Q8NFF5 (FAD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
FAD synthase
EC=2.7.7.2

Alternative name(s):
FAD pyrophosphorylase
FMN adenylyltransferase
Flavin adenine dinucleotide synthase

Including the following 2 domains:

1. Molybdenum cofactor biosynthesis protein-like region
2. FAD synthase region

Gene names

Name:	FLAD1
ORF Names:	PP591

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	587 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.
Catalytic activity	ATP + FMN = diphosphate + FAD. Ref.1
Cofactor	Magnesium. Ref.1 Ref.9
Pathway	Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
Domain	The molybdenum cofactor biosynthesis protein-like region may not be functional.
Sequence similarities	In the N-terminal section; belongs to the MoaB/Mog family. In the C-terminal section; belongs to the PAPS reductase family. FAD1 subfamily.
Biophysicochemical properties	Kinetic parameters: KM=1.5 µM for FMN (Ref.1) Ref.1 Ref.9 KM=0.36 µM for FMN (isoform 2) (Ref.9) Vmax=6.1 nmol/min/mg enzyme (Ref.1) Vmax=3.9 nmol/min/mg enzyme (isoform 2) (Ref.9)

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding FAD FMN Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	FAD biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway Mo-molybdopterin cofactor biosynthetic process Inferred from electronic annotation. Source: InterPro riboflavin metabolic process Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW FMN adenylyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8NFF5-1)

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.

Isoform 2 (identifier: Q8NFF5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.

Isoform 3 (identifier: Q8NFF5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: Missing.
     544-587: Missing.

Isoform 4 (identifier: Q8NFF5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.
     31-124: LEGSTRTPAL...IIIVGDEILK → MQPSSSTPPLHPYSTDGLIFPFNPQ
     374-393: SSLGKKVAGALQTIETSLAQ → RDLMEEGHYAQSHWWHPRSQ
     394-587: Missing.

Isoform 5 (identifier: Q8NFF5-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: Missing.
     31-124: LEGSTRTPAL...IIIVGDEILK → MQPSSSTPPLHPYSTDGLIFPFNPQ
     374-437: SSLGKKVAGA...PNPLQILYIR → NYLMFQTPSR...WMGPFPGQQG
     438-587: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 587	587	FAD synthase		PRO_0000302737
Regions
	Region	114 – 205	92	Molybdenum cofactor biosynthesis protein-like
	Region	398 – 555	158	FAD synthase
Amino acid modifications
	Modified residue	106	1	Phosphoserine Ref.10 Ref.11
	Modified residue	563	1	Phosphoserine Ref.10 Ref.12
Natural variations
	Alternative sequence	1 – 97	97	Missing in isoform 2 and isoform 3.		VSP_027947
	Alternative sequence	1 – 30	30	Missing in isoform 4 and isoform 5.		VSP_027948
	Alternative sequence	31 – 124	94	LEGST…DEILK → MQPSSSTPPLHPYSTDGLIF PFNPQ in isoform 4 and isoform 5.		VSP_027949
	Alternative sequence	374 – 437	64	SSLGK…ILYIR → NYLMFQTPSRSCISAASPLS LSWNSFYRTLSREQAIPENQ IASPPSEAKGAEEPWMGPFP GQQG in isoform 5.		VSP_027950
	Alternative sequence	374 – 393	20	SSLGK…TSLAQ → RDLMEEGHYAQSHWWHPRSQ in isoform 4.		VSP_027951
	Alternative sequence	394 – 587	194	Missing in isoform 4.		VSP_027952
	Alternative sequence	438 – 587	150	Missing in isoform 5.		VSP_027953
	Alternative sequence	544 – 587	44	Missing in isoform 3.		VSP_027954

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: F95918B15D9D8106	FASTA	587	65,266
	10 20 30 40 50 60 MGWDLGTRLF QRQEQRSRLS RIWLEKTRVF LEGSTRTPAL PHCLFWLLQV PSTQDPLFPG 70 80 90 100 110 120 YGPQCPVDLA GPPCLRPLFG GLGGYWRALQ RGREGRTMTS RASELSPGRS VTAGIIIVGD 130 140 150 160 170 180 EILKGHTQDT NTFFLCRTLR SLGVQVCRVS VVPDEVATIA AEVTSFSNRF THVLTAGGIG 190 200 210 220 230 240 PTHDDVTFEA VAQAFGDELK PHPKLEAATK ALGGEGWEKL SLVPSSARLH YGTDPCTGQP 250 260 270 280 290 300 FRFPLVSVRN VYLFPGIPEL LRRVLEGMKG LFQNPAVQFH SKELYVAADE ASIAPILAEA 310 320 330 340 350 360 QAHFGRRLGL GSYPDWGSNY YQVKLTLDSE EEGPLEECLA YLTARLPQGS LVPYMPNAVE 370 380 390 400 410 420 QASEAVYKLA ESGSSLGKKV AGALQTIETS LAQYSLTQLC VGFNGGKDCT ALLHLFHAAV 430 440 450 460 470 480 QRKLPDVPNP LQILYIRSIS PFPELEQFLQ DTIKRYNLQM LEAEGSMKQA LGELQARHPQ 490 500 510 520 530 540 LEAVLMGTRR TDPYSCSLCP FSPTDPGWPA FMRINPLLDW TYRDIWDFLR QLFVPYCILY 550 560 570 580 DRGYTSLGSR ENTVRNPALK CLSPGGHPTY RPAYLLENEE EERNSRT
	Isoform 2 [UniParc]. Checksum: 633D7949AB88E059	FASTA	490	54,188
	10 20 30 40 50 60 MTSRASELSP GRSVTAGIII VGDEILKGHT QDTNTFFLCR TLRSLGVQVC RVSVVPDEVA 70 80 90 100 110 120 TIAAEVTSFS NRFTHVLTAG GIGPTHDDVT FEAVAQAFGD ELKPHPKLEA ATKALGGEGW 130 140 150 160 170 180 EKLSLVPSSA RLHYGTDPCT GQPFRFPLVS VRNVYLFPGI PELLRRVLEG MKGLFQNPAV 190 200 210 220 230 240 QFHSKELYVA ADEASIAPIL AEAQAHFGRR LGLGSYPDWG SNYYQVKLTL DSEEEGPLEE 250 260 270 280 290 300 CLAYLTARLP QGSLVPYMPN AVEQASEAVY KLAESGSSLG KKVAGALQTI ETSLAQYSLT 310 320 330 340 350 360 QLCVGFNGGK DCTALLHLFH AAVQRKLPDV PNPLQILYIR SISPFPELEQ FLQDTIKRYN 370 380 390 400 410 420 LQMLEAEGSM KQALGELQAR HPQLEAVLMG TRRTDPYSCS LCPFSPTDPG WPAFMRINPL 430 440 450 460 470 480 LDWTYRDIWD FLRQLFVPYC ILYDRGYTSL GSRENTVRNP ALKCLSPGGH PTYRPAYLLE 490 NEEEERNSRT
	Isoform 3 [UniParc]. Checksum: 2983E4FA84020CDF	FASTA	446	49,198
	10 20 30 40 50 60 MTSRASELSP GRSVTAGIII VGDEILKGHT QDTNTFFLCR TLRSLGVQVC RVSVVPDEVA 70 80 90 100 110 120 TIAAEVTSFS NRFTHVLTAG GIGPTHDDVT FEAVAQAFGD ELKPHPKLEA ATKALGGEGW 130 140 150 160 170 180 EKLSLVPSSA RLHYGTDPCT GQPFRFPLVS VRNVYLFPGI PELLRRVLEG MKGLFQNPAV 190 200 210 220 230 240 QFHSKELYVA ADEASIAPIL AEAQAHFGRR LGLGSYPDWG SNYYQVKLTL DSEEEGPLEE 250 260 270 280 290 300 CLAYLTARLP QGSLVPYMPN AVEQASEAVY KLAESGSSLG KKVAGALQTI ETSLAQYSLT 310 320 330 340 350 360 QLCVGFNGGK DCTALLHLFH AAVQRKLPDV PNPLQILYIR SISPFPELEQ FLQDTIKRYN 370 380 390 400 410 420 LQMLEAEGSM KQALGELQAR HPQLEAVLMG TRRTDPYSCS LCPFSPTDPG WPAFMRINPL 430 440 LDWTYRDIWD FLRQLFVPYC ILYDRG
	Isoform 4 [UniParc]. Checksum: 5CEF3426F7FEDEF5	FASTA	294	32,369
	10 20 30 40 50 60 MQPSSSTPPL HPYSTDGLIF PFNPQGHTQD TNTFFLCRTL RSLGVQVCRV SVVPDEVATI 70 80 90 100 110 120 AAEVTSFSNR FTHVLTAGGI GPTHDDVTFE AVAQAFGDEL KPHPKLEAAT KALGGEGWEK 130 140 150 160 170 180 LSLVPSSARL HYGTDPCTGQ PFRFPLVSVR NVYLFPGIPE LLRRVLEGMK GLFQNPAVQF 190 200 210 220 230 240 HSKELYVAAD EASIAPILAE AQAHFGRRLG LGSYPDWGSN YYQVKLTLDS EEEGPLEECL 250 260 270 280 290 AYLTARLPQG SLVPYMPNAV EQASEAVYKL AESGRDLMEE GHYAQSHWWH PRSQ
	Isoform 5 [UniParc]. Checksum: 2BB52386763E2A9B	FASTA	338	36,865
	10 20 30 40 50 60 MQPSSSTPPL HPYSTDGLIF PFNPQGHTQD TNTFFLCRTL RSLGVQVCRV SVVPDEVATI 70 80 90 100 110 120 AAEVTSFSNR FTHVLTAGGI GPTHDDVTFE AVAQAFGDEL KPHPKLEAAT KALGGEGWEK 130 140 150 160 170 180 LSLVPSSARL HYGTDPCTGQ PFRFPLVSVR NVYLFPGIPE LLRRVLEGMK GLFQNPAVQF 190 200 210 220 230 240 HSKELYVAAD EASIAPILAE AQAHFGRRLG LGSYPDWGSN YYQVKLTLDS EEEGPLEECL 250 260 270 280 290 300 AYLTARLPQG SLVPYMPNAV EQASEAVYKL AESGNYLMFQ TPSRSCISAA SPLSLSWNSF 310 320 330 YRTLSREQAI PENQIASPPS EAKGAEEPWM GPFPGQQG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Over-expression in Escherichia coli and characterization of two recombinant isoforms of human FAD synthetase." Brizio C., Galluccio M., Wait R., Torchetti E.M., Bafunno V., Accardi R., Gianazza E., Indiveri C., Barile M. Biochem. Biophys. Res. Commun. 344:1008-1016(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 2), CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR. Tissue: Skin.
[2]	"Cloning, expression and characterization of a human FAD synthetase." Fischer M.J., Kempter K., Bacher A. Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Liver.
[3]	Chen X.G., Li Y. Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Skin.
[4]	"Large-scale cDNA transfection screening for genes related to cancer development and progression." Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J. Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
[5]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 10-587 (ISOFORM 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 256-587 (ISOFORM 1). Tissue: Brain, Colon, Placenta and Skin.
[8]	"Large-scale concatenation cDNA sequencing." Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A. Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 151-587 (ISOFORM 1). Tissue: Brain.
[9]	"Over-expression in Escherichia coli, purification and characterization of isoform 2 of human FAD synthetase." Galluccio M., Brizio C., Torchetti E.M., Ferranti P., Gianazza E., Indiveri C., Barile M. Protein Expr. Purif. 52:175-181(2007) [PubMed] [Europe PMC] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
[10]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-563, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, MASS SPECTROMETRY.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ458779 mRNA. Translation: ABE65383.1. AF481877 mRNA. Translation: AAO49318.1. AF520568 mRNA. Translation: AAM77338.1. AF218022 mRNA. Translation: AAG17264.1. AL451085 Genomic DNA. Translation: CAI13259.1. AL451085 Genomic DNA. Translation: CAI13260.1. AL451085 Genomic DNA. Translation: CAI13261.1. AL451085 Genomic DNA. Translation: CAI13262.1. CH471121 Genomic DNA. Translation: EAW53154.1. CH471121 Genomic DNA. Translation: EAW53155.1. CH471121 Genomic DNA. Translation: EAW53158.1. CH471121 Genomic DNA. Translation: EAW53159.1. BC011378 mRNA. Translation: AAH11378.1. BC014012 mRNA. Translation: AAH14012.2. BC020253 mRNA. Translation: AAH20253.1. BC021096 mRNA. Translation: AAH21096.2. BC032323 mRNA. Translation: AAH32323.1. U79241 mRNA. Translation: AAB50199.1.
IPI	IPI00220299. IPI00387088. IPI00398214. IPI00642864. IPI00855871.
RefSeq	NP_001171820.1. NM_001184891.1. NP_001171821.1. NM_001184892.1. NP_079483.3. NM_025207.4. NP_958800.1. NM_201398.2.
UniGene	Hs.118666.
3D structure databases
ProteinModelPortal	Q8NFF5.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8NFF5. 5 interactions.
MINT	MINT-3042841.
STRING	9606.ENSP00000292180.
PTM databases
PhosphoSite	Q8NFF5.
Polymorphism databases
DMDM	74751275.
Proteomic databases
PaxDb	Q8NFF5.
PRIDE	Q8NFF5.
Protocols and materials databases
DNASU	80308.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000292180; ENSP00000292180; ENSG00000160688. ENST00000315144; ENSP00000317296; ENSG00000160688. ENST00000368431; ENSP00000357416; ENSG00000160688. ENST00000368432; ENSP00000357417; ENSG00000160688. ENST00000405236; ENSP00000384323; ENSG00000160688.
GeneID	80308.
KEGG	hsa:80308.
UCSC	uc001fgc.3. human. uc001fgd.2. human.
Organism-specific databases
CTD	80308.
GeneCards	GC01P154955.
HGNC	HGNC:24671. FLAD1.
HPA	HPA028476. HPA028486. HPA028563.
MIM	610595. gene.
neXtProt	NX_Q8NFF5.
PharmGKB	PA142671759.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0175.
HOVERGEN	HBG058211.
InParanoid	Q8NFF5.
KO	K00953.
OMA	AIAVEIS.
OrthoDB	EOG4P2Q27.
PhylomeDB	Q8NFF5.
Enzyme and pathway databases
BioCyc	MetaCyc:HS08520-MONOMER.
BRENDA	2.7.7.2. 2681.
Reactome	REACT_111217. Metabolism.
SABIO-RK	Q8NFF5.
UniPathway	UPA00277; UER00407.
Gene expression databases
ArrayExpress	Q8NFF5.
Bgee	Q8NFF5.
CleanEx	HS_FLAD1.
Genevestigator	Q8NFF5.
Family and domain databases
Gene3D	3.40.50.620. 1 hit. 3.40.980.10. 1 hit.
InterPro	IPR012183. FAD_synth_Mopterin-bd. IPR001453. Mopterin-bd_dom. IPR002500. PAPS_reduct. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view]
Pfam	PF00994. MoCF_biosynth. 1 hit. PF01507. PAPS_reduct. 2 hits. [Graphical view]
PIRSF	PIRSF036620. MPTbdFAD. 1 hit.
SMART	SM00852. MoCF_biosynth. 1 hit. [Graphical view]
SUPFAM	SSF53218. MoCF_biosynth. 1 hit.
ProtoNet	Search...
Other
ChiTaRS	FLAD1. human.
GenomeRNAi	80308.
NextBio	70783.
SOURCE	Search...

Entry information

Entry name

FAD1_HUMAN

Accession

Primary (citable) accession number: Q8NFF5
Secondary accession number(s): Q8N5J1 , Q8N686, Q8WU93, Q8WUJ4, Q96CR8, Q99764, Q9HBN6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	October 1, 2002
Last modified:	May 1, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.