DHE3_MOUSE
ID DHE3_MOUSE Reviewed; 558 AA.
AC P26443; Q8C273;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Glutamate dehydrogenase 1, mitochondrial;
DE Short=GDH 1;
DE EC=1.4.1.3 {ECO:0000269|PubMed:20670938};
DE Flags: Precursor;
GN Name=Glud1; Synonyms=Glud;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=1711373; DOI=10.1016/0167-4781(91)90017-g;
RA Tzimagiorgis G., Moschonas N.K.;
RT "Molecular cloning, structure and expression analysis of a full-length
RT mouse brain glutamate dehydrogenase cDNA.";
RL Biochim. Biophys. Acta 1089:250-253(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 61-76; 108-123; 125-136; 152-183; 192-200; 212-231;
RP 275-318; 327-346; 353-363; 366-386; 400-420; 461-476; 481-496; 504-516;
RP 528-545 AND 549-558.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP ADP-RIBOSYLATION, AND FUNCTION.
RX PubMed=16959573; DOI=10.1016/j.cell.2006.06.057;
RA Haigis M.C., Mostoslavsky R., Haigis K.M., Fahie K., Christodoulou D.C.,
RA Murphy A.J., Valenzuela D.M., Yancopoulos G.D., Karow M., Blander G.,
RA Wolberger C., Prolla T.A., Weindruch R., Alt F.W., Guarente L.;
RT "SIRT4 inhibits glutamate dehydrogenase and opposes the effects of calorie
RT restriction in pancreatic beta cells.";
RL Cell 126:941-954(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-128, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-135, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-128, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH HADH, ACTIVITY REGULATION, CATALYTIC ACTIVITY, FUNCTION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=20670938; DOI=10.1074/jbc.m110.123638;
RA Li C., Chen P., Palladino A., Narayan S., Russell L.K., Sayed S., Xiong G.,
RA Chen J., Stokes D., Butt Y.M., Jones P.M., Collins H.W., Cohen N.A.,
RA Cohen A.S., Nissim I., Smith T.J., Strauss A.W., Matschinsky F.M.,
RA Bennett M.J., Stanley C.A.;
RT "Mechanism of hyperinsulinism in short-chain 3-hydroxyacyl-CoA
RT dehydrogenase deficiency involves activation of glutamate dehydrogenase.";
RL J. Biol. Chem. 285:31806-31818(2010).
RN [10]
RP FUNCTION, AND ADP-RIBOSYLATION.
RX PubMed=23663782; DOI=10.1016/j.cell.2013.04.023;
RA Csibi A., Fendt S.M., Li C., Poulogiannis G., Choo A.Y., Chapski D.J.,
RA Jeong S.M., Dempsey J.M., Parkhitko A., Morrison T., Henske E.P.,
RA Haigis M.C., Cantley L.C., Stephanopoulos G., Yu J., Blenis J.;
RT "The mTORC1 pathway stimulates glutamine metabolism and cell proliferation
RT by repressing SIRT4.";
RL Cell 153:840-854(2013).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-503; LYS-527 AND LYS-545,
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-84; LYS-162; LYS-183;
RP LYS-191; LYS-200; LYS-346; LYS-352; LYS-363; LYS-365; LYS-390; LYS-477;
RP LYS-480; LYS-503; LYS-527 AND LYS-545, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-84; LYS-90; LYS-110; LYS-162;
RP LYS-171; LYS-187; LYS-191; LYS-211; LYS-326; LYS-346; LYS-352; LYS-363;
RP LYS-365; LYS-390; LYS-399; LYS-415; LYS-457; LYS-477; LYS-480; LYS-503;
RP LYS-527; LYS-545 AND LYS-548, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Mitochondrial glutamate dehydrogenase that converts L-
CC glutamate into alpha-ketoglutarate (PubMed:20670938). Plays a key role
CC in glutamine anaplerosis by producing alpha-ketoglutarate, an important
CC intermediate in the tricarboxylic acid cycle (By similarity). Plays a
CC role in insulin homeostasis (PubMed:16959573). 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:16959573, ECO:0000269|PubMed:20670938,
CC ECO:0000269|PubMed:23663782}.
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:20670938};
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
CC ADP. Inhibited by GTP and ATP. ADP can occupy the NADH binding site and
CC activate the enzyme. Inhibited by SIRT4 (By similarity). Inhibited by
CC HADH (PubMed:20670938). {ECO:0000250|UniProtKB:P00367,
CC ECO:0000269|PubMed:20670938}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=107 uM for 2-oxoglutarate {ECO:0000269|PubMed:20670938};
CC -!- SUBUNIT: Homohexamer (By similarity). Interacts with HADH; this
CC interaction inhibits the activation of GLUD1 (PubMed:20670938).
CC {ECO:0000250|UniProtKB:P00366, ECO:0000269|PubMed:20670938}.
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: Acetylation of Lys-84 is observed in liver mitochondria from
CC fasted mice but not from fed mice.
CC -!- PTM: ADP-ribosylated by SIRT4, leading to inactivate glutamate
CC dehydrogenase activity (PubMed:16959573). Stoichiometry shows that ADP-
CC ribosylation occurs in one subunit per catalytically active homohexamer
CC (By similarity). {ECO:0000250|UniProtKB:P00367,
CC ECO:0000269|PubMed:16959573}.
CC -!- SIMILARITY: Belongs to the Glu/Leu/Phe/Val dehydrogenases family.
CC {ECO:0000305}.
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DR EMBL; X57024; CAA40341.1; -; mRNA.
DR EMBL; AK089152; BAC40767.1; -; mRNA.
DR EMBL; BC052724; AAH52724.1; -; mRNA.
DR EMBL; BC057347; AAH57347.1; -; mRNA.
DR CCDS; CCDS26935.1; -.
DR PIR; S16239; S16239.
DR RefSeq; NP_032159.1; NM_008133.4.
DR AlphaFoldDB; P26443; -.
DR SMR; P26443; -.
DR BioGRID; 199956; 15.
DR IntAct; P26443; 11.
DR MINT; P26443; -.
DR STRING; 10090.ENSMUSP00000022322; -.
DR iPTMnet; P26443; -.
DR PhosphoSitePlus; P26443; -.
DR SwissPalm; P26443; -.
DR REPRODUCTION-2DPAGE; P26443; -.
DR SWISS-2DPAGE; P26443; -.
DR UCD-2DPAGE; P26443; -.
DR CPTAC; non-CPTAC-3785; -.
DR EPD; P26443; -.
DR jPOST; P26443; -.
DR MaxQB; P26443; -.
DR PaxDb; P26443; -.
DR PeptideAtlas; P26443; -.
DR PRIDE; P26443; -.
DR ProteomicsDB; 277333; -.
DR DNASU; 14661; -.
DR Ensembl; ENSMUST00000022322; ENSMUSP00000022322; ENSMUSG00000021794.
DR GeneID; 14661; -.
DR KEGG; mmu:14661; -.
DR UCSC; uc007tas.2; mouse.
DR CTD; 2746; -.
DR MGI; MGI:95753; Glud1.
DR VEuPathDB; HostDB:ENSMUSG00000021794; -.
DR eggNOG; KOG2250; Eukaryota.
DR GeneTree; ENSGT00390000000854; -.
DR HOGENOM; CLU_025763_1_0_1; -.
DR InParanoid; P26443; -.
DR OMA; PCFAAFP; -.
DR OrthoDB; 692851at2759; -.
DR PhylomeDB; P26443; -.
DR TreeFam; TF313945; -.
DR BRENDA; 1.4.1.3; 3474.
DR Reactome; R-MMU-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-MMU-8964539; Glutamate and glutamine metabolism.
DR BioGRID-ORCS; 14661; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Glud1; mouse.
DR PRO; PR:P26443; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; P26443; protein.
DR Bgee; ENSMUSG00000021794; Expressed in left lobe of liver and 276 other tissues.
DR ExpressionAtlas; P26443; baseline and differential.
DR Genevisible; P26443; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0043531; F:ADP binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0004352; F:glutamate dehydrogenase (NAD+) activity; IDA:UniProtKB.
DR GO; GO:0004354; F:glutamate dehydrogenase (NADP+) activity; IEA:RHEA.
DR GO; GO:0004353; F:glutamate dehydrogenase [NAD(P)+] activity; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0070728; F:leucine binding; ISO:MGI.
DR GO; GO:0070403; F:NAD+ binding; ISO:MGI.
DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR GO; GO:0006538; P:glutamate catabolic process; IBA:GO_Central.
DR GO; GO:0006541; P:glutamine metabolic process; IMP:UniProtKB.
DR GO; GO:0007616; P:long-term memory; IEA:Ensembl.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IGI:MGI.
DR GO; GO:0010044; P:response to aluminum ion; ISO:MGI.
DR GO; GO:0072350; P:tricarboxylic acid metabolic process; IMP:UniProtKB.
DR CDD; cd01076; NAD_bind_1_Glu_DH; 1.
DR InterPro; IPR046346; Aminiacid_DH-like_N_sf.
DR InterPro; IPR006095; Glu/Leu/Phe/Val_DH.
DR InterPro; IPR033524; Glu/Leu/Phe/Val_DH_AS.
DR InterPro; IPR006096; Glu/Leu/Phe/Val_DH_C.
DR InterPro; IPR006097; Glu/Leu/Phe/Val_DH_dimer_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR033922; NAD_bind_Glu_DH.
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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF53223; SSF53223; 1.
DR PROSITE; PS00074; GLFV_DEHYDROGENASE; 1.
PE 1: Evidence at protein level;
KW Acetylation; ADP-ribosylation; ATP-binding; Direct protein sequencing;
KW Endoplasmic reticulum; GTP-binding; Hydroxylation; Mitochondrion; NADP;
KW Nucleotide-binding; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..53
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P00367"
FT CHAIN 54..558
FT /note="Glutamate dehydrogenase 1, mitochondrial"
FT /id="PRO_0000007212"
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:0000250|UniProtKB:P00366"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 171
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 176
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 252
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 266
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 270
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 319
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 322
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 438
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 444
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 450
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT BINDING 516
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 68
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 84
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 84
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 90
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 110
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 110
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 135
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
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:0007744|PubMed:23576753"
FT MOD_RES 162
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 171
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
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:0000250|UniProtKB:P00366"
FT MOD_RES 183
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 187
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 191
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 191
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 200
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 211
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00367"
FT MOD_RES 326
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 346
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 346
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 352
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 352
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 363
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 363
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 365
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 365
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 384
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00367"
FT MOD_RES 386
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 390
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 390
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 399
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
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:0007744|PubMed:23576753"
FT MOD_RES 415
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 457
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 457
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 457
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P00366"
FT MOD_RES 477
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 477
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 480
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 480
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 503
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 503
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 503
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
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:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 527
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000250"
FT MOD_RES 527
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 545
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753,
FT ECO:0007744|PubMed:23806337"
FT MOD_RES 545
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 548
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT CONFLICT 495
FT /note="D -> G (in Ref. 2; BAC40767)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 558 AA; 61337 MW; 92738AA5A133838A CRC64;
MYRRLGEALL LSRAGPAALG SAAADSAALL GWARGQPSAA PQPGLTPVAR RHYSEAAADR
EDDPNFFKMV EGFFDRGASI VEDKLVEDLK TRESEEQKRN RVRGILRIIK PCNHVLSLSF
PIRRDDGSWE VIEGYRAQHS QHRTPCKGGI RYSTDVSVDE VKALASLMTY KCAVVDVPFG
GAKAGVKINP KNYTDNELEK ITRRFTMELA KKGFIGPGID VPAPDMSTGE REMSWIADTY
ASTIGHYDIN AHACVTGKPI SQGGIHGRIS ATGRGVFHGI ENFINEASYM SILGMTPGFG
DKTFVVQGFG NVGLHSMRYL HRFGAKCVGV GESDGSIWNP DGIDPKELED FKLQHGSILG
FPKAKVYEGS ILEADCDILI PAASEKQLTK SNAPRVKAKI IAEGANGPTT PEADKIFLER
NIMVIPDLYL NAGGVTVSYF EWLKNLNHVS YGRLTFKYER DSNYHLLMSV QESLERKFGK
HGGTIPVVPT AEFQDRISGA SEKDIVHSGL AYTMERSARQ IMRTAMKYNL GLDLRTAAYV
NAIEKVFKVY NEAGVTFT
