ETV6_HUMAN - dbPTM
ETV6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ETV6_HUMAN
UniProt AC P41212
Protein Name Transcription factor ETV6
Gene Name ETV6
Organism Homo sapiens (Human).
Sequence Length 452
Subcellular Localization Nucleus.
Protein Description Transcriptional repressor; binds to the DNA sequence 5'-CCGGAAGT-3'. Plays a role in hematopoiesis and malignant transformation..
Protein Sequence MSETPAQCSIKQERISYTPPESPVPSYASSTPLHVPVPRALRMEEDSIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYRSPHSGDVLYELLQHILKQRKPRILFSPFFHPGNSIHTQPEVILHQNHEEDNCVQRTPRPSVDNVHHNPPTIELLHRSRSPITTNHRPSPDPEQRPLRSPLDNMIRRLSPAERAQGPRPHQENNHQESYPLSVSPMENNHCPASSESHPKPSSPRQESTRVIQLMPSPIMHPLILNPRHSVDFKQSRLSEDGLHREGKPINLSHREDLAYMNHIMVSVSPPEEHAMPIGRIADCRLLWDYVYQLLSDSRYENFIRWEDKESKIFRIVDPNGLARLWGNHKNRTNMTYEKMSRALRHYYKLNIIRKEPGQRLLFRFMKTPDEIMSGRTDRLEHLESQELDEQIYQEDEC
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
2Phosphorylation------MSETPAQCS
------CCCCCCCCC		50.6130108239
4Phosphorylation----MSETPAQCSIK
----CCCCCCCCCCC		19.3330108239
9PhosphorylationSETPAQCSIKQERIS
CCCCCCCCCCEEECC		22.2723401153
11SumoylationTPAQCSIKQERISYT
CCCCCCCCEEECCCC		29.79-
11AcetylationTPAQCSIKQERISYT
CCCCCCCCEEECCCC		29.7919608861
11SumoylationTPAQCSIKQERISYT
CCCCCCCCEEECCCC		29.7928112733
16PhosphorylationSIKQERISYTPPESP
CCCEEECCCCCCCCC		29.2222167270
17PhosphorylationIKQERISYTPPESPV
CCEEECCCCCCCCCC		22.3922167270
18PhosphorylationKQERISYTPPESPVP
CEEECCCCCCCCCCC		26.1022167270
22PhosphorylationISYTPPESPVPSYAS
CCCCCCCCCCCCCCC		36.6522167270
26PhosphorylationPPESPVPSYASSTPL
CCCCCCCCCCCCCCC		33.3022167270
27PhosphorylationPESPVPSYASSTPLH
CCCCCCCCCCCCCCC		12.3922167270
29PhosphorylationSPVPSYASSTPLHVP
CCCCCCCCCCCCCCC		26.8922167270
30PhosphorylationPVPSYASSTPLHVPV
CCCCCCCCCCCCCCC		26.3522167270
31PhosphorylationVPSYASSTPLHVPVP
CCCCCCCCCCCCCCC		27.6322167270
47PhosphorylationALRMEEDSIRLPAHL
CCCCCCCCCCCCCEE		16.9423312004
60PhosphorylationHLRLQPIYWSRDDVA
EEEECCCCCCHHHHH		12.1922817900
86PhosphorylationLRPIDSNTFEMNGKA
CCCCCCCCEEECCEE		25.5630631047
98PhosphorylationGKALLLLTKEDFRYR
CEEEEEEEHHHHCCC		32.1530631047
99SumoylationKALLLLTKEDFRYRS
EEEEEEEHHHHCCCC		56.08-
99SumoylationKALLLLTKEDFRYRS
EEEEEEEHHHHCCCC		56.08-
114PhosphorylationPHSGDVLYELLQHIL
CCCHHHHHHHHHHHH		12.3620068231
131PhosphorylationRKPRILFSPFFHPGN
CCCCEEEECCCCCCC		19.8323401153
139PhosphorylationPFFHPGNSIHTQPEV
CCCCCCCCCCCCCEE		22.9723401153
142PhosphorylationHPGNSIHTQPEVILH
CCCCCCCCCCEEEEC		44.1227251275
161PhosphorylationEDNCVQRTPRPSVDN
CCCCCCCCCCCCCCC		13.4229255136
165PhosphorylationVQRTPRPSVDNVHHN
CCCCCCCCCCCCCCC		43.3028464451
175PhosphorylationNVHHNPPTIELLHRS
CCCCCCCHHHHHHCC		28.4827794612
182PhosphorylationTIELLHRSRSPITTN
HHHHHHCCCCCCCCC		26.7727794612
184PhosphorylationELLHRSRSPITTNHR
HHHHCCCCCCCCCCC		23.1523401153
187PhosphorylationHRSRSPITTNHRPSP
HCCCCCCCCCCCCCC		25.5727794612
188PhosphorylationRSRSPITTNHRPSPD
CCCCCCCCCCCCCCC		29.7327794612
193PhosphorylationITTNHRPSPDPEQRP
CCCCCCCCCCHHHCC		41.7223401153
203PhosphorylationPEQRPLRSPLDNMIR
HHHCCCCCHHHHHHH		37.1823401153
213PhosphorylationDNMIRRLSPAERAQG
HHHHHHCCHHHHHCC		21.9123401153
232PhosphorylationQENNHQESYPLSVSP
CCCCCCCCCCCCCCC		26.0223927012
233PhosphorylationENNHQESYPLSVSPM
CCCCCCCCCCCCCCC		13.8723927012
236PhosphorylationHQESYPLSVSPMENN
CCCCCCCCCCCCCCC		18.9523927012
238PhosphorylationESYPLSVSPMENNHC
CCCCCCCCCCCCCCC		18.3623927012
248PhosphorylationENNHCPASSESHPKP
CCCCCCCCCCCCCCC		21.5623927012
249PhosphorylationNNHCPASSESHPKPS
CCCCCCCCCCCCCCC		45.2723927012
251PhosphorylationHCPASSESHPKPSSP
CCCCCCCCCCCCCCC		47.2223927012
256PhosphorylationSESHPKPSSPRQEST
CCCCCCCCCCCCCCC		60.1323927012
257PhosphorylationESHPKPSSPRQESTR
CCCCCCCCCCCCCCC		32.4023927012
271PhosphorylationRVIQLMPSPIMHPLI
CEEEECCCCCCCCHH		17.0629255136
284PhosphorylationLILNPRHSVDFKQSR
HHCCCCCCCCCCHHH		25.3526657352
288UbiquitinationPRHSVDFKQSRLSED
CCCCCCCCHHHCCCC		42.79-
288SumoylationPRHSVDFKQSRLSED
CCCCCCCCHHHCCCC		42.7928112733
290PhosphorylationHSVDFKQSRLSEDGL
CCCCCCHHHCCCCCC		35.4623401153
293PhosphorylationDFKQSRLSEDGLHRE
CCCHHHCCCCCCCCC		32.3123401153
302UbiquitinationDGLHREGKPINLSHR
CCCCCCCCCCCCCCH		37.6619608861
302SumoylationDGLHREGKPINLSHR
CCCCCCCCCCCCCCH		37.6628112733
302AcetylationDGLHREGKPINLSHR
CCCCCCCCCCCCCCH		37.6619608861
307PhosphorylationEGKPINLSHREDLAY
CCCCCCCCCHHHHHH		18.9328674419
314PhosphorylationSHREDLAYMNHIMVS
CCHHHHHHCCCEEEE		13.0222817900
321PhosphorylationYMNHIMVSVSPPEEH
HCCCEEEECCCCHHH		10.2530266825
323PhosphorylationNHIMVSVSPPEEHAM
CCEEEECCCCHHHCC		27.5130266825
384UbiquitinationARLWGNHKNRTNMTY
HHHHCCCCCCCCCCH		52.72-
393UbiquitinationRTNMTYEKMSRALRH
CCCCCHHHHHHHHHH		31.59-
395PhosphorylationNMTYEKMSRALRHYY
CCCHHHHHHHHHHHH		26.0124719451
401PhosphorylationMSRALRHYYKLNIIR
HHHHHHHHHHHCEEE		8.8922817900
402PhosphorylationSRALRHYYKLNIIRK
HHHHHHHHHHCEEEC		11.6822817900
403SumoylationRALRHYYKLNIIRKE
HHHHHHHHHCEEECC		28.0828112733
403UbiquitinationRALRHYYKLNIIRKE
HHHHHHHHHCEEECC		28.08-
421SumoylationRLLFRFMKTPDEIMS
EEEEEECCCHHHHHC		54.95-
421SumoylationRLLFRFMKTPDEIMS
EEEEEECCCHHHHHC		54.9528112733
421UbiquitinationRLLFRFMKTPDEIMS
EEEEEECCCHHHHHC		54.95-
422PhosphorylationLLFRFMKTPDEIMSG
EEEEECCCHHHHHCC		24.9628450419
431PhosphorylationDEIMSGRTDRLEHLE
HHHHCCCCHHHHHHH		29.0627251275
439PhosphorylationDRLEHLESQELDEQI
HHHHHHHHHHHHHHH		35.0030108239
447PhosphorylationQELDEQIYQEDEC--
HHHHHHHHHHHCC--		12.9228796482
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
17YPhosphorylationKinasePDGFRBP09619
PSP
22SPhosphorylationKinaseMAPK14Q16539
GPS
27YPhosphorylationKinasePDGFRBP09619
PSP
213SPhosphorylationKinaseMAPK3P27361
GPS
257SPhosphorylationKinaseMAPK3P27361
GPS
257SPhosphorylationKinaseP38AQ16539
PSP
-KUbiquitinationE3 ubiquitin ligaseICP0P08393
PMID:32416261
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
257SPhosphorylation

12435397
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 ETV6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GAB2_HUMANGAB2physical
15143164
ETV6_HUMANETV6physical
9695962
GRB2_HUMANGRB2physical
15143164
CRKL_HUMANCRKLphysical
15143164
ACTS_HUMANACTA1physical
9695962
KAT5_HUMANKAT5physical
12737628
FLI1_HUMANFLI1physical
9651344
ETV6_HUMANETV6physical
9651344
FBXL6_HUMANFBXL6physical
18426905
LMBL1_HUMANL3MBTL1physical
12588862
SIN3A_HUMANSIN3Aphysical
11439334
HDAC3_HUMANHDAC3physical
11439334
NCOR1_HUMANNCOR1physical
11001911
UBC9_HUMANUBE2Iphysical
10377438
SUMO1_HUMANSUMO1physical
11078523
SOCS1_HUMANSOCS1physical
11314018
ETV6_HUMANETV6physical
12626745
AP1M1_HUMANAP1M1physical
25416956
NTAQ1_HUMANWDYHV1physical
25416956
LRP6_HUMANLRP6physical
26186194
LRP5_HUMANLRP5physical
26186194
NID2_HUMANNID2physical
26186194
NID2_HUMANNID2physical
28514442
LRP5_HUMANLRP5physical
28514442
LRP6_HUMANLRP6physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
Note=A chromosomal aberration involving ETV6 is found in a form of chronic myelomonocytic leukemia (CMML). Translocation t(5
12)(q33
p13) with PDGFRB. It is characterized by abnormal clonal myeloid proliferation and by progression to acute myelogenous leukemia (AML).
131440
601626Leukemia, acute myelogenous (AML)
Note=A chromosomal aberration involving ETV6 is found in acute lymphoblastic leukemia. Translocation t(9
12)(p13
p13) with PAX5.
616216
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ETV6_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 LYS-11 AND LYS-302, AND MASSSPECTROMETRY.
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-16; THR-18 AND SER-22,AND MASS SPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; SER-22 AND SER-213,AND MASS SPECTROMETRY.
"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 THR-18 AND SER-22, AND MASSSPECTROMETRY.
"Functional regulation of TEL by p38-induced phosphorylation.";
Arai H., Maki K., Waga K., Sasaki K., Nakamura Y., Imai Y.,Kurokawa M., Hirai H., Mitani K.;
Biochem. Biophys. Res. Commun. 299:116-125(2002).
Cited for: PHOSPHORYLATION AT SER-22 AND SER-257, AND MUTAGENESIS OF SER-213;SER-238 AND SER-257.

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