Reviewed, UniProtKB/Swiss-Prot Q8BFP9 (PDK1_MOUSE)

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	434 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity.
Catalytic activity	ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate.
Subcellular location	Mitochondrion matrix By similarity.
Sequence similarities	Belongs to the PDK/BCKDK protein kinase family. Contains 1 histidine kinase domain.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-histidine phosphorylation Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW pyruvate dehydrogenase (acetyl-transferring) kinase activity Inferred from electronic annotation. Source: EC two-component sensor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 26	26	Mitochondrion Potential
	Chain	27 – 434	408	[Pyruvate dehydrogenase [lipoamide]] kinase isozyme 1, mitochondrial		PRO_0000023438
Regions
	Domain	161 – 391	231	Histidine kinase
	Nucleotide binding	277 – 284	8	ATP By similarity
	Nucleotide binding	335 – 336	2	ATP By similarity
	Nucleotide binding	352 – 357	6	ATP By similarity
Sites
	Binding site	316	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8BFP9-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 97E797EB89696110	FASTA	434	48,926
	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 VPLSKIDRLF NYMYSTAPRP RVETSRAVPL AGFGYGLPIS 370 380 390 400 410 420 RLYAQYFQGD LKLYSLEGYG TDAVIYIKAL STESVERLPV YNKAAWKHYK ANHEADDWCV 430 PSREPKDMTT FRSS

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. , 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.

+

Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK046805 mRNA. Translation: BAC32879.1.
IPI	IPI00221407.
UniGene	Mm.34411
3D structure databases
SMR	Q8BFP9. Positions 41-421.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8BFP9.
PTM databases
PhosphoSite	Q8BFP9.
Proteomic databases
PRIDE	Q8BFP9.
Genome annotation databases
Ensembl	ENSMUST00000006669; ENSMUSP00000006669; ENSMUSG00000006494; Mus musculus. [Genome view]
Organism-specific databases
MGI	MGI:1926119. Pdk1.
Phylogenomic databases
HOGENOM	HBG382024.
HOVERGEN	Q8BFP9.
InParanoid	Q8BFP9.
PhylomeDB	Q8BFP9.
Enzyme and pathway databases
BRENDA	2.7.11.2. 244.
Gene expression databases
ArrayExpress	Q8BFP9.
Bgee	Q8BFP9.
CleanEx	MM_PDK1.
Genevestigator	Q8BFP9.
GermOnline	ENSMUSG00000006494. Mus musculus.
Family and domain databases
InterPro	IPR003594. ATPase-like_ATP-bd. IPR018955. BCDHK/PDK_mit. IPR005467. Sig_transdc_His_kinase_core. [Graphical view]
Gene3D	G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
Pfam	PF10436. BCDHK_Adom3. 1 hit. PF02518. HATPase_c. 1 hit. [Graphical view]
SMART	SM00387. HATPase_c. 1 hit. [Graphical view]
PROSITE	PS50109. HIS_KIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

Entry information

Entry name

PDK1_MOUSE

Accession

Primary (citable) accession number: Q8BFP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 1, 2003
Last modified:	January 19, 2010
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)