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Q9D051

- ODPB_MOUSE

UniProt

Q9D051 - ODPB_MOUSE

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Protein

Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

Gene

Pdhb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

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.By similarity

Catalytic activityi

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

Cofactori

Thiamine pyrophosphate.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei89 – 891Thiamine pyrophosphateBy similarity

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC
  2. pyruvate dehydrogenase activity Source: UniProtKB

GO - Biological processi

  1. acetyl-CoA biosynthetic process from pyruvate Source: UniProtKB
  2. glucose metabolic process Source: UniProtKB-KW
  3. tricarboxylic acid cycle Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism, Tricarboxylic acid cycle

Keywords - Ligandi

Pyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

ReactomeiREACT_226284. Regulation of pyruvate dehydrogenase (PDH) complex.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1915513. Pdhb.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. mitochondrion Source: MGI
  3. nucleus Source: Ensembl
  4. pyruvate dehydrogenase complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3030MitochondrionBy similarityAdd
BLAST
Chaini31 – 359329Pyruvate dehydrogenase E1 component subunit beta, mitochondrialPRO_0000020458Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei67 – 671Phosphotyrosine1 Publication
Modified residuei354 – 3541N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9D051.
PaxDbiQ9D051.
PRIDEiQ9D051.

2D gel databases

REPRODUCTION-2DPAGEQ9D051.
UCD-2DPAGEQ9D051.

PTM databases

PhosphoSiteiQ9D051.

Expressioni

Gene expression databases

BgeeiQ9D051.
CleanExiMM_PDHB.
GenevestigatoriQ9D051.

Interactioni

Subunit structurei

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 (By similarity).By similarity

Protein-protein interaction databases

BioGridi212768. 2 interactions.
IntActiQ9D051. 9 interactions.
MINTiMINT-1860720.

Structurei

3D structure databases

ProteinModelPortaliQ9D051.
SMRiQ9D051. Positions 30-359.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0022.
GeneTreeiENSGT00530000063423.
HOGENOMiHOG000281450.
HOVERGENiHBG000917.
InParanoidiQ9D051.
KOiK00162.
OMAiYASWYAH.
OrthoDBiEOG7KSX8S.
PhylomeDBiQ9D051.
TreeFamiTF105674.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProiIPR027110. PDHB.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view]
PANTHERiPTHR11624:SF56. PTHR11624:SF56. 1 hit.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9D051-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAVVAGLVRG PLRQASGLLK RRFHRSAPAA VQLTVREAIN QGMDEELERD
60 70 80 90 100
EKVFLLGEEV AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA
110 120 130 140 150
MAGLRPICEF MTFNFSMQAI DQVINSAAKT YYMSAGLQPV PIVFRGPNGA
160 170 180 190 200
SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS EDAKGLIKSA IRDNNPVVML
210 220 230 240 250
ENELMYGVAF ELPAEAQSKD FLIPIGKAKI ERQGTHITVV AHSRPVGHCL
260 270 280 290 300
EAAAVLSKEG IECEVINLRT IRPMDIEAIE ASVMKTNHLV TVEGGWPQFG
310 320 330 340 350
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKVLED NSVPQVKDII

FAVKKTLNI
Length:359
Mass (Da):38,937
Last modified:June 1, 2001 - v1
Checksum:iF5CD2A186DF58DDE
GO

Sequence cautioni

The sequence AAH02188.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti237 – 2371I → M in BAE38906. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK011810 mRNA. Translation: BAB27855.1.
AK153058 mRNA. Translation: BAE31684.1.
AK166631 mRNA. Translation: BAE38906.1.
BC002188 mRNA. Translation: AAH02188.1. Different initiation.
BC019512 mRNA. Translation: AAH19512.1.
BC094468 mRNA. Translation: AAH94468.1.
CCDSiCCDS36800.1.
PIRiPT0096.
RefSeqiNP_077183.1. NM_024221.3.
UniGeneiMm.301527.

Genome annotation databases

EnsembliENSMUST00000022268; ENSMUSP00000022268; ENSMUSG00000021748.
GeneIDi68263.
KEGGimmu:68263.
UCSCiuc007sev.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK011810 mRNA. Translation: BAB27855.1 .
AK153058 mRNA. Translation: BAE31684.1 .
AK166631 mRNA. Translation: BAE38906.1 .
BC002188 mRNA. Translation: AAH02188.1 . Different initiation.
BC019512 mRNA. Translation: AAH19512.1 .
BC094468 mRNA. Translation: AAH94468.1 .
CCDSi CCDS36800.1.
PIRi PT0096.
RefSeqi NP_077183.1. NM_024221.3.
UniGenei Mm.301527.

3D structure databases

ProteinModelPortali Q9D051.
SMRi Q9D051. Positions 30-359.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 212768. 2 interactions.
IntActi Q9D051. 9 interactions.
MINTi MINT-1860720.

PTM databases

PhosphoSitei Q9D051.

2D gel databases

REPRODUCTION-2DPAGE Q9D051.
UCD-2DPAGE Q9D051.

Proteomic databases

MaxQBi Q9D051.
PaxDbi Q9D051.
PRIDEi Q9D051.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022268 ; ENSMUSP00000022268 ; ENSMUSG00000021748 .
GeneIDi 68263.
KEGGi mmu:68263.
UCSCi uc007sev.1. mouse.

Organism-specific databases

CTDi 5162.
MGIi MGI:1915513. Pdhb.

Phylogenomic databases

eggNOGi COG0022.
GeneTreei ENSGT00530000063423.
HOGENOMi HOG000281450.
HOVERGENi HBG000917.
InParanoidi Q9D051.
KOi K00162.
OMAi YASWYAH.
OrthoDBi EOG7KSX8S.
PhylomeDBi Q9D051.
TreeFami TF105674.

Enzyme and pathway databases

Reactomei REACT_226284. Regulation of pyruvate dehydrogenase (PDH) complex.

Miscellaneous databases

ChiTaRSi PDHB. mouse.
NextBioi 326854.
PROi Q9D051.
SOURCEi Search...

Gene expression databases

Bgeei Q9D051.
CleanExi MM_PDHB.
Genevestigatori Q9D051.

Family and domain databases

Gene3Di 3.40.50.920. 1 hit.
3.40.50.970. 1 hit.
InterProi IPR027110. PDHB.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005475. Transketolase-like_Pyr-bd.
IPR005476. Transketolase_C.
[Graphical view ]
PANTHERi PTHR11624:SF56. PTHR11624:SF56. 1 hit.
Pfami PF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
[Graphical view ]
SMARTi SM00861. Transket_pyr. 1 hit.
[Graphical view ]
SUPFAMi SSF52518. SSF52518. 1 hit.
SSF52922. SSF52922. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow and Embryo.
  2. "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].
    Strain: FVB/N-3.
    Tissue: Liver and Mammary tumor.
  3. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 309-324, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  4. "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
    Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
    J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  5. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiODPB_MOUSE
AccessioniPrimary (citable) accession number: Q9D051
Secondary accession number(s): Q3TL86, Q505N8, Q99LW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

External Data

Dasty 3