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Q8BFP9 (PDK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
[Pyruvate dehydrogenase [lipoamide]] kinase isozyme 1, mitochondrial
EC=2.7.11.2
Alternative name(s):
Pyruvate dehydrogenase kinase isoform 1
Gene names
Name:Pdk1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length434 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the E1 alpha subunit, thus contributing to the regulation of glucose metabolism. Phosphorylates PRKCD and PRKCZ kinases By similarity.

Catalytic activity

ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate.

Subunit structure

Interacts (via N-terminus region) with PRKCD and PRKCZ. Interacts with PDK1 (via C-terminal kinase domain); the interaction stimulates PDK1 kinase activity that induces an increase of the PI(3,4,5)P-3-dependent 'Thr-308' and 'Ser-473' kinase activity of AKT1. Interacts with PtdIns(3,4,5)P3 By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Post-translational modification

Autophosphorylated; autophosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2 By similarity.

Sequence similarities

Belongs to the PDK/BCKDK protein kinase family.

Contains 1 histidine kinase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2626Mitochondrion Potential
Chain27 – 434408[Pyruvate dehydrogenase [lipoamide]] kinase isozyme 1, mitochondrial
PRO_0000023438

Regions

Domain161 – 391231Histidine kinase
Nucleotide binding277 – 2848ATP By similarity
Nucleotide binding335 – 3362ATP By similarity
Nucleotide binding352 – 3576ATP By similarity

Sites

Binding site3161ATP By similarity

Experimental info

Sequence conflict3241R → S in BAC32879. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8BFP9 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 8A514C863E751040

FASTA43448,995
        10         20         30         40         50         60 
MRLARLLRGG TSVRPLCAVP CASRSLASAS ASGSGPASEL GVPGQVDFYA RFSPSPLSMK 

        70         80         90        100        110        120 
QFLDFGSVNA CEKTSFMFLR QELPVRLANI MKEISLLPDN LLRTPSVQLV QSWYIQSLQE 

       130        140        150        160        170        180 
LLDFKDKSAE DAKTIYEFTD TVIRIRNRHN DVIPTMAQGV TEYKESFGVD PVTSQNVQYF 

       190        200        210        220        230        240 
LDRFYMSRIS IRMLLNQHSL LFGGKGSPSH RKHIGSINPN CDVVEVIKDG YENARRLCDL 

       250        260        270        280        290        300 
YYVNSPELEL EELNAKSPGQ TIQVVYVPSH LYHMVFELFK NAMRATMEHH ADKGVYPPIQ 

       310        320        330        340        350        360 
VHVTLGEEDL TVKMSDRGGG VPLRKIDRLF NYMYSTAPRP RVETSRAVPL AGFGYGLPIS 

       370        380        390        400        410        420 
RLYAQYFQGD LKLYSLEGYG TDAVIYIKAL STESVERLPV YNKAAWKHYK ANHEADDWCV 

       430 
PSREPKDMTT FRSS

« Hide

References

[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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Medulla oblongata and Thymus.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK046805 mRNA. Translation: BAC32879.1.
AK153649 mRNA. Translation: BAE32134.1.
AL928963 Genomic DNA. Translation: CAM26372.1.
CH466519 Genomic DNA. Translation: EDL27100.1.
CH466519 Genomic DNA. Translation: EDL27102.1.
CH466519 Genomic DNA. Translation: EDL27104.1.
IPIIPI00221407.
RefSeqNP_766253.2. NM_172665.4.
UniGeneMm.34411.

3D structure databases

ProteinModelPortalQ8BFP9.
SMRQ8BFP9. Positions 41-421.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8BFP9.

PTM databases

PhosphoSiteQ8BFP9.

Proteomic databases

PRIDEQ8BFP9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000006669; ENSMUSP00000006669; ENSMUSG00000006494.
GeneID228026.
KEGGmmu:228026.

Organism-specific databases

CTD5163.
MGIMGI:1926119. Pdk1.

Phylogenomic databases

HOGENOMHBG382024.
HOVERGENHBG000511.
InParanoidQ8BFP9.
OrthoDBEOG4THVT4.
PhylomeDBQ8BFP9.

Gene expression databases

ArrayExpressQ8BFP9.
BgeeQ8BFP9.
CleanExMM_PDK1.
GenevestigatorQ8BFP9.
GermOnlineENSMUSG00000006494. Mus musculus.

Family and domain databases

InterProIPR003594. ATPase-like_ATP-bd.
IPR018955. BCDHK/PDK_N.
IPR005467. Sig_transdc_His_kinase_core.
[Graphical view]
Gene3DG3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
G3DSA:1.20.140.20. BCDHK/PDK_N. 1 hit.
KOK12077.
PfamPF10436. BCDHK_Adom3. 1 hit.
PF02518. HATPase_c. 1 hit.
[Graphical view]
SMARTSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMSSF55874. ATP_bd_ATPase. 1 hit.
SSF69012. BCDHK/PDK_N. 1 hit.
PROSITEPS50109. HIS_KIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

SOURCESearch...

Entry information

Entry namePDK1_MOUSE
AccessionPrimary (citable) accession number: Q8BFP9
Secondary accession number(s): Q3U5E5
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: July 27, 2011
Last modified: January 25, 2012
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents