation-12.2927642862
329 (in isoform 3)Phosphorylation-11.4324719451
332 (in isoform 3)Phosphorylation-33.3327251275
349AcetylationLELLTDKSCQSFISW
HHHHCCCCCHHHEEC		21.8719608861
377UbiquitinationEVARRWGKRKNKPKM
HHHHHHHHCCCCCCC		53.92-
383UbiquitinationGKRKNKPKMNYEKLS
HHCCCCCCCCHHHHH		41.19-
388SumoylationKPKMNYEKLSRGLRY
CCCCCHHHHHHHHHH		41.21-
388SumoylationKPKMNYEKLSRGLRY
CCCCCHHHHHHHHHH		41.21-
388UbiquitinationKPKMNYEKLSRGLRY
CCCCCHHHHHHHHHH		41.21-
395PhosphorylationKLSRGLRYYYDKNII
HHHHHHHHHHHCCCE		16.06-
399UbiquitinationGLRYYYDKNIIHKTA
HHHHHHHCCCEECCC		33.65-
404UbiquitinationYDKNIIHKTAGKRYV
HHCCCEECCCCCHHH		29.66-
405PhosphorylationDKNIIHKTAGKRYVY
HCCCEECCCCCHHHH		26.8724719451
408UbiquitinationIIHKTAGKRYVYRFV
CEECCCCCHHHHHHH		37.78-
410PhosphorylationHKTAGKRYVYRFVCD
ECCCCCHHHHHHHHH		12.8124719451
449 (in isoform 3)Phosphorylation-24719451
454 (in isoform 3)Phosphorylation-24719451
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
38TPhosphorylationKinaseMAPK7Q13164
GPS
38TPhosphorylationKinaseMAPK-FAMILY-GPS
38TPhosphorylationKinaseMAPK-Uniprot
38TPhosphorylationKinaseMAPK_GROUP-PhosphoELM
251SPhosphorylationKinaseKCC2AQ9UQM7
PhosphoELM
257SPhosphorylationKinaseKCC2AQ9UQM7
PhosphoELM
282SPhosphorylationKinaseKCC2AQ9UQM7
PhosphoELM
283YPhosphorylationKinaseSRCP12931
PSP
283YPhosphorylationKinaseYESP07947
PSP
285SPhosphorylationKinaseKCC2AQ9UQM7
PhosphoELM
-KUbiquitinationE3 ubiquitin ligasePIAS4Q8N2W9
PMID:17456046
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
15KSumoylation

19608861
227KSumoylation

-
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DAXX_HUMANDAXXphysical
10698492
TYDP2_HUMANTDP2physical
12743594
MAF_HUMANMAFphysical
9566892
RUNX2_HUMANRUNX2physical
9794229
UBC9_HUMANUBE2Iphysical
9333025
PIAS4_HUMANPIAS4physical
17456046
DAXX_HUMANDAXXphysical
16861237
CBP_HUMANCREBBPphysical
15572696
EP300_HUMANEP300physical
15572696
MED23_HUMANMED23physical
15572696
EP300_HUMANEP300physical
10358095
CBP_HUMANCREBBPphysical
9528793
PLEC_HUMANPLECphysical
20842667
MK07_HUMANMAPK7physical
12048211
P53_HUMANTP53physical
18374905
ATF2_HUMANATF2physical
7774816
CBP_HUMANCREBBPphysical
7774816
SP100_HUMANSP100physical
15247905
A4_HUMANAPPphysical
21832049
EPAS1_HUMANEPAS1physical
12464608
SRA1_HUMANSRA1physical
20398657
P53_HUMANTP53physical
14586398
MEIS1_HUMANMEIS1physical
18692240
SRS11_HUMANSRSF11physical
21988832
JUN_HUMANJUNphysical
20195357
CQ062_HUMANC17orf62physical
20195357
ARI4B_HUMANARID4Bphysical
20195357
IF2P_HUMANEIF5Bphysical
20195357
APLP2_HUMANAPLP2physical
20195357
RL13A_HUMANRPL13Aphysical
20195357
AR6P4_HUMANARL6IP4physical
20195357
NUCL_HUMANNCLphysical
20195357
ZBT7A_HUMANZBTB7Aphysical
24857950
P53_HUMANTP53physical
24857950
MK01_HUMANMAPK1physical
25241761
ANDR_HUMANARphysical
25241761
NFKB1_HUMANNFKB1physical
25241761
SMAD3_HUMANSMAD3physical
25241761
KPYM_HUMANPKMphysical
25609649
CH3L2_HUMANCHI3L2physical
25609649
THUM1_HUMANTHUMPD1physical
25609649
AT2B1_HUMANATP2B1physical
25609649
SP1_HUMANSP1physical
25363021
TBP_HUMANTBPphysical
25363021
Drug and Disease Associations
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.
Regulatory Network of ETS1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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 MET-1; LYS-2; LYS-8; LYS-15 ANDLYS-305, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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-270 AND SER-285, ANDMASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-205 AND TYR-223, ANDMASS SPECTROMETRY.

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