ETV1_HUMAN - dbPTM
ETV1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ETV1_HUMAN
UniProt AC P50549
Protein Name ETS translocation variant 1
Gene Name ETV1
Organism Homo sapiens (Human).
Sequence Length 477
Subcellular Localization Nucleus .
Protein Description Transcriptional activator that binds to DNA sequences containing the consensus pentanucleotide 5'-CGGA[AT]-3'..
Protein Sequence MDGFYDQQVPYMVTNSQRGRNCNEKPTNVRKRKFINRDLAHDSEELFQDLSQLQETWLAEAQVPDNDEQFVPDYQAESLAFHGLPLKIKKEPHSPCSEISSACSQEQPFKFSYGEKCLYNVSAYDQKPQVGMRPSNPPTPSSTPVSPLHHASPNSTHTPKPDRAFPAHLPPSQSIPDSSYPMDHRFRRQLSEPCNSFPPLPTMPREGRPMYQRQMSEPNIPFPPQGFKQEYHDPVYEHNTMVGSAASQSFPPPLMIKQEPRDFAYDSEVPSCHSIYMRQEGFLAHPSRTEGCMFEKGPRQFYDDTCVVPEKFDGDIKQEPGMYREGPTYQRRGSLQLWQFLVALLDDPSNSHFIAWTGRGMEFKLIEPEEVARRWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKFVCDPEALFSMAFPDNQRPLLKTDMERHINEEDTVPLSHFDESMAYMPEGGCCNPHPYNEGYVY
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
5Phosphorylation---MDGFYDQQVPYM
---CCCCCCCCCCEE
20.55-
33AcetylationPTNVRKRKFINRDLA
CCCHHHHHHCCCCCC
54.3412917345
58AcetylationSQLQETWLAEAQVPD
HHHHHHHHHHCCCCC
3.9412917345
89SumoylationHGLPLKIKKEPHSPC
CCCCCEECCCCCCCH
49.88-
94PhosphorylationKIKKEPHSPCSEISS
EECCCCCCCHHHHHH
38.0125850435
97PhosphorylationKEPHSPCSEISSACS
CCCCCCHHHHHHHHC
41.1525850435
98AcetylationEPHSPCSEISSACSQ
CCCCCHHHHHHHHCC
54.3212917345
100PhosphorylationHSPCSEISSACSQEQ
CCCHHHHHHHHCCCC
14.0825002506
101PhosphorylationSPCSEISSACSQEQP
CCHHHHHHHHCCCCC
38.6725002506
104PhosphorylationSEISSACSQEQPFKF
HHHHHHHCCCCCCCC
36.1522210691
116AcetylationFKFSYGEKCLYNVSA
CCCCCCCEEEEEEEC
25.7712917345
139PhosphorylationMRPSNPPTPSSTPVS
CCCCCCCCCCCCCCC
36.7412917345
143PhosphorylationNPPTPSSTPVSPLHH
CCCCCCCCCCCCCCC
31.8612917345
146PhosphorylationTPSSTPVSPLHHASP
CCCCCCCCCCCCCCC
23.9712917345
191PhosphorylationHRFRRQLSEPCNSFP
HHHHHHHCCCHHCCC
31.0212569367
196PhosphorylationQLSEPCNSFPPLPTM
HHCCCHHCCCCCCCC
45.9427251275
216PhosphorylationPMYQRQMSEPNIPFP
CCCCCCCCCCCCCCC
41.3828112733
317SumoylationEKFDGDIKQEPGMYR
CCCCCCCCCCCCCCC
54.0428112733
334PhosphorylationPTYQRRGSLQLWQFL
CCCCCCCHHHHHHHH
15.9012569367
386PhosphorylationKNRPAMNYDKLSRSL
CCCCCCCHHHHHHHH
11.0226657352
390PhosphorylationAMNYDKLSRSLRYYY
CCCHHHHHHHHHHHH
26.0926657352
392PhosphorylationNYDKLSRSLRYYYEK
CHHHHHHHHHHHHHH
17.5225954137
410PhosphorylationQKVAGERYVYKFVCD
HHHCCCCEEEEEEEC
12.11-

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
191SPhosphorylationKinasePRKACAP17612
GPS
191SPhosphorylationKinaseKS6A1Q15418
PhosphoELM
191SPhosphorylationKinaseRPS6KA1Q63531
GPS
191SPhosphorylationKinaseRPS6KA5O75582
Uniprot
216SPhosphorylationKinasePRKACAP17612
GPS
216SPhosphorylationKinaseKS6A1Q15418
PhosphoELM
216SPhosphorylationKinaseRPS6KA1Q63531
GPS
216SPhosphorylationKinaseRPS6KA5O75582
Uniprot
334SPhosphorylationKinasePRKACAP00517
GPS
334SPhosphorylationKinasePKACAP17612
PSP
334SPhosphorylationKinaseKS6A1Q15418
PhosphoELM
334SPhosphorylationKinaseRPS6KA1Q63531
GPS
-KUbiquitinationE3 ubiquitin ligaseCOP1Q8NHY2
PMID:20062082

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
191SPhosphorylation

12213813
216SPhosphorylation

12213813

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 ETV1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KAT2B_HUMANKAT2Bphysical
12917345
NCOA3_HUMANNCOA3physical
14747462
STK40_HUMANSTK40physical
26186194
RFWD2_HUMANRFWD2physical
26186194
DET1_HUMANDET1physical
26186194
TERT_HUMANTERTgenetic
23284306
RFWD2_HUMANRFWD2physical
28514442
STK40_HUMANSTK40physical
28514442
DET1_HUMANDET1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612219Ewing sarcoma (ES)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ETV1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Regulation of the ER81 transcription factor and its coactivators bymitogen- and stress-activated protein kinase 1 (MSK1).";
Janknecht R.;
Oncogene 22:746-755(2003).
Cited for: PHOSPHORYLATION AT SER-191 AND SER-216, AND MUTAGENESIS OF SER-191 ANDSER-216.
"Regulation of the ETS transcription factor ER81 by the 90-kDaribosomal S6 kinase 1 and protein kinase A.";
Wu J., Janknecht R.;
J. Biol. Chem. 277:42669-42679(2002).
Cited for: PHOSPHORYLATION AT SER-191 AND SER-216.

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