FLAD1 flavin adenine dinucleotide synthetase 1 [Homo sapiens (human)] - Gene

Summary

Official Symbol: FLAD1provided by HGNC
Official Full Name: flavin adenine dinucleotide synthetase 1provided by HGNC
Primary source: HGNC:HGNC:24671
See related: Ensembl:ENSG00000160688 MIM:610595; AllianceGenome:HGNC:24671
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as: FAD1; FADS; PP591; LSMFLAD
Summary: This gene encodes the enzyme that catalyzes adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme. Alternatively spliced transcript variants encoding distinct isoforms have been observed. [provided by RefSeq, Jul 2008]
Expression: Ubiquitous expression in thyroid (RPKM 5.9), lymph node (RPKM 5.8) and 25 other tissues See more
Orthologs: mouse all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: 1q21.3

Exon count:: 7

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCh38.p14 (GCF_000001405.40)	1	NC_000001.11 (154983344..154993111)
RS_2024_08	current	T2T-CHM13v2.0 (GCF_009914755.1)	1	NC_060925.1 (154122705..154132467)
RS_2024_09	previous assembly	GRCh37.p13 (GCF_000001405.25)	1	NC_000001.10 (154955820..154965587)

Chromosome 1 - NC_000001.11 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help

See details

Project title: HPA RNA-seq normal tissues
Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
BioProject: PRJEB4337
Publication: PMID 24309898
Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Structural insights into the bifunctional enzyme human FAD synthase.
Title: Structural insights into the bifunctional enzyme human FAD synthase.
Retrograde response to mitochondrial dysfunctions associated to LOF variations in FLAD1 exon 2: unraveling the importance of RFVT2.
Title: Retrograde response to mitochondrial dysfunctions associated to LOF variations in FLAD1 exon 2: unraveling the importance of RFVT2.
FLAD1 is up-regulated in Gastric Cancer and is a potential prediction of prognosis.
Title: FLAD1 is up-regulated in Gastric Cancer and is a potential prediction of prognosis.
FLAD1-associated multiple acyl-CoA dehydrogenase deficiency identified by newborn screening.
Title: FLAD1-associated multiple acyl-CoA dehydrogenase deficiency identified by newborn screening.
Mutation of Aspartate 238 in FAD Synthase Isoform 6 Increases the Specific Activity by Weakening the FAD Binding.
Title: Mutation of Aspartate 238 in FAD Synthase Isoform 6 Increases the Specific Activity by Weakening the FAD Binding.
Frameshift mutation in the FADS gene is Associated with Multiple Acyl-CoA Dehydrogenase and Combined Respiratory-Chain Deficiency.
Title: Riboflavin-Responsive and -Non-responsive Mutations in FAD Synthase Cause Multiple Acyl-CoA Dehydrogenase and Combined Respiratory-Chain Deficiency.
Our data show that a reduction in electron transport proteins, namely FAD synthetase, RFK, CYC1, and SDHB, is seen in patients with ALS.
Title: Specific electron transport chain abnormalities in amyotrophic lateral sclerosis.

Submit: New GeneRIF Correction

Phenotypes

Go to the top of the page Help

Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Associated conditions

Description	Tests
Myopathy with abnormal lipid metabolism MedGen: C4310822 OMIM: 255100 GeneReviews: Not available	Compare labs

EBI GWAS Catalog

Description
Identification of 23 new prostate cancer susceptibility loci using the iCOGS custom genotyping array. EBI GWAS Catalog EBI GWAS CatalogPubMed

Variation

Go to the top of the page Help

See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

HIV-1 interactions

Go to the top of the page Help

Protein interactions

Protein	Gene	Interaction	Pubs
retropepsin	gag-pol	HIV-1 PR is identified to have a physical interaction with flavin adenine dinucleotide synthetase homolog (FLAD1) in human HEK293 and/or Jurkat cell lines by using affinity tagging and purification mass spectrometry analyses	PubMed

Go to the HIV-1, Human Interaction Database

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Markers

RH64598 (e-PCR)
- UniSTS:52000

RH71261 (e-PCR)
- UniSTS:52001

D8S2279 (e-PCR)
- UniSTS:473907

D15S1477 (e-PCR)
- UniSTS:474482

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables FMN adenylyltransferase activity	IBA Inferred from Biological aspect of Ancestor more info
enables FMN adenylyltransferase activity	IDA Inferred from Direct Assay more info	PubMed
enables FMN adenylyltransferase activity	TAS Traceable Author Statement more info
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in FAD biosynthetic process	IBA Inferred from Biological aspect of Ancestor more info
involved_in FAD biosynthetic process	IDA Inferred from Direct Assay more info	PubMed
involved_in FAD biosynthetic process	IEA Inferred from Electronic Annotation more info
involved_in riboflavin metabolic process	TAS Traceable Author Statement more info

Component	Evidence Code	Pubs
is_active_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	IDA Inferred from Direct Assay more info
located_in cytosol	TAS Traceable Author Statement more info
is_active_in mitochondrial matrix	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	HTP more info	PubMed
located_in plasma membrane	IDA Inferred from Direct Assay more info

General protein information

Go to the top of the page Help

Preferred Names: FAD synthase

Names: FAD pyrophosphorylase; FAD-adenylyl transferase; FAD-synthetase; FMN adenylyltransferase; Fad1, flavin adenine dinucleotide synthetase, homolog

NP_001171820.1

EC 2.7.7.2

NP_001171821.1

EC 2.7.7.2

NP_079483.3

EC 2.7.7.2

NP_958800.1

EC 2.7.7.2

XP_047286896.1

EC 2.7.7.2

XP_047286897.1

EC 2.7.7.2

XP_047286901.1

EC 2.7.7.2

XP_054194845.1

EC 2.7.7.2

XP_054194846.1

EC 2.7.7.2

XP_054194847.1

EC 2.7.7.2

XP_054194848.1

EC 2.7.7.2

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

NG_042310.1 RefSeqGene

Range

5051..14818

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NM_001184891.2 → NP_001171820.1 FAD synthase isoform 3

See identical proteins and their annotated locations for NP_001171820.1

Status: REVIEWED

Description

Transcript Variant: This variant (3) differs in its 5' and 3' ends and uses a downstream start codon, compared to variant 1. The resulting protein (isoform 3) has a shorter N-terminus and a distinct and shorter C-terminus when it is compared to isoform 1.

Source sequence(s)

AF520568, BC011378, DC371856

Consensus CDS

CCDS53371.1

UniProtKB/Swiss-Prot

Q8NFF5

Related

ENSP00000357417.1, ENST00000368432.5

Conserved Domains (3) summary

COG1058
Location:13 → 249

CinA; Predicted nucleotide-utilizing enzyme related to molybdopterin-biosynthesis enzyme MoeA [General function prediction only]

cd00885
Location:15 → 169

cinA; Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of ...

cd01713
Location:301 → 446

PAPS_reductase; This domain is found in phosphoadenosine phosphosulphate (PAPS) reductase enzymes or PAPS sulphotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. A highly ...
NM_001184892.2 → NP_001171821.1 FAD synthase isoform 4

See identical proteins and their annotated locations for NP_001171821.1

Status: REVIEWED

Description

Transcript Variant: This variant (4) has multiple differences and initiates translation at an alternate start codon, compared to variant 1. The encoded protein (isoform 4) has a distinct N- and C-termini and is shorter when it is compared to isoform 1.

Source sequence(s)

AF218022, DC371856

Consensus CDS

CCDS53372.1

UniProtKB/Swiss-Prot

Q8NFF5

Related

ENSP00000357416.3, ENST00000368431.7

Conserved Domains (2) summary

COG1058
Location:26 → 247

CinA; Predicted nucleotide-utilizing enzyme related to molybdopterin-biosynthesis enzyme MoeA [General function prediction only]

cl00451
Location:26 → 167

MoCF_BD; MoCF_BD: molybdenum cofactor (MoCF) binding domain (BD). This domain is found a variety of proteins involved in biosynthesis of molybdopterin cofactor, like MoaB, MogA, and MoeA. The domain is presumed to bind molybdopterin.
NM_025207.5 → NP_079483.3 FAD synthase isoform 1

See identical proteins and their annotated locations for NP_079483.3

Status: REVIEWED

Description

Transcript Variant: This variant (1) encodes the longest protein (isoform 1).

Source sequence(s)

AF520568, DC371856

Consensus CDS

CCDS1078.1

UniProtKB/Swiss-Prot

Q8N5J1, Q8N686, Q8NFF5, Q8WU93, Q8WUJ4, Q96CR8, Q99764, Q9HBN6

Related

ENSP00000292180.3, ENST00000292180.8

Conserved Domains (3) summary

COG1058
Location:110 → 346

CinA; Predicted nucleotide-utilizing enzyme related to molybdopterin-biosynthesis enzyme MoeA [General function prediction only]

cd00885
Location:112 → 266

cinA; Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of ...

cd01713
Location:398 → 548

PAPS_reductase; This domain is found in phosphoadenosine phosphosulphate (PAPS) reductase enzymes or PAPS sulphotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. A highly ...
NM_201398.3 → NP_958800.1 FAD synthase isoform 2

See identical proteins and their annotated locations for NP_958800.1

Status: REVIEWED

Description

Transcript Variant: This variant (2) differs in the 5' UTR and uses a downstream start codon, compared to variant 1. The resulting protein (isoform 2) has a shorter N-terminus compared to isoform 1.

Source sequence(s)

BC021096, DC371856

Consensus CDS

CCDS1079.1

UniProtKB/Swiss-Prot

Q8NFF5

Related

ENSP00000317296.10, ENST00000315144.14

Conserved Domains (2) summary

cd00885
Location:15 → 169

cinA; Competence-damaged protein. CinA is the first gene in the competence- inducible (cin) operon and is thought to be specifically required at some stage in the process of transformation. This domain is closely related to a domain, found in a variety of ...

cd01713
Location:301 → 451

PAPS_reductase; This domain is found in phosphoadenosine phosphosulphate (PAPS) reductase enzymes or PAPS sulphotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPases and ATP sulphurylases. A highly ...