KPYM_FELCA
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 03-AUG-2022, entry version 174.
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 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; 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}.
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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.ENSFCAP00000000606; -.
DR iPTMnet; P11979; -.
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: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; 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 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
