ID KPYM_FELCA Reviewed; 531 AA. AC P11979; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 24-JAN-2024, entry version 182. DE RecName: Full=Pyruvate kinase PKM; DE EC=2.7.1.40; 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; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis. OX NCBI_TaxID=9685; RN [1] RP PROTEIN SEQUENCE OF 2-531, AND ACETYLATION AT SER-2. RX PubMed=3519210; DOI=10.1002/j.1460-2075.1986.tb04236.x; RA Muirhead H., Clayden D.A., Barford D., Lorimer C.G., RA Fothergill-Gilmore L.A., Schiltz E., Schmitt W.; RT "The structure of cat muscle pyruvate kinase."; RL EMBO J. 5:475-481(1986). RN [2] RP PROTEIN SEQUENCE OF 200-236. RA McAleese S.M., Hoar C.G., Dunbar B., Fothergill-Gilmore L.A.; RT "Hydroxylamine cleavage of cat skeletal-muscle pyruvate kinase: separation RT of the fragments and N-terminal sequence analysis."; RL Biochem. Soc. Trans. 10:444-445(1982). RN [3] RP PROTEIN SEQUENCE OF 314-330. RX PubMed=6628384; DOI=10.1111/j.1432-1033.1983.tb07747.x; RA Harkins R.N., Nocton J.C., Russell M.P., Fothergill-Gilmore L.A., RA Muirhead H.; RT "A comparison of the structure and activity of cat and trout muscle RT pyruvate kinases."; RL Eur. J. Biochem. 136:341-346(1983). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=537059; DOI=10.1016/0022-2836(79)90416-9; RA Stuart D.I., Levine M., Muirhead H., Stammers D.K.; RT "Crystal structure of cat muscle pyruvate kinase at a resolution of 2.6 RT A."; RL J. Mol. Biol. 134:109-142(1979). RN [5] RP X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS). RX PubMed=875020; DOI=10.1016/s0022-2836(77)80146-0; RA Stammers D.K., Muirhead H.; RT "Three-dimensional structure of cat muscle pyruvate kinase at 3.1-A RT resolution."; RL J. Mol. Biol. 112:309-316(1977). RN [6] RP X-RAY CRYSTALLOGRAPHY (6.0 ANGSTROMS). RX PubMed=1185780; DOI=10.1016/0022-2836(75)90391-5; RA Stammers D.K., Muirhead H.; RT "Three-dimensional structure of cat muscle pyruvate kinase at 6-A RT resolution."; RL J. Mol. Biol. 95:213-225(1975). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=15299671; DOI=10.1107/s0907444995016040; RA Allen S.C., Muirhead H.; RT "Refined three-dimensional structure of cat-muscle (M1) pyruvate kinase at RT a resolution of 2.6 A."; RL Acta Crystallogr. D 52:499-504(1996). 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 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. Interacts with TSC22D2; the interaction results in CC reduced nuclear levels of PKM isoform M2, leading to repression of CC cyclin CCND1 transcription and reduced cell growth (By similarity). CC {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; Synonyms=PKM1; CC IsoId=P11979-1; Sequence=Displayed; CC Name=M2; Synonyms=PKM2; CC IsoId=P11979-2; Sequence=Not described; 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}. 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 PIR; A25091; A25091. DR PDB; 1PKM; X-ray; 2.60 A; A=2-531. DR PDBsum; 1PKM; -. DR AlphaFoldDB; P11979; -. DR SMR; P11979; -. DR STRING; 9685.ENSFCAP00000041670; -. DR iPTMnet; P11979; -. DR PaxDb; 9685-ENSFCAP00000000606; -. DR eggNOG; KOG2323; Eukaryota. DR InParanoid; P11979; -. DR TreeFam; TF300390; -. DR UniPathway; UPA00109; UER00188. DR EvolutionaryTrace; P11979; -. DR Proteomes; UP000011712; Unplaced. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005791; C:rough endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. 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; IBA:GO_Central. DR GO; GO:0032869; P:cellular response to insulin stimulus; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. 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 CDD; cd00288; Pyruvate_Kinase; 1. DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1. DR Gene3D; 2.40.33.10; PK beta-barrel domain-like; 1. DR Gene3D; 3.40.1380.20; Pyruvate kinase, C-terminal domain; 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 NCBIfam; TIGR01064; pyruv_kin; 1. DR PANTHER; PTHR11817; PYRUVATE KINASE; 1. DR PANTHER; PTHR11817:SF101; PYRUVATE KINASE PKM; 1. DR Pfam; PF00224; PK; 1. DR Pfam; PF02887; PK_C; 1. DR PRINTS; PR01050; PYRUVTKNASE. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1. DR SUPFAM; SSF52935; PK C-terminal domain-like; 1. DR PROSITE; PS00110; PYRUVATE_KINASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Allosteric enzyme; Alternative splicing; KW ATP-binding; Cytoplasm; Direct protein sequencing; Glycolysis; KW Isopeptide bond; Kinase; Magnesium; Metal-binding; Methylation; KW Nucleotide-binding; Nucleus; Phosphoprotein; Potassium; Pyruvate; KW Reference proteome; Transferase; Translation regulation; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:3519210" FT CHAIN 2..531 FT /note="Pyruvate kinase PKM" FT /id="PRO_0000112087" FT REGION 307..531 FT /note="Interaction with POU5F1" FT /evidence="ECO:0000250|UniProtKB:P14618" 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 2 FT /note="N-acetylserine" FT /evidence="ECO:0000269|PubMed:3519210" 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:0000250|UniProtKB:P11980" FT MOD_RES 100 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P11980" 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 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 CONFLICT 209 FT /note="V -> A (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 226..227 FT /note="IQ -> FE (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 232 FT /note="G -> Q (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 235 FT /note="Q -> R (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 18..21 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 26..31 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 45..50 FT /evidence="ECO:0007829|PDB:1PKM" FT TURN 53..55 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 58..66 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 69..75 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 81..96 FT /evidence="ECO:0007829|PDB:1PKM" FT TURN 97..100 FT /evidence="ECO:0007829|PDB:1PKM" FT TURN 102..104 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 109..113 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 139..143 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 148..151 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 154..160 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 164..167 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 173..176 FT /evidence="ECO:0007829|PDB:1PKM" FT TURN 177..180 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 181..188 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 190..199 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 208..210 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 223..234 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 238..243 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 248..258 FT /evidence="ECO:0007829|PDB:1PKM" FT TURN 259..264 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 265..271 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 275..278 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 280..286 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 287..293 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 294..300 FT /evidence="ECO:0007829|PDB:1PKM" FT TURN 303..305 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 306..320 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 324..331 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 332..335 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 342..354 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 357..362 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 363..366 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 371..387 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 391..402 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 408..423 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 428..431 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 433..435 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 436..443 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 450..455 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 457..462 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 463..465 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 469..473 FT /evidence="ECO:0007829|PDB:1PKM" FT HELIX 482..499 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 508..513 FT /evidence="ECO:0007829|PDB:1PKM" FT STRAND 524..529 FT /evidence="ECO:0007829|PDB:1PKM" SQ SEQUENCE 531 AA; 58046 MW; 302475E32D6109A8 CRC64; MSKPHSDVGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT IGPASRSVEI LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRAATESFAS DPIRYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENVLWLD YKNICKVVEV GSKVYVDDGL ISLLVKEKGA DFLVTEVENG GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV FASFIRKASD VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM LSGETAKGDY PLEAVRMQHL IAREAEAAMF HRKLFEELVR GSSHSTDLME AMAMGSVEAS YKCLAAALIV LTESGRSAHQ VARYRPRAPI IAVTRNHQTA RQAHLYRGIF PVVCKDPVQE AWAEDVDLRV NLAMNVGKAR GFFKHGDVVI VLTGWRPGSG FTNTMRVVPV P //