Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - O60869 (EDF1_HUMAN)

(max 400 entries)x

Your basket is currently empty. i

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Endothelial differentiation-related factor 1

Gene

EDF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.4 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi92 – 111H-T-H motifPROSITE-ProRule annotationAdd BLAST20

GO - Molecular functioni

  • calmodulin binding Source: UniProtKB-KW
  • RNA binding Source: UniProtKB
  • sequence-specific DNA binding Source: InterPro
  • transcription coactivator activity Source: UniProtKB
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • endothelial cell differentiation Source: UniProtKB
  • multicellular organism development Source: ProtInc
  • positive regulation of DNA binding Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of lipid metabolic process Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionActivator, Calmodulin-binding, Developmental protein, DNA-binding
Biological processDifferentiation, Transcription, Transcription regulation

Enzyme and pathway databases

SIGNORiO60869

Names & Taxonomyi

Protein namesi
Recommended name:
Endothelial differentiation-related factor 1
Short name:
EDF-1
Alternative name(s):
Multiprotein-bridging factor 1
Short name:
MBF1
Gene namesi
Name:EDF1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

EuPathDBiHostDB:ENSG00000107223.12
HGNCiHGNC:3164 EDF1
MIMi605107 gene
neXtProtiNX_O60869

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi40T → D: Loss of interaction with CALM; when associated with D-58; D-91 and D-111. 1 Publication1
Mutagenesisi58T → D: Loss of interaction with CALM; when associated with D-40; D-91 and D-111. 1 Publication1
Mutagenesisi65T → D: No effect on CALM-binding. No effect; when associated with D-74. 1 Publication1
Mutagenesisi74T → D: No effect on CALM-binding. No effect; when associated with D-65. 1 Publication1
Mutagenesisi87S → A: No effect on CALM-binding. 1 Publication1
Mutagenesisi87S → D: Loss of interaction with CALM and higher affinity for TBP. Same effect; when associated with D-65 and D-74. 1 Publication1
Mutagenesisi91T → A: No effect on CALM-binding. 1 Publication1
Mutagenesisi91T → D: Partial loss of interaction with CALM. Complete loss of interaction; when associated with D-40; D-58 and D-111. 1 Publication1
Mutagenesisi111S → D: Loss of interaction with CALM; when associated with D-40; D-58 and D-91. 1 Publication1

Organism-specific databases

DisGeNETi8721
OpenTargetsiENSG00000107223
PharmGKBiPA27604

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00001497952 – 148Endothelial differentiation-related factor 1Add BLAST147

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei4PhosphoserineCombined sources1
Modified residuei25N6-methyllysineCombined sources1

Post-translational modificationi

Phosphorylated (by PKA and PKC).2 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiO60869
MaxQBiO60869
PaxDbiO60869
PeptideAtlasiO60869
PRIDEiO60869
ProteomicsDBi49636
49637 [O60869-2]
TopDownProteomicsiO60869-1 [O60869-1]

PTM databases

iPTMnetiO60869
PhosphoSitePlusiO60869

Expressioni

Tissue specificityi

Expressed in brain, liver, lung, kidney and heart (at protein level). Ubiquitously expressed. More abundant in heart, pancreas, liver, intestine and adipose tissues.3 Publications

Developmental stagei

Expressed in fetal tissues. More abundant in kidney.1 Publication

Inductioni

Down-regulated by HIV-1 Tat or phorbol ester (TPA) treatment in endothelial cells (at mRNA and protein levels).1 Publication

Gene expression databases

BgeeiENSG00000107223
CleanExiHS_EDF1
GenevisibleiO60869 HS

Organism-specific databases

HPAiHPA035642

Interactioni

Subunit structurei

Interacts with TBP and the transcription factor IID (TFIID) complex, NR5A2, NR1H3 and PPARG. Interaction with TBP is regulated by phosphorylation. Binds NR5A1, ATF1, FOS and JUN via their conserved basic region. Binding to calmodulin is regulated by calcium and phosphorylation of the IQ motif.4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi114260, 26 interactors
IntActiO60869, 19 interactors
MINTiO60869
STRINGi9606.ENSP00000224073

Structurei

Secondary structure

1148
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi76 – 86Combined sources11
Turni87 – 89Combined sources3
Helixi92 – 99Combined sources8
Helixi103 – 111Combined sources9
Helixi118 – 128Combined sources11
Turni135 – 138Combined sources4
Beta strandi140 – 143Combined sources4

3D structure databases

ProteinModelPortaliO60869
SMRiO60869
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO60869

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini81 – 135HTH cro/C1-typePROSITE-ProRule annotationAdd BLAST55

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni37 – 113Interaction with NR5A2, PPARG and NR1H31 PublicationAdd BLAST77
Regioni69 – 108Interaction with TBP and NR5A11 PublicationAdd BLAST40

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi81 – 88IQ motif8

Domaini

The IQ motif, which is involved in calmodulin binding, overlaps with the binding domain for nuclear receptors and transcription factors. Its phosphorylation probably allows a switch between the two activities of the protein (By similarity).By similarity

Phylogenomic databases

eggNOGiKOG3398 Eukaryota
COG1813 LUCA
GeneTreeiENSGT00390000008519
HOGENOMiHOG000195726
HOVERGENiHBG051440
InParanoidiO60869
KOiK03627
OMAiIADYECG
OrthoDBiEOG091G0RRN
PhylomeDBiO60869
TreeFamiTF300064

Family and domain databases

CDDicd00093 HTH_XRE, 1 hit
InterProiView protein in InterPro
IPR001387 Cro/C1-type_HTH
IPR010982 Lambda_DNA-bd_dom_sf
IPR013729 MBF1_N
PfamiView protein in Pfam
PF01381 HTH_3, 1 hit
PF08523 MBF1, 1 hit
SMARTiView protein in SMART
SM00530 HTH_XRE, 1 hit
SUPFAMiSSF47413 SSF47413, 1 hit
PROSITEiView protein in PROSITE
PS50943 HTH_CROC1, 1 hit

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O60869-1) [UniParc]FASTAAdd to basket
Also known as: Alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAESDWDTVT VLRKKGPTAA QAKSKQAILA AQRRGEDVET SKKWAAGQNK 
        60         70         80         90        100
QHSITKNTAK LDRETEELHH DRVTLEVGKV IQQGRQSKGL TQKDLATKIN 
       110        120        130        140 
EKPQVIADYE SGRAIPNNQV LGKIERAIGL KLRGKDIGKP IEKGPRAK
Length:148
Mass (Da):16,369
Last modified:August 1, 1998 - v1
Checksum:iADC2C5384BF85C11
GO
Isoform 2 (identifier: O60869-2) [UniParc]FASTAAdd to basket
Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     130-148: LKLRGKDIGKPIEKGPRAK → ECPSTLRRVR

Show »
Length:139
Mass (Da):15,481
Checksum:i9F30DE6890D7E801
GO
Isoform 3 (identifier: O60869-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     129-148: GLKLRGKDIGKPIEKGPRAK → DVGTRSARVLRAQ

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:141
Mass (Da):15,636
Checksum:iE31C8E26A4679A23
GO

Sequence cautioni

The sequence CAI12698 differs from that shown. Reason: Erroneous gene model prediction.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_054701129 – 148GLKLR…GPRAK → DVGTRSARVLRAQ in isoform 3. CuratedAdd BLAST20
Alternative sequenceiVSP_013336130 – 148LKLRG…GPRAK → ECPSTLRRVR in isoform 2. 1 PublicationAdd BLAST19

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ005259 mRNA Translation: CAA06446.1
AB002282 mRNA Translation: BAA88073.1
AB002283 mRNA Translation: BAA88074.1
CR541914 mRNA Translation: CAG46712.1
BT009863 mRNA Translation: AAP88865.1
AL355987 Genomic DNA Translation: CAI12697.1
AL355987 Genomic DNA Translation: CAI12698.1 Sequence problems.
AL355987 Genomic DNA Translation: CAI12699.1
BC015500 mRNA Translation: AAH15500.1
CCDSiCCDS65193.1 [O60869-3]
CCDS7011.1 [O60869-1]
CCDS7012.1 [O60869-2]
RefSeqiNP_001268226.1, NM_001281297.1 [O60869-3]
NP_001268227.1, NM_001281298.1
NP_001268228.1, NM_001281299.1
NP_003783.1, NM_003792.3 [O60869-1]
NP_694880.1, NM_153200.2 [O60869-2]
UniGeneiHs.174050

Genome annotation databases

EnsembliENST00000224073; ENSP00000224073; ENSG00000107223 [O60869-1]
ENST00000371648; ENSP00000360711; ENSG00000107223 [O60869-2]
ENST00000371649; ENSP00000360712; ENSG00000107223 [O60869-3]
GeneIDi8721
KEGGihsa:8721
UCSCiuc004cjt.3 human [O60869-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiEDF1_HUMAN
AccessioniPrimary (citable) accession number: O60869
Secondary accession number(s): Q5T5T2, Q9UIM1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: August 1, 1998
Last modified: June 20, 2018
This is version 161 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health