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Homo sapiens pyruvate dehyrogenase phosphatase catalytic subunit 1 (PDP1), transcript variant 5, mRNA.

RefSeq Accession Definition Service Stock Status Price *Turnaround time Order
NM_018444 Homo sapiens pyruvate dehyrogenase phosphatase catalytic subunit 1 (PDP1), transcript variant 5, mRNA. GenEZ ORF Cloning On-demand $699.00 18

*Business Day

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RefSeq Version NM_018444.3, 239985429
Length 4291 bp
Structure linear
Update Date 03-MAY-2014
Organism Homo sapiens (human)
Definition Homo sapiens pyruvate dehyrogenase phosphatase catalytic subunit 1 (PDP1), transcript variant 5, mRNA.
Product pyruvate dehyrogenase phosphatase catalytic subunit 1 isoform 3

Summary: Pyruvate dehydrogenase (E1) is one of the three components (E1, E2, and E3) of the large pyruvate dehydrogenase complex. Pyruvate dehydrogenase kinases catalyze phosphorylation of serine residues of E1 to inactivate the E1 component and inhibit the complex. Pyruvate dehydrogenase phosphatases catalyze the dephosphorylation and activation of the E1 component to reverse the effects of pyruvate dehydrogenase kinases. Pyruvate dehydrogenase phosphatase is a heterodimer consisting of catalytic and regulatory subunits. Two catalytic subunits have been reported; one is predominantly expressed in skeletal muscle and another one is is much more abundant in the liver. The catalytic subunit, encoded by this gene, is the former, and belongs to the protein phosphatase 2C (PP2C) superfamily. Along with the pyruvate dehydrogenase complex and pyruvate dehydrogenase kinases, this enzyme is located in the mitochondrial matrix. Mutation in this gene causes pyruvate dehydrogenase phosphatase deficiency. Multiple alternatively spliced transcript variants encoding different isoforms have been identified.[provided by RefSeq, Jun 2009].

Transcript Variant: This variant (5) lacks an internal segment, compared to variant 2. The difference causes translation initiation at a downstream AUG and results in an isoform (3) with a shorter N-terminus, compared to isoform 2.

RefSeq NP_060914.2
CDS 270..1883
Misc Feature(1)84..86
Misc Feature(2)84..86
Misc Feature(3)594..1844
Misc Feature(4)594..1844
Misc Feature(5)order(627..629,639..644,699..707,1521..1523,1815..1817)
Misc Feature(6)873..875
Exon (1)1..225
Gene Synonym:PDH; PDP; PDPC; PPM2C
Exon (2)226..4278
Gene Synonym:PDH; PDP; PDPC; PPM2C
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Position Chain Variation Link
134+c, tdbSNP:202016823
203+a, cdbSNP:372548037
228+a, gdbSNP:368896704
243+c, tdbSNP:76597597
257+c, gdbSNP:373914341
283+c, gdbSNP:376864107
294+c, tdbSNP:371323550
360+c, tdbSNP:201452113
397+a, gdbSNP:201081450
423+c, tdbSNP:140713866
464+c, tdbSNP:375147234
471+a, gdbSNP:374758737
508+c, tdbSNP:79439881
530+c, tdbSNP:144544236
546+g, tdbSNP:267606938
553+a, gdbSNP:368756677
636+a, c, gdbSNP:144604949
646+a, gdbSNP:147845975
674+c, tdbSNP:376531662
675+a, cdbSNP:201131767
687+c, tdbSNP:141399719
690+a, gdbSNP:151019488
692+a, gdbSNP:368265235
779+a, tdbSNP:200661557
815+c, tdbSNP:202034256
910+c, tdbSNP:200145429
926+c, tdbSNP:374859758
938+c, tdbSNP:138512618
940+c, tdbSNP:140780685
947+c, gdbSNP:199977411
950+a, gdbSNP:369055053
958+g, tdbSNP:201467137
986+c, gdbSNP:150112501
1022+a, gdbSNP:138553326
1049+c, tdbSNP:140224111
1051+a, gdbSNP:145915456
1124+c, tdbSNP:201021364
1161+a, gdbSNP:373016029
1175+c, tdbSNP:138488258
1178+c, tdbSNP:146222349
1182+c, tdbSNP:149633208
1236+a, gdbSNP:370143029
1248+c, tdbSNP:373354872
1262+a, gdbSNP:200054483
1290+c, gdbSNP:144339806
1482+c, tdbSNP:377342640
1497+g, tdbSNP:369447724
1502+a, gdbSNP:374326474
1511+a, gdbSNP:148348306
1543+a, gdbSNP:200222464
1550+c, gdbSNP:141493326
1632+c, gdbSNP:373946288
1671+a, gdbSNP:377553463
1686+c, tdbSNP:201132164
1700+c, tdbSNP:147477305
1703+a, gdbSNP:117294206
1715+c, tdbSNP:137975172
1716+a, gdbSNP:370390664
1724+c, tdbSNP:374262682
1765+a, gdbSNP:376060350
1789+c, gdbSNP:145358369
1803+c, tdbSNP:202225648
1827+a, gdbSNP:202145000
1839+c, gdbSNP:147237491
1883+c, gdbSNP:139199750
1908+c, gdbSNP:41272415
1919+c, tdbSNP:4735258
1932+a, cdbSNP:192535454
1934+g, tdbSNP:149521176
1948+a, gdbSNP:144036151
1954+c, tdbSNP:148691545
1976+a, gdbSNP:144473673
2256+c, tdbSNP:185126352
2374+g, tdbSNP:41272417
2392+g, tdbSNP:199846257
2449+c, tdbSNP:78884124
2493+a, gdbSNP:190420045
2512+a, gdbSNP:192629673
complement(2514)-g, cdbSNP:911
complement(2522)-g, adbSNP:147461233
2538+a, gdbSNP:185015320
2549+, gdbSNP:139623857
2690+a, cdbSNP:188727327
2793+a, tdbSNP:7461396
2813+a, gdbSNP:180752222
2840+a, gdbSNP:75265995
2885..2886+, gdbSNP:35866235
2890+a, gdbSNP:185360919
3086..3087+, gdbSNP:35793146
3302+a, cdbSNP:201779185
3370+a, tdbSNP:189435075
3447+a, cdbSNP:111728711
3492+a, gdbSNP:186669527
3531+, gdbSNP:145384326
3532+g, tdbSNP:377214447
3533+g, tdbSNP:192025344
3544+, tdbSNP:60316663
3619+c, gdbSNP:116788695
3690+a, tdbSNP:77734416
3805+a, tdbSNP:139839619
3958+, adbSNP:368109978
3978+c, tdbSNP:115434133
4138+c, tdbSNP:183503324
4140+a, tdbSNP:367694582
4146+c, tdbSNP:145337691
4184..4185+, adbSNP:371346130
4219+a, tdbSNP:186410170
4236+g, tdbSNP:190113849
Gene SymbolPDP1
Gene SynonymPDH; PDP; PDPC; PPM2C
Locus Map8q22.1
All Transcripts
RefSeq Accession Definition Stock Status Price Turnaround time Business Day Select
NM_001161779 Homo sapiens pyruvate dehyrogenase phosphatase catalytic subunit 1 (PDP1), transcript variant 2, mRNA. On-demand $699.00 18
NM_001161781 Homo sapiens pyruvate dehyrogenase phosphatase catalytic subunit 1 (PDP1), transcript variant 4, mRNA. On-demand $699.00 18
NM_001161780 Homo sapiens pyruvate dehyrogenase phosphatase catalytic subunit 1 (PDP1), transcript variant 3, mRNA. On-demand $699.00 18
NM_018444 Homo sapiens pyruvate dehyrogenase phosphatase catalytic subunit 1 (PDP1), transcript variant 5, mRNA. On-demand $699.00 18
XM_005250986 PREDICTED: Homo sapiens pyruvate dehyrogenase phosphatase catalytic subunit 1 (PDP1), transcript variant X1, mRNA. On-demand $849.00 20
XM_006716592 PREDICTED: Homo sapiens pyruvate dehyrogenase phosphatase catalytic subunit 1 (PDP1), transcript variant X2, mRNA. On-demand $699.00 18
Title Tyr phosphorylation of PDP1 toggles recruitment between ACAT1 and SIRT3 to regulate the pyruvate dehydrogenase complex .
Author Fan J, Shan C, Kang HB, Elf S, Xie J, Tucker M, Gu TL, Aguiar M, Lonning S, Chen H, Mohammadi M, Britton LM, Garcia BA, Aleckovic M, Kang Y, Kaluz S, Devi N, Van Meir EG, Hitosugi T, Seo JH, Lonial S, Gaddh M, Arellano M, Khoury HJ, Khuri FR, Boggon TJ, Kang S and Chen J.
Journal Mol. Cell 53 (4), 534-548 (2014)
Title Exercise-induced pyruvate dehydrogenase activation is not affected by 7 days of bed rest .
Author Kiilerich K, Ringholm S, Bienso RS, Fisher JP, Iversen N, van Hall G, Wojtaszewski JF, Saltin B, Lundby C, Calbet JA and Pilegaard H.
Journal J. Appl. Physiol. 111 (3), 751-757 (2011)
Title Crystallization and preliminary crystallographic studies of the catalytic subunits of human pyruvate dehydrogenase phosphatase isoforms 1 and 2 .
Author Kato J and Kato M.
Journal Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 66 (PT 3), 342-345 (2010)
Title Genetic variants in nuclear-encoded mitochondrial genes influence .
Author Hendrickson SL, Lautenberger JA, Chinn LW, Malasky M, Sezgin E, Kingsley LA, Goedert JJ, Kirk GD, Gomperts ED, Buchbinder SP, Troyer JL and O'Brien SJ.
Journal PLoS ONE 5 (9), E12862 (2010)
Title Pyruvate dehydrogenase phosphatase 1 (PDP1) null mutation produces a lethal infantile phenotype .
Author Cameron JM, Maj M, Levandovskiy V, Barnett CP, Blaser S, Mackay N, Raiman J, Feigenbaum A, Schulze A and Robinson BH.
Journal Hum. Genet. 125 (3), 319-326 (2009)
Title Isoenzymes of pyruvate dehydrogenase phosphatase. DNA-derived amino acid sequences, expression, and regulation .
Author Huang B, Gudi R, Wu P, Harris RA, Hamilton J and Popov KM.
Journal J. Biol. Chem. 273 (28), 17680-17688 (1998)
Title Mutagenesis studies of the phosphorylation sites of recombinant human pyruvate dehydrogenase. Site-specific regulation .
Author Korotchkina LG and Patel MS.
Journal J. Biol. Chem. 270 (24), 14297-14304 (1995)
Title Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase and sequence similarity with protein phosphatase 2C .
Author Lawson JE, Niu XD, Browning KS, Trong HL, Yan J and Reed LJ.
Journal Biochemistry 32 (35), 8987-8993 (1993)
Title Decrease of pyruvate dehydrogenase phosphatase activity in patients with congenital lactic acidemia .
Author Ito M, Kobashi H, Naito E, Saijo T, Takeda E, Huq AH and Kuroda Y.
Journal Clin. Chim. Acta 209 (1-2), 1-7 (1992)
Title Pyruvate dehydrogenase phosphatase deficiency: a cause of congenital chronic lactic acidosis in infancy .
Author Robinson,B.H. and Sherwood,W.G.
Journal Pediatr. Res. 9 (12), 935-939 (1975)

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