P11177 (ODPB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
Short name=PDHE1-B
EC=1.2.4.1

Gene names

Name:	PDHB
Synonyms:	PHE1B

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	359 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.18 Ref.19
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2. Ref.19
Cofactor	Thiamine pyrophosphate. Ref.17 Ref.19
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.15 Ref.18 Ref.19
Subcellular location	Mitochondrion matrix.
Involvement in disease	Pyruvate dehydrogenase E1-beta deficiency (PDHBD) [MIM:614111]: 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.20

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism Tricarboxylic acid cycle
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Transit peptide
Ligand	Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	acetyl-CoA biosynthetic process from pyruvate Inferred from direct assay Ref.19. Source: UniProtKB glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of acetyl-CoA biosynthetic process from pyruvate Traceable author statement. Source: Reactome tricarboxylic acid cycle Inferred from direct assay Ref.19. Source: UniProtKB
Cellular_component	mitochondrial matrix Traceable author statement. Source: Reactome pyruvate dehydrogenase complex Inferred from direct assay Ref.19. Source: UniProtKB
Molecular_function	pyruvate dehydrogenase (acetyl-transferring) activity Traceable author statement Ref.3. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P11177-1)

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: P11177-2)

The sequence of this isoform differs from the canonical sequence as follows:
     16-33: Missing.

Note: No experimental confirmation available.

Isoform 3 (identifier: P11177-3)

The sequence of this isoform differs from the canonical sequence as follows:
     135-152: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 30

30

Mitochondrion Ref.13 Ref.14

Chain

31 – 359

329

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

PRO_0000020457

Sites

Binding site

89

1

Thiamine pyrophosphate

Amino acid modifications

Modified residue

67

1

Phosphotyrosine By similarity

Natural variations

Alternative sequence

16 – 33

18

Missing in isoform 2.

VSP_012675

Alternative sequence

135 – 152

18

Missing in isoform 3.

VSP_043364

Natural variant

31

1

L → V. Ref.3 Ref.5

VAR_004967

Natural variant

132

1

Y → C in PDHBD. Ref.20
Corresponds to variant rs28935769 [ dbSNP | Ensembl ].

VAR_030954

Natural variant

344

1

P → S in PDHBD. Ref.20
Corresponds to variant rs28933391 [ dbSNP | Ensembl ].

VAR_021058

Experimental info

Sequence conflict

9 – 13

5

RRPLR → AETPS Ref.5

Sequence conflict

43

1

M → G AA sequence Ref.13

Sequence conflict

160

1

Q → G Ref.5

Sequence conflict

213 – 221

9

PPEAQSKDF → LRKLSQKIL Ref.5

Sequence conflict

213

1

P → L in AAA88097. Ref.4

Sequence conflict

213

1

P → L in BAA14123. Ref.4

Sequence conflict

310 – 312

3

MEG → NGS Ref.5

Secondary structure

1

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359

Helix Strand Turn

Details...

Beta strand

32 – 34

3

Helix

35 – 49

15

Beta strand

53 – 57

5

Turn

58 – 61

4

Turn

69 – 72

4

Helix

73 – 77

5

Turn

79 – 81

3

Beta strand

82 – 84

3

Helix

89 – 101

13

Beta strand

105 – 109

5

Helix

113 – 119

7

Helix

120 – 124

5

Turn

125 – 129

5

Helix

130 – 133

4

Turn

134 – 136

3

Beta strand

143 – 147

5

Helix

156 – 158

3

Helix

163 – 167

5

Beta strand

173 – 175

3

Helix

180 – 192

13

Beta strand

193 – 195

3

Beta strand

197 – 201

5

Turn

203 – 207

5

Beta strand

209 – 211

3

Helix

214 – 217

4

Beta strand

229 – 232

4

Beta strand

235 – 241

7

Helix

245 – 257

13

Turn

258 – 260

3

Beta strand

263 – 267

5

Beta strand

270 – 272

3

Helix

276 – 286

11

Beta strand

289 – 292

4

Helix

301 – 311

11

Helix

315 – 317

3

Beta strand

323 – 325

3

Beta strand

329 – 331

3

Helix

336 – 340

5

Helix

346 – 357

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 6, 2007. Version 3. Checksum: AB459B1259FBDBD3	FASTA	359	39,233
	10 20 30 40 50 60 MAAVSGLVRR PLREVSGLLK RRFHWTAPAA LQVTVRDAIN QGMDEELERD EKVFLLGEEV 70 80 90 100 110 120 AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI 130 140 150 160 170 180 DQVINSAAKT YYMSGGLQPV PIVFRGPNGA SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS 190 200 210 220 230 240 EDAKGLIKSA IRDNNPVVVL ENELMYGVPF EFPPEAQSKD FLIPIGKAKI ERQGTHITVV 250 260 270 280 290 300 SHSRPVGHCL EAAAVLSKEG VECEVINMRT IRPMDMETIE ASVMKTNHLV TVEGGWPQFG 310 320 330 340 350 VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII FAIKKTLNI
	Isoform 2 [UniParc]. Checksum: B4F137127819BB38	FASTA	341	37,200
	10 20 30 40 50 60 MAAVSGLVRR PLREVTVRDA INQGMDEELE RDEKVFLLGE EVAQYDGAYK VSRGLWKKYG 70 80 90 100 110 120 DKRIIDTPIS EMGFAGIAVG AAMAGLRPIC EFMTFNFSMQ AIDQVINSAA KTYYMSGGLQ 130 140 150 160 170 180 PVPIVFRGPN GASAGVAAQH SQCFAAWYGH CPGLKVVSPW NSEDAKGLIK SAIRDNNPVV 190 200 210 220 230 240 VLENELMYGV PFEFPPEAQS KDFLIPIGKA KIERQGTHIT VVSHSRPVGH CLEAAAVLSK 250 260 270 280 290 300 EGVECEVINM RTIRPMDMET IEASVMKTNH LVTVEGGWPQ FGVGAEICAR IMEGPAFNFL 310 320 330 340 DAPAVRVTGA DVPMPYAKIL EDNSIPQVKD IIFAIKKTLN I
	Isoform 3 [UniParc]. Checksum: 89F0A32D89507E9D	FASTA	341	37,514
	10 20 30 40 50 60 MAAVSGLVRR PLREVSGLLK RRFHWTAPAA LQVTVRDAIN QGMDEELERD EKVFLLGEEV 70 80 90 100 110 120 AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI 130 140 150 160 170 180 DQVINSAAKT YYMSGVAAQH SQCFAAWYGH CPGLKVVSPW NSEDAKGLIK SAIRDNNPVV 190 200 210 220 230 240 VLENELMYGV PFEFPPEAQS KDFLIPIGKA KIERQGTHIT VVSHSRPVGH CLEAAAVLSK 250 260 270 280 290 300 EGVECEVINM RTIRPMDMET IEASVMKTNH LVTVEGGWPQ FGVGAEICAR IMEGPAFNFL 310 320 330 340 DAPAVRVTGA DVPMPYAKIL EDNSIPQVKD IIFAIKKTLN I

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and cDNA sequence of the beta-subunit component of human pyruvate dehydrogenase complex." Ho L., Patel M.S. Gene 86:297-302(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Isolation, characterization and chromosomal localization of cDNA clones for the E1 beta subunit of the pyruvate dehydrogenase complex." Chun K., MacKay N., Willard H.F., Robinson B.H. Eur. J. Biochem. 194:587-592(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Characterization of two cDNA clones for pyruvate dehydrogenase E1 beta subunit and its regulation in tricarboxylic acid cycle-deficient fibroblast." Huh T.L., Casazza J.P., Huh J.W., Chi Y.T., Song B.J. J. Biol. Chem. 265:13320-13326(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT VAL-31.
[4]	"Molecular cloning and characterization of human pyruvate dehydrogenase beta subunit gene." Koike K., Urata Y., Koike M. Proc. Natl. Acad. Sci. U.S.A. 87:5594-5597(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[5]	"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], VARIANT VAL-31.
[6]	"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs." Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A. Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[7]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]	"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 1 AND 3). Tissue: Brain cortex.
[9]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]	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].
[11]	"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: Lung.
[12]	"Identification of a cDNA clone for the beta-subunit of the pyruvate dehydrogenase component of human pyruvate dehydrogenase complex." Ho L., Javed A.A., Pepin R.A., Thekkumkara T.J., Raefsky C., Mole J.E., Caliendo A.M., Kwon M.S., Kerr D.S., Patel M.S. Biochem. Biophys. Res. Commun. 150:904-908(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 23-69.
[13]	"The human myocardial two-dimensional gel protein database: update 1994." Corbett J.M., Wheeler C.H., Baker C.S., Yacoub M.H., Dunn M.J. Electrophoresis 15:1459-1465(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 31-43. Tissue: Heart.
[14]	"Isolation of tryptic fragment of antigen from mitochondrial inner membrane proteins reacting with antimitochondrial antibody in sera of patients with primary biliary cirrhosis." Muno D., Kominami E., Ishii H., Usui K., Saifuku K., Sakakibara Y., Namihisa T. Hepatology 11:16-23(1990) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 31-55.
[15]	"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.
[16]	"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].
[17]	"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) OF 32-359 IN COMPLEX WITH THIAMINE PYROPHOSPHATE, COFACTOR.
[18]	"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 (1.90 ANGSTROMS) OF 32-359, SUBUNIT, FUNCTION.
[19]	"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 31-359, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, FUNCTION.
[20]	"Mutations in the gene for the E1beta subunit: a novel cause of pyruvate dehydrogenase deficiency." Brown R.M., Head R.A., Boubriak I.I., Leonard J.V., Thomas N.H., Brown G.K. Hum. Genet. 115:123-127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PDHBD CYS-132 AND SER-344.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M34479 mRNA. Translation: AAA36428.1.
M19123 mRNA. Translation: AAA60052.1. Sequence problems.
M54788 mRNA. Translation: AAA60053.1.
M34055 mRNA. Translation: AAA60233.1.
M34056 mRNA. Translation: AAA60054.1.
D90086 Genomic DNA. Translation: BAA14123.1.
J03576 mRNA. Translation: AAA88097.1.
AL117618 mRNA. Translation: CAB56017.1.
CR541911 mRNA. Translation: CAG46709.1.
AK293153 mRNA. Translation: BAG56698.1.
AK313022 mRNA. Translation: BAG35857.1.
AC135507 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW65371.1.
BC000439 mRNA. Translation: AAH00439.1.
BC001924 mRNA. Translation: AAH01924.1.
X57778 mRNA. Translation: CAA40924.1.

IPI

IPI00003925.
IPI00549885.
IPI00946404.

PIR

DEHUPB. JU0145.

RefSeq

NP_000916.2. NM_000925.3.
NP_001166939.1. NM_001173468.1.

UniGene

Hs.161357.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NI4	X-ray	1.95	B/D	31-359	[»]
2OZL	X-ray	1.90	B/D	32-359	[»]
3EXE	X-ray	1.98	B/D/F/H	31-359	[»]
3EXF	X-ray	3.00	B/D/F/H	31-359	[»]
3EXG	X-ray	3.01	2/4/6/B/D/F/H/J/L/N/P/R/T/V/X/Z	31-359	[»]
3EXH	X-ray	2.44	B/D/F/H	31-359	[»]
3EXI	X-ray	2.20	B	31-359	[»]

ProteinModelPortal

P11177.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-37651N.

IntAct

P11177. 7 interactions.

MINT

MINT-3007546.

STRING

9606.ENSP00000307241.

PTM databases

PhosphoSite

P11177.

Polymorphism databases

DMDM

134044259.

2D gel databases

REPRODUCTION-2DPAGE

IPI00549885.

SWISS-2DPAGE

P11177.

UCD-2DPAGE

P11177.

Proteomic databases

PaxDb

P11177.

PRIDE

P11177.

Protocols and materials databases

DNASU

5162.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000302746; ENSP00000307241; ENSG00000168291.
ENST00000383714; ENSP00000373220; ENSG00000168291.
ENST00000485460; ENSP00000417267; ENSG00000168291.

GeneID

5162.

KEGG

hsa:5162.

UCSC

uc003dke.4. human.
uc003dkg.4. human.

Organism-specific databases

CTD

5162.

GeneCards

GC03M058388.

HGNC

HGNC:8808. PDHB.

HPA

HPA036744.

MIM

179060. gene.
614111. phenotype.

neXtProt

NX_P11177.

Orphanet

255138. Pyruvate dehydrogenase E1-beta deficiency.

PharmGKB

PA33152.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0022.

HOGENOM

HOG000281450.

HOVERGEN

HBG000917.

InParanoid

P11177.

KO

K00162.

OMA

QHSQDYS.

OrthoDB

EOG4CJVHD.

PhylomeDB

P11177.

Enzyme and pathway databases

BioCyc

MetaCyc:HS09727-MONOMER.

Reactome

REACT_111217. Metabolism.

SABIO-RK

P11177.

Gene expression databases

ArrayExpress

P11177.

Bgee

P11177.

CleanEx

HS_PDHB.

Genevestigator

P11177.

GermOnline

ENSG00000168291. Homo sapiens.

Family and domain databases

Gene3D

3.40.50.920. 1 hit.

InterPro

IPR027110. PDHB.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]

PANTHER

PTHR11624:SF11. PTHR11624:SF11. 1 hit.

Pfam

PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]

SMART

SM00861. Transket_pyr. 1 hit.
[Graphical view]

SUPFAM

SSF52922. Transketo_C_like. 1 hit.

ProtoNet

Search...

Other

ChEMBL

CHEMBL4882.

ChiTaRS

PDHB. human.

DrugBank

DB00157. NADH.
DB00119. Pyruvic acid.

EvolutionaryTrace

P11177.

GenomeRNAi

5162.

NextBio

19970.

SOURCE

Search...

Entry information

Entry name

ODPB_HUMAN

Accession

Primary (citable) accession number: P11177
Secondary accession number(s): B2R7L0 , B4DDD7, Q6FH45, Q9BQ27, Q9UFK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	March 6, 2007
Last modified:	May 1, 2013
This is version 158 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.