P08559 (ODPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
EC=1.2.4.1

Alternative name(s):
PDHE1-A type I

Gene names

Name:	PDHA1
Synonyms:	PHE1A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2, and thereby links the glycolytic pathway to the tricarboxylic cycle. Ref.16 Ref.30
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. Ref.16 Ref.29 Ref.30
Cofactor	Thiamine pyrophosphate. Ref.27 Ref.30
Enzyme regulation	Pyruvate dehydrogenase activity is inhibited by phosphorylation of PDHA1; it is reactivated by dephosphorylation. Ref.16 Ref.29 Ref.30
Subunit structure	Heterotetramer of two PDHA1 and two PDHB subunits. The heterotetramer interacts with DLAT, and is part of the multimeric pyruvate dehydrogenase complex that contains multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (DLAT, E2) and lipoamide dehydrogenase (DLD, E3). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules. Ref.18 Ref.30
Subcellular location	Mitochondrion matrix.
Tissue specificity	Ubiquitous.
Post-translational modification	Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient. Dephosphorylation at all three sites, i.e. at Ser-232, Ser-293 and Ser-300, is required for reactivation.
Involvement in disease	Pyruvate dehydrogenase E1-alpha deficiency (PDHAD) [MIM:312170]: An enzymatic defect causing primary lactic acidosis in children. It is associated with a broad clinical spectrum ranging from fatal lactic acidosis in the newborn to chronic neurologic dysfunction with structural abnormalities in the central nervous system without systemic acidosis. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.15 Ref.31 Ref.32 Ref.33 Ref.35 Ref.36 Ref.37 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.46 X-linked Leigh syndrome (X-LS) [MIM:308930]: Early-onset progressive neurodegenerative disorder with a characteristic neuropathology consisting of focal, bilateral lesions in one or more areas of the central nervous system, including the brainstem, thalamus, basal ganglia, cerebellum, and spinal cord. The lesions are areas of demyelination, gliosis, necrosis, spongiosis, or capillary proliferation. Clinical symptoms depend on which areas of the central nervous system are involved. The most common underlying cause is a defect in oxidative phosphorylation. LS may be a feature of a deficiency of any of the mitochondrial respiratory chain complexes. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.31 Ref.34 Ref.38 Ref.40 Ref.45
Sequence caution	The sequence AAA60055.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence AAB59581.1 differs from that shown. Reason: Frameshift at positions 106 and 175.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism Tricarboxylic acid cycle
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Leigh syndrome
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from pyruvate Inferred from direct assay Ref.30. Source: UniProtKB glycolysis Inferred from electronic annotation. Source: InterPro regulation of acetyl-CoA biosynthetic process from pyruvate Traceable author statement. Source: Reactome tricarboxylic acid cycle Inferred from direct assay Ref.30. Source: UniProtKB
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome pyruvate dehydrogenase complex Inferred from direct assay Ref.30. Source: UniProtKB
Molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity Inferred from electronic annotation. Source: EC pyruvate dehydrogenase activity Inferred from direct assay Ref.30. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P08559-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P08559-2)

The sequence of this isoform differs from the canonical sequence as follows:
     96-96: G → GQFLLPLT

Note: No experimental confirmation available.

Isoform 3 (identifier: P08559-3)

The sequence of this isoform differs from the canonical sequence as follows:
     170-200: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: P08559-4)

The sequence of this isoform differs from the canonical sequence as follows:
     19-19: P → PRHGLATLPSLVSISRLKQSSHLGLPKCWDYSHSLKTRQ

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 29

29

Mitochondrion

Chain

30 – 390

361

Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

PRO_0000020440

Amino acid modifications

Modified residue

232

1

Phosphoserine; by PDK1 Ref.17 Ref.24 Ref.26

Modified residue

289

1

Phosphotyrosine By similarity

Modified residue

293

1

Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 Ref.17 Ref.29 Ref.30

Modified residue

295

1

Phosphoserine By similarity

Modified residue

300

1

Phosphoserine; by PDK1, PDK2, PDK3 and PDK4 Ref.17 Ref.30

Modified residue

301

1

Phosphotyrosine By similarity

Modified residue

321

1

N6-acetyllysine Ref.23

Natural variations

Alternative sequence

19

1

P → PRHGLATLPSLVSISRLKQS SHLGLPKCWDYSHSLKTRQ in isoform 4.

VSP_043363

Alternative sequence

96

1

G → GQFLLPLT in isoform 2.

VSP_042569

Alternative sequence

170 – 200

31

Missing in isoform 3.

VSP_042570

Natural variant

10

1

R → P in PDHAD; affects mitochondrial import of precursor protein. Ref.41

VAR_010238

Natural variant

72

1

R → C in PDHAD. Ref.40 Ref.43

VAR_004949

Natural variant

113

1

H → D in PDHAD. Ref.43

VAR_004950

Natural variant

162

1

G → R in PDHAD. Ref.43

VAR_004951

Natural variant

167

1

V → M in PDHAD. Ref.35

VAR_004952

Natural variant

199

1

A → T in PDHAD. Ref.35

VAR_004953

Natural variant

205

1

F → L in X-LS; PDHAD. Ref.38 Ref.40

VAR_004954

Natural variant

210

1

M → V in PDHAD. Ref.44

VAR_004955

Natural variant

217

1

P → L in PDHAD. Ref.42

VAR_004956

Natural variant

231

1

T → A in PDHAD. Ref.35

VAR_004957

Natural variant

243

1

Y → N in PDHAD. Ref.36

VAR_021053

Natural variant

258

1

D → A in X-LS; PDHAD. Ref.34

VAR_004958

Natural variant

263

1

R → G in PDHAD and X-LS. Ref.35 Ref.40 Ref.43 Ref.45
Corresponds to variant rs28936081 [ dbSNP | Ensembl ].

VAR_004959

Natural variant

263

1

R → Q in PDHAD. Ref.39

VAR_004960

Natural variant

282

1

M → L. Ref.10 Ref.14 Ref.36
Corresponds to variant rs2229137 [ dbSNP | Ensembl ].

VAR_021054

Natural variant

288

1

R → H in PDHAD. Ref.43

VAR_021055

Natural variant

292

1

H → L in PDHAD. Ref.35

VAR_004961

Natural variant

302

1

R → C in PDHAD; loss of activity; common mutation. Ref.33 Ref.43 Ref.46

VAR_004962

Natural variant

302

1

R → H in PDHAD. Ref.46

VAR_004963

Natural variant

305

1

E → EDSYRTRE in PDHAD.

VAR_020908

Natural variant

307

1

I → IPPHSYRTREEI in PDHAD.

VAR_020909

Natural variant

311

1

Missing in PDHAD. Ref.40 Ref.44

VAR_004964

Natural variant

313

1

Missing in PDHAD. Ref.31

VAR_004965

Natural variant

315

1

D → N in PDHAD. Ref.36
Corresponds to variant rs28935187 [ dbSNP | Ensembl ].

VAR_021056

Natural variant

333

1

E → D.
Corresponds to variant rs2228067 [ dbSNP | Ensembl ].

VAR_050436

Natural variant

378

1

R → H in X-LS; PDHAD. Ref.31 Ref.36 Ref.40

VAR_004966

Experimental info

Mutagenesis

232

1

S → A: Abolishes inactivation by phosphorylation; when associated with A-293 and A-300. Ref.16 Ref.29

Mutagenesis

293

1

S → A: Reduces enzyme activity. Abolishes inactivation by phosphorylation; when associated with A-232 and A-300. Ref.16 Ref.29

Mutagenesis

293

1

S → E: Interferes with substrate binding. Ref.16 Ref.29

Mutagenesis

300

1

S → A: Abolishes inactivation by phosphorylation; when associated with A-232 and A-293. Ref.16

Sequence conflict

301

1

Y → S in AAD23857. Ref.14

Sequence conflict

306

1

E → D in AAD23857. Ref.14

Sequence conflict

349

1

A → P in AAA60055. Ref.6

Sequence conflict

354

1

T → A in AAA60055. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

390

Helix Strand Turn

Details...

Beta strand

32 – 37

6

Beta strand

42 – 45

4

Beta strand

52 – 57

6

Helix

58 – 83

26

Beta strand

85 – 87

3

Helix

98 – 106

9

Beta strand

112 – 115

4

Helix

121 – 126

6

Helix

131 – 138

8

Turn

145 – 148

4

Helix

151 – 153

3

Turn

167 – 169

3

Helix

170 – 184

15

Beta strand

190 – 195

6

Helix

198 – 200

3

Helix

202 – 213

12

Beta strand

218 – 224

7

Beta strand

226 – 228

3

Helix

233 – 236

4

Helix

242 – 244

3

Turn

245 – 248

4

Beta strand

251 – 255

5

Helix

259 – 274

16

Turn

275 – 277

3

Beta strand

280 – 285

6

Beta strand

300 – 302

3

Helix

304 – 314

11

Helix

316 – 326

11

Helix

332 – 355

24

Helix

361 – 363

3

Beta strand

367 – 371

5

Beta strand

375 – 378

4

Beta strand

385 – 388

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1992. Version 3. Checksum: 4D685BBE44A92D4B	FASTA	390	43,296
	10 20 30 40 50 60 MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED 70 80 90 100 110 120 GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA 130 140 150 160 170 180 HGFTFTRGLS VREILAELTG RKGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA 190 200 210 220 230 240 CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST 250 260 270 280 290 300 DYYKRGDFIP GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS 310 320 330 340 350 360 YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP 370 380 390 LEELGYHIYS SDPPFEVRGA NQWIKFKSVS
	Isoform 2 [UniParc]. Checksum: 4BE156001F9994A5	FASTA	397	44,109
	10 20 30 40 50 60 MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED 70 80 90 100 110 120 GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQFLL PLTQEACCVG LEAGINPTDH 130 140 150 160 170 180 LITAYRAHGF TFTRGLSVRE ILAELTGRKG GCAKGKGGSM HMYAKNFYGG NGIVGAQVPL 190 200 210 220 230 240 GAGIALACKY NGKDEVCLTL YGDGAANQGQ IFEAYNMAAL WKLPCIFICE NNRYGMGTSV 250 260 270 280 290 300 ERAAASTDYY KRGDFIPGLR VDGMDILCVR EATRFAAAYC RSGKGPILME LQTYRYHGHS 310 320 330 340 350 360 MSDPGVSYRT REEIQEVRSK SDPIMLLKDR MVNSNLASVE ELKEIDVEVR KEIEDAAQFA 370 380 390 TADPEPPLEE LGYHIYSSDP PFEVRGANQW IKFKSVS
	Isoform 3 [UniParc]. Checksum: 7E94F39FC1293065	FASTA	359	40,188
	10 20 30 40 50 60 MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED 70 80 90 100 110 120 GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA 130 140 150 160 170 180 HGFTFTRGLS VREILAELTG RKGGCAKGKG GSMHMYAKNF YGGNGIVGAQ GQIFEAYNMA 190 200 210 220 230 240 ALWKLPCIFI CENNRYGMGT SVERAAASTD YYKRGDFIPG LRVDGMDILC VREATRFAAA 250 260 270 280 290 300 YCRSGKGPIL MELQTYRYHG HSMSDPGVSY RTREEIQEVR SKSDPIMLLK DRMVNSNLAS 310 320 330 340 350 VEELKEIDVE VRKEIEDAAQ FATADPEPPL EELGYHIYSS DPPFEVRGAN QWIKFKSVS
	Isoform 4 [UniParc]. Checksum: 14FE765CFF2C7120	FASTA	428	47,580
	10 20 30 40 50 60 MRKMLAAVSR VLSGASQKPR HGLATLPSLV SISRLKQSSH LGLPKCWDYS HSLKTRQASR 70 80 90 100 110 120 VLVASRNFAN DATFEIKKCD LHRLEEGPPV TTVLTREDGL KYYRMMQTVR RMELKADQLY 130 140 150 160 170 180 KQKIIRGFCH LCDGQEACCV GLEAGINPTD HLITAYRAHG FTFTRGLSVR EILAELTGRK 190 200 210 220 230 240 GGCAKGKGGS MHMYAKNFYG GNGIVGAQVP LGAGIALACK YNGKDEVCLT LYGDGAANQG 250 260 270 280 290 300 QIFEAYNMAA LWKLPCIFIC ENNRYGMGTS VERAAASTDY YKRGDFIPGL RVDGMDILCV 310 320 330 340 350 360 REATRFAAAY CRSGKGPILM ELQTYRYHGH SMSDPGVSYR TREEIQEVRS KSDPIMLLKD 370 380 390 400 410 420 RMVNSNLASV EELKEIDVEV RKEIEDAAQF ATADPEPPLE ELGYHIYSSD PPFEVRGANQ WIKFKSVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization and nucleotide sequence of the gene encoding the human pyruvate dehydrogenase alpha-subunit." Koike K., Urata Y., Matsuo S., Koike M. Gene 93:307-311(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Leukocyte.
[2]	"Characterization of cDNAs encoding human pyruvate dehydrogenase alpha subunit." Ho L., Wexler I.D., Liu T.C., Thekkumkara T.J., Patel M.S. Proc. Natl. Acad. Sci. U.S.A. 86:5330-5334(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	Huh T.L., Chi Y.T., Casazza J.P., Veech R.L., Song B.J. Submitted (APR-1990) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain and Liver.
[4]	"The human pyruvate dehydrogenase complex. Isolation of cDNA clones for the E1 alpha subunit, sequence analysis, and characterization of the mRNA." Dahl H.-H.M., Hunt S.M., Hutchison W.M., Brown G.K. J. Biol. Chem. 262:7398-7403(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"Structural organization of the gene for the E1 alpha subunit of the human pyruvate dehydrogenase complex." Maragos C., Hutchinson W.M., Hayasaki K., Brown G.K., Dahl H.-H.M. J. Biol. Chem. 264:12294-12298(1989) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[6]	"Isolation of a full-length complementary DNA coding for human E1 alpha subunit of the pyruvate dehydrogenase complex." de Meirleir L., MacKay N., Wah A.M.L.H., Robinson B.H. J. Biol. Chem. 263:1991-1995(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[7]	"Cloning and sequencing of cDNAs encoding alpha and beta subunits of human pyruvate dehydrogenase." Koike K., Ohta S., Urata Y., Kagawa Y., Koike M. Proc. Natl. Acad. Sci. U.S.A. 85:41-45(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[8]	Okajima K. Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[9]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4). Tissue: Thalamus.
[10]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-282. Tissue: Dermoid cancer.
[11]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Muscle.
[14]	"X chromosome evidence for ancient human histories." Harris E.E., Hey J. Proc. Natl. Acad. Sci. U.S.A. 96:3320-3324(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 202-336, VARIANT LEU-282.
[15]	"Mutation of E1 alpha gene in a female patient with pyruvate dehydrogenase deficiency due to rapid degradation of E1 protein." Ito M., Huq A.H., Naito E., Saijo T., Takeda E., Kuroda Y. J. Inherit. Metab. Dis. 15:848-856(1992) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN PDHAD.
[16]	"Mutagenesis studies of the phosphorylation sites of recombinant human pyruvate dehydrogenase. Site-specific regulation." Korotchkina L.G., Patel M.S. J. Biol. Chem. 270:14297-14304(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION, MUTAGENESIS OF SER-232; SER-293 AND SER-300.
[17]	"Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase." Korotchkina L.G., Patel M.S. J. Biol. Chem. 276:37223-37229(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-232; SER-293 AND SER-300.
[18]	"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." Hiromasa Y., Fujisawa T., Aso Y., Roche T.E. J. Biol. Chem. 279:6921-6933(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[19]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[20]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[21]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[22]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[23]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-321, MASS SPECTROMETRY.
[24]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[25]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232, MASS SPECTROMETRY.
[27]	"Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase." Ciszak E.M., Korotchkina L.G., Dominiak P.M., Sidhu S., Patel M.S. J. Biol. Chem. 278:21240-21246(2003) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH THIAMINE PYROPHOSPHATE, COFACTOR.
[28]	"Mutations and polymorphisms in the pyruvate dehydrogenase E1 alpha gene." Dahl H.-H.M., Brown G.K., Brown R.M., Hansen L.L., Kerr D.S., Wexler I.D., Patel M.S., de Meirleir L., Lissens W., Chun K., McKay N., Robinson B.H. Hum. Mutat. 1:97-102(1992) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS.
[29]	"Phosphorylation of serine 264 impedes active site accessibility in the E1 component of the human pyruvate dehydrogenase multienzyme complex." Seifert F., Ciszak E., Korotchkina L., Golbik R., Spinka M., Dominiak P., Sidhu S., Brauer J., Patel M.S., Tittmann K. Biochemistry 46:6277-6287(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 30-390, ENZYME REGULATION, CATALYTIC ACTIVITY, MUTAGENESIS OF SER-293, PHOSPHORYLATION AT SER-293.
[30]	"Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops." Kato M., Wynn R.M., Chuang J.L., Tso S.C., Machius M., Li J., Chuang D.T. Structure 16:1849-1859(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF 30-390 IN COMPLEX WITH PDHB, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, PHOSPHORYLATION AT SER-293 AND SER-300 BY PDK4.
[31]	"Characterization of the mutations in three patients with pyruvate dehydrogenase E1 alpha deficiency." Hansen L.L., Brown G.K., Kirby D.M., Dahl H.-H.M. J. Inherit. Metab. Dis. 14:140-151(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PDHAD LYS-313 DEL, VARIANT X-LS HIS-378.
[32]	"Pyruvate dehydrogenase (PDH) deficiency caused by a 21-base pair insertion mutation in the E1 alpha subunit." De Meirleir L., Lissens W., Vamos E., Liebaers I. Hum. Genet. 88:649-652(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PDHAD ASP-SER-TYR-ARG-THR-ARG-GLU-305 INS.
[33]	"X-linked pyruvate dehydrogenase E1 alpha subunit deficiency in heterozygous females: variable manifestation of the same mutation." Dahl H.-H.M., Hansen L.L., Brown R.M., Danks D.M., Rogers J.G., Brown G.K. J. Inherit. Metab. Dis. 15:835-847(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PDHAD CYS-302.
[34]	"Molecular genetic characterization of an X-linked form of Leigh's syndrome." Matthews P.M., Marchington D.R., Squier M., Land J., Brown R.M., Brown G.K. Ann. Neurol. 33:652-655(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT X-LS ALA-258.
[35]	"Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase leading to deficiency of the pyruvate dehydrogenase complex." Chun K., McKay N., Petrova-Benedict R., Robinson B.H. Hum. Mol. Genet. 2:449-454(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PDHAD MET-167; THR-199; ALA-231; GLY-263 AND LEU-292.
[36]	"Pyruvate dehydrogenase deficiency. Clinical presentation and molecular genetic characterization of five new patients." Matthews P.M., Brown R.M., Otero L.J., Marchington D.R., LeGris M., Howes R., Meadows L.S., Shevell M., Scriver C.R., Brown G.K. Brain 117:435-443(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PDHAD ASN-243; ASN-315 AND HIS-378, VARIANT LEU-282.
[37]	"Pyruvate dehydrogenase deficiency caused by a 33 base pair duplication in the PDH E1 alpha subunit." Hansen L.L., Horn N., Dahl H.-H.M., Kruse T.A. Hum. Mol. Genet. 3:1021-1022(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PDHAD PRO-PRO-HIS-SER-TYR-ARG-THR-ARG-GLU-GLU-ILE-307 INS.
[38]	"Pyruvate dehydrogenase deficiency in a male caused by a point mutation (F205L) in the E1 alpha subunit." Dahl H.-H.M., Brown G.K. Hum. Mutat. 3:152-155(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT X-LS LEU-205.
[39]	"Characterization of a point mutation in the pyruvate dehydrogenase E1 alpha gene from two boys with primary lactic acidaemia." Awata H., Endo F., Tanoue A., Kitano A., Matsuda I. J. Inherit. Metab. Dis. 17:189-195(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PDHAD GLN-263.
[40]	"Mutations in the X-linked E1 alpha subunit of pyruvate dehydrogenase: exon skipping, insertion of duplicate sequence, and missense mutations leading to the deficiency of the pyruvate dehydrogenase complex." Chun K., MacKay N., Petrova-Benedict R., Federico A., Fois A., Cole D.E.C., Robertson E., Robinson B.H. Am. J. Hum. Genet. 56:558-569(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PDHAD CYS-72; GLY-263 AND ARG-311 DEL, VARIANTS X-LS LEU-205 AND HIS-378.
[41]	"An amino acid substitution in the pyruvate dehydrogenase E1 alpha gene, affecting mitochondrial import of the precursor protein." Takakubo F., Cartwright P., Hoogenraad N., Thorburn D.R., Collins F., Lithgow T., Dahl H.-H.M. Am. J. Hum. Genet. 57:772-780(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PDHAD PRO-10.
[42]	"Pyruvate dehydrogenase complex deficiency due to a point mutation (P188L) within the thiamine pyrophosphate binding loop of the E1 alpha subunit." Hemalatha S.G., Kerr D.S., Wexler I.D., Lusk M.M., Kaung M., Du Y., Kolli M., Schelper R.L., Patel M.S. Hum. Mol. Genet. 4:315-318(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PDHAD LEU-217.
[43]	"Mutation analysis of the pyruvate dehydrogenase E1 alpha gene in eight patients with a pyruvate dehydrogenase complex deficiency." Lissens W., de Meirleir L., Seneca S., Benelli C., Marsac C., Poll-The B.T., Briones P., Ruitenbeek W., van Diggelen O., Chaigne D., Ramaekers V., Liebaers I. Hum. Mutat. 7:46-51(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PDHAD CYS-72; ASP-113; ARG-162; GLY-263; HIS-288 AND CYS-302.
[44]	"Three new mutations of the pyruvate dehydrogenase alpha subunit: a point mutation (M181V), 3 bp deletion (-R282), and 16 bp insertion/frameshift (K358SVS-->TVDQS)." Tripatara A., Kerr D.S., Lusk M.M., Kolli M., Tan J., Patel M.S. Hum. Mutat. 8:180-182(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PDHAD VAL-210 AND ARG-311 DEL.
[45]	"Biochemical and molecular analysis of an X-linked case of Leigh syndrome associated with thiamin-responsive pyruvate dehydrogenase deficiency." Naito E., Ito M., Yokota I., Saijo T., Matsuda J., Osaka H., Kimura S., Kuroda Y. J. Inherit. Metab. Dis. 20:539-548(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT X-LS GLY-263.
[46]	"Arginine 302 mutations in the pyruvate dehydrogenase E1alpha subunit gene: identification of further patients and in vitro demonstration of pathogenicity." Otero L.J., Brown R.M., Brown G.K. Hum. Mutat. 12:114-121(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PDHAD CYS-302 AND HIS-302.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D90084 Genomic DNA. Translation: BAA14121.1.
M24848 mRNA. Translation: AAA36533.1.
X52709 mRNA. Translation: CAA36933.1.
X52710 mRNA. Translation: CAA36934.1.
M27257 , M29155, M29156, M29157, M29158, M29159, M29160, M29161, M29162, M29163, M29164 Genomic DNA. Translation: AAA60051.1.
L13318 mRNA. Translation: AAA60227.1.
J03503 mRNA. Translation: AAA60055.1. Different initiation.
J03575 mRNA. Translation: AAA60050.1.
L48690 mRNA. Translation: AAB59581.1. Frameshift.
EF590117 mRNA. Translation: ABQ59099.1.
AK293250 mRNA. Translation: BAH11476.1.
AK296457 mRNA. Translation: BAH12361.1.
AK296341 mRNA. Translation: BAH12323.1.
AK222740 mRNA. Translation: BAD96460.1.
AL732326 Genomic DNA. Translation: CAI41291.1.
CH471074 Genomic DNA. Translation: EAW98960.1.
BC002406 mRNA. Translation: AAH02406.1.
AF125053 Genomic DNA. Translation: AAD23841.1.
AF125054 Genomic DNA. Translation: AAD23842.1.
AF125055 Genomic DNA. Translation: AAD23843.1.
AF125056 Genomic DNA. Translation: AAD23844.1.
AF125057 Genomic DNA. Translation: AAD23845.1.
AF125058 Genomic DNA. Translation: AAD23846.1.
AF125059 Genomic DNA. Translation: AAD23847.1.
AF125060 Genomic DNA. Translation: AAD23848.1.
AF125061 Genomic DNA. Translation: AAD23849.1.
AF125062 Genomic DNA. Translation: AAD23850.1.
AF125063 Genomic DNA. Translation: AAD23851.1.
AF125064 Genomic DNA. Translation: AAD23852.1.
AF125065 Genomic DNA. Translation: AAD23853.1.
AF125066 Genomic DNA. Translation: AAD23854.1.
AF125067 Genomic DNA. Translation: AAD23855.1.
AF125068 Genomic DNA. Translation: AAD23856.1.
AF125069 Genomic DNA. Translation: AAD23857.1.
AF125070 Genomic DNA. Translation: AAD23858.1.
AF125071 Genomic DNA. Translation: AAD23859.1.
AF125072 Genomic DNA. Translation: AAD23860.1.
AF125073 Genomic DNA. Translation: AAD23861.1.
AF125074 Genomic DNA. Translation: AAD23862.1.
AF125075 Genomic DNA. Translation: AAD23863.1.
AF125076 Genomic DNA. Translation: AAD23864.1.
AF125078 Genomic DNA. Translation: AAD23866.1.
AF125079 Genomic DNA. Translation: AAD23867.1.
AF125080 Genomic DNA. Translation: AAD23868.1.
AF125081 Genomic DNA. Translation: AAD23869.1.
AF125082 Genomic DNA. Translation: AAD23870.1.
AF125083 Genomic DNA. Translation: AAD23871.1.
AF125084 Genomic DNA. Translation: AAD23872.1.
AF125085 Genomic DNA. Translation: AAD23873.1.
AF125086 Genomic DNA. Translation: AAD23874.1.
AF125087 Genomic DNA. Translation: AAD23875.1.
AF125088 Genomic DNA. Translation: AAD23876.1.

IPI

IPI00306301.
IPI00643575.
IPI00922697.

PIR

DEHUPA. JQ0770.

RefSeq

NP_000275.1. NM_000284.3.
NP_001166925.1. NM_001173454.1.
NP_001166926.1. NM_001173455.1.
NP_001166927.1. NM_001173456.1.

UniGene

Hs.530331.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NI4	X-ray	1.95	A/C	30-390	[»]
2OZL	X-ray	1.90	A/C	30-390	[»]
3EXE	X-ray	1.98	A/C/E/G	30-390	[»]
3EXF	X-ray	3.00	A/C/E/G	30-390	[»]
3EXG	X-ray	3.01	1/3/5/A/C/E/G/I/K/M/O/Q/S/U/W/Y	30-390	[»]
3EXH	X-ray	2.44	A/C/E/G	30-390	[»]
3EXI	X-ray	2.20	A	30-390	[»]

ProteinModelPortal

P08559.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-37652N.

IntAct

P08559. 6 interactions.

STRING

9606.ENSP00000394382.

PTM databases

PhosphoSite

P08559.

Polymorphism databases

DMDM

129063.

2D gel databases

REPRODUCTION-2DPAGE

IPI00306301.

UCD-2DPAGE

P08559.

Proteomic databases

PaxDb

P08559.

PeptideAtlas

P08559.

PRIDE

P08559.

Protocols and materials databases

DNASU

5160.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000379806; ENSP00000369134; ENSG00000131828.
ENST00000422285; ENSP00000394382; ENSG00000131828.
ENST00000540249; ENSP00000440761; ENSG00000131828.
ENST00000545074; ENSP00000438550; ENSG00000131828.

GeneID

5160.

KEGG

hsa:5160.

UCSC

uc004czg.4. human.

Organism-specific databases

CTD

5160.

GeneCards

GC0XP019271.

HGNC

HGNC:8806. PDHA1.

MIM

300502. gene.
308930. phenotype.
312170. phenotype.

neXtProt

NX_P08559.

Orphanet

70474. Leigh syndrome with cardiomyopathy.
79243. Pyruvate dehydrogenase E1-alpha deficiency.

PharmGKB

PA33150.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1071.

HOGENOM

HOG000281336.

HOVERGEN

HBG001863.

InParanoid

P08559.

KO

K00161.

OMA

FAQNDPE.

OrthoDB

EOG4W0XD6.

PhylomeDB

P08559.

Enzyme and pathway databases

BioCyc

MetaCyc:HS05573-MONOMER.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P08559.

Gene expression databases

ArrayExpress

P08559.

Bgee

P08559.

CleanEx

HS_PDHA1.

Genevestigator

P08559.

GermOnline

ENSG00000131828. Homo sapiens.

Family and domain databases

InterPro

IPR001017. DH_E1.
IPR017597. Pyrv_DH_E1_asu_subgrp-y.
[Graphical view]

Pfam

PF00676. E1_dh. 1 hit.
[Graphical view]

TIGRFAMs

TIGR03182. PDH_E1_alph_y. 1 hit.

ProtoNet

Search...

Other

ChEMBL

CHEMBL2092.

ChiTaRS

PDHA1. human.

DrugBank

DB00157. NADH.

EvolutionaryTrace

P08559.

GenomeRNAi

5160.

NextBio

19962.

SOURCE

Search...

Entry information

Entry name

ODPA_HUMAN

Accession

Primary (citable) accession number: P08559
Secondary accession number(s): A5YVE9 , B7Z3T7, B7Z3X5, Q53H41, Q5JPT8, Q9NP12, Q9UBJ8, Q9UBU0, Q9UNG4, Q9UNG5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	May 1, 1992
Last modified:	May 1, 2013
This is version 168 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.