ID DHE3_BOVIN Reviewed; 558 AA. AC P00366; Q3SYY0; Q7YS29; Q8HZ49; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 2. DT 24-JAN-2024, entry version 178. DE RecName: Full=Glutamate dehydrogenase 1, mitochondrial; DE Short=GDH 1; DE EC=1.4.1.3 {ECO:0000269|PubMed:14659072, ECO:0000269|PubMed:4365183}; DE Flags: Precursor; GN Name=GLUD1; Synonyms=GLUD; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES. RC TISSUE=Brain; RX PubMed=14659072; DOI=10.5483/bmbrep.2003.36.6.545; RA Kim D.W., Eum W.S., Jang S.H., Yoon C.S., Kim Y.H., Choi S.H., Choi H.S., RA Kim S.Y., Kwon H.Y., Kang J.H., Kwon O.-S., Cho S.-W., Park J., Choi S.Y.; RT "Molecular gene cloning, expression, and characterization of bovine brain RT glutamate dehydrogenase."; RL J. Biochem. Mol. Biol. 36:545-551(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Crossbred X Angus; TISSUE=Ileum; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP PROTEIN SEQUENCE OF 58-558. RC TISSUE=Liver; RX PubMed=4735572; DOI=10.1016/s0021-9258(19)44011-8; RA Moon K., Smith E.L.; RT "Sequence of bovine liver glutamate dehydrogenase. 8. Peptides produced by RT specific chemical cleavages; the complete sequence of the protein."; RL J. Biol. Chem. 248:3082-3088(1973). RN [4] RP SEQUENCE REVISION TO 440-441. RX PubMed=429360; DOI=10.1016/s0021-9258(18)50777-8; RA Julliard J.H., Smith E.L.; RT "Partial amino acid sequence of the glutamate dehydrogenase of human liver RT and a revision of the sequence of the bovine enzyme."; RL J. Biol. Chem. 254:3427-3438(1979). RN [5] RP CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=4365183; DOI=10.1111/j.1432-1033.1974.tb03415.x; RA Witzemann V., Koberstein R., Sund H., Rasched I., Joernvall H., Noack K.; RT "Studies of glutamate dehydrogenase: chemical modification and quantitative RT determination of tryptophan residues."; RL Eur. J. Biochem. 43:319-325(1974). RN [6] RP PRELIMINARY STUDIES OF SUBSTRATE-BINDING SITE. RX PubMed=4856315; DOI=10.1111/j.1432-1033.1974.tb03302.x; RA Rasched I., Joernvall H., Sund H.; RT "Studies of glutamate dehydrogenase. Identification of an amino group RT involved in the substrate binding."; RL Eur. J. Biochem. 41:603-606(1974). RN [7] RP ACETYLATION AT LYS-84; LYS-90; LYS-110; LYS-162; LYS-183; LYS-191; LYS-363; RP LYS-365; LYS-386; LYS-399; LYS-415; LYS-457; LYS-480; LYS-503; LYS-527 AND RP LYS-545, MALONYLATION AT LYS-457; LYS-503 AND LYS-527, AND SUCCINYLATION AT RP LYS-84; LYS-110; LYS-162; LYS-363; LYS-415; LYS-457; LYS-503; LYS-527 AND RP LYS-545. RX PubMed=22076378; DOI=10.1126/science.1207861; RA Du J., Zhou Y., Su X., Yu J.J., Khan S., Jiang H., Kim J., Woo J., RA Kim J.H., Choi B.H., He B., Chen W., Zhang S., Cerione R.A., Auwerx J., RA Hao Q., Lin H.; RT "Sirt5 is a NAD-dependent protein lysine demalonylase and desuccinylase."; RL Science 334:806-809(2011). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 58-558. RC TISSUE=Liver; RX PubMed=10425679; DOI=10.1016/s0969-2126(99)80101-4; RA Peterson P.E., Smith T.J.; RT "The structure of bovine glutamate dehydrogenase provides insights into the RT mechanism of allostery."; RL Structure 7:769-782(1999). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 58-558 IN COMPLEX WITH SUBSTRATE; RP NADH AND GTP. RX PubMed=11254391; DOI=10.1006/jmbi.2001.4499; RA Smith T.J., Peterson P.E., Schmidt T., Fang J., Stanley C.A.; RT "Structures of bovine glutamate dehydrogenase complexes elucidate the RT mechanism of purine regulation."; RL J. Mol. Biol. 307:707-720(2001). RN [10] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 25-520 ALONE AND IN COMPLEX WITH RP ADP, AND HOMOHEXAMERIZATION. RX PubMed=12653548; DOI=10.1021/bi0206917; RA Banerjee S., Schmidt T., Fang J., Stanley C.A., Smith T.J.; RT "Structural studies on ADP activation of mammalian glutamate dehydrogenase RT and the evolution of regulation."; RL Biochemistry 42:3446-3456(2003). CC -!- FUNCTION: Mitochondrial glutamate dehydrogenase that converts L- CC glutamate into alpha-ketoglutarate. Plays a key role in glutamine CC anaplerosis by producing alpha-ketoglutarate, an important intermediate CC in the tricarboxylic acid cycle (PubMed:4365183, PubMed:14659072). CC Plays a role in insulin homeostasis (By similarity). May be involved in CC learning and memory reactions by increasing the turnover of the CC excitatory neurotransmitter glutamate (By similarity). CC {ECO:0000250|UniProtKB:P00367, ECO:0000250|UniProtKB:P10860, CC ECO:0000269|PubMed:14659072, ECO:0000269|PubMed:4365183}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutamate + NAD(+) = 2-oxoglutarate + H(+) + NADH + CC NH4(+); Xref=Rhea:RHEA:15133, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.4.1.3; CC Evidence={ECO:0000269|PubMed:14659072, ECO:0000269|PubMed:4365183}; CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + NADPH + CC NH4(+); Xref=Rhea:RHEA:11612, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.4.1.3; CC Evidence={ECO:0000250|UniProtKB:P00367}; CC -!- ACTIVITY REGULATION: Subject to allosteric regulation. Activated by ADP CC (PubMed:14659072). Inhibited by GTP and ATP (PubMed:14659072). ADP can CC occupy the NADH binding site and activate the enzyme. Inhibited by CC SIRT4 (By similarity). Inhibited by HADH (By similarity). CC {ECO:0000250|UniProtKB:P00367, ECO:0000250|UniProtKB:P26443, CC ECO:0000269|PubMed:14659072}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.1 mM for NAD(+) {ECO:0000269|PubMed:14659072}; CC Vmax=100 umol/min/mg enzyme with NAD(+)as substrate CC {ECO:0000269|PubMed:14659072}; CC -!- SUBUNIT: Homohexamer (PubMed:11254391, PubMed:12653548). Interacts with CC HADH; this interaction inhibits the activation of GLUD1 (By CC similarity). {ECO:0000250|UniProtKB:P26443, CC ECO:0000269|PubMed:11254391, ECO:0000269|PubMed:12653548}. CC -!- INTERACTION: CC P00366; P00366: GLUD1; NbExp=2; IntAct=EBI-1221442, EBI-1221442; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P00367}. CC Endoplasmic reticulum {ECO:0000250|UniProtKB:P00367}. Note=Mostly CC translocates into the mitochondria, only a small amount of the protein CC localizes to the endoplasmic reticulum. {ECO:0000250|UniProtKB:P00367}. CC -!- PTM: ADP-ribosylated by SIRT4, leading to inactivate glutamate CC dehydrogenase activity. Stoichiometry shows that ADP-ribosylation CC occurs in one subunit per catalytically active homohexamer. CC {ECO:0000250|UniProtKB:P00367}. CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family. CC {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 EMBL; AY138843; AAN15276.1; -; mRNA. DR EMBL; AY256856; AAP55683.1; -; mRNA. DR EMBL; BC103336; AAI03337.1; -; mRNA. DR PIR; A92129; DEBOE. DR RefSeq; NP_872593.2; NM_182652.2. DR PDB; 1HWY; X-ray; 3.20 A; A/B/C/D/E/F=58-558. DR PDB; 1NQT; X-ray; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L=63-558. DR PDB; 1NR7; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L=63-558. DR PDB; 3ETD; X-ray; 2.50 A; A/B/C/D/E/F=58-558. DR PDB; 3ETE; X-ray; 3.00 A; A/B/C/D/E/F=58-558. DR PDB; 3ETG; X-ray; 2.50 A; A/B/C/D/E/F=58-558. DR PDB; 3JCZ; EM; 3.26 A; A/B/C/D/E/F=58-558. DR PDB; 3JD0; EM; 3.47 A; A/B/C/D/E/F=58-558. DR PDB; 3JD1; EM; 3.30 A; A/B/C/D/E/F=58-558. DR PDB; 3JD2; EM; 3.30 A; A/B/C/D/E/F=58-558. DR PDB; 3JD3; EM; 3.60 A; A/B/C/D/E/F=58-558. DR PDB; 3JD4; EM; 3.40 A; A/B/C/D/E/F=58-558. DR PDB; 5K12; EM; 1.80 A; A/B/C/D/E/F=1-558. DR PDB; 6DHD; X-ray; 2.50 A; A/B/C/D/E/F=58-558. DR PDB; 6DHK; X-ray; 3.50 A; A/B/C/D/E/F/G/H/I/J/K/L=63-558. DR PDB; 6DHL; X-ray; 3.62 A; A/B/C/D/E/F/G/H/I/J/K/L=63-558. DR PDB; 6DHM; X-ray; 3.00 A; A/B/C/D/E/F=1-558. DR PDB; 6DHN; X-ray; 3.30 A; A/B/C/D/E/F=1-558. DR PDB; 6DHQ; X-ray; 2.30 A; A/B/C/D/E/F=58-558. DR PDB; 7VDA; EM; 2.26 A; A/B/C/D/E/F=1-558. DR PDB; 8EW0; EM; 2.70 A; A/B/C/D/E/F=1-558. DR PDBsum; 1HWY; -. DR PDBsum; 1NQT; -. DR PDBsum; 1NR7; -. DR PDBsum; 3ETD; -. DR PDBsum; 3ETE; -. DR PDBsum; 3ETG; -. DR PDBsum; 3JCZ; -. DR PDBsum; 3JD0; -. DR PDBsum; 3JD1; -. DR PDBsum; 3JD2; -. DR PDBsum; 3JD3; -. DR PDBsum; 3JD4; -. DR PDBsum; 5K12; -. DR PDBsum; 6DHD; -. DR PDBsum; 6DHK; -. DR PDBsum; 6DHL; -. DR PDBsum; 6DHM; -. DR PDBsum; 6DHN; -. DR PDBsum; 6DHQ; -. DR PDBsum; 7VDA; -. DR PDBsum; 8EW0; -. DR AlphaFoldDB; P00366; -. DR EMDB; EMD-28639; -. DR EMDB; EMD-31912; -. DR EMDB; EMD-6630; -. DR EMDB; EMD-6631; -. DR EMDB; EMD-6632; -. DR EMDB; EMD-6633; -. DR EMDB; EMD-6634; -. DR EMDB; EMD-6635; -. DR EMDB; EMD-8194; -. DR PCDDB; P00366; -. DR SMR; P00366; -. DR DIP; DIP-39002N; -. DR IntAct; P00366; 1. DR MINT; P00366; -. DR STRING; 9913.ENSBTAP00000009923; -. DR BindingDB; P00366; -. DR ChEMBL; CHEMBL4628; -. DR iPTMnet; P00366; -. DR PaxDb; 9913-ENSBTAP00000009923; -. DR PeptideAtlas; P00366; -. DR GeneID; 281785; -. DR KEGG; bta:281785; -. DR CTD; 2746; -. DR eggNOG; KOG2250; Eukaryota. DR HOGENOM; CLU_025763_1_0_1; -. DR InParanoid; P00366; -. DR OrthoDB; 45283at2759; -. DR TreeFam; TF313945; -. DR BRENDA; 1.4.1.2; 908. DR SABIO-RK; P00366; -. DR EvolutionaryTrace; P00366; -. DR Proteomes; UP000009136; Unplaced. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:AgBase. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; ISS:AgBase. DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA. DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; ISS:AgBase. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0006538; P:glutamate catabolic process; ISS:AgBase. DR GO; GO:0006541; P:glutamine metabolic process; ISS:UniProtKB. DR GO; GO:0072350; P:tricarboxylic acid metabolic process; ISS:UniProtKB. DR CDD; cd01076; NAD_bind_1_Glu_DH; 1. DR Gene3D; 1.10.287.140; -; 1. DR Gene3D; 3.40.50.10860; Leucine Dehydrogenase, chain A, domain 1; 1. DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1. DR InterPro; IPR046346; Aminoacid_DH-like_N_sf. DR InterPro; IPR006095; Glu/Leu/Phe/Val/Trp_DH. DR InterPro; IPR006096; Glu/Leu/Phe/Val/Trp_DH_C. DR InterPro; IPR006097; Glu/Leu/Phe/Val/Trp_DH_dimer. DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS. DR InterPro; IPR036291; NAD(P)-bd_dom_sf. DR InterPro; IPR033922; NAD_bind_Glu_DH. DR PANTHER; PTHR11606; GLUTAMATE DEHYDROGENASE; 1. DR PANTHER; PTHR11606:SF13; GLUTAMATE DEHYDROGENASE 1, MITOCHONDRIAL; 1. DR Pfam; PF00208; ELFV_dehydrog; 1. DR Pfam; PF02812; ELFV_dehydrog_N; 1. DR PRINTS; PR00082; GLFDHDRGNASE. DR SMART; SM00839; ELFV_dehydrog; 1. DR SUPFAM; SSF53223; Aminoacid dehydrogenase-like, N-terminal domain; 1. DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1. DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ADP-ribosylation; ATP-binding; KW Direct protein sequencing; Endoplasmic reticulum; GTP-binding; KW Hydroxylation; Mitochondrion; NADP; Nucleotide-binding; Oxidoreductase; KW Phosphoprotein; Reference proteome; Transit peptide. FT TRANSIT 1..57 FT /note="Mitochondrion" FT /evidence="ECO:0000269|PubMed:4735572" FT CHAIN 58..558 FT /note="Glutamate dehydrogenase 1, mitochondrial" FT /id="PRO_0000007205" FT ACT_SITE 183 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10011" FT BINDING 141..143 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:11254391" FT BINDING 147 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:11254391" FT BINDING 171 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:11254391" FT BINDING 176 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:11254391" FT BINDING 252 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:11254391" FT BINDING 266 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:11254391" FT BINDING 270 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:11254391" FT BINDING 319 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:11254391" FT BINDING 322 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000269|PubMed:11254391" FT BINDING 438 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:11254391" FT BINDING 444 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000269|PubMed:11254391" FT BINDING 450 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|PubMed:12653548" FT BINDING 516 FT /ligand="ADP" FT /ligand_id="ChEBI:CHEBI:456216" FT /evidence="ECO:0000269|PubMed:12653548" FT MOD_RES 68 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 79 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 84 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 84 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 90 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 110 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 110 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 128 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 135 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 147 FT /note="N6-(2-hydroxyisobutyryl)lysine" FT /evidence="ECO:0000250|UniProtKB:P00367" FT MOD_RES 162 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 162 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 171 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 172 FT /note="ADP-ribosylcysteine" FT /evidence="ECO:0000250|UniProtKB:P00367" FT MOD_RES 183 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 183 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 187 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 191 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 191 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 200 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 211 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 227 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00367" FT MOD_RES 326 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 346 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 346 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 352 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 352 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 363 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 363 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 365 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 365 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 384 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00367" FT MOD_RES 386 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 390 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 390 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 399 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 410 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P10860" FT MOD_RES 415 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 415 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 457 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 457 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 457 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 477 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 477 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 480 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 480 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P26443" FT MOD_RES 503 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 503 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 503 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 512 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P00367" FT MOD_RES 527 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 527 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 527 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 545 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT MOD_RES 545 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000269|PubMed:22076378" FT CONFLICT 4 FT /note="Y -> C (in Ref. 2; AAI03337)" FT /evidence="ECO:0000305" FT CONFLICT 14 FT /note="A -> I (in Ref. 2; AAI03337)" FT /evidence="ECO:0000305" FT CONFLICT 22..23 FT /note="AS -> VA (in Ref. 2; AAI03337)" FT /evidence="ECO:0000305" FT CONFLICT 28 FT /note="A -> V (in Ref. 2; AAI03337)" FT /evidence="ECO:0000305" FT CONFLICT 32 FT /note="W -> R (in Ref. 2; AAI03337)" FT /evidence="ECO:0000305" FT CONFLICT 37..38 FT /note="PA -> AAAAV (in Ref. 2; AAI03337)" FT /evidence="ECO:0000305" FT CONFLICT 93..95 FT /note="ETE -> QTQ (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 104 FT /note="S -> G (in Ref. 2; AAI03337 and 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 141..142 FT /note="QH -> HQ (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 196..197 FT /note="NE -> ED (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 225 FT /note="D -> N (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 257..259 FT /note="GKP -> KPG (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 278..279 FT /note="HG -> GH (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 305 FT /note="V -> A (in Ref. 2; AAI03337 and 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 328 FT /note="I -> V (in Ref. 2; AAI03337 and 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 329 FT /note="T -> A (in Ref. 2; AAI03337)" FT /evidence="ECO:0000305" FT CONFLICT 389 FT /note="T -> P (in Ref. 1; AAP55683)" FT /evidence="ECO:0000305" FT CONFLICT 412 FT /note="E -> Q (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 441..442 FT /note="EW -> QI (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 444 FT /note="N -> K (in Ref. 2; AAI03337 and 3; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 60..62 FT /evidence="ECO:0007829|PDB:3ETD" FT HELIX 66..87 FT /evidence="ECO:0007829|PDB:7VDA" FT TURN 88..90 FT /evidence="ECO:0007829|PDB:6DHK" FT STRAND 91..93 FT /evidence="ECO:0007829|PDB:7VDA" FT HELIX 95..109 FT /evidence="ECO:0007829|PDB:7VDA" FT STRAND 113..123 FT /evidence="ECO:0007829|PDB:5K12" FT STRAND 125..127 FT /evidence="ECO:0007829|PDB:1HWY" FT STRAND 129..138 FT /evidence="ECO:0007829|PDB:5K12" FT STRAND 143..155 FT /evidence="ECO:0007829|PDB:5K12" FT HELIX 158..174 FT /evidence="ECO:0007829|PDB:5K12" FT STRAND 180..187 FT /evidence="ECO:0007829|PDB:5K12" FT HELIX 190..192 FT /evidence="ECO:0007829|PDB:5K12" FT HELIX 195..211 FT /evidence="ECO:0007829|PDB:5K12" FT STRAND 214..216 FT /evidence="ECO:0007829|PDB:5K12" FT TURN 217..219 FT /evidence="ECO:0007829|PDB:5K12" FT STRAND 220..223 FT /evidence="ECO:0007829|PDB:5K12" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:7VDA" FT HELIX 230..242 FT /evidence="ECO:0007829|PDB:5K12" FT TURN 243..245 FT /evidence="ECO:0007829|PDB:5K12" FT HELIX 251..253 FT /evidence="ECO:0007829|PDB:5K12" FT STRAND 255..257 FT /evidence="ECO:0007829|PDB:3ETG" FT HELIX 260..262 FT /evidence="ECO:0007829|PDB:5K12" FT STRAND 268..270 FT /evidence="ECO:0007829|PDB:3ETG" FT HELIX 271..281 FT /evidence="ECO:0007829|PDB:5K12" FT HELIX 287..293 FT /evidence="ECO:0007829|PDB:7VDA" FT STRAND 297..299 FT /evidence="ECO:0007829|PDB:7VDA" FT STRAND 303..308 FT /evidence="ECO:0007829|PDB:7VDA" FT HELIX 311..322 FT /evidence="ECO:0007829|PDB:7VDA" FT STRAND 326..332 FT /evidence="ECO:0007829|PDB:7VDA" FT STRAND 335..338 FT /evidence="ECO:0007829|PDB:7VDA" FT HELIX 345..355 FT /evidence="ECO:0007829|PDB:7VDA" FT STRAND 356..358 FT /evidence="ECO:0007829|PDB:7VDA" FT STRAND 364..366 FT /evidence="ECO:0007829|PDB:7VDA" FT HELIX 371..373 FT /evidence="ECO:0007829|PDB:7VDA" FT STRAND 377..381 FT /evidence="ECO:0007829|PDB:7VDA" FT STRAND 383..385 FT /evidence="ECO:0007829|PDB:7VDA" FT TURN 390..392 FT /evidence="ECO:0007829|PDB:7VDA" FT HELIX 393..395 FT /evidence="ECO:0007829|PDB:7VDA" FT STRAND 399..402 FT /evidence="ECO:0007829|PDB:7VDA" FT STRAND 405..407 FT /evidence="ECO:0007829|PDB:7VDA" FT HELIX 411..419 FT /evidence="ECO:0007829|PDB:7VDA" FT STRAND 423..425 FT /evidence="ECO:0007829|PDB:7VDA" FT HELIX 430..432 FT /evidence="ECO:0007829|PDB:5K12" FT HELIX 433..447 FT /evidence="ECO:0007829|PDB:5K12" FT TURN 451..455 FT /evidence="ECO:0007829|PDB:5K12" FT HELIX 456..474 FT /evidence="ECO:0007829|PDB:5K12" FT TURN 475..477 FT /evidence="ECO:0007829|PDB:5K12" FT STRAND 480..482 FT /evidence="ECO:0007829|PDB:6DHQ" FT HELIX 491..497 FT /evidence="ECO:0007829|PDB:5K12" FT HELIX 502..525 FT /evidence="ECO:0007829|PDB:5K12" FT TURN 527..529 FT /evidence="ECO:0007829|PDB:1NQT" FT HELIX 535..545 FT /evidence="ECO:0007829|PDB:5K12" FT HELIX 551..553 FT /evidence="ECO:0007829|PDB:3JCZ" FT TURN 554..556 FT /evidence="ECO:0007829|PDB:3ETD" SQ SEQUENCE 558 AA; 61512 MW; 194D74A33F2310E7 CRC64; MYRYLGEALL LSRAGPAALG SASADSAALL GWARGQPAAA PQPGLVPPAR RHYSEAAADR EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRETEEQKRN RVRSILRIIK PCNHVLSLSF PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGVD VPAPDMSTGE REMSWIADTY ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG DKTFVVQGFG NVGLHSMRYL HRFGAKCITV GESDGSIWNP DGIDPKELED FKLQHGTILG FPKAKIYEGS ILEVDCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER NIMVIPDLYL NAGGVTVSYF EWLNNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK HGGTIPIVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV NAIEKVFRVY NEAGVTFT //