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   27-MAR-2024, entry version 186.
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.
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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; 86.
DR   IntAct; O94808; 16.
DR   STRING; 9606.ENSP00000253778; -.
DR   DrugBank; DB00130; L-Glutamine.
DR   MEROPS; C44.972; -.
DR   iPTMnet; O94808; -.
DR   PhosphoSitePlus; O94808; -.
DR   SwissPalm; O94808; -.
DR   BioMuta; GFPT2; -.
DR   EPD; O94808; -.
DR   jPOST; O94808; -.
DR   MassIVE; O94808; -.
DR   MaxQB; O94808; -.
DR   PaxDb; 9606-ENSP00000253778; -.
DR   PeptideAtlas; O94808; -.
DR   ProteomicsDB; 50448; -.
DR   Pumba; O94808; -.
DR   Antibodypedia; 29588; 223 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   AGR; HGNC:4242; -.
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; GCTAKYW; -.
DR   OrthoDB; 1705390at2759; -.
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; 7 hits in 1148 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 154 other cell types or tissues.
DR   ExpressionAtlas; O94808; baseline and differential.
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; cd00714; GFAT; 1.
DR   CDD; cd05008; SIS_GlmS_GlmD_1; 1.
DR   CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR005855; GFAT.
DR   InterPro; IPR047084; GFAT_N.
DR   InterPro; IPR035466; GlmS/AgaS_SIS.
DR   InterPro; IPR035490; GlmS/FrlB_SIS.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR001347; SIS_dom.
DR   InterPro; IPR046348; SIS_dom_sf.
DR   NCBIfam; TIGR01135; glmS; 1.
DR   PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1.
DR   PANTHER; PTHR10937:SF10; GLUTAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE [ISOMERIZING] 2; 1.
DR   Pfam; PF13522; GATase_6; 1.
DR   Pfam; PF01380; SIS; 2.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   SUPFAM; SSF53697; SIS domain; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS51464; SIS; 2.
DR   Genevisible; O94808; HS.
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
//