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Pyruvate dehydrogenase protein X component, mitochondrial (Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex) (E3-binding protein) (E3BP) (Lipoyl-containing pyruvate dehydrogenase complex component X) (proX)

 ODPX_HUMAN              Reviewed;         501 AA.
O00330; B4DW62; D3DR11; E9PB14; E9PBP7; O60221; Q96FV8; Q99783;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
24-JAN-2001, sequence version 3.
25-OCT-2017, entry version 179.
RecName: Full=Pyruvate dehydrogenase protein X component, mitochondrial;
AltName: Full=Dihydrolipoamide dehydrogenase-binding protein of pyruvate dehydrogenase complex;
AltName: Full=E3-binding protein;
Short=E3BP;
AltName: Full=Lipoyl-containing pyruvate dehydrogenase complex component X;
AltName: Full=proX;
Flags: Precursor;
Name=PDHX; Synonyms=PDX1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT CYS-23.
PubMed=9242632; DOI=10.1074/jbc.272.32.19746;
Harris R.A., Bowker-Kinley M.M., Wu P., Jeng J., Popov K.M.;
"Dihydrolipoamide dehydrogenase-binding protein of the human pyruvate
dehydrogenase complex. DNA-derived amino acid sequence, expression,
and reconstitution of the pyruvate dehydrogenase complex.";
J. Biol. Chem. 272:19746-19751(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INVOLVEMENT IN PDHXD.
TISSUE=Liver;
PubMed=9399911; DOI=10.1086/301653;
Aral B., Benelli C., Ait-Ghezala G., Amessou M., Fouque F.,
Maunoury C., Creau N., Kamoun P., Marsac C.;
"Mutations in PDX1, the human lipoyl-containing component X of the
pyruvate dehydrogenase-complex gene on chromosome 11p1, in congenital
lactic acidosis.";
Am. J. Hum. Genet. 61:1318-1326(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9467010; DOI=10.1093/hmg/7.3.501;
Ling M., McEachern G., Seyda A., Mackay N., Scherer S.W.,
Bratinova S., Beatty B., Giovannucci-Uzielli M.L., Robinson B.H.;
"Detection of a homozygous four base pair deletion in the protein X
gene in a case of pyruvate dehydrogenase complex deficiency.";
Hum. Mol. Genet. 7:501-505(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Aral B., Dey R., Marsac C.;
"Human gene sequence for PDX1, the human lipoyl-containing component X
of the pyruvate dehydrogenase complex.";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Synovium;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
VAL-370.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-501 (ISOFORM 1).
TISSUE=Brain;
PubMed=9110174;
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W.,
Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.;
"Large-scale concatenation cDNA sequencing.";
Genome Res. 7:353-358(1997).
[10]
SUBUNIT.
PubMed=14638692; DOI=10.1074/jbc.M308172200;
Hiromasa Y., Fujisawa T., Aso Y., Roche T.E.;
"Organization of the cores of the mammalian pyruvate dehydrogenase
complex formed by E2 and E2 plus the E3-binding protein and their
capacities to bind the E1 and E3 components.";
J. Biol. Chem. 279:6921-6933(2004).
[11]
INTERACTION WITH DLD, AND MUTAGENESIS OF ASN-190; ARG-208 AND ILE-210.
PubMed=20160912; DOI=10.1016/j.molcatb.2009.05.001;
Patel M.S., Korotchkina L.G., Sidhu S.;
"Interaction of E1 and E3 components with the core proteins of the
human pyruvate dehydrogenase complex.";
J. Mol. Catal., B Enzym. 61:2-6(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-194, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
INTERACTION WITH DLD.
PubMed=20385101; DOI=10.1016/j.bbrc.2010.04.038;
Park Y.H., Patel M.S.;
"Characterization of interactions of dihydrolipoamide dehydrogenase
with its binding protein in the human pyruvate dehydrogenase
complex.";
Biochem. Biophys. Res. Commun. 395:416-419(2010).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
INTERACTION WITH SIRT4, LIPOYLATION AT LYS-97, AND DELIPOYLATION AT
LYS-97.
PubMed=25525879; DOI=10.1016/j.cell.2014.11.046;
Mathias R.A., Greco T.M., Oberstein A., Budayeva H.G., Chakrabarti R.,
Rowland E.A., Kang Y., Shenk T., Cristea I.M.;
"Sirtuin 4 is a lipoamidase regulating pyruvate dehydrogenase complex
activity.";
Cell 159:1615-1625(2014).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[18]
X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 54-274 IN COMPLEX WITH DLD.
PubMed=16263718; DOI=10.1074/jbc.M507850200;
Ciszak E.M., Makal A., Hong Y.S., Vettaikkorumakankauv A.K.,
Korotchkina L.G., Patel M.S.;
"How dihydrolipoamide dehydrogenase-binding protein binds
dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase
complex.";
J. Biol. Chem. 281:648-655(2006).
[19]
X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 174-230 IN COMPLEX WITH DLD,
AND MUTAGENESIS OF ARG-183; SER-185; PRO-186; ALA-187; ARG-189;
ASN-190; GLU-193; ARG-208; ILE-210; LYS-213 AND GLU-214.
PubMed=16442803; DOI=10.1016/j.str.2006.01.001;
Brautigam C.A., Wynn R.M., Chuang J.L., Machius M., Tomchick D.R.,
Chuang D.T.;
"Structural insight into interactions between dihydrolipoamide
dehydrogenase (E3) and E3 binding protein of human pyruvate
dehydrogenase complex.";
Structure 14:611-621(2006).
[20]
STRUCTURE BY NMR OF 57-141.
RIKEN structural genomics initiative (RSGI);
"Solution structure of RSGI RUH-054, a lipoyl domain from human 2-
oxoacid dehydrogenase.";
Submitted (OCT-2006) to the PDB data bank.
[21]
CRYO-ELECTRON MICROSCOPY (18.3 ANGSTROMS) OF INNER CORE OF THE
COMPLEX, AND SUBUNIT.
PubMed=20361979; DOI=10.1016/j.jmb.2010.03.043;
Vijayakrishnan S., Kelly S.M., Gilbert R.J., Callow P., Bhella D.,
Forsyth T., Lindsay J.G., Byron O.;
"Solution structure and characterisation of the human pyruvate
dehydrogenase complex core assembly.";
J. Mol. Biol. 399:71-93(2010).
-!- FUNCTION: Required for anchoring dihydrolipoamide dehydrogenase
(E3) to the dihydrolipoamide transacetylase (E2) core of the
pyruvate dehydrogenase complexes of eukaryotes. This specific
binding is essential for a functional PDH complex.
-!- SUBUNIT: Part of the inner core of the multimeric pyruvate
dehydrogenase complex that is composed of about 48 DLAT and 12
PDHX molecules (PubMed:14638692, PubMed:20361979). This core binds
multiple copies of pyruvate dehydrogenase (subunits PDH1A and
PDHB, E1), dihydrolipoamide acetyltransferase (DLAT, E2) and
lipoamide dehydrogenase (DLD, E3) (PubMed:14638692). Interacts
with SIRT4 (PubMed:25525879). Interacts with DLD (PubMed:20385101,
PubMed:16263718, PubMed:16442803, PubMed:20160912,
PubMed:20361979). {ECO:0000269|PubMed:14638692,
ECO:0000269|PubMed:16263718, ECO:0000269|PubMed:16442803,
ECO:0000269|PubMed:20160912, ECO:0000269|PubMed:20361979,
ECO:0000269|PubMed:20385101, ECO:0000269|PubMed:25525879}.
-!- INTERACTION:
Q6RW13:AGTRAP; NbExp=4; IntAct=EBI-751566, EBI-741181;
P09622:DLD; NbExp=3; IntAct=EBI-751566, EBI-353366;
Q9Y6E7:SIRT4; NbExp=4; IntAct=EBI-751566, EBI-2606540;
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O00330-1; Sequence=Displayed;
Name=2;
IsoId=O00330-2; Sequence=VSP_045271;
Note=No experimental confirmation available.;
Name=3;
IsoId=O00330-3; Sequence=VSP_053817;
Note=No experimental confirmation available. Gene prediction
based on EST data.;
-!- PTM: Delipoylated at Lys-97 by SIRT4, delipoylation decreases the
PHD complex activity. {ECO:0000269|PubMed:25525879}.
-!- DISEASE: Pyruvate dehydrogenase E3-binding protein deficiency
(PDHXD) [MIM:245349]: A metabolic disorder characterized by
decreased activity of the pyruvate dehydrogenase complex without
observable reduction in the activities of enzymes E1, E2, or E3.
Clinical features include hypotonia and psychomotor retardation.
{ECO:0000269|PubMed:9399911}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
{ECO:0000305}.
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EMBL; AF001437; AAB66315.1; -; mRNA.
EMBL; Y13145; CAA73606.1; -; mRNA.
EMBL; U82328; AAC39661.1; -; mRNA.
EMBL; AJ298105; CAC18649.1; -; Genomic_DNA.
EMBL; AK301384; BAG62924.1; -; mRNA.
EMBL; AC107928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL138810; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL356215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471064; EAW68158.1; -; Genomic_DNA.
EMBL; CH471064; EAW68160.1; -; Genomic_DNA.
EMBL; BC010389; AAH10389.1; -; mRNA.
EMBL; U79296; AAB50223.1; -; mRNA.
CCDS; CCDS44569.1; -. [O00330-3]
CCDS; CCDS53616.1; -. [O00330-2]
CCDS; CCDS7896.1; -. [O00330-1]
RefSeq; NP_001128496.1; NM_001135024.1. [O00330-3]
RefSeq; NP_001159630.1; NM_001166158.1. [O00330-2]
RefSeq; NP_003468.2; NM_003477.2. [O00330-1]
UniGene; Hs.502315; -.
PDB; 1ZY8; X-ray; 2.59 A; K/L/M/N/O=54-274.
PDB; 2DNC; NMR; -; A=57-141.
PDB; 2F5Z; X-ray; 2.18 A; K/L/M/N/O=173-228.
PDB; 2F60; X-ray; 1.55 A; K=173-228.
PDBsum; 1ZY8; -.
PDBsum; 2DNC; -.
PDBsum; 2F5Z; -.
PDBsum; 2F60; -.
ProteinModelPortal; O00330; -.
SMR; O00330; -.
BioGrid; 113737; 31.
DIP; DIP-29026N; -.
IntAct; O00330; 13.
MINT; MINT-1482590; -.
STRING; 9606.ENSP00000227868; -.
iPTMnet; O00330; -.
PhosphoSitePlus; O00330; -.
SwissPalm; O00330; -.
BioMuta; PDHX; -.
EPD; O00330; -.
MaxQB; O00330; -.
PaxDb; O00330; -.
PeptideAtlas; O00330; -.
PRIDE; O00330; -.
DNASU; 8050; -.
Ensembl; ENST00000227868; ENSP00000227868; ENSG00000110435. [O00330-1]
Ensembl; ENST00000430469; ENSP00000415695; ENSG00000110435. [O00330-2]
Ensembl; ENST00000448838; ENSP00000389404; ENSG00000110435. [O00330-3]
GeneID; 8050; -.
KEGG; hsa:8050; -.
UCSC; uc001mvt.4; human. [O00330-1]
CTD; 8050; -.
DisGeNET; 8050; -.
EuPathDB; HostDB:ENSG00000110435.11; -.
GeneCards; PDHX; -.
HGNC; HGNC:21350; PDHX.
HPA; HPA038484; -.
HPA; HPA038485; -.
MalaCards; PDHX; -.
MIM; 245349; phenotype.
MIM; 608769; gene.
neXtProt; NX_O00330; -.
OpenTargets; ENSG00000110435; -.
Orphanet; 255182; Pyruvate dehydrogenase E3-binding protein deficiency.
PharmGKB; PA134976445; -.
eggNOG; KOG0557; Eukaryota.
eggNOG; COG0508; LUCA.
GeneTree; ENSGT00890000139393; -.
HOGENOM; HOG000281566; -.
HOVERGEN; HBG005063; -.
InParanoid; O00330; -.
KO; K13997; -.
OMA; SWRLGCD; -.
OrthoDB; EOG091G0CAV; -.
PhylomeDB; O00330; -.
TreeFam; TF332256; -.
BioCyc; MetaCyc:ENSG00000110435-MONOMER; -.
Reactome; R-HSA-204174; Regulation of pyruvate dehydrogenase (PDH) complex.
Reactome; R-HSA-389661; Glyoxylate metabolism and glycine degradation.
Reactome; R-HSA-5362517; Signaling by Retinoic Acid.
Reactome; R-HSA-70268; Pyruvate metabolism.
ChiTaRS; PDHX; human.
EvolutionaryTrace; O00330; -.
GeneWiki; E3_binding_protein; -.
GenomeRNAi; 8050; -.
PRO; PR:O00330; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000110435; -.
CleanEx; HS_PDHX; -.
CleanEx; HS_PDX1; -.
ExpressionAtlas; O00330; baseline and differential.
Genevisible; O00330; HS.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:UniProtKB.
GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:InterPro.
GO; GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
GO; GO:0061732; P:mitochondrial acetyl-CoA biosynthetic process from pyruvate; IC:MGI.
GO; GO:0006090; P:pyruvate metabolic process; TAS:Reactome.
GO; GO:0010510; P:regulation of acetyl-CoA biosynthetic process from pyruvate; TAS:Reactome.
Gene3D; 4.10.320.10; -; 1.
InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
InterPro; IPR000089; Biotin_lipoyl.
InterPro; IPR004167; E3-bd.
InterPro; IPR036625; E3-bd_dom_sf.
InterPro; IPR011053; Single_hybrid_motif.
Pfam; PF00198; 2-oxoacid_dh; 1.
Pfam; PF00364; Biotin_lipoyl; 1.
Pfam; PF02817; E3_binding; 1.
SUPFAM; SSF47005; SSF47005; 1.
SUPFAM; SSF51230; SSF51230; 1.
PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PROSITE; PS00189; LIPOYL; 1.
PROSITE; PS51826; PSBD; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Lipoyl; Mitochondrion; Phosphoprotein; Polymorphism;
Reference proteome; Transit peptide.
TRANSIT 1 53 Mitochondrion. {ECO:0000250}.
CHAIN 54 501 Pyruvate dehydrogenase protein X
component, mitochondrial.
/FTId=PRO_0000020484.
DOMAIN 56 132 Lipoyl-binding. {ECO:0000255|PROSITE-
ProRule:PRU01066}.
DOMAIN 183 220 Peripheral subunit-binding (PSBD).
{ECO:0000255|PROSITE-ProRule:PRU01170}.
COMPBIAS 149 170 Pro-rich.
MOD_RES 97 97 N6-lipoyllysine. {ECO:0000255|PROSITE-
ProRule:PRU01066,
ECO:0000269|PubMed:25525879}.
MOD_RES 194 194 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 196 196 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 394 394 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8BKZ9}.
VAR_SEQ 2 53 AASWRLGCDPRLLRYLVGFPGRRSVGLVKGALGWSVSRGAN
WRWFHSTQWLR -> QSGGAEGSPGAGRTGRGPGSGKAPPA
EISSGAPDFPG (in isoform 3).
{ECO:0000305}.
/FTId=VSP_053817.
VAR_SEQ 115 341 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_045271.
VARIANT 23 23 R -> C (in dbSNP:rs1049306).
{ECO:0000269|PubMed:9242632}.
/FTId=VAR_046619.
VARIANT 101 101 T -> A (in dbSNP:rs11539202).
/FTId=VAR_046620.
VARIANT 370 370 D -> V (in dbSNP:rs17850649).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_046621.
MUTAGEN 183 183 R->A: Strongly decreased DLD binding.
{ECO:0000269|PubMed:16442803}.
MUTAGEN 185 185 S->A: Strongly decreased DLD binding.
{ECO:0000269|PubMed:16442803}.
MUTAGEN 186 186 P->A: Strongly decreased DLD binding.
{ECO:0000269|PubMed:16442803}.
MUTAGEN 187 187 A->M: Strongly decreased DLD binding.
{ECO:0000269|PubMed:16442803}.
MUTAGEN 189 189 R->A: Strongly decreased DLD binding.
{ECO:0000269|PubMed:16442803}.
MUTAGEN 190 190 N->A: Decreased DLD binding.
{ECO:0000269|PubMed:16442803,
ECO:0000269|PubMed:20160912}.
MUTAGEN 190 190 N->K: Moderately decreased interaction
with DLD. {ECO:0000269|PubMed:20160912}.
MUTAGEN 193 193 E->A: Strongly decreased DLD binding.
{ECO:0000269|PubMed:16442803}.
MUTAGEN 208 208 R->A: Strongly decreased DLD binding.
{ECO:0000269|PubMed:16442803}.
MUTAGEN 208 208 R->D: Decreased interaction with DLD.
{ECO:0000269|PubMed:20160912}.
MUTAGEN 210 210 I->A: Strongly decreased DLD binding.
{ECO:0000269|PubMed:16442803}.
MUTAGEN 210 210 I->R: Decreased interaction with DLD.
{ECO:0000269|PubMed:20160912}.
MUTAGEN 210 210 I->S: Decreased interaction with DLD.
{ECO:0000269|PubMed:20160912}.
MUTAGEN 213 213 K->A: Strongly decreased DLD binding.
{ECO:0000269|PubMed:16442803}.
MUTAGEN 214 214 E->A: Strongly decreased DLD binding.
{ECO:0000269|PubMed:16442803}.
CONFLICT 41 41 A -> R (in Ref. 3; AAC39661).
{ECO:0000305}.
CONFLICT 251 251 A -> S (in Ref. 1; AAB66315 and 2;
CAA73606). {ECO:0000305}.
CONFLICT 344 344 P -> S (in Ref. 5; BAG62924).
{ECO:0000305}.
STRAND 57 60 {ECO:0000244|PDB:2DNC}.
STRAND 69 71 {ECO:0000244|PDB:2DNC}.
STRAND 73 78 {ECO:0000244|PDB:2DNC}.
STRAND 88 94 {ECO:0000244|PDB:2DNC}.
STRAND 99 103 {ECO:0000244|PDB:2DNC}.
STRAND 108 112 {ECO:0000244|PDB:2DNC}.
STRAND 122 125 {ECO:0000244|PDB:2DNC}.
STRAND 127 132 {ECO:0000244|PDB:2DNC}.
HELIX 180 183 {ECO:0000244|PDB:2F60}.
HELIX 186 194 {ECO:0000244|PDB:2F60}.
HELIX 199 201 {ECO:0000244|PDB:2F60}.
HELIX 207 209 {ECO:0000244|PDB:2F60}.
HELIX 213 230 {ECO:0000244|PDB:2F60}.
SEQUENCE 501 AA; 54122 MW; 9CF0C1DAE9E12EF9 CRC64;
MAASWRLGCD PRLLRYLVGF PGRRSVGLVK GALGWSVSRG ANWRWFHSTQ WLRGDPIKIL
MPSLSPTMEE GNIVKWLKKE GEAVSAGDAL CEIETDKAVV TLDASDDGIL AKIVVEEGSK
NIRLGSLIGL IVEEGEDWKH VEIPKDVGPP PPVSKPSEPR PSPEPQISIP VKKEHIPGTL
RFRLSPAARN ILEKHSLDAS QGTATGPRGI FTKEDALKLV QLKQTGKITE SRPTPAPTAT
PTAPSPLQAT AGPSYPRPVI PPVSTPGQPN AVGTFTEIPA SNIRRVIAKR LTESKSTVPH
AYATADCDLG AVLKVRQDLV KDDIKVSVND FIIKAAAVTL KQMPDVNVSW DGEGPKQLPF
IDISVAVATD KGLLTPIIKD AAAKGIQEIA DSVKALSKKA RDGKLLPEEY QGGSFSISNL
GMFGIDEFTA VINPPQACIL AVGRFRPVLK LTEDEEGNAK LQQRQLITVT MSSDSRVVDD
ELATRFLKSF KANLENPIRL A


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