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}.
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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
//
