Protein detail

FAD1

Bifunctional FAD diphosphatase/FAD synthase [Includes: FAD diphosphatase (EC 3.6.1.18) (EC 3.6.1.22) (FAD pyrophosphatase) (FADPPase) (FADHy) (NADH diphosphatase); FAD synthase (FADSy) (EC 2.7.7.2) (FMN adenylyltransferase) (FMNAT) (Flavin adenine dinucleotide synthase)]

Entry name
FAD1
UniProt ID
Q8NFF5
EVMP confidence score
0.50
Supporting publications (n)
7
Transmembrane count
Protein classification
Disease related genesEnzymesHuman disease related genesMetabolic proteinsPotential drug targetsPredicted intracellular proteins
EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information11
Protein Names
Bifunctional FAD diphosphatase/FAD synthase [Includes: FAD diphosphatase (EC 3.6.1.18) (EC 3.6.1.22) (FAD pyrophosphatase) (FADPPase) (FADHy) (NADH diphosphatase); FAD synthase (FADSy) (EC 2.7.7.2) (FMN adenylyltransferase) (FMNAT) (Flavin adenine dinucleotide synthase)]
Protein Class (6)
Disease related genesEnzymesHuman disease related genesMetabolic proteinsPotential drug targetsPredicted intracellular proteins
Protein Function (6)
  • Human disease related genes:Congenital disorders of metabolism:Congenital disorders of cofactor/vitamin metabolism
  • Predicted intracellular proteins
  • ENZYME proteins:Transferases
  • Potential drug targets
  • Enzymes
  • Disease related genes
Ensembl
ENSG00000160688
Entrez Gene Symbol
FLAD1
Gene Synonym (2)
FAD1PP591
Gene Description
Flavin adenine dinucleotide synthetase 1
Chromosome
1
Position
154983338-154993111
Supporting publications (n)
7
EVMP confidence score
0.50
Fluorescence & Localization5
Tissue SpecificbrainCell SpecificBasal prostatic cellsSingle-Nuclei Brain SpecificleukocyteBlood Cell SpecificgdT-cellBlood Lineage SpecificT-cells
Function & Pathway8
Protein Function (6)
  • Human disease related genes:Congenital disorders of metabolism:Congenital disorders of cofactor/vitamin metabolism
  • Predicted intracellular proteins
  • ENZYME proteins:Transferases
  • Potential drug targets
  • Enzymes
  • Disease related genes
Cellular Component (4)
Molecular Function (4)
Biological Process (3)
KEGG (3)
Reactome (3)
Canonical Pathways (3)
  • M264 Pid toll endogenous pathway
  • M5883 Naba secreted factors
  • M5885 Naba matrisome associated
Mediation Categories
Metabolism mediation
Relations & Evidence9

Ligand-Receptor Signaling (4)

4 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo

Protein Complex Composition (4)

4 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
FLAD1FUOMTAFA3A2VDF0Q7Z5A8Q8NFF50:0:0hu.MAP2
FLAD1NUDT21RCC1O43809P18754Q8NFF51:1:1CompleatCFinderCompleat:HC4937
CSNK2BCYP3A4FLAD1FTH1HMGCS1JMJD6NDUFS1P02794P08684P28331P67870Q01581Q6NYC1Q8NFF51:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC4383
FLAD1Q8NFF54PDBPDB:8ron

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyImmunoaffinity CaptureOlink Proximity Extension Assay；Mass Spectrometry23370951040098346
Sequence, Structure & Domains12

Sequences

Length
587
Mass
65,266
Sequence
MGWDLGTRLFQRQEQRSRLSRIWLEKTRVFLEGSTRTPALPHCLFWLLQVPSTQDPLFPGYGPQCPVDLAGPPCLRPLFGGLGGYWRALQRGREGRTMTSRASELSPGRSVTAGIIIVGDEILKGHTQDTNTFFLCRTLRSLGVQVCRVSVVPDEVATIAAEVTSFSNRFTHVLTAGGIGPTHDDVTFEAVAQAFGDELKPHPKLEAATKALGGEGWEKLSLVPSSARLHYGTDPCTGQPFRFPLVSVRNVYLFPGIPELLRRVLEGMKGLFQNPAVQFHSKELYVAADEASIAPILAEAQAHFGRRLGLGSYPDWGSNYYQVKLTLDSEEEGPLEECLAYLTARLPQGSLVPYMPNAVEQASEAVYKLAESGSSLGKKVAGALQTIETSLAQYSLTQLCVGFNGGKDCTALLHLFHAAVQRKLPDVPNPLQILYIRSISPFPELEQFLQDTIKRYNLQMLEAEGSMKQALGELQARHPQLEAVLMGTRRTDPYSCSLCPFSPTDPGWPAFMRINPLLDWTYRDIWDFLRQLFVPYCILYDRGYTSLGSRENTVRNPALKCLSPGGHPTYRPAYLLENEEEERNSRT
Alternative Products
Event=Alternative splicing; Named isoforms=5; Name=1; Synonyms=FADS1; IsoId=Q8NFF5-1; Sequence=Displayed; Name=2; Synonyms=FADS2; IsoId=Q8NFF5-2; Sequence=VSP_027947; Name=3; IsoId=Q8NFF5-3; Sequence=VSP_027947, VSP_027954; Name=4; IsoId=Q8NFF5-4; Sequence=VSP_027948, VSP_027949, VSP_027951, VSP_027952; Name=5; IsoId=Q8NFF5-5; Sequence=VSP_027948, VSP_027949, VSP_027950, VSP_027953
Alternative Sequence
1..97; Missing (in isoform 2 and isoform 3); 1..30; Missing (in isoform 4 and isoform 5); 31..124; LEGSTRTPALPHCLFWLLQVPSTQDPLFPGYGPQCPVDLAGPPCLRPLFGGLGGYWRALQRGREGRTMTSRASELSPGRSVTAGIIIVGDEILK -> MQPSSSTPPLHPYSTDGLIFPFNPQ (in isoform 4 and isoform 5); 374..437; SSLGKKVAGALQTIETSLAQYSLTQLCVGFNGGKDCTALLHLFHAAVQRKLPDVPNPLQILYIR -> NYLMFQTPSRSCISAASPLSLSWNSFYRTLSREQAIPENQIASPPSEAKGAEEPWMGPFPGQQG (in isoform 5); 374..393; SSLGKKVAGALQTIETSLAQ -> RDLMEEGHYAQSHWWHPRSQ (in isoform 4); 394..587; Missing (in isoform 4); 438..587; Missing (in isoform 5); 544..587; Missing (in isoform 3)

3D Structural Models

Turn
235..237; 358..361; 396..398; 516..519; 550..552
Helix
120..124; 131..141; 156..169; 187..194; 203..211; 218..221; 258..268; 269..272; 290..304; 333..345; 362..370; 375..393; 407..423; 443..456; 467..477; 493..496; 522..531; 538..541; 579..584
Beta Strand
112..118; 145..152; 171..177; 180..182; 199..201; 222..224; 228..230; 238..240; 245..248; 251..254; 280..288; 309..314; 322..332; 372..374; 399..402; 425..427; 432..437; 459..466; 483..485; 500..503; 506..508; 512..514
3D Structure
X-ray crystallography (2)

Domain & Motif Annotations

Region
110..354; FAD diphosphatase; 355..587; FAD synthase
Protein Families (2)
  • MoaB/Mog family
  • PAPS reductase family, FAD1 subfamily
Sequence Similarities
In the N-terminal section; belongs to the MoaB/Mog family.; SIMILARITY: In the C-terminal section; belongs to the PAPS reductase family. FAD1 subfamily.
Clinical Relevance5
Disease Involvement (2)
Disease variantPrimary mitochondrial disease
Antibody (3)
HPA028476HPA028486HPA028563
Interaction Protein
ENSG00000124762
Interaction Count
1
Interaction Dataset
intact_biogrid
Supporting Publications7
PMIDTitleAbstract
34265469Proteomic Landscape of Exosomes Reveals the Functional Contributions of CD151 in Triple-Negative Breast Cancer.Furthermore, utilizing quantitative proteomics approach to reveal the proteomes of CD151-deleted exosomes and cells, we found that exosomal CD151 facilitated secretion of ribosomal proteins via exosomes while inhibiting exosome secretion of complement proteins. Moreover, we proved that CD151-deleted exosomes significantly decreased the migration and invasion of TNBC cells. Most importantly, we found that the tetraspanin CD151 expression levels in TNBC-derived serum exosomes were significantly higher than those exosomes from healthy subjects, and we validated our findings with samples from 16 additional donors. This is the first comparative study of the proteomes of TNBC patient-derived and CD151-deleted exosomes.
36573687Proteomic and phosphoproteomic landscape of salivary extracellular vesicles to assess OSCC therapeutical outcomes.No abstract available
37403840Phosphoproteome analysis of cerebrospinal fluid extracellular vesicles in primary central nervous system lymphoma.No abstract available
38037300Proteomic profiling of paired human liver homogenate and tissue derived extracellular vesicles.No abstract available
38576002Therapy-induced senescent tumor cell-derived extracellular vesicles promote colorectal cancer progression through SERPINE1-mediated NF-κB p65 nuclear translocation.No abstract available
39996590Surface Double Dendritic Magnetic Microfibrils for Rapid Isolation and Proteomic Profiling of Extracellular Vesicles from Microliters of Biofluids.No abstract available
40689422Defining the Ovarian Cancer Precancerous Landscape through Modeling Fallopian Tube Epithelium Reprogramming Driven by Extracellular Vesicles.No abstract available