dbPTM

ETV4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ETV4_HUMAN
UniProt AC	P43268
Protein Name	ETS translocation variant 4
Gene Name	ETV4
Organism	Homo sapiens (Human).
Sequence Length	484
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'..
Protein Sequence	MERRMKAGYLDQQVPYTFSSKSPGNGSLREALIGPLGKLMDPGSLPPLDSEDLFQDLSHFQETWLAEAQVPDSDEQFVPDFHSENLAFHSPTTRIKKEPQSPRTDPALSCSRKPPLPYHHGEQCLYSSAYDPPRQIAIKSPAPGALGQSPLQPFPRAEQRNFLRSSGTSQPHPGHGYLGEHSSVFQQPLDICHSFTSQGGGREPLPAPYQHQLSEPCPPYPQQSFKQEYHDPLYEQAGQPAVDQGGVNGHRYPGAGVVIKQEQTDFAYDSDVTGCASMYLHTEGFSGPSPGDGAMGYGYEKPLRPFPDDVCVVPEKFEGDIKQEGVGAFREGPPYQRRGALQLWQFLVALLDDPTNAHFIAWTGRGMEFKLIEPEEVARLWGIQKNRPAMNYDKLSRSLRYYYEKGIMQKVAGERYVYKFVCEPEALFSLAFPDNQRPALKAEFDRPVSEEDTVPLSHLDESPAYLPELAGPAQPFGPKGGYSY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Acetylation	--MERRMKAGYLDQQ --CCCCCCCCCCCCC	36.53	21543453
6	Sumoylation	--MERRMKAGYLDQQ --CCCCCCCCCCCCC	36.53	28112733
16	Phosphorylation	YLDQQVPYTFSSKSP CCCCCCCCEECCCCC	22.89	23312004
17	Phosphorylation	LDQQVPYTFSSKSPG CCCCCCCEECCCCCC	15.80	23312004
19	Phosphorylation	QQVPYTFSSKSPGNG CCCCCEECCCCCCCC	29.11	23312004
20	Phosphorylation	QVPYTFSSKSPGNGS CCCCEECCCCCCCCC	32.72	23312004
21	Acetylation	VPYTFSSKSPGNGSL CCCEECCCCCCCCCH	60.51	21543453
22	Phosphorylation	PYTFSSKSPGNGSLR CCEECCCCCCCCCHH	39.73	23312004
27	Phosphorylation	SKSPGNGSLREALIG CCCCCCCCHHHHHCC	28.40	23312004
38	Acetylation	ALIGPLGKLMDPGSL HHCCCHHHHCCCCCC	48.60	21543453
58	Ubiquitination	EDLFQDLSHFQETWL HHHHHCHHHHHHHHH	30.46	22505724
73	Phosphorylation	AEAQVPDSDEQFVPD HHCCCCCCCCCCCCC	36.66	-
96	Sumoylation	HSPTTRIKKEPQSPR CCCCCCCCCCCCCCC	48.03	28112733
96	Acetylation	HSPTTRIKKEPQSPR CCCCCCCCCCCCCCC	48.03	21543453
96	Ubiquitination	HSPTTRIKKEPQSPR CCCCCCCCCCCCCCC	48.03	PubMed
96	Sumoylation	HSPTTRIKKEPQSPR CCCCCCCCCCCCCCC	48.03	-
97	Ubiquitination	SPTTRIKKEPQSPRT CCCCCCCCCCCCCCC	72.72	22505724
101	Phosphorylation	RIKKEPQSPRTDPAL CCCCCCCCCCCCCCC	27.37	19307308
104	Phosphorylation	KEPQSPRTDPALSCS CCCCCCCCCCCCCCC	50.12	23312004
109	Phosphorylation	PRTDPALSCSRKPPL CCCCCCCCCCCCCCC	16.50	23312004
113	Acetylation	PALSCSRKPPLPYHH CCCCCCCCCCCCCCC	34.39	21543453
139	Acetylation	PPRQIAIKSPAPGAL CCCEEEEECCCCCCC	41.17	21543453
140	Phosphorylation	PRQIAIKSPAPGALG CCEEEEECCCCCCCC	21.85	25159151
149	Phosphorylation	APGALGQSPLQPFPR CCCCCCCCCCCCCCH	26.27	25159151
214	Phosphorylation	APYQHQLSEPCPPYP CCCCCCCCCCCCCCC	32.68	-
226	Sumoylation	PYPQQSFKQEYHDPL CCCCCCHHHHHCCHH	47.68	-
226	Sumoylation	PYPQQSFKQEYHDPL CCCCCCHHHHHCCHH	47.68	25755297
226	Ubiquitination	PYPQQSFKQEYHDPL CCCCCCHHHHHCCHH	47.68	PubMed
260	Sumoylation	PGAGVVIKQEQTDFA CCCEEEEEECCCCCC	35.85	-
260	Acetylation	PGAGVVIKQEQTDFA CCCEEEEEECCCCCC	35.85	21543453
260	Sumoylation	PGAGVVIKQEQTDFA CCCEEEEEECCCCCC	35.85	-
260	Ubiquitination	PGAGVVIKQEQTDFA CCCEEEEEECCCCCC	35.85	PubMed
301	Acetylation	AMGYGYEKPLRPFPD CCCCCCCCCCCCCCC	40.65	21543453
316	Acetylation	DVCVVPEKFEGDIKQ CEEECCCCCCCCCCC	42.52	21543453
322	Sumoylation	EKFEGDIKQEGVGAF CCCCCCCCCCCCCCH	47.22	-
322	Sumoylation	EKFEGDIKQEGVGAF CCCCCCCCCCCCCCH	47.22	-
392	Phosphorylation	KNRPAMNYDKLSRSL CCCCCCCHHHHHHHH	11.02	26657352
396	Phosphorylation	AMNYDKLSRSLRYYY CCCHHHHHHHHHHHH	26.09	26657352
398	Phosphorylation	NYDKLSRSLRYYYEK CHHHHHHHHHHHHHH	17.52	25954137
416	Phosphorylation	QKVAGERYVYKFVCE HHHCCCCEEEEEEEC	12.11	-
441	Acetylation	DNQRPALKAEFDRPV CCCCCCCCCCCCCCC	48.23	21543453
441	Sumoylation	DNQRPALKAEFDRPV CCCCCCCCCCCCCCC	48.23	-
449	Phosphorylation	AEFDRPVSEEDTVPL CCCCCCCCHHHCCCH	37.64	23898821

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	P78317	PMID:19307308
-	K	Ubiquitination	E3 ubiquitin ligase	COP1	Q8NHY2	PMID:20062082

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
96	K	Phosphorylation	19307308
Sumoylation at Lys-96 probably requires phosphorylation at Ser-101.
96	K	Sumoylation	19307308
Sumoylation at Lys-96 probably requires phosphorylation at Ser-101.
101	S	Phosphorylation	19307308
Sumoylation at Lys-96 probably requires phosphorylation at Ser-101.
101	S	Sumoylation	19307308
Sumoylation at Lys-96 probably requires phosphorylation at Ser-101.

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 ETV4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HXD4_HUMAN	HOXD4	physical	20211142
A4_HUMAN	APP	physical	21832049
STK11_HUMAN	STK11	physical	21150337
STK11_HUMAN	STK11	physical	16912160
JUN_HUMAN	JUN	physical	16786139
CARM1_HUMAN	CARM1	physical	28514442

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 ETV4_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-140 AND SER-149, ANDMASS SPECTROMETRY.	18669648 [Abstract]
Sumoylation
Reference	PubMed
"Extracellular signal-regulated kinase mitogen-activated proteinkinase signaling initiates a dynamic interplay between sumoylation andubiquitination to regulate the activity of the transcriptionalactivator PEA3."; Guo B., Sharrocks A.D.; Mol. Cell. Biol. 29:3204-3218(2009). Cited for: FUNCTION, SUMOYLATION AT LYS-96; LYS-226 AND LYS-260, DESUMOYLATION BYSENP1, UBIQUITINATION BY RNF4, DEUBIQUITINATION BY UPS2, ANDMUTAGENESIS OF LYS-96; GLU-98; SER-101; PRO-102; LYS-226; GLU-228;LYS-260; GLU-262; GLU-324 AND GLU-443.	19307308 [Abstract]

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