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DHE3_BOVIN
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   03-AUG-2022, entry version 172.
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   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   AlphaFoldDB; P00366; -.
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; P00366; -.
DR   PeptideAtlas; P00366; -.
DR   PRIDE; 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; 692851at2759; -.
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   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   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
 
 
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