PDHB

Functionⁱ

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.2 Publications

Catalytic activityⁱ

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO₂.1 Publication

Cofactorⁱ

thiamine diphosphate2 Publications

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Binding siteⁱ	89	Thiamine pyrophosphate1 Publication		1
Siteⁱ	319	Important for interaction with DLAT1 Publication		1

GO - Molecular functionⁱ

pyruvate dehydrogenase (acetyl-transferring) activity
Source: ProtInc
Traceable author statementⁱ
- 2376596
pyruvate dehydrogenase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 19081061

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

acetyl-CoA biosynthetic process from pyruvate
Source: UniProtKB
Inferred from direct assayⁱ
- 19081061
glucose metabolic process Source: UniProtKB-KW
mitochondrial acetyl-CoA biosynthetic process from pyruvate
Source: MGI
Inferred by curatorⁱ
- 18164639
tricarboxylic acid cycle
Source: UniProtKB
Inferred from direct assayⁱ
- 19081061

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Oxidoreductase
Biological process	Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle
Ligand	Pyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS09727-MONOMER
Reactomeⁱ	R-HSA-204174 Regulation of pyruvate dehydrogenase (PDH) complex R-HSA-389661 Glyoxylate metabolism and glycine degradation R-HSA-5362517 Signaling by Retinoic Acid R-HSA-70268 Pyruvate metabolism
SABIO-RKⁱ	P11177

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Pyruvate dehydrogenase E1 component subunit beta, mitochondrial (EC:1.2.4.1) Short name: PDHE1-B
Gene namesⁱ	Name:PDHB Synonyms:PHE1B
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 3

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000168291.12
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:8808 PDHB
MIMⁱ	179060 gene
neXtProtⁱ	NX_P11177

Keywords - Cellular componentⁱ

Mitochondrion

Pathology & Biotechⁱ

Involvement in diseaseⁱ

Pyruvate dehydrogenase E1-beta deficiency (PDHBD)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_030954	132	Y → C in PDHBD. 1 PublicationCorresponds to variant dbSNP:rs28935769EnsemblClinVar.		1
Natural variantⁱVAR_021058	344	P → S in PDHBD. 1 PublicationCorresponds to variant dbSNP:rs28933391EnsemblClinVar.		1

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	259	E → A or Q: Does not affect interaction with DLAT. 1 Publication	1
Mutagenesisⁱ	262	E → A or Q: Does not affect interaction with DLAT. 1 Publication	1
Mutagenesisⁱ	264	E → A or Q: Does not affect interaction with DLAT. 1 Publication	1
Mutagenesisⁱ	319	D → A: Inhibits interaction with DLAT. Does not affect pyruvate decarboxylase activity. Loss of multienzyme pyruvate dehydrogenase complex activity. 1 Publication	1
Mutagenesisⁱ	319	D → N: Reduces interaction with DLAT. Reduces multienzyme pyruvate dehydrogenase complex activity. Does not affect pyruvate decarboxylase activity. 1 Publication	1
Mutagenesisⁱ	359	I → A: Reduces pyruvate decarboxylase and multienzyme pyruvate dehydrogenase complex activity. Does not affect interaction with DLAT. 1 Publication	1
Mutagenesisⁱ	359	Missing : Reduces pyruvate decarboxylase and multienzyme pyruvate dehydrogenase complex activity. Does not affect interaction with DLAT. 1 Publication	1

Keywords - Diseaseⁱ

Disease mutation

Organism-specific databases

DisGeNET More...DisGeNETⁱ	5162
MalaCards human disease database More...MalaCardsⁱ	PDHB
MIMⁱ	614111 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000168291
Orphanetⁱ	255138 Pyruvate dehydrogenase E1-beta deficiency
PharmGKBⁱ	PA33152

Chemistry databases

Drug and drug target database More...DrugBankⁱ	DB00157 NADH DB00119 Pyruvic acid

DrugBankⁱ

DB00157 NADH
DB00119 Pyruvic acid

Polymorphism and mutation databases

BioMutaⁱ	PDHB
DMDMⁱ	134044259

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transit peptideⁱ	1 – 30	Mitochondrion2 PublicationsAdd BLAST		30
ChainⁱPRO_0000020457	31 – 359	Pyruvate dehydrogenase E1 component subunit beta, mitochondrialAdd BLAST		329

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	67	PhosphotyrosineBy similarity		1
Modified residueⁱ	354	N6-acetyllysineBy similarity		1

Keywords - PTMⁱ

Acetylation, Phosphoprotein

Proteomic databases

EPDⁱ	P11177
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	P11177
PaxDbⁱ	P11177
PeptideAtlas More...PeptideAtlasⁱ	P11177
PRIDEⁱ	P11177
ProteomicsDBⁱ	52715 52716 [P11177-2] 52717 [P11177-3]
TopDownProteomicsⁱ	P11177-1 [P11177-1]

2D gel databases

REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEⁱ	IPI00549885
SWISS-2DPAGEⁱ	P11177
UCD-2DPAGEⁱ	P11177

PTM databases

iPTMnetⁱ	P11177
PhosphoSitePlusⁱ	P11177
SwissPalmⁱ	P11177

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000168291 Expressed in 237 organ(s), highest expression level in myocardium
CleanExⁱ	HS_PDHB
ExpressionAtlasⁱ	P11177 baseline and differential
Genevisibleⁱ	P11177 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB033794 HPA036744 HPA036745

HPAⁱ

CAB033794
HPA036744
HPA036745

Interactionⁱ

Subunit structureⁱ

Heterotetramer of two PDHA1 and two PDHB subunits (PubMed:12651851, PubMed:17474719, PubMed:19081061). 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) (PubMed:14638692). These subunits are bound to an inner core composed of about 48 DLAT and 12 PDHX molecules (PubMed:14638692). Interacts with DLAT (PubMed:20160912).5 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
DLAT	P10515	7	EBI-1035872,EBI-2959723
PDHA1	P08559	6	EBI-1035872,EBI-715747

Protein-protein interaction databases

BioGridⁱ	111188, 73 interactors
ComplexPortalⁱ	CPX-376 Pyruvate dehydrogenase E1 heterotetramer
Database of interacting proteins More...DIPⁱ	DIP-37651N
IntActⁱ	P11177, 33 interactors
Molecular INTeraction database More...MINTⁱ	P11177
STRINGⁱ	9606.ENSP00000307241

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	32 – 34	Combined sources	3
Helixⁱ	35 – 49	Combined sources	15
Beta strandⁱ	53 – 57	Combined sources	5
Turnⁱ	58 – 61	Combined sources	4
Turnⁱ	69 – 72	Combined sources	4
Helixⁱ	73 – 77	Combined sources	5
Turnⁱ	79 – 81	Combined sources	3
Beta strandⁱ	82 – 84	Combined sources	3
Helixⁱ	89 – 101	Combined sources	13
Beta strandⁱ	105 – 109	Combined sources	5
Helixⁱ	113 – 119	Combined sources	7
Helixⁱ	120 – 124	Combined sources	5
Turnⁱ	125 – 129	Combined sources	5
Helixⁱ	130 – 133	Combined sources	4
Turnⁱ	134 – 136	Combined sources	3
Beta strandⁱ	143 – 147	Combined sources	5
Helixⁱ	156 – 158	Combined sources	3
Helixⁱ	163 – 167	Combined sources	5
Beta strandⁱ	173 – 175	Combined sources	3
Helixⁱ	180 – 192	Combined sources	13
Beta strandⁱ	193 – 195	Combined sources	3
Beta strandⁱ	197 – 201	Combined sources	5
Turnⁱ	203 – 207	Combined sources	5
Beta strandⁱ	209 – 211	Combined sources	3
Helixⁱ	214 – 217	Combined sources	4
Beta strandⁱ	229 – 232	Combined sources	4
Beta strandⁱ	235 – 241	Combined sources	7
Helixⁱ	245 – 257	Combined sources	13
Turnⁱ	258 – 260	Combined sources	3
Beta strandⁱ	263 – 267	Combined sources	5
Beta strandⁱ	270 – 272	Combined sources	3
Helixⁱ	276 – 286	Combined sources	11
Beta strandⁱ	289 – 292	Combined sources	4
Helixⁱ	301 – 311	Combined sources	11
Helixⁱ	315 – 317	Combined sources	3
Beta strandⁱ	323 – 325	Combined sources	3
Beta strandⁱ	329 – 331	Combined sources	3
Helixⁱ	336 – 340	Combined sources	5
Helixⁱ	346 – 357	Combined sources	12

Show more details

3D structure databases

ProteinModelPortalⁱ	P11177
SMRⁱ	P11177
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P11177

EvolutionaryTraceⁱ

P11177

Family & Domainsⁱ

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

eggNOGⁱ	KOG0524 Eukaryota COG0022 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00530000063423
HOGENOMⁱ	HOG000281450
HOVERGENⁱ	HBG000917
InParanoidⁱ	P11177
KEGG Orthology (KO) More...KOⁱ	K00162
OMAⁱ	SRMRHHC
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0D37
PhylomeDBⁱ	P11177
TreeFamⁱ	TF105674

Family and domain databases

Gene3Dⁱ	3.40.50.920, 1 hit
InterProⁱ	View protein in InterPro IPR029061 THDP-binding IPR009014 Transketo_C/PFOR_II IPR005475 Transketolase-like_Pyr-bd IPR033248 Transketolase_C
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF02779 Transket_pyr, 1 hit PF02780 Transketolase_C, 1 hit
SMARTⁱ	View protein in SMART SM00861 Transket_pyr, 1 hit
SUPFAMⁱ	SSF52518 SSF52518, 1 hit SSF52922 SSF52922, 1 hit

Sequences (3+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: P11177-1) [UniParc]FASTA Add to basket

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.

« Hide

        10         20         30         40         50
MAAVSGLVRR PLREVSGLLK RRFHWTAPAA LQVTVRDAIN QGMDEELERD 
        60         70         80         90        100
EKVFLLGEEV AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA 
       110        120        130        140        150
MAGLRPICEF MTFNFSMQAI DQVINSAAKT YYMSGGLQPV PIVFRGPNGA 
       160        170        180        190        200
SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS EDAKGLIKSA IRDNNPVVVL 
       210        220        230        240        250
ENELMYGVPF EFPPEAQSKD FLIPIGKAKI ERQGTHITVV SHSRPVGHCL 
       260        270        280        290        300
EAAAVLSKEG VECEVINMRT IRPMDMETIE ASVMKTNHLV TVEGGWPQFG 
       310        320        330        340        350
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII 

FAIKKTLNI

Length:359

Mass (Da):39,233

Last modified:March 6, 2007 - v3

Checksum:ⁱAB459B1259FBDBD3

GO

Isoform 2 (identifier: P11177-2) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MAAVSGLVRR PLREVTVRDA INQGMDEELE RDEKVFLLGE EVAQYDGAYK 
        60         70         80         90        100
VSRGLWKKYG DKRIIDTPIS EMGFAGIAVG AAMAGLRPIC EFMTFNFSMQ 
       110        120        130        140        150
AIDQVINSAA KTYYMSGGLQ PVPIVFRGPN GASAGVAAQH SQCFAAWYGH 
       160        170        180        190        200
CPGLKVVSPW NSEDAKGLIK SAIRDNNPVV VLENELMYGV PFEFPPEAQS 
       210        220        230        240        250
KDFLIPIGKA KIERQGTHIT VVSHSRPVGH CLEAAAVLSK EGVECEVINM 
       260        270        280        290        300
RTIRPMDMET IEASVMKTNH LVTVEGGWPQ FGVGAEICAR IMEGPAFNFL 
       310        320        330        340 
DAPAVRVTGA DVPMPYAKIL EDNSIPQVKD IIFAIKKTLN I

Note: No experimental confirmation available.

Show »

Length:341

Mass (Da):37,200

Checksum:ⁱB4F137127819BB38

GO

Isoform 3 (identifier: P11177-3) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MAAVSGLVRR PLREVSGLLK RRFHWTAPAA LQVTVRDAIN QGMDEELERD 
        60         70         80         90        100
EKVFLLGEEV AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA 
       110        120        130        140        150
MAGLRPICEF MTFNFSMQAI DQVINSAAKT YYMSGVAAQH SQCFAAWYGH 
       160        170        180        190        200
CPGLKVVSPW NSEDAKGLIK SAIRDNNPVV VLENELMYGV PFEFPPEAQS 
       210        220        230        240        250
KDFLIPIGKA KIERQGTHIT VVSHSRPVGH CLEAAAVLSK EGVECEVINM 
       260        270        280        290        300
RTIRPMDMET IEASVMKTNH LVTVEGGWPQ FGVGAEICAR IMEGPAFNFL 
       310        320        330        340 
DAPAVRVTGA DVPMPYAKIL EDNSIPQVKD IIFAIKKTLN I

Note: No experimental confirmation available.

Show »

Length:341

Mass (Da):37,514

Checksum:ⁱ89F0A32D89507E9D

GO

Computationally mapped potential isoform sequencesⁱ

There are 2 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

C9J634	C9J634_HUMAN	Pyruvate dehydrogenase E1 component... Pyruvate dehydrogenase E1 component subunit beta, mitochondrial	PDHB	350	Annotation score:
F8WF02	F8WF02_HUMAN	Pyruvate dehydrogenase E1 component... Pyruvate dehydrogenase E1 component subunit beta, mitochondrial	PDHB	251	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	9 – 13	RRPLR → AETPS (PubMed:3422424).Curated	5
Sequence conflictⁱ	43	M → G AA sequence (PubMed:7895732).Curated	1
Sequence conflictⁱ	160	Q → G (PubMed:3422424).Curated	1
Sequence conflictⁱ	213 – 221	PPEAQSKDF → LRKLSQKIL (PubMed:3422424).Curated	9
Sequence conflictⁱ	213	P → L in AAA88097 (PubMed:2377599).Curated	1
Sequence conflictⁱ	213	P → L in BAA14123 (PubMed:2377599).Curated	1
Sequence conflictⁱ	310 – 312	MEG → NGS (PubMed:3422424).Curated	3

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_004967	31	L → V2 Publications	1
Natural variantⁱVAR_030954	132	Y → C in PDHBD. 1 PublicationCorresponds to variant dbSNP:rs28935769EnsemblClinVar.	1
Natural variantⁱVAR_021058	344	P → S in PDHBD. 1 PublicationCorresponds to variant dbSNP:rs28933391EnsemblClinVar.	1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_012675	16 – 33	Missing in isoform 2. 1 PublicationAdd BLAST		18
Alternative sequenceⁱVSP_043364	135 – 152	Missing in isoform 3. 1 PublicationAdd BLAST		18

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS2890.1 [P11177-1] CCDS54602.1 [P11177-3] CCDS82795.1 [P11177-2]
PIRⁱ	JU0145 DEHUPB
NCBI Reference Sequences More...RefSeqⁱ	NP_000916.2, NM_000925.3 [P11177-1] NP_001166939.1, NM_001173468.1 [P11177-3] NP_001302465.1, NM_001315536.1 [P11177-2]
UniGeneⁱ	Hs.161357

Genome annotation databases

Ensemblⁱ	ENST00000302746; ENSP00000307241; ENSG00000168291 [P11177-1] ENST00000383714; ENSP00000373220; ENSG00000168291 [P11177-2] ENST00000485460; ENSP00000417267; ENSG00000168291 [P11177-3]
GeneIDⁱ	5162
KEGGⁱ	hsa:5162
UCSC genome browser More...UCSCⁱ	uc003dkf.4 human [P11177-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P11177	PDHB isoform 2		PANTR		359	UniRef100_P11177
Uncharacterized protein		CERAT		359
Uncharacterized protein		CHLSB		359
Pyruvate dehydrogenase E1 beta subunit		GORGO		359
Uncharacterized protein		MACFA		359
+2
P11177-2	PDHB isoform 2		PONAB		341	UniRef100_A0A2J8T1E9
PDHB isoform 1		PANTR		341
Pyruvate dehydrogenase E1 beta subunit		GORGO		341
P11177-3	PDHB isoform 8		PANTR		341	UniRef100_A0A2I3RWR8
Uncharacterized protein		CERAT		341
Uncharacterized protein		MANLE		341
Pyruvate dehydrogenase E1 beta subunit		GORGO		341
Uncharacterized protein		MACFA		341
+1

Protein	Similar proteins		Species	Score	Length	Source
P11177	Pyruvate dehydrogenase E1 component subunit beta, mitochondrial		RAT		359	UniRef90_P11177
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial		BOVIN		359
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial		MOUSE		359
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial		PONAB		359
PDHB isoform 2		PANTR		359
+161

Protein	Similar proteins		Species	Score	Length	Source
P11177	Pyruvate dehydrogenase E1 component subunit beta, mitochondrial		PONAB		359	UniRef50_P11177
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial		RAT		359
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial		MOUSE		359
Pyruvate dehydrogenase E1 component subunit beta, mitochondrial		BOVIN		359
Pyruvate dehydrogenase E1 component subunit beta-1, mitochondrial		ARATH		363
+1926

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	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
CCDSⁱ	CCDS2890.1 [P11177-1] CCDS54602.1 [P11177-3] CCDS82795.1 [P11177-2]
PIRⁱ	JU0145 DEHUPB
RefSeqⁱ	NP_000916.2, NM_000925.3 [P11177-1] NP_001166939.1, NM_001173468.1 [P11177-3] NP_001302465.1, NM_001315536.1 [P11177-2]
UniGeneⁱ	Hs.161357

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB 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	[»]
	6CER	X-ray	2.69	B/D/F/H	31-359	[»]
	6CFO	X-ray	2.70	B/D	31-359	[»]
ProteinModelPortalⁱ	P11177
SMRⁱ	P11177
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	111188, 73 interactors
ComplexPortalⁱ	CPX-376 Pyruvate dehydrogenase E1 heterotetramer
DIPⁱ	DIP-37651N
IntActⁱ	P11177, 33 interactors
MINTⁱ	P11177
STRINGⁱ	9606.ENSP00000307241

Chemistry databases

DrugBankⁱ	DB00157 NADH DB00119 Pyruvic acid

DrugBankⁱ

DB00157 NADH
DB00119 Pyruvic acid

PTM databases

iPTMnetⁱ	P11177
PhosphoSitePlusⁱ	P11177
SwissPalmⁱ	P11177

Polymorphism and mutation databases

BioMutaⁱ	PDHB
DMDMⁱ	134044259

2D gel databases

REPRODUCTION-2DPAGEⁱ	IPI00549885
SWISS-2DPAGEⁱ	P11177
UCD-2DPAGEⁱ	P11177

Proteomic databases

EPDⁱ	P11177
MaxQBⁱ	P11177
PaxDbⁱ	P11177
PeptideAtlasⁱ	P11177
PRIDEⁱ	P11177
ProteomicsDBⁱ	52715 52716 [P11177-2] 52717 [P11177-3]
TopDownProteomicsⁱ	P11177-1 [P11177-1]

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	5162
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000302746; ENSP00000307241; ENSG00000168291 [P11177-1] ENST00000383714; ENSP00000373220; ENSG00000168291 [P11177-2] ENST00000485460; ENSP00000417267; ENSG00000168291 [P11177-3]
GeneIDⁱ	5162
KEGGⁱ	hsa:5162
UCSCⁱ	uc003dkf.4 human [P11177-1]

Organism-specific databases

CTDⁱ	5162
DisGeNETⁱ	5162
EuPathDBⁱ	HostDB:ENSG00000168291.12
GeneCardsⁱ	PDHB
HGNCⁱ	HGNC:8808 PDHB
HPAⁱ	CAB033794 HPA036744 HPA036745
MalaCardsⁱ	PDHB
MIMⁱ	179060 gene 614111 phenotype
neXtProtⁱ	NX_P11177
OpenTargetsⁱ	ENSG00000168291
Orphanetⁱ	255138 Pyruvate dehydrogenase E1-beta deficiency
PharmGKBⁱ	PA33152
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG0524 Eukaryota COG0022 LUCA
GeneTreeⁱ	ENSGT00530000063423
HOGENOMⁱ	HOG000281450
HOVERGENⁱ	HBG000917
InParanoidⁱ	P11177
KOⁱ	K00162
OMAⁱ	SRMRHHC
OrthoDBⁱ	EOG091G0D37
PhylomeDBⁱ	P11177
TreeFamⁱ	TF105674

Enzyme and pathway databases

BioCycⁱ	MetaCyc:HS09727-MONOMER
Reactomeⁱ	R-HSA-204174 Regulation of pyruvate dehydrogenase (PDH) complex R-HSA-389661 Glyoxylate metabolism and glycine degradation R-HSA-5362517 Signaling by Retinoic Acid R-HSA-70268 Pyruvate metabolism
SABIO-RKⁱ	P11177

Miscellaneous databases

ChiTaRSⁱ	PDHB human
EvolutionaryTraceⁱ	P11177
GeneWikiⁱ	Pyruvate_dehydrogenase_(lipoamide)_beta
GenomeRNAiⁱ	5162
Protein Ontology More...PROⁱ	PR:P11177
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000168291 Expressed in 237 organ(s), highest expression level in myocardium
CleanExⁱ	HS_PDHB
ExpressionAtlasⁱ	P11177 baseline and differential
Genevisibleⁱ	P11177 HS

Family and domain databases

Gene3Dⁱ	3.40.50.920, 1 hit
InterProⁱ	View protein in InterPro IPR029061 THDP-binding IPR009014 Transketo_C/PFOR_II IPR005475 Transketolase-like_Pyr-bd IPR033248 Transketolase_C
Pfamⁱ	View protein in Pfam PF02779 Transket_pyr, 1 hit PF02780 Transketolase_C, 1 hit
SMARTⁱ	View protein in SMART SM00861 Transket_pyr, 1 hit
SUPFAMⁱ	SSF52518 SSF52518, 1 hit SSF52922 SSF52922, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ODPB_HUMAN
Accessionⁱ	P11177Primary (citable) accession number: P11177 Secondary accession number(s): B2R7L0 , B4DDD7, Q6FH45, Q9BQ27, Q9UFK3
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
	Last sequence update:	March 6, 2007
	Last modified:	November 7, 2018
	This is version 215 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

Human chromosome 3
Human chromosome 3: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

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UniProtKB - P11177 (ODPB_HUMAN)

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Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

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Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

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Keywords - Domainⁱ

Keywords - Coding sequence diversityⁱ

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Keywords - Technical termⁱ