Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Endothelial differentiation-related factor 1  

UniProtKB / Swiss-Prot ID :  EDF1_HUMAN

Gene Name (Synonyms) : 
EDF1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. Note=Also nuclear upon binding to NR5A1 and treatment of cells with TPA or forskolin. 

Protein Function :  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 MAESDWDTVTVLRKKGPTAAQAKSKQAILAAQRRGEDVETSKKWAAGQNKQHSITKNTAKLDRETEELHH...
Predicted Secondary Structure CCCCCCCCCEEECCCCCHHHHHHHHHHHHHHHHCCCCCCCCHHHCCCCCCCCCCCCHHHECCCCCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAESDW
---CCCCCC
25.63UniProtKB
Link-
4Phosphoserine-MAESDWDT
-CCCCCCCC
34.17HPRD
Link-
4Phosphoserine.-MAESDWDT
-CCCCCCCC
34.17UniProtKB
Link-
53PhosphoserineNKQHSITKN
CCCCCCCCH
29.47HPRD
Link-
53PhosphoserineNKQHSITKN
CCCCCCCCH
29.47Phosphositeplus
Link-
74PhosphothreonineHDRVTLEVG
CCCCCHHHH
20.35HPRD
Link
74PhosphothreonineHDRVTLEVG
CCCCCHHHH
20.35Phosphositeplus
Link
91Phosphothreonine (PRKCA)SKGLTQKDL
HCCCCHHHH
42.09HPRD
Link
102Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KINEKPQVI
HCCCCHHHH
35.94Phosphositeplus
Link
109PhosphotyrosineVIADYESGR
HHHHHHHCC
11.72Phosphositeplus
Link
123N6-acetyllysineQVLGKIERA
HHHHHHHHH
36.91HPRD
Link
123N6-acetyllysineQVLGKIERA
HHHHHHHHH
36.91Phosphositeplus
Link
123N6-acetyllysine.QVLGKIERA
HHHHHHHHH
36.91UniProtKB
Link
143Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KPIEKGPRA
CCCCCCCCC
74.96Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
STF1_HUMANcolocalizationEBI-874649
intact10567391
NR5A2_HUMANphysical interaction
physical interaction
EBI-781351
EBI-781466
intact12040021
12040021
PPARG_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
EBI-781497
EBI-781420
EBI-781
intact12040021
12040021
12040021
12040021
NR1H3_HUMANphysical interaction
physical interaction
physical interaction
physical interaction
EBI-781475
EBI-781379
EBI-781
intact12040021
12040021
12040021
12040021
RXRA_HUMANphysical interactionEBI-781426
intact12040021
CALM_HUMANin vitro
in vivo
HPRD:09235HPRD10816571
ATF1_HUMANin vitroHPRD:09235HPRD10567391
CREB1_HUMANin vitroHPRD:09235HPRD10567391
ATF2_HUMANin vitroHPRD:09235HPRD10567391
STF1_HUMANin vitro
in vivo
HPRD:09235HPRD10567391
RXRA_HUMANin vitroHPRD:09235HPRD12040021
TAF1_HUMANin vitroHPRD:09235HPRD12040021
TBP_HUMANin vivoHPRD:09235HPRD10816571
PPARG_HUMANin vitroHPRD:09235HPRD12040021
NR1H3_HUMANin vitroHPRD:09235HPRD12040021
TBP_HUMANENSP00000224073STRING
CALM_HUMANENSP00000224073STRING
NR1H3_HUMANENSP00000224073STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.
"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.
Phosphorylation
ReferencePubMed
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures