GFPT2_HUMAN
ID GFPT2_HUMAN Reviewed; 682 AA.
AC O94808; Q53XM2; Q9BWS4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2;
DE EC=2.6.1.16 {ECO:0000250|UniProtKB:P82808};
DE AltName: Full=D-fructose-6-phosphate amidotransferase 2;
DE AltName: Full=Glutamine:fructose-6-phosphate amidotransferase 2;
DE Short=GFAT 2;
DE Short=GFAT2;
DE AltName: Full=Hexosephosphate aminotransferase 2;
GN Name=GFPT2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=10198162; DOI=10.1006/geno.1999.5785;
RA Oki T., Yamazaki K., Kuromitsu J., Okada M., Tanaka I.;
RT "cDNA cloning and mapping of a novel subtype of glutamine:fructose-6-
RT phosphate amidotransferase (GFAT2) in human and mouse.";
RL Genomics 57:227-234(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-471.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Controls the flux of glucose into the hexosamine pathway.
CC Most likely involved in regulating the availability of precursors for
CC N- and O-linked glycosylation of proteins.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-
CC phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16;
CC Evidence={ECO:0000250|UniProtKB:P82808};
CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-
CC glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-
CC fructose 6-phosphate: step 1/1. {ECO:0000250|UniProtKB:P82808}.
CC -!- INTERACTION:
CC O94808; Q9NUX5: POT1; NbExp=2; IntAct=EBI-6916534, EBI-752420;
CC -!- TISSUE SPECIFICITY: Highest levels of expression in heart, placenta,
CC and spinal cord.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB016789; BAA74731.1; -; mRNA.
DR EMBL; BT009818; AAP88820.1; -; mRNA.
DR EMBL; BC000012; AAH00012.1; -; mRNA.
DR CCDS; CCDS43411.1; -.
DR RefSeq; NP_005101.1; NM_005110.3.
DR AlphaFoldDB; O94808; -.
DR SMR; O94808; -.
DR BioGRID; 115270; 81.
DR IntAct; O94808; 14.
DR STRING; 9606.ENSP00000253778; -.
DR DrugBank; DB00130; L-Glutamine.
DR MEROPS; C44.972; -.
DR iPTMnet; O94808; -.
DR PhosphoSitePlus; O94808; -.
DR BioMuta; GFPT2; -.
DR EPD; O94808; -.
DR jPOST; O94808; -.
DR MassIVE; O94808; -.
DR MaxQB; O94808; -.
DR PaxDb; O94808; -.
DR PeptideAtlas; O94808; -.
DR PRIDE; O94808; -.
DR ProteomicsDB; 50448; -.
DR Antibodypedia; 29588; 198 antibodies from 27 providers.
DR DNASU; 9945; -.
DR Ensembl; ENST00000253778.13; ENSP00000253778.8; ENSG00000131459.13.
DR GeneID; 9945; -.
DR KEGG; hsa:9945; -.
DR MANE-Select; ENST00000253778.13; ENSP00000253778.8; NM_005110.4; NP_005101.1.
DR UCSC; uc003mlw.2; human.
DR CTD; 9945; -.
DR DisGeNET; 9945; -.
DR GeneCards; GFPT2; -.
DR HGNC; HGNC:4242; GFPT2.
DR HPA; ENSG00000131459; Tissue enhanced (adipose).
DR MIM; 603865; gene.
DR neXtProt; NX_O94808; -.
DR OpenTargets; ENSG00000131459; -.
DR PharmGKB; PA28652; -.
DR VEuPathDB; HostDB:ENSG00000131459; -.
DR eggNOG; KOG1268; Eukaryota.
DR GeneTree; ENSGT00940000156413; -.
DR HOGENOM; CLU_012520_5_2_1; -.
DR InParanoid; O94808; -.
DR OMA; TSYYSGC; -.
DR OrthoDB; 262871at2759; -.
DR PhylomeDB; O94808; -.
DR TreeFam; TF300864; -.
DR PathwayCommons; O94808; -.
DR Reactome; R-HSA-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR SignaLink; O94808; -.
DR UniPathway; UPA00113; UER00528.
DR BioGRID-ORCS; 9945; 6 hits in 1068 CRISPR screens.
DR ChiTaRS; GFPT2; human.
DR GenomeRNAi; 9945; -.
DR Pharos; O94808; Tbio.
DR PRO; PR:O94808; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O94808; protein.
DR Bgee; ENSG00000131459; Expressed in pericardium and 152 other tissues.
DR ExpressionAtlas; O94808; baseline and differential.
DR Genevisible; O94808; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0006112; P:energy reserve metabolic process; TAS:ProtInc.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central.
DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; TAS:Reactome.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central.
DR CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR005855; GlmS_trans.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF53697; SSF53697; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01135; glmS; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
PE 1: Evidence at protein level;
KW Aminotransferase; Glutamine amidotransferase; Phosphoprotein;
KW Reference proteome; Repeat; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..682
FT /note="Glutamine--fructose-6-phosphate aminotransferase
FT [isomerizing] 2"
FT /id="PRO_0000135283"
FT DOMAIN 2..288
FT /note="Glutamine amidotransferase type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609"
FT DOMAIN 360..499
FT /note="SIS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT DOMAIN 531..672
FT /note="SIS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797"
FT ACT_SITE 2
FT /note="For GATase activity"
FT /evidence="ECO:0000250|UniProtKB:P14742"
FT BINDING 377..378
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT BINDING 422..424
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT BINDING 427
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT BINDING 578
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q06210"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 471
FT /note="I -> V (in dbSNP:rs2303007)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_013311"
SQ SEQUENCE 682 AA; 76931 MW; A090D75526F3192B CRC64;
MCGIFAYMNY RVPRTRKEIF ETLIKGLQRL EYRGYDSAGV AIDGNNHEVK ERHIQLVKKR
GKVKALDEEL YKQDSMDLKV EFETHFGIAH TRWATHGVPS AVNSHPQRSD KGNEFVVIHN
GIITNYKDLR KFLESKGYEF ESETDTETIA KLIKYVFDNR ETEDITFSTL VERVIQQLEG
AFALVFKSVH YPGEAVATRR GSPLLIGVRS KYKLSTEQIP ILYRTCTLEN VKNICKTRMK
RLDSSACLHA VGDKAVEFFF ASDASAIIEH TNRVIFLEDD DIAAVADGKL SIHRVKRSAS
DDPSRAIQTL QMELQQIMKG NFSAFMQKEI FEQPESVFNT MRGRVNFETN TVLLGGLKDH
LKEIRRCRRL IVIGCGTSYH AAVATRQVLE ELTELPVMVE LASDFLDRNT PVFRDDVCFF
ISQSGETADT LLALRYCKDR GALTVGVTNT VGSSISRETD CGVHINAGPE IGVASTKAYT
SQFISLVMFG LMMSEDRISL QNRRQEIIRG LRSLPELIKE VLSLEEKIHD LALELYTQRS
LLVMGRGYNY ATCLEGALKI KEITYMHSEG ILAGELKHGP LALIDKQMPV IMVIMKDPCF
AKCQNALQQV TARQGRPIIL CSKDDTESSK FAYKTIELPH TVDCLQGILS VIPLQLLSFH
LAVLRGYDVD FPRNLAKSVT VE
