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Q8NFF5

- FAD1_HUMAN

UniProt

Q8NFF5 - FAD1_HUMAN

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Protein

FAD synthase

Gene

FLAD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the adenylation of flavin mononucleotide (FMN) to form flavin adenine dinucleotide (FAD) coenzyme.

Catalytic activityi

ATP + FMN = diphosphate + FAD.1 Publication

Cofactori

Magnesium.2 Publications

Kineticsi

  1. KM=1.5 µM for FMN2 Publications
  2. KM=0.36 µM for FMN (isoform 2)2 Publications

Vmax=6.1 nmol/min/mg enzyme2 Publications

Vmax=3.9 nmol/min/mg enzyme (isoform 2)2 Publications

Pathwayi

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. FMN adenylyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. FAD biosynthetic process Source: UniProtKB-UniPathway
  2. Mo-molybdopterin cofactor biosynthetic process Source: InterPro
  3. riboflavin metabolic process Source: Reactome
  4. small molecule metabolic process Source: Reactome
  5. vitamin metabolic process Source: Reactome
  6. water-soluble vitamin metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

ATP-binding, FAD, Flavoprotein, FMN, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS08520-MONOMER.
BRENDAi2.7.7.2. 2681.
ReactomeiREACT_11070. Vitamin B2 (riboflavin) metabolism.
SABIO-RKQ8NFF5.
UniPathwayiUPA00277; UER00407.

Names & Taxonomyi

Protein namesi
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:
Molybdenum cofactor biosynthesis protein-like region
FAD synthase region
Gene namesi
Name:FLAD1
ORF Names:PP591
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:24671. FLAD1.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671759.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1717MitochondrionSequence AnalysisAdd
BLAST
Chaini18 – 587570FAD synthasePRO_0000302737Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei106 – 1061Phosphoserine2 Publications
Modified residuei378 – 3781N6-acetyllysine; alternateBy similarity
Modified residuei378 – 3781N6-succinyllysine; alternateBy similarity
Modified residuei563 – 5631Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8NFF5.
PaxDbiQ8NFF5.
PRIDEiQ8NFF5.

PTM databases

PhosphoSiteiQ8NFF5.

Expressioni

Gene expression databases

BgeeiQ8NFF5.
CleanExiHS_FLAD1.
ExpressionAtlasiQ8NFF5. baseline and differential.
GenevestigatoriQ8NFF5.

Organism-specific databases

HPAiHPA028476.
HPA028486.
HPA028563.

Interactioni

Protein-protein interaction databases

BioGridi123221. 20 interactions.
IntActiQ8NFF5. 13 interactions.
MINTiMINT-3042841.
STRINGi9606.ENSP00000292180.

Structurei

3D structure databases

ProteinModelPortaliQ8NFF5.
SMRiQ8NFF5. Positions 113-269, 349-560.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni114 – 20592Molybdenum cofactor biosynthesis protein-likeAdd
BLAST
Regioni398 – 555158FAD synthaseAdd
BLAST

Domaini

The molybdenum cofactor biosynthesis protein-like region may not be functional.

Sequence similaritiesi

In the N-terminal section; belongs to the MoaB/Mog family.Curated
In the C-terminal section; belongs to the PAPS reductase family. FAD1 subfamily.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0175.
GeneTreeiENSGT00390000007266.
HOVERGENiHBG058211.
InParanoidiQ8NFF5.
KOiK00953.
OMAiAIAVEIS.
OrthoDBiEOG7C5M9F.
PhylomeDBiQ8NFF5.
TreeFamiTF314056.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
3.40.980.10. 1 hit.
InterProiIPR012183. FAD_synth_Mopterin-bd.
IPR001453. Mopterin-bd_dom.
IPR002500. PAPS_reduct.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00994. MoCF_biosynth. 1 hit.
PF01507. PAPS_reduct. 2 hits.
[Graphical view]
PIRSFiPIRSF036620. MPTbdFAD. 1 hit.
SMARTiSM00852. MoCF_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF53218. SSF53218. 1 hit.

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8NFF5-1) [UniParc]FASTAAdd to Basket

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
MGWDLGTRLF QRQEQRSRLS RIWLEKTRVF LEGSTRTPAL PHCLFWLLQV
60 70 80 90 100
PSTQDPLFPG YGPQCPVDLA GPPCLRPLFG GLGGYWRALQ RGREGRTMTS
110 120 130 140 150
RASELSPGRS VTAGIIIVGD EILKGHTQDT NTFFLCRTLR SLGVQVCRVS
160 170 180 190 200
VVPDEVATIA AEVTSFSNRF THVLTAGGIG PTHDDVTFEA VAQAFGDELK
210 220 230 240 250
PHPKLEAATK ALGGEGWEKL SLVPSSARLH YGTDPCTGQP FRFPLVSVRN
260 270 280 290 300
VYLFPGIPEL LRRVLEGMKG LFQNPAVQFH SKELYVAADE ASIAPILAEA
310 320 330 340 350
QAHFGRRLGL GSYPDWGSNY YQVKLTLDSE EEGPLEECLA YLTARLPQGS
360 370 380 390 400
LVPYMPNAVE QASEAVYKLA ESGSSLGKKV AGALQTIETS LAQYSLTQLC
410 420 430 440 450
VGFNGGKDCT ALLHLFHAAV QRKLPDVPNP LQILYIRSIS PFPELEQFLQ
460 470 480 490 500
DTIKRYNLQM LEAEGSMKQA LGELQARHPQ LEAVLMGTRR TDPYSCSLCP
510 520 530 540 550
FSPTDPGWPA FMRINPLLDW TYRDIWDFLR QLFVPYCILY DRGYTSLGSR
560 570 580
ENTVRNPALK CLSPGGHPTY RPAYLLENEE EERNSRT
Length:587
Mass (Da):65,266
Last modified:October 1, 2002 - v1
Checksum:iF95918B15D9D8106
GO
Isoform 2 (identifier: Q8NFF5-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:490
Mass (Da):54,188
Checksum:i633D7949AB88E059
GO
Isoform 3 (identifier: Q8NFF5-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:446
Mass (Da):49,198
Checksum:i2983E4FA84020CDF
GO
Isoform 4 (identifier: Q8NFF5-4) [UniParc]FASTAAdd to Basket

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.

Show »
Length:294
Mass (Da):32,369
Checksum:i5CEF3426F7FEDEF5
GO
Isoform 5 (identifier: Q8NFF5-5) [UniParc]FASTAAdd to Basket

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.

Show »
Length:338
Mass (Da):36,865
Checksum:i2BB52386763E2A9B
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9797Missing in isoform 2 and isoform 3. 2 PublicationsVSP_027947Add
BLAST
Alternative sequencei1 – 3030Missing in isoform 4 and isoform 5. 2 PublicationsVSP_027948Add
BLAST
Alternative sequencei31 – 12494LEGST…DEILK → MQPSSSTPPLHPYSTDGLIF PFNPQ in isoform 4 and isoform 5. 2 PublicationsVSP_027949Add
BLAST
Alternative sequencei374 – 43764SSLGK…ILYIR → NYLMFQTPSRSCISAASPLS LSWNSFYRTLSREQAIPENQ IASPPSEAKGAEEPWMGPFP GQQG in isoform 5. 1 PublicationVSP_027950Add
BLAST
Alternative sequencei374 – 39320SSLGK…TSLAQ → RDLMEEGHYAQSHWWHPRSQ in isoform 4. 1 PublicationVSP_027951Add
BLAST
Alternative sequencei394 – 587194Missing in isoform 4. 1 PublicationVSP_027952Add
BLAST
Alternative sequencei438 – 587150Missing in isoform 5. 1 PublicationVSP_027953Add
BLAST
Alternative sequencei544 – 58744Missing in isoform 3. 1 PublicationVSP_027954Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS1078.1. [Q8NFF5-1]
CCDS1079.1. [Q8NFF5-2]
CCDS53371.1. [Q8NFF5-3]
CCDS53372.1. [Q8NFF5-4]
RefSeqiNP_001171820.1. NM_001184891.1. [Q8NFF5-3]
NP_001171821.1. NM_001184892.1. [Q8NFF5-4]
NP_079483.3. NM_025207.4. [Q8NFF5-1]
NP_958800.1. NM_201398.2. [Q8NFF5-2]
UniGeneiHs.118666.

Genome annotation databases

EnsembliENST00000292180; ENSP00000292180; ENSG00000160688. [Q8NFF5-1]
ENST00000315144; ENSP00000317296; ENSG00000160688. [Q8NFF5-2]
ENST00000368431; ENSP00000357416; ENSG00000160688. [Q8NFF5-4]
ENST00000368432; ENSP00000357417; ENSG00000160688. [Q8NFF5-3]
GeneIDi80308.
KEGGihsa:80308.
UCSCiuc001fgc.3. human. [Q8NFF5-4]
uc001fgd.2. human. [Q8NFF5-1]

Polymorphism databases

DMDMi74751275.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS1078.1. [Q8NFF5-1 ]
CCDS1079.1. [Q8NFF5-2 ]
CCDS53371.1. [Q8NFF5-3 ]
CCDS53372.1. [Q8NFF5-4 ]
RefSeqi NP_001171820.1. NM_001184891.1. [Q8NFF5-3 ]
NP_001171821.1. NM_001184892.1. [Q8NFF5-4 ]
NP_079483.3. NM_025207.4. [Q8NFF5-1 ]
NP_958800.1. NM_201398.2. [Q8NFF5-2 ]
UniGenei Hs.118666.

3D structure databases

ProteinModelPortali Q8NFF5.
SMRi Q8NFF5. Positions 113-269, 349-560.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123221. 20 interactions.
IntActi Q8NFF5. 13 interactions.
MINTi MINT-3042841.
STRINGi 9606.ENSP00000292180.

PTM databases

PhosphoSitei Q8NFF5.

Polymorphism databases

DMDMi 74751275.

Proteomic databases

MaxQBi Q8NFF5.
PaxDbi Q8NFF5.
PRIDEi Q8NFF5.

Protocols and materials databases

DNASUi 80308.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000292180 ; ENSP00000292180 ; ENSG00000160688 . [Q8NFF5-1 ]
ENST00000315144 ; ENSP00000317296 ; ENSG00000160688 . [Q8NFF5-2 ]
ENST00000368431 ; ENSP00000357416 ; ENSG00000160688 . [Q8NFF5-4 ]
ENST00000368432 ; ENSP00000357417 ; ENSG00000160688 . [Q8NFF5-3 ]
GeneIDi 80308.
KEGGi hsa:80308.
UCSCi uc001fgc.3. human. [Q8NFF5-4 ]
uc001fgd.2. human. [Q8NFF5-1 ]

Organism-specific databases

CTDi 80308.
GeneCardsi GC01P154955.
HGNCi HGNC:24671. FLAD1.
HPAi HPA028476.
HPA028486.
HPA028563.
MIMi 610595. gene.
neXtProti NX_Q8NFF5.
PharmGKBi PA142671759.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0175.
GeneTreei ENSGT00390000007266.
HOVERGENi HBG058211.
InParanoidi Q8NFF5.
KOi K00953.
OMAi AIAVEIS.
OrthoDBi EOG7C5M9F.
PhylomeDBi Q8NFF5.
TreeFami TF314056.

Enzyme and pathway databases

UniPathwayi UPA00277 ; UER00407 .
BioCyci MetaCyc:HS08520-MONOMER.
BRENDAi 2.7.7.2. 2681.
Reactomei REACT_11070. Vitamin B2 (riboflavin) metabolism.
SABIO-RK Q8NFF5.

Miscellaneous databases

ChiTaRSi FLAD1. human.
GenomeRNAii 80308.
NextBioi 70783.
PROi Q8NFF5.
SOURCEi Search...

Gene expression databases

Bgeei Q8NFF5.
CleanExi HS_FLAD1.
ExpressionAtlasi Q8NFF5. baseline and differential.
Genevestigatori Q8NFF5.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
3.40.980.10. 1 hit.
InterProi IPR012183. FAD_synth_Mopterin-bd.
IPR001453. Mopterin-bd_dom.
IPR002500. PAPS_reduct.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
Pfami PF00994. MoCF_biosynth. 1 hit.
PF01507. PAPS_reduct. 2 hits.
[Graphical view ]
PIRSFi PIRSF036620. MPTbdFAD. 1 hit.
SMARTi SM00852. MoCF_biosynth. 1 hit.
[Graphical view ]
SUPFAMi SSF53218. SSF53218. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: SUBCELLULAR LOCATION.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiFAD1_HUMAN
AccessioniPrimary (citable) accession number: Q8NFF5
Secondary accession number(s): Q8N5J1
, Q8N686, Q8WU93, Q8WUJ4, Q96CR8, Q99764, Q9HBN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: October 1, 2002
Last modified: October 29, 2014
This is version 104 of the entry and version 1 of the sequence. [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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3