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P47856 (GFPT1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1

EC=2.6.1.16
Alternative name(s):
D-fructose-6-phosphate amidotransferase 1
Glutamine:fructose-6-phosphate amidotransferase 1
Short name=GFAT 1
Short name=GFAT1
Hexosephosphate aminotransferase 1
Gene names
Name:Gfpt1
Synonyms:Gfpt
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length697 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins. Regulates the circadian expression of clock genes ARNTL/BMAL1 and CRY1. Ref.7

Catalytic activity

L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate.

Pathway

Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1.

Subunit structure

Homotetramer, may also exist as homodimers By similarity.

Tissue specificity

Isoform 1 is predominantly expressed in hindlimb muscle and is also expressed weakly in the heart. Seems to be selectively expressed in striated muscle. Ref.2

Induction

Expression in the liver oscillates in an ultradian manner (with a 12 hour period/cycle). Ref.7

Sequence similarities

Contains 1 glutamine amidotransferase type-2 domain.

Contains 2 SIS domains.

Ontologies

Keywords
   Biological processBiological rhythms
   Coding sequence diversityAlternative splicing
   DomainGlutamine amidotransferase
Repeat
   Molecular functionAminotransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processUDP-N-acetylglucosamine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

carbohydrate biosynthetic process

Inferred from electronic annotation. Source: InterPro

cellular response to insulin stimulus

Inferred from electronic annotation. Source: Ensembl

circadian regulation of gene expression

Inferred from mutant phenotype Ref.7. Source: UniProtKB

fructose 6-phosphate metabolic process

Inferred from electronic annotation. Source: Ensembl

glucosamine biosynthetic process

Inferred from electronic annotation. Source: Ensembl

glutamine metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of glycogen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

protein homotetramerization

Inferred from electronic annotation. Source: Ensembl

response to sucrose

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionamino acid binding

Inferred from electronic annotation. Source: Ensembl

carbohydrate binding

Inferred from electronic annotation. Source: Ensembl

glutamine-fructose-6-phosphate transaminase (isomerizing) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P47856-1)

Also known as: GFAT1m;

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: P47856-2)

The sequence of this isoform differs from the canonical sequence as follows:
     229-244: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 697696Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1
PRO_0000135281

Regions

Domain2 – 303302Glutamine amidotransferase type-2
Domain375 – 514140SIS 1
Domain546 – 687142SIS 2
Region311 – 678368Isomerase By similarity
Region392 – 3932Substrate-binding By similarity
Region437 – 4393Substrate-binding By similarity

Sites

Active site21For GATase activity By similarity
Binding site4421Substrate By similarity
Binding site5821Substrate By similarity

Amino acid modifications

Modified residue2591Phosphoserine Ref.5 Ref.6

Natural variations

Alternative sequence229 – 24416Missing in isoform 2.
VSP_007498

Experimental info

Sequence conflict991H → T in AAH10516. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (GFAT1m) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: B7B01F6CD4CEB655

FASTA69778,539
        10         20         30         40         50         60 
MCGIFAYLNY HVPRTRREIL ETLIKGLQRL EYRGYDSAGV GLDGGNDKDW EANACKIQLI 

        70         80         90        100        110        120 
KKKGKVKALD EEVHKQQDMD LDIEFDVHLG IAHTRWATHG EPNPVNSHPQ RSDKNNEFIV 

       130        140        150        160        170        180 
IHNGIITNYK DLKKFLESKG YDFESETDTE TIAKLVKYMY DNWESQDVSF TTLVERVIQQ 

       190        200        210        220        230        240 
LEGAFALVFK SVHFPGQAVG TRRGSPLLIG VRSEHKLSTD HIPILYRTAR TQIGSTWWGS 

       250        260        270        280        290        300 
QAERGKDKKG SCGLSRVDST TCLFPVEEKA VEYYFASDAS AVIEHTNRVI FLEDDDVAAV 

       310        320        330        340        350        360 
VDGRLSIHRI KRTAGDHPGR AVQTLQMELQ QIMKGNFSSF MQKEIFEQPE SVVNTMRGRV 

       370        380        390        400        410        420 
NFDDYTVNLG GLKDHIKEIQ RCRRLILIAC GTSYHAGVAT RQVLEELTEL PVMVELASDF 

       430        440        450        460        470        480 
LDRNTPVFRD DVCFFISQSG ETADTLMGLR YCKERGALTV GITNTVGSSI SRETDCGVHI 

       490        500        510        520        530        540 
NAGPEIGVAS TKAYTSQFVS LVMFALMMCD DRISMQERRK EIMLGLKRLP DLIKEVLSMD 

       550        560        570        580        590        600 
DEIQKLATEL YHQKSVLIMG RGYHYATCLE GALKIKEITY MHSEGILAGE LKHGPLALVD 

       610        620        630        640        650        660 
KLMPVIMIIM RDHTYAKCQN ALQQVVARQG RPVVICDKED TETIKNTKRT IKVPHSVDCL 

       670        680        690 
QGILSVIPLQ LLAFHLAVLR GYDVDFPRNL AKSVTVE 

« Hide

Isoform 2 [UniParc].

Checksum: BE358A1054107D0B
Show »

FASTA68176,723

References

« Hide 'large scale' references
[1]"The murine glutamine:fructose-6-phosphate amidotransferase-encoding cDNA sequence."
Sayeski P.P., Paterson A.J., Kudlow J.E.
Gene 140:289-290(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Strain: Swiss.
[2]"A novel variant of glutamine:fructose-6-phosphate amidotransferase-1 (GFAT1) mRNA is selectively expressed in striated muscle."
DeHaven J.E., Robinson K.A., Nelson B.A., Buse M.G.
Diabetes 50:2419-2424(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Strain: C57BL/6.
Tissue: Skeletal muscle.
[3]"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. expand/collapse author list , 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] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Testis.
[4]"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 2).
Tissue: Mammary gland, Salivary gland and Testis.
[5]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[6]"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[7]"O-GlcNAc signaling entrains the circadian clock by inhibiting BMAL1/CLOCK ubiquitination."
Li M.D., Ruan H.B., Hughes M.E., Lee J.S., Singh J.P., Jones S.P., Nitabach M.N., Yang X.
Cell Metab. 17:303-310(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U00932 mRNA. Translation: AAC27348.1.
AF334736 mRNA. Translation: AAK15341.1.
AK019852 mRNA. Translation: BAB31882.1.
BC002283 mRNA. Translation: AAH02283.1.
BC010516 mRNA. Translation: AAH10516.1.
BC050762 mRNA. Translation: AAH50762.1.
CCDSCCDS39545.1. [P47856-2]
PIRI53743.
RefSeqNP_038556.1. NM_013528.3. [P47856-2]
UniGeneMm.19893.

3D structure databases

ProteinModelPortalP47856.
SMRP47856. Positions 2-697.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199902. 1 interaction.
IntActP47856. 2 interactions.
MINTMINT-4096028.

Protein family/group databases

MEROPSC44.970.

PTM databases

PhosphoSiteP47856.

Proteomic databases

MaxQBP47856.
PaxDbP47856.
PRIDEP47856.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032057; ENSMUSP00000032057; ENSMUSG00000029992. [P47856-1]
ENSMUST00000113658; ENSMUSP00000109288; ENSMUSG00000029992. [P47856-2]
GeneID14583.
KEGGmmu:14583.
UCSCuc009csz.2. mouse. [P47856-2]
uc009cta.2. mouse. [P47856-1]

Organism-specific databases

CTD2673.
MGIMGI:95698. Gfpt1.

Phylogenomic databases

eggNOGCOG0449.
GeneTreeENSGT00390000010049.
HOGENOMHOG000258898.
HOVERGENHBG051724.
KOK00820.
OMAMYDNRDS.
OrthoDBEOG73NG2S.
PhylomeDBP47856.
TreeFamTF300864.

Enzyme and pathway databases

UniPathwayUPA00113; UER00528.

Gene expression databases

ArrayExpressP47856.
BgeeP47856.
CleanExMM_GFPT1.
GenevestigatorP47856.

Family and domain databases

Gene3D3.60.20.10. 2 hits.
InterProIPR017932. GATase_2_dom.
IPR000583. GATase_dom.
IPR005855. GlmS_trans.
IPR029055. Ntn_hydrolases_N.
IPR001347. SIS.
[Graphical view]
PfamPF00310. GATase_2. 2 hits.
PF01380. SIS. 2 hits.
[Graphical view]
SUPFAMSSF56235. SSF56235. 2 hits.
TIGRFAMsTIGR01135. glmS. 1 hit.
PROSITEPS51278. GATASE_TYPE_2. 1 hit.
PS51464. SIS. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio286318.
PROP47856.
SOURCESearch...

Entry information

Entry nameGFPT1_MOUSE
AccessionPrimary (citable) accession number: P47856
Secondary accession number(s): Q91XG9, Q99LP7, Q99MJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot