KPYM_RAT
ID KPYM_RAT Reviewed; 531 AA.
AC P11980; P11981;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Pyruvate kinase PKM;
DE EC=2.7.1.40 {ECO:0000250|UniProtKB:P14618};
DE AltName: Full=Pyruvate kinase muscle isozyme;
DE AltName: Full=Threonine-protein kinase PKM2 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:P14618};
DE AltName: Full=Tyrosine-protein kinase PKM2 {ECO:0000305};
DE EC=2.7.10.2 {ECO:0000250|UniProtKB:P14618};
GN Name=Pkm; Synonyms=Pkm2, Pykm;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS M1 AND M2).
RX PubMed=3020052; DOI=10.1016/s0021-9258(18)67091-7;
RA Noguchi T., Inoue H., Tanaka T.;
RT "The M1- and M2-type isozymes of rat pyruvate kinase are produced from the
RT same gene by alternative RNA splicing.";
RL J. Biol. Chem. 261:13807-13812(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS M1 AND M2), AND SEQUENCE
RP REVISION.
RX PubMed=2914912; DOI=10.1016/s0021-9258(18)94185-2;
RA Takenaka M., Noguchi T., Inoue H., Yamada K., Matsuda T., Tanaka T.;
RT "Rat pyruvate kinase M gene: its complete structure and characterization of
RT the 5'-flanking region.";
RL J. Biol. Chem. 264:2363-2367(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM M1).
RC TISSUE=Pituitary;
RX PubMed=2780321; DOI=10.1093/nar/17.17.7106;
RA Parkinson C., Kato H., Cheng S.;
RT "The nucleotide sequence of a full length cDNA encoding rat pituitary
RT pyruvate kinase.";
RL Nucleic Acids Res. 17:7106-7106(1989).
RN [4]
RP PROTEIN SEQUENCE OF 33-56; 74-89; 93-115; 174-186; 208-246; 279-294;
RP 343-376; 393-400; 423-436; 476-498 AND 505-526, PROTEIN SEQUENCE OF 384-399
RP (ISOFORM M2), AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
RL Submitted (JUL-2007) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-97 AND SER-100, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Catalyzes the final rate-limiting step of glycolysis by
CC mediating the transfer of a phosphoryl group from phosphoenolpyruvate
CC (PEP) to ADP, generating ATP. The ratio between the highly active
CC tetrameric form and nearly inactive dimeric form determines whether
CC glucose carbons are channeled to biosynthetic processes or used for
CC glycolytic ATP production. The transition between the 2 forms
CC contributes to the control of glycolysis and is important for tumor
CC cell proliferation and survival. {ECO:0000250|UniProtKB:P14618}.
CC -!- FUNCTION: [Isoform M2]: Isoform specifically expressed during
CC embryogenesis that has low pyruvate kinase activity by itself and
CC requires allosteric activation by D-fructose 1,6-bisphosphate (FBP) for
CC pyruvate kinase activity. In addition to its pyruvate kinase activity
CC in the cytoplasm, also acts as a regulator of transcription in the
CC nucleus by acting as a protein kinase. Translocates into the nucleus in
CC response to various signals, such as EGF receptor activation, and
CC homodimerizes, leading to its conversion into a protein threonine- and
CC tyrosine-protein kinase. Catalyzes phosphorylation of STAT3 at 'Tyr-
CC 705' and histone H3 at 'Thr-11' (H3T11ph), leading to activate
CC transcription. Its ability to activate transcription plays a role in
CC cancer cells by promoting cell proliferation and promote tumorigenesis
CC (By similarity). Promotes the expression of the immune checkpoint
CC protein CD274 in ARNTL/BMAL1-deficient macrophages. May also act as a
CC translation regulator for a subset of mRNAs, independently of its
CC pyruvate kinase activity: associates with subpools of endoplasmic
CC reticulum-associated ribosomes, binds directly to the mRNAs translated
CC at the endoplasmic reticulum and promotes translation of these
CC endoplasmic reticulum-destined mRNAs (By similarity). Plays a role in
CC caspase independent cell death of tumor cells (By similarity).
CC {ECO:0000250|UniProtKB:P14618, ECO:0000250|UniProtKB:P52480}.
CC -!- FUNCTION: [Isoform M1]: Pyruvate kinase isoform expressed in adult
CC tissues, which replaces isoform M2 after birth. In contrast to isoform
CC M2, has high pyruvate kinase activity by itself and does not require
CC allosteric activation by D-fructose 1,6-bisphosphate (FBP) for
CC activity. {ECO:0000250|UniProtKB:P14618}.
CC -!- CATALYTIC ACTIVITY: [Isoform M2]:
CC Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=2.7.1.40; Evidence={ECO:0000250|UniProtKB:P14618};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18159;
CC Evidence={ECO:0000250|UniProtKB:P14618};
CC -!- CATALYTIC ACTIVITY: [Isoform M1]:
CC Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate;
CC Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216;
CC EC=2.7.1.40; Evidence={ECO:0000250|UniProtKB:P14618};
CC -!- CATALYTIC ACTIVITY: [Isoform M2]:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000250|UniProtKB:P14618};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10597;
CC Evidence={ECO:0000250|UniProtKB:P14618};
CC -!- CATALYTIC ACTIVITY: [Isoform M2]:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P14618};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000250|UniProtKB:P14618};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P14618};
CC -!- COFACTOR:
CC Name=K(+); Xref=ChEBI:CHEBI:29103;
CC Evidence={ECO:0000250|UniProtKB:P14618};
CC -!- ACTIVITY REGULATION: [Isoform M2]: Isoform M2 is allosterically
CC activated by D-fructose 1,6-bisphosphate (FBP). Inhibited by oxalate
CC and 3,3',5-triiodo-L-thyronine (T3). The activity of the tetrameric
CC form is inhibited by PML. Selective binding to tyrosine-phosphorylated
CC peptides releases the allosteric activator FBP, leading to inhibition
CC of PKM enzymatic activity, this diverts glucose metabolites from energy
CC production to anabolic processes when cells are stimulated by certain
CC growth factors. Glycolytic flux are highly dependent on de novo
CC biosynthesis of serine and glycine, and serine is a natural ligand and
CC allosteric activator of isoform M2. {ECO:0000250|UniProtKB:P14618}.
CC -!- ACTIVITY REGULATION: [Isoform M1]: Has high pyruvate kinase activity by
CC itself and does not require allosteric activation by D-fructose 1,6-
CC bisphosphate (FBP) for activity. {ECO:0000250|UniProtKB:P14618}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 5/5. {ECO:0000250|UniProtKB:P14618}.
CC -!- SUBUNIT: [Isoform M2]: Monomer and homotetramer; exists as a monomer in
CC the absence of D-fructose 1,6-bisphosphate (FBP), and reversibly
CC associates to form a homotetramer in the presence of FBP. The monomeric
CC form binds 3,3',5-triiodo-L-thyronine (T3). Tetramer formation induces
CC pyruvate kinase activity. The tetrameric form has high affinity for the
CC substrate and is associated within the glycolytic enzyme complex. FBP
CC stimulates the formation of tetramers from dimers. Homodimer; exists in
CC a dimeric form in tumor cells and the dimeric form has less affinity
CC for the phosphoenolpyruvate substrate. The homodimer converts into a
CC protein kinase. Interacts with HERC1, POU5F1 and PML. Interacts with
CC EGLN3; the interaction hydroxylates PKM under hypoxia and enhances
CC binding to HIF1A. Interacts with HIF1A; the interaction is enhanced by
CC binding of EGLN3, promoting enhanced transcription activity under
CC hypoxia. Interacts with TRIM35; this interaction prevents FGFR1-
CC dependent tyrosine phosphorylation. Interacts with JMJD8. Interacts
CC with TRAF4. Interacts with (phosphorylated) CTNNB1; leading to activate
CC transcription. {ECO:0000250|UniProtKB:P14618}.
CC -!- SUBCELLULAR LOCATION: [Isoform M2]: Cytoplasm
CC {ECO:0000250|UniProtKB:P14618}. Nucleus {ECO:0000250|UniProtKB:P14618}.
CC Note=Translocates to the nucleus in response to various signals, such
CC as EGF receptor activation or apoptotic stimuli.
CC {ECO:0000250|UniProtKB:P14618}.
CC -!- SUBCELLULAR LOCATION: [Isoform M1]: Cytoplasm
CC {ECO:0000250|UniProtKB:P14618}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=M1 {ECO:0000303|PubMed:3020052}; Synonyms=PKM1
CC {ECO:0000303|PubMed:3020052};
CC IsoId=P11980-1; Sequence=Displayed;
CC Name=M2 {ECO:0000303|PubMed:3020052}; Synonyms=PKM2
CC {ECO:0000303|PubMed:3020052};
CC IsoId=P11980-2, P11981-1;
CC Sequence=VSP_011107;
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P14618}.
CC -!- PTM: Under hypoxia, hydroxylated by EGLN3.
CC {ECO:0000250|UniProtKB:P14618}.
CC -!- PTM: Acetylation at Lys-305 is stimulated by high glucose
CC concentration, it decreases enzyme activity and promotes its lysosomal-
CC dependent degradation via chaperone-mediated autophagy.
CC {ECO:0000250|UniProtKB:P14618}.
CC -!- PTM: [Isoform M2]: Acetylated by EP300, leading to impair
CC phosphoenolpyruvate substrate-binding and promote its homodimerization
CC and subsequent translocation to the nucleus. Deacetylation by SIRT6
CC promotes its nuclear export into the cytoplasm, leading to suppress its
CC nuclear localization and oncogenic function.
CC {ECO:0000250|UniProtKB:P14618}.
CC -!- PTM: FGFR1-dependent tyrosine phosphorylation is reduced by interaction
CC with TRIM35. {ECO:0000250|UniProtKB:P14618}.
CC -!- MISCELLANEOUS: There are 4 isozymes of pyruvate kinase in mammals (L,
CC R, M1, M2) encoded by 2 different genes: PKLR and PKM. The L and R
CC isozymes are generated from the PKLR by differential splicing of RNA;
CC the M1 and M2 forms are produced from the PKM gene by differential
CC splicing. L type is major isozyme in the liver, R is found in red
CC cells, M1 is the main form in muscle, heart and brain, and M2 is found
CC in early fetal tissues as well as in most cancer cells.
CC {ECO:0000250|UniProtKB:P14618}.
CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}.
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DR EMBL; M24359; AAB93666.1; -; Genomic_DNA.
DR EMBL; M24359; AAB93667.1; -; Genomic_DNA.
DR EMBL; M14377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X15800; CAA33799.1; -; mRNA.
DR PIR; A26186; A26186.
DR PIR; B26186; B26186.
DR RefSeq; NP_445749.1; NM_053297.2. [P11980-1]
DR RefSeq; XP_006243250.2; XM_006243188.3. [P11980-2]
DR AlphaFoldDB; P11980; -.
DR SMR; P11980; -.
DR BioGRID; 247659; 8.
DR CORUM; P11980; -.
DR IntAct; P11980; 6.
DR MINT; P11980; -.
DR STRING; 10116.ENSRNOP00000015331; -.
DR BindingDB; P11980; -.
DR ChEMBL; CHEMBL4994; -.
DR MoonProt; P11980; -.
DR iPTMnet; P11980; -.
DR PhosphoSitePlus; P11980; -.
DR World-2DPAGE; 0004:P11980; -.
DR jPOST; P11980; -.
DR PaxDb; P11980; -.
DR PRIDE; P11980; -.
DR DNASU; 25630; -.
DR GeneID; 25630; -.
DR KEGG; rno:25630; -.
DR UCSC; RGD:3337; rat. [P11980-1]
DR CTD; 5315; -.
DR RGD; 3337; Pkm.
DR VEuPathDB; HostDB:ENSRNOG00000011329; -.
DR eggNOG; KOG2323; Eukaryota.
DR HOGENOM; CLU_015439_0_1_1; -.
DR InParanoid; P11980; -.
DR OMA; QVPIVQK; -.
DR OrthoDB; 933620at2759; -.
DR PhylomeDB; P11980; -.
DR TreeFam; TF300390; -.
DR SABIO-RK; P11980; -.
DR UniPathway; UPA00109; UER00188.
DR PRO; PR:P11980; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000011329; Expressed in skeletal muscle tissue and 19 other tissues.
DR ExpressionAtlas; P11980; baseline and differential.
DR Genevisible; P11980; RN.
DR GO; GO:0005929; C:cilium; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:1902912; C:pyruvate kinase complex; IDA:CAFA.
DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0043531; F:ADP binding; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IDA:CAFA.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0004743; F:pyruvate kinase activity; IDA:CAFA.
DR GO; GO:0070324; F:thyroid hormone binding; IDA:CAFA.
DR GO; GO:0031100; P:animal organ regeneration; IDA:RGD.
DR GO; GO:0006754; P:ATP biosynthetic process; IDA:RGD.
DR GO; GO:0061621; P:canonical glycolysis; ISO:RGD.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IDA:RGD.
DR GO; GO:0006096; P:glycolytic process; IDA:CAFA.
DR GO; GO:0001889; P:liver development; IDA:RGD.
DR GO; GO:2000767; P:positive regulation of cytoplasmic translation; ISS:UniProtKB.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0012501; P:programmed cell death; ISO:RGD.
DR GO; GO:0042866; P:pyruvate biosynthetic process; IDA:RGD.
DR GO; GO:0009629; P:response to gravity; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0032868; P:response to insulin; IEP:RGD.
DR GO; GO:0014870; P:response to muscle inactivity; IEP:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0043403; P:skeletal muscle tissue regeneration; IDA:RGD.
DR CDD; cd00288; Pyruvate_Kinase; 1.
DR Gene3D; 2.40.33.10; -; 1.
DR Gene3D; 3.20.20.60; -; 1.
DR Gene3D; 3.40.1380.20; -; 2.
DR InterPro; IPR001697; Pyr_Knase.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR InterPro; IPR018209; Pyrv_Knase_AS.
DR InterPro; IPR015793; Pyrv_Knase_brl.
DR InterPro; IPR015795; Pyrv_Knase_C.
DR InterPro; IPR036918; Pyrv_Knase_C_sf.
DR InterPro; IPR015806; Pyrv_Knase_insert_dom_sf.
DR PANTHER; PTHR11817; PTHR11817; 1.
DR Pfam; PF00224; PK; 1.
DR Pfam; PF02887; PK_C; 1.
DR PRINTS; PR01050; PYRUVTKNASE.
DR SUPFAM; SSF50800; SSF50800; 1.
DR SUPFAM; SSF51621; SSF51621; 1.
DR SUPFAM; SSF52935; SSF52935; 1.
DR TIGRFAMs; TIGR01064; pyruv_kin; 1.
DR PROSITE; PS00110; PYRUVATE_KINASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Allosteric enzyme; Alternative splicing; ATP-binding;
KW Cytoplasm; Direct protein sequencing; Glycolysis; Hydroxylation;
KW Isopeptide bond; Kinase; Magnesium; Metal-binding; Methylation;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Potassium; Pyruvate;
KW Reference proteome; Transferase; Translation regulation; Ubl conjugation.
FT CHAIN 1..531
FT /note="Pyruvate kinase PKM"
FT /id="PRO_0000112092"
FT REGION 307..531
FT /note="Interaction with POU5F1"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT REGION 389..433
FT /note="Intersubunit contact"
FT BINDING 70
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 73
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 75..78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 75
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 77
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 106
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 113
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 114
FT /ligand="K(+)"
FT /ligand_id="ChEBI:CHEBI:29103"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 270
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 295
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 296
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 296
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 328
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P30613"
FT BINDING 432..437
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 464
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 482
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 489
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT BINDING 516..521
FT /ligand="beta-D-fructose 1,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:32966"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT SITE 270
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P00549"
FT MOD_RES 3
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT MOD_RES 41
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT MOD_RES 62
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT MOD_RES 66
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52480"
FT MOD_RES 89
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 105
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT MOD_RES 148
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P52480"
FT MOD_RES 166
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT MOD_RES 166
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52480"
FT MOD_RES 175
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT MOD_RES 195
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT MOD_RES 266
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT MOD_RES 270
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52480"
FT MOD_RES 305
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT MOD_RES 322
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52480"
FT MOD_RES 322
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52480"
FT MOD_RES 408
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT MOD_RES 475
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52480"
FT MOD_RES 498
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52480"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT CROSSLNK 266
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT CROSSLNK 270
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P14618"
FT VAR_SEQ 389..433
FT /note="VFHRLLFEELARASSQSTDPLEAMAMGSVEASYKCLAAALIVLTE -> IYH
FT LQLFEELRRLAPITSDPTEAAAVGAVEASFKCCSGAIIVLTK (in isoform M2)"
FT /evidence="ECO:0000305"
FT /id="VSP_011107"
SQ SEQUENCE 531 AA; 57818 MW; F0B133FDDD5991A9 CRC64;
MPKPDSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSAPI TARNTGIICT IGPASRSVEM
LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRAATESFAS DPILYRPVAV ALDTKGPEIR
TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICKVVEV GSKIYVDDGL
ISLQVKEKGA DYLVTEVENG GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV
FASFIRKAAD VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE
IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM
LSGETAKGDY PLEAVRMQHL IAREAEAAVF HRLLFEELAR ASSQSTDPLE AMAMGSVEAS
YKCLAAALIV LTESGRSAHQ VARYRPRAPI IAVTRNPQTA RQAHLYRGIF PVLCKDAVLD
AWAEDVDLRV NLAMNVGKAR GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P
