dbPTM

EDF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EDF1_HUMAN
UniProt AC	O60869
Protein Name	Endothelial differentiation-related factor 1
Gene Name	EDF1
Organism	Homo sapiens (Human).
Sequence Length	148
Subcellular Localization	Cytoplasm. Nucleus. Also nuclear upon binding to NR5A1 and treatment of cells with TPA or forskolin.
Protein Description	Transcriptional coactivator stimulating NR5A1 and ligand-dependent NR1H3/LXRA and PPARG transcriptional activities. Enhances the DNA-binding activity of ATF1, ATF2, CREB1 and NR5A1. Regulates nitric oxid synthase activity probably by sequestering calmodulin in the cytoplasm. May function in endothelial cells differentiation, hormone-induced cardiomyocytes hypertrophy and lipid metabolism..
Protein Sequence	MAESDWDTVTVLRKKGPTAAQAKSKQAILAAQRRGEDVETSKKWAAGQNKQHSITKNTAKLDRETEELHHDRVTLEVGKVIQQGRQSKGLTQKDLATKINEKPQVIADYESGRAIPNNQVLGKIERAIGLKLRGKDIGKPIEKGPRAK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAESDWDTV ------CCCCCCCCC	25.63	22223895
4 (in isoform 2)	Phosphorylation	-	34.17	-
4	Phosphorylation	----MAESDWDTVTV ----CCCCCCCCCHH	34.17	25159151
8	Phosphorylation	MAESDWDTVTVLRKK CCCCCCCCCHHHHHH	17.52	22496350
10	Phosphorylation	ESDWDTVTVLRKKGP CCCCCCCHHHHHHCC	18.86	29514088
13	Methylation	WDTVTVLRKKGPTAA CCCCHHHHHHCCCHH	34.01	-
15	Ubiquitination	TVTVLRKKGPTAAQA CCHHHHHHCCCHHHH	64.78	24816145
23	Ubiquitination	GPTAAQAKSKQAILA CCCHHHHHHHHHHHH	46.21	29967540
25	Ubiquitination	TAAQAKSKQAILAAQ CHHHHHHHHHHHHHH	42.94	32015554
25	2-Hydroxyisobutyrylation	TAAQAKSKQAILAAQ CHHHHHHHHHHHHHH	42.94	-
25	Methylation	TAAQAKSKQAILAAQ CHHHHHHHHHHHHHH	42.94	24129315
25	Malonylation	TAAQAKSKQAILAAQ CHHHHHHHHHHHHHH	42.94	26320211
40	Phosphorylation	RRGEDVETSKKWAAG HCCCCHHHHHHHHCC	45.77	26074081
41	Phosphorylation	RGEDVETSKKWAAGQ CCCCHHHHHHHHCCC	20.80	26074081
42	Ubiquitination	GEDVETSKKWAAGQN CCCHHHHHHHHCCCC	60.81	33845483
42	Acetylation	GEDVETSKKWAAGQN CCCHHHHHHHHCCCC	60.81	30588345
50	2-Hydroxyisobutyrylation	KWAAGQNKQHSITKN HHHCCCCCCCCCCCC	41.31	-
50	Ubiquitination	KWAAGQNKQHSITKN HHHCCCCCCCCCCCC	41.31	29967540
50	Acetylation	KWAAGQNKQHSITKN HHHCCCCCCCCCCCC	41.31	25953088
53 (in isoform 2)	Phosphorylation	-	29.47	-
53	Phosphorylation	AGQNKQHSITKNTAK CCCCCCCCCCCCCHH	29.47	28674151
55	Phosphorylation	QNKQHSITKNTAKLD CCCCCCCCCCCHHCC	22.66	20068231
58	Phosphorylation	QHSITKNTAKLDRET CCCCCCCCHHCCHHH	27.07	26074081
60	Acetylation	SITKNTAKLDRETEE CCCCCCHHCCHHHHH	49.21	25953088
65	Phosphorylation	TAKLDRETEELHHDR CHHCCHHHHHHCCCC	35.34	28555341
72	Methylation	TEELHHDRVTLEVGK HHHHCCCCCHHHHHH	20.97	-
74 (in isoform 2)	Phosphorylation	-	20.35	-
74	Phosphorylation	ELHHDRVTLEVGKVI HHCCCCCHHHHHHHH	20.35	20068231
79	Ubiquitination	RVTLEVGKVIQQGRQ CCHHHHHHHHHHHHH	41.14	23000965
79	Acetylation	RVTLEVGKVIQQGRQ CCHHHHHHHHHHHHH	41.14	26051181
81	Ubiquitination	TLEVGKVIQQGRQSK HHHHHHHHHHHHHCC	2.63	20972266
84	Ubiquitination	VGKVIQQGRQSKGLT HHHHHHHHHHCCCCC	17.14	20972266
91	Phosphorylation	GRQSKGLTQKDLATK HHHCCCCCHHHHHHH	42.09	10816571
91 (in isoform 2)	Phosphorylation	-	42.09	-
93	Malonylation	QSKGLTQKDLATKIN HCCCCCHHHHHHHHC	49.85	26320211
93	Ubiquitination	QSKGLTQKDLATKIN HCCCCCHHHHHHHHC	49.85	33845483
93	Acetylation	QSKGLTQKDLATKIN HCCCCCHHHHHHHHC	49.85	23749302
97	Phosphorylation	LTQKDLATKINEKPQ CCHHHHHHHHCCCCC	39.49	24719451
98	Acetylation	TQKDLATKINEKPQV CHHHHHHHHCCCCCE	37.62	25953088
98	2-Hydroxyisobutyrylation	TQKDLATKINEKPQV CHHHHHHHHCCCCCE	37.62	-
98	Malonylation	TQKDLATKINEKPQV CHHHHHHHHCCCCCE	37.62	26320211
98	Ubiquitination	TQKDLATKINEKPQV CHHHHHHHHCCCCCE	37.62	22817900
102 (in isoform 1)	Ubiquitination	-	35.94	21890473
102	2-Hydroxyisobutyrylation	LATKINEKPQVIADY HHHHHCCCCCEEEEC	35.94	-
102 (in isoform 2)	Ubiquitination	-	35.94	21906983
102	Ubiquitination	LATKINEKPQVIADY HHHHHCCCCCEEEEC	35.94	22817900
102	Acetylation	LATKINEKPQVIADY HHHHHCCCCCEEEEC	35.94	26051181
105	Acetylation	KINEKPQVIADYESG HHCCCCCEEEECCCC	5.45	19608861
105	Ubiquitination	KINEKPQVIADYESG HHCCCCCEEEECCCC	5.45	32015554
109	Phosphorylation	KPQVIADYESGRAIP CCCEEEECCCCCCCC	11.72	28796482
111	Phosphorylation	QVIADYESGRAIPNN CEEEECCCCCCCCCC	27.61	28796482
114	Ubiquitination	ADYESGRAIPNNQVL EECCCCCCCCCCCHH	25.72	24816145
117	Ubiquitination	ESGRAIPNNQVLGKI CCCCCCCCCCHHHHH	45.51	24816145
118	Ubiquitination	SGRAIPNNQVLGKIE CCCCCCCCCHHHHHH	28.16	23000965
121	Ubiquitination	AIPNNQVLGKIERAI CCCCCCHHHHHHHHH	4.10	23000965
122	Ubiquitination	IPNNQVLGKIERAIG CCCCCHHHHHHHHHC	30.00	23000965
123	Acetylation	PNNQVLGKIERAIGL CCCCHHHHHHHHHCC	36.91	23954790
123	Ubiquitination	PNNQVLGKIERAIGL CCCCHHHHHHHHHCC	36.91	32015554
123 (in isoform 2)	Acetylation	-	36.91	-
125	Ubiquitination	NQVLGKIERAIGLKL CCHHHHHHHHHCCEE	39.27	23000965
127	Ubiquitination	VLGKIERAIGLKLRG HHHHHHHHHCCEECC	6.34	23000965
130	Ubiquitination	KIERAIGLKLRGKDI HHHHHHCCEECCCCC	3.74	23000965
131	Acetylation	IERAIGLKLRGKDIG HHHHHCCEECCCCCC	30.81	25953088
131	Ubiquitination	IERAIGLKLRGKDIG HHHHHCCEECCCCCC	30.81	-
131	Malonylation	IERAIGLKLRGKDIG HHHHHCCEECCCCCC	30.81	26320211
135	Ubiquitination	IGLKLRGKDIGKPIE HCCEECCCCCCCCCC	39.47	24816145
135	Acetylation	IGLKLRGKDIGKPIE HCCEECCCCCCCCCC	39.47	26051181
139	Ubiquitination	LRGKDIGKPIEKGPR ECCCCCCCCCCCCCC	43.06	23000965
143 (in isoform 1)	Ubiquitination	-	74.96	21890473
143	Acetylation	DIGKPIEKGPRAK-- CCCCCCCCCCCCC--	74.96	25953088
143	Ubiquitination	DIGKPIEKGPRAK-- CCCCCCCCCCCCC--	74.96	23000965
148	Ubiquitination	IEKGPRAK------- CCCCCCCC-------	63.25	23000965

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
Oops, there are no upstream regulatory protein records of EDF1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EDF1_HUMAN !!

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 EDF1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NR5A2_HUMAN	NR5A2	physical	12040021
NR1H3_HUMAN	NR1H3	physical	12040021
PPARG_HUMAN	PPARG	physical	12040021
RXRA_HUMAN	RXRA	physical	12040021
TBP_HUMAN	TBP	physical	12040021
TBP_HUMAN	TBP	physical	10816571
TBP_HUMAN	TBP	physical	10567391
STF1_HUMAN	NR5A1	physical	10567391
NRL_HUMAN	NRL	physical	16880509
JUN_HUMAN	JUN	physical	16880509
CEBPA_HUMAN	CEBPA	physical	16880509
IDH3G_HUMAN	IDH3G	physical	22939629
DNJB1_HUMAN	DNAJB1	physical	26344197
HNRPF_HUMAN	HNRNPF	physical	26344197

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 EDF1_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-4, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-123, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-4, AND MASS SPECTROMETRY.	19413330 [Abstract]