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Protein Page:
Tel (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
Tel Transcriptional repressor; binds to the DNA sequence 5'- CCGGAAGT-3'. 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). Chromosomal aberrations involving ETV6 are found in a form of acute myeloid leukemia (AML). Translocation t(12;22)(p13;q11) with MN1; translocation t(4;12)(q12;p13) with CHIC2. Chromosomal aberrations involving ETV6 are found in childhood acute lymphoblastic leukemia (ALL). Translocations t(12;21)(p12;q22) and t(12;21)(p13;q22) with RUNX1/AML1. A chromosomal aberration involving ETV6 is found in a form of pre-B acute myeloid leukemia. Translocation t(9;12)(p24;p13) with JAK2. A chromosomal aberration involving ETV6 is found in myelodysplastic syndrome (MDS) with basophilia. Translocation t(5;12)(q31;p13) with ACSL6. A chromosomal aberration involving ETV6 is found in acute eosinophilic leukemia (AEL). Translocation t(5;12)(q31;p13) with ACSL6. A chromosomal aberration involving ETV6 is found in myelodysplastic syndrome (MDS). Translocation t(1;12)(p36.1;p13) with MDS2. Defects in ETV6 are a cause of myeloproliferative disorder chronic with eosinophilia (MPE). A hematologic disorder characterized by malignant eosinophils proliferation. A chromosomal aberration involving ETV6 is found in many instances of myeloproliferative disorder chronic with eosinophilia. Translocation t(5;12) with PDGFRB on chromosome 5 creating an ETV6-PDGFRB fusion protein. Defects in ETV6 are a cause of acute myelogenous leukemia (AML). AML is a malignant disease in which hematopoietic precursors are arrested in an early stage of development. A chromosomal aberration involving ETV6 is found in acute lymphoblastic leukemia. Translocation t(9;12)(p13;p13) with PAX5. Belongs to the ETS family. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Transcription factor; DNA binding protein
Cellular Component: cytoplasm; nucleolus
Molecular Function: protein domain specific binding; protein binding; transcription factor activity
Biological Process: regulation of transcription from RNA polymerase II promoter; transcription from RNA polymerase II promoter; negative regulation of transcription from RNA polymerase II promoter; cell differentiation
Reference #:  P41212 (UniProtKB)
Alt. Names/Synonyms: ETS translocation variant 6; ets variant 6; ets variant gene 6 (TEL oncogene); ETS-related protein Tel1; ETV6; ETV6-NTRK3 fusion partner; TEL; TEL/ABL; TEL1; TEL1 oncogene; Transcription factor ETV6
Gene Symbols: ETV6
Molecular weight: 53,000 Da
Basal Isoelectric point: 6.95  Predict pI for various phosphorylation states
Select Structure to View Below

Tel

Protein Structure Not Found.


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Sites Implicated In
cell differentiation, altered: S213‑p, S257‑p
cell growth, altered: S213‑p, S257‑p
transcription, induced: K99‑sm, S257‑p
transcription, inhibited: S213‑p, S257‑p
activity, induced: Y314‑p
activity, inhibited: S213‑p, S257‑p
intracellular localization: K99‑sm, S257‑p
molecular association, regulation: S213‑p, S257‑p, Y314‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T4-p ____MSEtPAQCSIk
0 1 K11-ac tPAQCSIkQERIsyt
1 0 K11-sm tPAQCSIkQERIsyt
0 10 S16-p SIkQERIsytPPEsP
1 13 Y17-p IkQERIsytPPEsPV
0 53 T18-p kQERIsytPPEsPVP
1 122 S22-p IsytPPEsPVPsyAs
0 3 S26-p PPEsPVPsyAsstPL
1 9 Y27-p PEsPVPsyAsstPLH
0 6 S29-p sPVPsyAsstPLHVP
0 5 S30-p PVPsyAsstPLHVPV
0 21 T31-p VPsyAsstPLHVPVP
0 3 Y60-p HLRLQPIyWSRDDVA
2 0 K99-sm KALLLLTkEDFRYRS
0 2 Y114 PHSGDVLYELLQHIL
0 8 S131-p RKPRILFsPFFHPGN
0 1 T142-p HPGNSIHtQPEVILH
0 1 T161-p EDNCVQRtPRPSVDN
0 2 P164 CVQRtPRPSVDNVHH
0 3 S182-p TIELLHRsRsPIttN
0 17 S184-p ELLHRsRsPIttNHR
0 3 T187-p HRsRsPIttNHRPsP
0 2 T188-p RsRsPIttNHRPsPD
0 26 S193-p IttNHRPsPDPEQRP
0 11 S203-p PEQRPLRsPLDNMIR
1 20 S213-p DNMIRRLsPAERAQG
0 3 Y233 ENNHQESYPLSVSPM
0 3 S236 HQESYPLSVSPMENN
0 13 S238 ESYPLSVSPMENNHC
0 2 S256 SESHPKPSsPRQEST
3 1 S257-p ESHPKPSsPRQESTR
0 8 S271-p RVIQLMPsPIMHPLI
0 1 S284-p LILNPRHsVDFKQSR
0 1 S293-p DFKQSRLsEDGLHRE
0 1 K302-ac DGLHREGkPINLSHR
1 1 Y314-p SHREDLAyMNHIMVS
0 2 S323-p NHIMVSVsPPEEHAM
0 1 Y346 RLLWDYVYQLLSDSR
0 3 Y401-p MSRALRHyyKLNIIR
0 3 Y402-p SRALRHyyKLNIIRK
0 7 Y447-p QELDEQIyQEDEC__
0 2 - gap
  mouse

 
T4 ____MSETPAQSSIK
K11 TPAQSSIKQERIsyt
K11 TPAQSSIKQERIsyt
S16-p SIKQERIsytPPEsP
Y17-p IKQERIsytPPEsPV
T18-p KQERIsytPPEsPVA
S22-p IsytPPEsPVASHRS
S26 PPEsPVASHRSstPL
H27 PEsPVASHRSstPLH
S29 sPVASHRSstPLHVH
S30-p PVASHRSstPLHVHT
T31-p VASHRSstPLHVHTV
Y61-p HLRLQPIyWSRDDVA
K100 KALLLLTKEDFRYRS
Y115-p PHSGDVLyELLQHIL
S132 RKSRMLFSPFFPPGD
T143 PPGDSIHTKPEVLLH
T162 EDNCVQRTPRtPAES
T165-p CVQRTPRtPAESVHH
P183 TIELLHRPRsPIttN
S185-p ELLHRPRsPIttNHR
T188-p HRPRsPIttNHRPsP
T189-p RPRsPIttNHRPsPD
S194-p IttNHRPsPDPEQQR
S205-p EQQRPQRsPLDNMSR
S215-p DNMSRRLsPVEKAQG
Y235-p ENNHQETyPLsVsPV
S238-p HQETyPLsVsPVENN
S240-p ETyPLsVsPVENNHC
S250-p ENNHCLPssPWQEST
S251-p NNHCLPssPWQESTR
S265-p RVIQLMPsPIMHPLI
S280 LNPRHSHSVDFKQSR
S289 DFKQSRHSEDGMNRE
K298 DGMNREGKPINLSHR
Y310 SHREDLAYLNHIMVS
S319-p NHIMVSMsPPEEHAM
Y342-p RLLWDYVyQLLSDSR
Y397-p MSRALRHyyKLNIIR
Y398-p SRALRHyyKLNIIRK
Y443-p QVLDEQTyQEDEPTI
S452-p EDEPTIAsPVGWPRG
  rat

 
T4 ____MSETPAQCSIK
K11 TPAQCSIKQERISSt
K11 TPAQCSIKQERISSt
S16 SIKQERISStPPEsP
S17 IKQERISStPPEsPV
T18-p KQERISStPPEsPVA
S22-p ISStPPEsPVASYGP
S26 PPEsPVASYGPSTPL
Y27 PEsPVASYGPSTPLH
P29 sPVASYGPSTPLHVP
S30 PVASYGPSTPLHVPV
T31 VASYGPSTPLHVPVP
Y60 HLRLQPIYWSRDDVA
K99 KALLLLTKEDFRYRS
Y114 PHSGDVLYELLQHIL
S131 RKPRILFSPFFHPGN
T142 HPGNSIHTKPEVLLH
T161 EDNCVQRTPRTPAES
T164 CVQRTPRTPAESLHH
P182 TIELLHRPRSPITTN
S184 ELLHRPRSPITTNHR
T187 HRPRSPITTNHRPsP
T188 RPRSPITTNHRPsPD
S193-p ITTNHRPsPDPEQQR
S204-p EQQRPLRsPLDNMIR
S214-p DNMIRRLsPAERAQG
Y234 ENNHQESYPLSVSPM
S237 HQESYPLSVSPMENN
S239 ESYPLSVSPMENNHC
S257 SESNPKPSsPWQEST
S258-p ESNPKPSsPWQESTR
S272 RVIQLMPSPIMHPLI
S285 LILNPRHSVDFKQSR
S294 DFKQSRISEDGMHRE
K303 DGMHREGKPINLSHR
Y315 SHREDLAYMNHIMVS
S324 NHIMVSVSPPEEHAM
Y347 RLLWDYVYQLLSDSR
Y402 MSRALRHYYKLNIIR
Y403 SRALRHYYKLNIIRK
Y448 QELDEQAYQEDEC__
- gap
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