ETV4_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ETV4_MOUSE
• UniProt AC: P28322
• Protein Name: ETS translocation variant 4
• Gene Name: Etv4
• Organism: Mus musculus (Mouse).
• Sequence Length: 485
• Subcellular Localization: Nucleus.
• Protein Description: Transcriptional activator that binds to the enhancer of the adenovirus E1A gene; the core-binding sequence is 5'[AC]GGA[AT]GT-3'. May play a regulatory role during embryogenesis..
• Protein Sequence: MERRMKGGYLDQRVPYTFCSKSPGNGSLGEALMVPQGKLMDPGSLPPSDSEDLFQDLSHFQETWLAEAQVPDSDEQFVPDFHSENSFHSPTTRIKKEPQSPRTDPALSCSRKPPLPYHHGEQCLYSSAYDSPRQIAIKSPAPGAPGQSPLQPFSRAEQQQSLLRASSSSQSHPGHGYLGEHSSVFQQPVDMCHSFTSPQGGGREPLPAPYQHQLSEPCPPYPQQNFKQEYHDPLYEQAGQPASSQGGVSGHRYPGAGVVIKQERTDFAYDSDVPGCASMYLHPEGFSGPSPGDGVMGYGYEKSLRPFPDDVCIVPEKFEGDIKQEGIGAFREGPPYQRRGALQLWQFLVALLDDPTNAHFIAWTGRGMEFKLIEPEEVARLWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKFVCEPEALFSLAFPDNQRPALKAEFDRPVSEEDTVPLSHLDESPAYLPELTGPAPPFGHRGGYSY

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
6	Acetylation	--MERRMKGGYLDQR --CCCCCCCCCCCCC	37.17	52746415
21	Acetylation	VPYTFCSKSPGNGSL CCCEEECCCCCCCCC	18.79	52746413
38	Acetylation	ALMVPQGKLMDPGSL EEEECCCCCCCCCCC	5.43	52746425
95	Acetylation	HSPTTRIKKEPQSPR CCCCCCCCCCCCCCC	31.79	52746401
95	Sumoylation	HSPTTRIKKEPQSPR CCCCCCCCCCCCCCC	31.79	-
100	Phosphorylation	RIKKEPQSPRTDPAL CCCCCCCCCCCCCCC	40.02	-
112	Acetylation	PALSCSRKPPLPYHH CCCCCCCCCCCCCCC	20.99	52746411
138	Acetylation	SPRQIAIKSPAPGAP CCCEEEECCCCCCCC	18.26	52746421
139	Phosphorylation	PRQIAIKSPAPGAPG CCEEEECCCCCCCCC	7.88	22006019
148	Phosphorylation	APGAPGQSPLQPFSR CCCCCCCCCCCCCCH	36.66	22006019
171	Sumoylation	RASSSSQSHPGHGYL HHCCCCCCCCCCCCC	48.03	-
215	Phosphorylation	APYQHQLSEPCPPYP CCCCCCCCCCCCCCC	47.47	-
227	Sumoylation	PYPQQNFKQEYHDPL CCCCCCHHHHHCCHH	48.05	-
261	Acetylation	PGAGVVIKQERTDFA CCCEEEEEEECCCCC	1.95	52746405
261	Sumoylation	PGAGVVIKQERTDFA CCCEEEEEEECCCCC	1.95	-
297	Sumoylation	SPGDGVMGYGYEKSL CCCCCCCCCCCCCCC	50.17	-
302	Acetylation	VMGYGYEKSLRPFPD CCCCCCCCCCCCCCC	33.72	52746417
317	Acetylation	DVCIVPEKFEGDIKQ CEEECCCCCCCCCCC	11.63	52746419
331	Sumoylation	QEGIGAFREGPPYQR CCCCCCCCCCCCCCH	34.20	-
386	Acetylation	ARLWGIQKNRPAMNY HHHHCCCCCCCCCCH	60.23	6568549
393	Sumoylation	KNRPAMNYDKLSRSL CCCCCCCHHHHHHHH	47.22	-
442	Acetylation	DNQRPALKAEFDRPV CCCCCCCCCCCCCCC	6.95	52746423

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
-	K	Ubiquitination	E3 ubiquitin ligase	Rnf4	Q9QZS2	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
95	K	Phosphorylation	Sumoylation at Lys-95 probably requires phosphorylation at Ser-100.	-
95	K	Sumoylation	Sumoylation at Lys-95 probably requires phosphorylation at Ser-100.	-
100	S	Phosphorylation	Sumoylation at Lys-95 probably requires phosphorylation at Ser-100.	-
100	S	Sumoylation	Sumoylation at Lys-95 probably requires phosphorylation at Ser-100.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ETV4_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of ETV4_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.