O94808 (GFPT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	682 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Domain	Glutamine amidotransferase Repeat
Molecular function	Aminotransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UDP-N-acetylglucosamine biosynthetic process Traceable author statement. Source: Reactome carbohydrate biosynthetic process Inferred from electronic annotation. Source: InterPro dolichol-linked oligosaccharide biosynthetic process Traceable author statement. Source: Reactome energy reserve metabolic process Traceable author statement Ref.1. Source: ProtInc fructose 6-phosphate metabolic process Traceable author statement Ref.1. Source: ProtInc glutamine metabolic process Inferred from electronic annotation. Source: UniProtKB-KW post-translational protein modification Traceable author statement. Source: Reactome protein N-linked glycosylation via asparagine Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome
Molecular_function	carbohydrate binding Inferred from electronic annotation. Source: InterPro glutamine-fructose-6-phosphate transaminase (isomerizing) activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 682	682	Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2		PRO_0000135283
Regions
	Domain	2 – 288	287	Glutamine amidotransferase type-2
	Domain	360 – 499	140	SIS 1
	Domain	531 – 672	142	SIS 2
Sites
	Active site	2	1	For GATase activity By similarity
Amino acid modifications
	Modified residue	245	1	Phosphoserine By similarity
Natural variations
	Natural variant	471	1	I → V. Ref.2 Corresponds to variant rs2303007 [ dbSNP | Ensembl ].		VAR_013311

Sequences

	Sequence		Length	Mass (Da)
	O94808 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A090D75526F3192B	FASTA	682	76,931
	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

References

	« Hide 'large scale' referencesShow '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.
IPI	IPI00216159.
RefSeq	NP_005101.1. NM_005110.2.
UniGene	Hs.696497.
3D structure databases
ProteinModelPortal	O94808.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000253778.
Protein family/group databases
MEROPS	C44.972.
PTM databases
PhosphoSite	O94808.
Proteomic databases
PaxDb	O94808.
PRIDE	O94808.
Protocols and materials databases
DNASU	9945.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000253778; ENSP00000253778; ENSG00000131459.
GeneID	9945.
KEGG	hsa:9945.
UCSC	uc003mlw.1. human.
Organism-specific databases
CTD	9945.
GeneCards	GC05M179727.
HGNC	HGNC:4242. GFPT2.
MIM	603865. gene.
neXtProt	NX_O94808.
PharmGKB	PA28652.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0449.
HOGENOM	HOG000258898.
HOVERGEN	HBG051724.
InParanoid	O94808.
KO	K00820.
OMA	SSANAHP.
OrthoDB	EOG4DV5KT.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00113; UER00528.
Gene expression databases
ArrayExpress	O94808.
Bgee	O94808.
CleanEx	HS_GFPT2.
Genevestigator	O94808.
GermOnline	ENSG00000131459. Homo sapiens.
Family and domain databases
InterPro	IPR017932. GATase_2_dom. IPR000583. GATase_dom. IPR005855. GlmS_trans. IPR001347. SIS. [Graphical view]
Pfam	PF00310. GATase_2. 2 hits. PF01380. SIS. 2 hits. [Graphical view]
TIGRFAMs	TIGR01135. glmS. 1 hit.
PROSITE	PS51278. GATASE_TYPE_2. 1 hit. PS51464. SIS. 2 hits. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00130. L-Glutamine.
GenomeRNAi	9945.
NextBio	37520.
SOURCE	Search...

Entry information

Entry name

GFPT2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 111 of the entry and version 3 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.