PGM2L_HUMAN
ID PGM2L_HUMAN Reviewed; 622 AA.
AC Q6PCE3; Q96MQ7; Q9UIK3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Glucose 1,6-bisphosphate synthase {ECO:0000305|PubMed:17804405};
DE EC=2.7.1.106 {ECO:0000269|PubMed:17804405};
DE AltName: Full=PMMLP;
DE AltName: Full=Phosphoglucomutase-2-like 1;
GN Name=PGM2L1 {ECO:0000312|HGNC:HGNC:20898}; Synonyms=BM32A;
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=Brain;
RA Mori K., Miyoshi Y., Nakamura Y.;
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-531.
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS PRO-14 AND ILE-531.
RC TISSUE=Placenta;
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17804405; DOI=10.1074/jbc.m706818200;
RA Maliekal P., Sokolova T., Vertommen D., Veiga-da-Cunha M.,
RA Van Schaftingen E.;
RT "Molecular identification of mammalian phosphopentomutase and glucose-1,6-
RT bisphosphate synthase, two members of the alpha-D-phosphohexomutase
RT family.";
RL J. Biol. Chem. 282:31844-31851(2007).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=18927083; DOI=10.1074/jbc.m805224200;
RA Veiga-da-Cunha M., Vleugels W., Maliekal P., Matthijs G.,
RA Van Schaftingen E.;
RT "Mammalian phosphomannomutase PMM1 is the brain IMP-sensitive glucose-1,6-
RT bisphosphatase.";
RL J. Biol. Chem. 283:33988-33993(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND IDENTIFICATION BY
RP 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Glucose 1,6-bisphosphate synthase using 1,3-
CC bisphosphoglycerate as a phosphate donor and a series of 1-phosphate
CC sugars, including glucose 1-phosphate, mannose 1-phosphate, ribose 1-
CC phosphate and deoxyribose 1-phosphate, as acceptors (PubMed:17804405).
CC In vitro, also exhibits very low phosphopentomutase and
CC phosphoglucomutase activity which are most probably not physiologically
CC relevant (PubMed:17804405). {ECO:0000269|PubMed:17804405,
CC ECO:0000269|PubMed:18927083}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate + alpha-D-glucose 1-
CC phosphate = (2R)-3-phosphoglycerate + alpha-D-glucose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:16769, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:58392,
CC ChEBI:CHEBI:58601; EC=2.7.1.106;
CC Evidence={ECO:0000269|PubMed:17804405, ECO:0000269|PubMed:18927083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16770;
CC Evidence={ECO:0000269|PubMed:18927083};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate + alpha-D-glucose 6-
CC phosphate = (2R)-3-phosphoglycerate + alpha-D-glucose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:70911, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58225, ChEBI:CHEBI:58272,
CC ChEBI:CHEBI:58392; Evidence={ECO:0000269|PubMed:17804405};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70912;
CC Evidence={ECO:0000305|PubMed:17804405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate + alpha-D-ribose 1-
CC phosphate = (2R)-3-phosphoglycerate + alpha-D-ribose 1,5-bisphosphate
CC + H(+); Xref=Rhea:RHEA:70899, ChEBI:CHEBI:15378, ChEBI:CHEBI:57604,
CC ChEBI:CHEBI:57720, ChEBI:CHEBI:58272, ChEBI:CHEBI:68688;
CC Evidence={ECO:0000269|PubMed:17804405};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70900;
CC Evidence={ECO:0000305|PubMed:17804405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate + 2-deoxy-alpha-D-ribose 1-
CC phosphate = (2R)-3-phosphoglycerate + 2-deoxy-alpha-D-ribose 1,5-
CC bisphosphate + H(+); Xref=Rhea:RHEA:70903, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57259, ChEBI:CHEBI:57604, ChEBI:CHEBI:58272,
CC ChEBI:CHEBI:190126; Evidence={ECO:0000269|PubMed:17804405};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70904;
CC Evidence={ECO:0000305|PubMed:17804405};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-3-phospho-glyceroyl phosphate + alpha-D-mannose 1-
CC phosphate = (2R)-3-phosphoglycerate + alpha-D-mannose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:70907, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:58409,
CC ChEBI:CHEBI:190127; Evidence={ECO:0000269|PubMed:17804405};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70908;
CC Evidence={ECO:0000305|PubMed:17804405};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.32 mM for alpha-D-glucose 1-phosphate (for glucose 1,6-
CC bisphosphate synthase activity) {ECO:0000269|PubMed:17804405};
CC KM=0.44 mM for alpha-D-ribose 1-phosphate (for aldose-bisphosphate
CC synthase activity) {ECO:0000269|PubMed:17804405};
CC KM=0.30 mM for 2-deoxyribose 1-phosphate (for aldose-bisphosphate
CC synthase activity) {ECO:0000269|PubMed:17804405};
CC KM=0.79 mM for alpha-D-mannose 1-phosphate (for aldose-bisphosphate
CC synthase activity) {ECO:0000269|PubMed:17804405};
CC KM=0.36 mM for alpha-D-glucose 6-phosphate (for aldose-bisphosphate
CC synthase activity) {ECO:0000269|PubMed:17804405};
CC Vmax=1.45 umol/min/mg enzyme for alpha-D-glucose 1-phosphate
CC {ECO:0000269|PubMed:17804405};
CC Vmax=1.93 umol/min/mg enzyme for alpha-D-ribose 1-phosphate
CC {ECO:0000269|PubMed:17804405};
CC Vmax=1.36 umol/min/mg enzyme for 2-deoxyribose 1-phosphate
CC {ECO:0000269|PubMed:17804405};
CC Vmax=1.38 umol/min/mg enzyme for alpha-D-mannose 1-phosphate
CC {ECO:0000269|PubMed:17804405};
CC Vmax=0.77 umol/min/mg enzyme for alpha-D-glucose 6-phosphate
CC {ECO:0000269|PubMed:17804405};
CC Vmax=0.14 umol/min/mg enzyme for alpha-D-Ribose 5-phosphate
CC {ECO:0000269|PubMed:17804405};
CC Vmax=0.04 umol/min/mg enzyme for 2-deoxyribose 5-phosphate
CC {ECO:0000269|PubMed:17804405};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:17804405}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; AB019210; BAA82756.1; -; mRNA.
DR EMBL; AK056591; BAB71227.1; -; mRNA.
DR EMBL; AP001085; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059360; AAH59360.1; -; mRNA.
DR CCDS; CCDS8231.1; -.
DR RefSeq; NP_775853.2; NM_173582.4.
DR AlphaFoldDB; Q6PCE3; -.
DR SMR; Q6PCE3; -.
DR BioGRID; 129496; 20.
DR IntAct; Q6PCE3; 7.
DR MINT; Q6PCE3; -.
DR STRING; 9606.ENSP00000298198; -.
DR iPTMnet; Q6PCE3; -.
DR PhosphoSitePlus; Q6PCE3; -.
DR BioMuta; PGM2L1; -.
DR DMDM; 317373530; -.
DR EPD; Q6PCE3; -.
DR jPOST; Q6PCE3; -.
DR MassIVE; Q6PCE3; -.
DR MaxQB; Q6PCE3; -.
DR PaxDb; Q6PCE3; -.
DR PeptideAtlas; Q6PCE3; -.
DR PRIDE; Q6PCE3; -.
DR ProteomicsDB; 67064; -.
DR Antibodypedia; 31067; 145 antibodies from 19 providers.
DR DNASU; 283209; -.
DR Ensembl; ENST00000298198.5; ENSP00000298198.4; ENSG00000165434.8.
DR GeneID; 283209; -.
DR KEGG; hsa:283209; -.
DR MANE-Select; ENST00000298198.5; ENSP00000298198.4; NM_173582.6; NP_775853.2.
DR UCSC; uc001ovb.2; human.
DR CTD; 283209; -.
DR GeneCards; PGM2L1; -.
DR HGNC; HGNC:20898; PGM2L1.
DR HPA; ENSG00000165434; Tissue enhanced (brain).
DR MIM; 611610; gene.
DR neXtProt; NX_Q6PCE3; -.
DR OpenTargets; ENSG00000165434; -.
DR PharmGKB; PA134938366; -.
DR VEuPathDB; HostDB:ENSG00000165434; -.
DR eggNOG; KOG1220; Eukaryota.
DR GeneTree; ENSGT00940000158353; -.
DR HOGENOM; CLU_016950_0_1_1; -.
DR InParanoid; Q6PCE3; -.
DR OMA; PQDNGYK; -.
DR OrthoDB; 1041556at2759; -.
DR PhylomeDB; Q6PCE3; -.
DR TreeFam; TF300692; -.
DR PathwayCommons; Q6PCE3; -.
DR Reactome; R-HSA-3322077; Glycogen synthesis.
DR Reactome; R-HSA-70171; Glycolysis.
DR Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
DR Reactome; R-HSA-70370; Galactose catabolism.
DR SABIO-RK; Q6PCE3; -.
DR SignaLink; Q6PCE3; -.
DR BioGRID-ORCS; 283209; 15 hits in 1078 CRISPR screens.
DR ChiTaRS; PGM2L1; human.
DR GenomeRNAi; 283209; -.
DR Pharos; Q6PCE3; Tbio.
DR PRO; PR:Q6PCE3; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6PCE3; protein.
DR Bgee; ENSG00000165434; Expressed in middle temporal gyrus and 186 other tissues.
DR Genevisible; Q6PCE3; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0047933; F:glucose-1,6-bisphosphate synthase activity; IDA:UniProtKB.
DR GO; GO:0016868; F:intramolecular transferase activity, phosphotransferases; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR005843; A-D-PHexomutase_C.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR Pfam; PF00408; PGM_PMM_IV; 1.
DR SUPFAM; SSF53738; SSF53738; 3.
DR SUPFAM; SSF55957; SSF55957; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Isomerase;
KW Magnesium; Metal-binding; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..622
FT /note="Glucose 1,6-bisphosphate synthase"
FT /id="PRO_0000147784"
FT ACT_SITE 175
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 73
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 175
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 175
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /note="via phosphate group"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 332
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 334
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 336
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 337
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 434
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 436
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT BINDING 448
FT /ligand="alpha-D-glucose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58392"
FT /evidence="ECO:0000250|UniProtKB:P00949"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 14
FT /note="L -> P (in dbSNP:rs12049823)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_028094"
FT VARIANT 531
FT /note="V -> I (in dbSNP:rs592644)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_028095"
FT VARIANT 608
FT /note="N -> I (in dbSNP:rs36014178)"
FT /id="VAR_056665"
FT CONFLICT 69
FT /note="T -> A (in Ref. 2; BAB71227)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 70442 MW; 8AE00403B5D973CA CRC64;
MAENTEGDLN SNLLHAPYHT GDPQLDTAIG QWLRWDKNPK TKEQIENLLR NGMNKELRDR
LCCRMTFGTA GLRSAMGAGF CYINDLTVIQ STQGMYKYLE RCFSDFKQRG FVVGYDTRGQ
VTSSCSSQRL AKLTAAVLLA KDVPVYLFSR YVPTPFVPYA VQKLKAVAGV MITASHNRKE
DNGYKVYWET GAQITSPHDK EILKCIEECV EPWNGSWNDN LVDTSPLKRD PLQDICRRYM
EDLKKICFYR ELNSKTTLKF VHTSFHGVGH DYVQLAFKVF GFKPPIPVPE QKDPDPDFST
VKCPNPEEGE SVLELSLRLA EKENARVVLA TDPDADRLAA AELQENGCWK VFTGNELAAL
FGWWMFDCWK KNKSRNADVK NVYMLATTVS SKILKAIALK EGFHFEETLP GFKWIGSRII
DLLENGKEVL FAFEESIGFL CGTSVLDKDG VSAAVVVAEM ASYLETMNIT LKQQLVKVYE
KYGYHISKTS YFLCYEPPTI KSIFERLRNF DSPKEYPKFC GTFAILHVRD VTTGYDSSQP
NKKSVLPVSK NSQMITFTFQ NGCVATLRTS GTEPKIKYYA EMCASPDQSD TALLEEELKK
LIDALIENFL QPSKNGLIWR SV
