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Q8R123

- FAD1_MOUSE

UniProt

Q8R123 - FAD1_MOUSE

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Protein

FAD synthase

Gene

Flad1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

ATP + FMN = diphosphate + FAD.

Cofactori

Mg2+By similarity

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
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

ReactomeiREACT_216155. Vitamin B2 (riboflavin) metabolism.
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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:2443030. Flad1.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 492492FAD synthasePRO_0000302738Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei283 – 2831N6-acetyllysine; alternate1 Publication
Modified residuei283 – 2831N6-succinyllysine; alternate1 Publication
Modified residuei468 – 4681PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8R123.
PaxDbiQ8R123.
PRIDEiQ8R123.

PTM databases

PhosphoSiteiQ8R123.

Expressioni

Gene expression databases

BgeeiQ8R123.
ExpressionAtlasiQ8R123. baseline and differential.
GenevestigatoriQ8R123.

Interactioni

Protein-protein interaction databases

IntActiQ8R123. 1 interaction.
MINTiMINT-4118484.

Structurei

3D structure databases

ProteinModelPortaliQ8R123.
SMRiQ8R123. Positions 18-174, 264-465.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 11092Molybdenum cofactor biosynthesis protein-likeAdd
BLAST
Regioni303 – 460158FAD 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

Phylogenomic databases

eggNOGiCOG0175.
GeneTreeiENSGT00390000007266.
HOGENOMiHOG000007185.
HOVERGENiHBG058211.
InParanoidiQ8R123.
KOiK00953.
OMAiSFMRINP.
OrthoDBiEOG7C5M9F.
PhylomeDBiQ8R123.
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. 1 hit.
[Graphical view]
PIRSFiPIRSF036620. MPTbdFAD. 1 hit.
SMARTiSM00852. MoCF_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF53218. SSF53218. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8R123-1) [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
MASRASELPP GSGRSVTAGI IIVGDEILKG HTQDTNTYFL CRTLRSLGVQ
60 70 80 90 100
VCRVSVVPDE VATIASEVNS FSRRFTHVLT AGGIGPTHDD VTFEAVAQAF
110 120 130 140 150
GEELKPHPEL QAAIKTLGGE GWEKLSMVPS SARLHYGTDP RTGHPFRFPL
160 170 180 190 200
VSVRNVYLFP GIPELLRRVL EGLKGLFQNT AVQFHLKELY VAASEGSIAP
210 220 230 240 250
ILSEAQAHFG RRLSLGSYPD WSSNYFQVKL ILDSEEKEPL EECLAYLTAR
260 270 280 290 300
LPQGSLVPYQ PDAVEKAGEA VYKLAESGSC LGKKVAGALQ TIETALAQYH
310 320 330 340 350
LSQLCVGFNG GKDCTALLHL FHAAVQRKFP DVPKPLQILY IRSISPFPEL
360 370 380 390 400
EQFLQDTIKR YNLQVLEAEG NMKQALGELQ EKHPQLEAVL MGTRRTDPYS
410 420 430 440 450
CSLSHFSPTD PGWPSFMRIN PLLDWTYRNI WEFLRQLFVP YCILYDRGYT
460 470 480 490
SLGSRENTTQ NPALKCLSPG GHPVYRPAYL LENEDEERNS RM
Length:492
Mass (Da):54,766
Last modified:June 1, 2002 - v1
Checksum:i75008DD249A7F43E
GO
Isoform 2 (identifier: Q8R123-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     492-492: M → IPKTPGASWPSPRMGHKELKKEPRTLL

Show »
Length:518
Mass (Da):57,673
Checksum:iBE331637181B8654
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731R → S in BAE36639. (PubMed:16141072)Curated
Sequence conflicti390 – 3901L → Q in BAE36639. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei492 – 4921M → IPKTPGASWPSPRMGHKELK KEPRTLL in isoform 2. 1 PublicationVSP_027955

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK044501 mRNA. Translation: BAC31952.1.
AK161929 mRNA. Translation: BAE36639.1.
BC009152 mRNA. Translation: AAH09152.2.
BC025817 mRNA. Translation: AAH25817.1.
BC046769 mRNA. Translation: AAH46769.1.
CCDSiCCDS38492.1. [Q8R123-1]
RefSeqiNP_796015.2. NM_177041.3. [Q8R123-1]
UniGeneiMm.258142.

Genome annotation databases

EnsembliENSMUST00000050398; ENSMUSP00000051366; ENSMUSG00000042642. [Q8R123-2]
ENSMUST00000107426; ENSMUSP00000103049; ENSMUSG00000042642. [Q8R123-1]
ENSMUST00000129308; ENSMUSP00000122252; ENSMUSG00000042642. [Q8R123-1]
GeneIDi319945.
KEGGimmu:319945.
UCSCiuc008pzh.2. mouse. [Q8R123-2]
uc008pzi.1. mouse. [Q8R123-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK044501 mRNA. Translation: BAC31952.1 .
AK161929 mRNA. Translation: BAE36639.1 .
BC009152 mRNA. Translation: AAH09152.2 .
BC025817 mRNA. Translation: AAH25817.1 .
BC046769 mRNA. Translation: AAH46769.1 .
CCDSi CCDS38492.1. [Q8R123-1 ]
RefSeqi NP_796015.2. NM_177041.3. [Q8R123-1 ]
UniGenei Mm.258142.

3D structure databases

ProteinModelPortali Q8R123.
SMRi Q8R123. Positions 18-174, 264-465.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8R123. 1 interaction.
MINTi MINT-4118484.

PTM databases

PhosphoSitei Q8R123.

Proteomic databases

MaxQBi Q8R123.
PaxDbi Q8R123.
PRIDEi Q8R123.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000050398 ; ENSMUSP00000051366 ; ENSMUSG00000042642 . [Q8R123-2 ]
ENSMUST00000107426 ; ENSMUSP00000103049 ; ENSMUSG00000042642 . [Q8R123-1 ]
ENSMUST00000129308 ; ENSMUSP00000122252 ; ENSMUSG00000042642 . [Q8R123-1 ]
GeneIDi 319945.
KEGGi mmu:319945.
UCSCi uc008pzh.2. mouse. [Q8R123-2 ]
uc008pzi.1. mouse. [Q8R123-1 ]

Organism-specific databases

CTDi 80308.
MGIi MGI:2443030. Flad1.

Phylogenomic databases

eggNOGi COG0175.
GeneTreei ENSGT00390000007266.
HOGENOMi HOG000007185.
HOVERGENi HBG058211.
InParanoidi Q8R123.
KOi K00953.
OMAi SFMRINP.
OrthoDBi EOG7C5M9F.
PhylomeDBi Q8R123.
TreeFami TF314056.

Enzyme and pathway databases

UniPathwayi UPA00277 ; UER00407 .
Reactomei REACT_216155. Vitamin B2 (riboflavin) metabolism.

Miscellaneous databases

NextBioi 395713.
PROi Q8R123.
SOURCEi Search...

Gene expression databases

Bgeei Q8R123.
ExpressionAtlasi Q8R123. baseline and differential.
Genevestigatori Q8R123.

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. 1 hit.
[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. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Olfactory bulb and Retina.
  2. "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] (ISOFORM 1).
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain, Liver and Mammary gland.
  3. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 230-237, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast and Liver.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiFAD1_MOUSE
AccessioniPrimary (citable) accession number: Q8R123
Secondary accession number(s): Q3TSN6, Q8BXQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: June 1, 2002
Last modified: November 26, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3