Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O94808 (GFPT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2

EC=2.6.1.16
Alternative name(s):
D-fructose-6-phosphate amidotransferase 2
Glutamine:fructose-6-phosphate amidotransferase 2
Short name=GFAT 2
Short name=GFAT2
Hexosephosphate aminotransferase 2
Gene names
Name:GFPT2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length682 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.

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.

Tissue specificity

Highest levels of expression in heart, placenta, and spinal cord.

Sequence similarities

Contains 1 glutamine amidotransferase type-2 domain.

Contains 2 SIS domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 682681Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2
PRO_0000135283

Regions

Domain2 – 288287Glutamine amidotransferase type-2
Domain360 – 499140SIS 1
Domain531 – 672142SIS 2

Sites

Active site21For GATase activity By similarity

Amino acid modifications

Modified residue2451Phosphoserine By similarity

Natural variations

Natural variant4711I → V. Ref.2
Corresponds to variant rs2303007 [ dbSNP | Ensembl ].
VAR_013311

Sequences

Sequence LengthMass (Da)Tools
O94808 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A090D75526F3192B

FASTA68276,931
        10         20         30         40         50         60 
MCGIFAYMNY RVPRTRKEIF ETLIKGLQRL EYRGYDSAGV AIDGNNHEVK ERHIQLVKKR 

        70         80         90        100        110        120 
GKVKALDEEL YKQDSMDLKV EFETHFGIAH TRWATHGVPS AVNSHPQRSD KGNEFVVIHN 

       130        140        150        160        170        180 
GIITNYKDLR KFLESKGYEF ESETDTETIA KLIKYVFDNR ETEDITFSTL VERVIQQLEG 

       190        200        210        220        230        240 
AFALVFKSVH YPGEAVATRR GSPLLIGVRS KYKLSTEQIP ILYRTCTLEN VKNICKTRMK 

       250        260        270        280        290        300 
RLDSSACLHA VGDKAVEFFF ASDASAIIEH TNRVIFLEDD DIAAVADGKL SIHRVKRSAS 

       310        320        330        340        350        360 
DDPSRAIQTL QMELQQIMKG NFSAFMQKEI FEQPESVFNT MRGRVNFETN TVLLGGLKDH 

       370        380        390        400        410        420 
LKEIRRCRRL IVIGCGTSYH AAVATRQVLE ELTELPVMVE LASDFLDRNT PVFRDDVCFF 

       430        440        450        460        470        480 
ISQSGETADT LLALRYCKDR GALTVGVTNT VGSSISRETD CGVHINAGPE IGVASTKAYT 

       490        500        510        520        530        540 
SQFISLVMFG LMMSEDRISL QNRRQEIIRG LRSLPELIKE VLSLEEKIHD LALELYTQRS 

       550        560        570        580        590        600 
LLVMGRGYNY ATCLEGALKI KEITYMHSEG ILAGELKHGP LALIDKQMPV IMVIMKDPCF 

       610        620        630        640        650        660 
AKCQNALQQV TARQGRPIIL CSKDDTESSK FAYKTIELPH TVDCLQGILS VIPLQLLSFH 

       670        680 
LAVLRGYDVD FPRNLAKSVT VE 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and mapping of a novel subtype of glutamine:fructose-6-phosphate amidotransferase (GFAT2) in human and mouse."
Oki T., Yamazaki K., Kuromitsu J., Okada M., Tanaka I.
Genomics 57:227-234(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Thymus.
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-471.
[3]"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].
Tissue: Kidney.
[4]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB016789 mRNA. Translation: BAA74731.1.
BT009818 mRNA. Translation: AAP88820.1.
BC000012 mRNA. Translation: AAH00012.1.
CCDSCCDS43411.1.
RefSeqNP_005101.1. NM_005110.2.
UniGeneHs.696497.

3D structure databases

ProteinModelPortalO94808.
SMRO94808. Positions 16-682.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115270. 4 interactions.
STRING9606.ENSP00000253778.

Chemistry

DrugBankDB00130. L-Glutamine.

Protein family/group databases

MEROPSC44.972.

PTM databases

PhosphoSiteO94808.

Proteomic databases

MaxQBO94808.
PaxDbO94808.
PRIDEO94808.

Protocols and materials databases

DNASU9945.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000253778; ENSP00000253778; ENSG00000131459.
GeneID9945.
KEGGhsa:9945.
UCSCuc003mlw.1. human.

Organism-specific databases

CTD9945.
GeneCardsGC05M179727.
HGNCHGNC:4242. GFPT2.
HPAHPA049528.
HPA056892.
MIM603865. gene.
neXtProtNX_O94808.
PharmGKBPA28652.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0449.
HOGENOMHOG000258898.
HOVERGENHBG051724.
InParanoidO94808.
KOK00820.
OMARCLPEMI.
OrthoDBEOG73NG2S.
PhylomeDBO94808.
TreeFamTF300864.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00113; UER00528.

Gene expression databases

ArrayExpressO94808.
BgeeO94808.
CleanExHS_GFPT2.
GenevestigatorO94808.

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

GenomeRNAi9945.
NextBio37520.
PROO94808.
SOURCESearch...

Entry information

Entry nameGFPT2_HUMAN
AccessionPrimary (citable) accession number: O94808
Secondary accession number(s): Q53XM2, Q9BWS4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 124 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM