Q15119 (PDK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
[Pyruvate dehydrogenase [lipoamide]] kinase isozyme 2, mitochondrial
EC=2.7.11.2

Alternative name(s):
Pyruvate dehydrogenase kinase isoform 2
Short name=PDH kinase 2
Short name=PDKII

Gene names

Name:	PDK2
Synonyms:	PDHK2

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	407 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	Serine/threonine kinase that plays a key role in the regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Inhibition of pyruvate dehydrogenase decreases glucose utilization and increases fat metabolism. Mediates cellular responses to insulin. Plays an important role in maintaining normal blood glucose levels and in metabolic adaptation to nutrient availability. Via its regulation of pyruvate dehydrogenase activity, plays an important role in maintaining normal blood pH and in preventing the accumulation of ketone bodies under starvation. Plays a role in the regulation of cell proliferation and in resistance to apoptosis under oxidative stress. Plays a role in p53/TP53-mediated apoptosis. Ref.1 Ref.6 Ref.10 Ref.11 Ref.12 Ref.13
Catalytic activity	ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate. Ref.1 Ref.8 Ref.9 Ref.11
Enzyme regulation	Activity is enhanced by binding to the pyruvate dehydrogenase subunit DLAT. Inhibited by ADP and pyruvate; these compounds interfere with DLAT binding and thereby inhibit kinase activity. Inhibited by dichloroacetate. Inhibited by AZD7545; this compound interferes with DLAT binding and thereby inhibits kinase activity. Ref.8 Ref.9 Ref.11
Subunit structure	Homodimer, and heterodimer with PDK1. Interacts with the pyruvate dehydrogenase complex subunit 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). Ref.7 Ref.8 Ref.9 Ref.11
Subcellular location	Mitochondrion matrix.
Tissue specificity	Expressed in many tissues, with the highest level in heart and skeletal muscle, intermediate levels in brain, kidney, pancreas and liver, and low levels in placenta and lung. Ref.1
Induction	Down-regulated by insulin. Up-regulated by reactive oxygen species and cigarette smoke extract. Ref.6 Ref.8 Ref.9 Ref.11 Ref.12
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
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to nutrient Inferred from sequence or structural similarity. Source: UniProtKB cellular response to reactive oxygen species Inferred from mutant phenotype Ref.12. Source: UniProtKB glucose homeostasis Inferred from sequence or structural similarity. Source: UniProtKB glucose metabolic process Traceable author statement Ref.1. Source: ProtInc insulin receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB intrinsic apoptotic signaling pathway by p53 class mediator Inferred from mutant phenotype Ref.13. Source: UniProtKB pyruvate metabolic process Traceable author statement. Source: Reactome regulation of acetyl-CoA biosynthetic process from pyruvate Inferred from sequence or structural similarity. Source: UniProtKB regulation of gluconeogenesis Inferred from sequence or structural similarity. Source: UniProtKB regulation of pH Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	mitochondrial pyruvate dehydrogenase complex Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from direct assay Ref.14. Source: UniProtKB protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW pyruvate dehydrogenase (acetyl-transferring) kinase activity Inferred from direct assay Ref.11. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15119-1)

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: Q15119-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-64: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – ?

Mitochondrion Potential

Chain

? – 407

[Pyruvate dehydrogenase [lipoamide]] kinase isozyme 2, mitochondrial

PRO_0000023440

Regions

Domain

135 – 364

230

Histidine kinase

Nucleotide binding

251 – 258

8

ATP

Nucleotide binding

309 – 310

2

ATP By similarity

Nucleotide binding

325 – 330

6

ATP

Sites

Binding site

290

1

ATP

Natural variations

Alternative sequence

1 – 64

64

Missing in isoform 2.

VSP_042549

Natural variant

342

1

G → R in a glioblastoma multiforme sample; somatic mutation. Ref.5 Ref.15
Corresponds to variant rs17855787 [ dbSNP | Ensembl ].

VAR_042296

Experimental info

Sequence conflict

80

1

S → T in AAC42010. Ref.1

Sequence conflict

407

1

S → T in AAC42010. Ref.1

Secondary structure

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407

Helix Strand Turn

Details...

Helix

16 – 23

8

Helix

33 – 40

8

Beta strand

41 – 43

3

Helix

46 – 68

23

Helix

73 – 77

5

Helix

79 – 96

18

Turn

97 – 100

4

Turn

106 – 109

4

Helix

110 – 123

14

Helix

126 – 141

16

Helix

145 – 175

31

Beta strand

177 – 179

3

Beta strand

191 – 196

6

Helix

197 – 216

20

Beta strand

222 – 228

7

Turn

230 – 233

4

Beta strand

237 – 240

4

Helix

242 – 262

21

Turn

263 – 266

4

Beta strand

273 – 279

7

Beta strand

281 – 290

10

Helix

297 – 303

7

Turn

306 – 309

4

Helix

329 – 339

11

Beta strand

343 – 349

7

Turn

350 – 352

3

Beta strand

353 – 363

11

Turn

364 – 366

3

Helix

376 – 379

4

Helix

380 – 382

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 6, 2002. Version 2. Checksum: 77DBA03EF922EF03	FASTA	407	46,154
	10 20 30 40 50 60 MRWVWALLKN ASLAGAPKYI EHFSKFSPSP LSMKQFLDFG SSNACEKTSF TFLRQELPVR 70 80 90 100 110 120 LANIMKEINL LPDRVLSTPS VQLVQSWYVQ SLLDIMEFLD KDPEDHRTLS QFTDALVTIR 130 140 150 160 170 180 NRHNDVVPTM AQGVLEYKDT YGDDPVSNQN IQYFLDRFYL SRISIRMLIN QHTLIFDGST 190 200 210 220 230 240 NPAHPKHIGS IDPNCNVSEV VKDAYDMAKL LCDKYYMASP DLEIQEINAA NSKQPIHMVY 250 260 270 280 290 300 VPSHLYHMLF ELFKNAMRAT VESHESSLIL PPIKVMVALG EEDLSIKMSD RGGGVPLRKI 310 320 330 340 350 360 ERLFSYMYST APTPQPGTGG TPLAGFGYGL PISRLYAKYF QGDLQLFSME GFGTDAVIYL 370 380 390 400 KALSTDSVER LPVYNKSAWR HYQTIQEAGD WCVPSTEPKN TSTYRVS
	Isoform 2 [UniParc]. Checksum: 27A955EC48BCA113	FASTA	343	38,864
	10 20 30 40 50 60 MKEINLLPDR VLSTPSVQLV QSWYVQSLLD IMEFLDKDPE DHRTLSQFTD ALVTIRNRHN 70 80 90 100 110 120 DVVPTMAQGV LEYKDTYGDD PVSNQNIQYF LDRFYLSRIS IRMLINQHTL IFDGSTNPAH 130 140 150 160 170 180 PKHIGSIDPN CNVSEVVKDA YDMAKLLCDK YYMASPDLEI QEINAANSKQ PIHMVYVPSH 190 200 210 220 230 240 LYHMLFELFK NAMRATVESH ESSLILPPIK VMVALGEEDL SIKMSDRGGG VPLRKIERLF 250 260 270 280 290 300 SYMYSTAPTP QPGTGGTPLA GFGYGLPISR LYAKYFQGDL QLFSMEGFGT DAVIYLKALS 310 320 330 340 TDSVERLPVY NKSAWRHYQT IQEAGDWCVP STEPKNTSTY RVS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Diversity of the pyruvate dehydrogenase kinase gene family in humans." Gudi R., Bowker-Kinley M.M., Kedishvili N.Y., Zhao Y., Popov K.M. J. Biol. Chem. 270:28989-28994(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY. Tissue: Liver.
[2]	"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 2). Tissue: Brain.
[3]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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), VARIANT ARG-342. Tissue: Lung, Prostate and Skin.
[6]	"Insulin downregulates pyruvate dehydrogenase kinase (PDK) mRNA: potential mechanism contributing to increased lipid oxidation in insulin-resistant subjects." Majer M., Popov K.M., Harris R.A., Bogardus C., Prochazka M. Mol. Genet. Metab. 65:181-186(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY INSULIN, FUNCTION.
[7]	"Facilitated interaction between the pyruvate dehydrogenase kinase isoform 2 and the dihydrolipoyl acetyltransferase." Hiromasa Y., Roche T.E. J. Biol. Chem. 278:33681-33693(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, INTERACTION WITH DLAT.
[8]	"Pyruvate dehydrogenase kinase isoform 2 activity limited and further inhibited by slowing down the rate of dissociation of ADP." Bao H., Kasten S.A., Yan X., Roche T.E. Biochemistry 43:13432-13441(2004) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, SUBUNIT, ENZYME REGULATION.
[9]	"Ligand-induced effects on pyruvate dehydrogenase kinase isoform 2." Hiromasa Y., Hu L., Roche T.E. J. Biol. Chem. 281:12568-12579(2006) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, INTERACTION WITH DLAT, SUBUNIT, ENZYME REGULATION.
[10]	"A mitochondria-K+ channel axis is suppressed in cancer and its normalization promotes apoptosis and inhibits cancer growth." Bonnet S., Archer S.L., Allalunis-Turner J., Haromy A., Beaulieu C., Thompson R., Lee C.T., Lopaschuk G.D., Puttagunta L., Bonnet S., Harry G., Hashimoto K., Porter C.J., Andrade M.A., Thebaud B., Michelakis E.D. Cancer Cell 11:37-51(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Pivotal role of the C-terminal DW-motif in mediating inhibition of pyruvate dehydrogenase kinase 2 by dichloroacetate." Li J., Kato M., Chuang D.T. J. Biol. Chem. 284:34458-34467(2009) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, FUNCTION, ENZYME REGULATION, INTERACTION WITH DLAT, SUBUNIT.
[12]	"Chronic CSE treatment induces the growth of normal oral keratinocytes via PDK2 upregulation, increased glycolysis and HIF1alpha stabilization." Sun W., Chang S.S., Fu Y., Liu Y., Califano J.A. PLoS ONE 6:E16207-E16207(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INDUCTION BY CIGARETTE SMOKE EXTRACT AND REACTIVE OXYGEN SPECIES.
[13]	"p53 negatively regulates transcription of the pyruvate dehydrogenase kinase Pdk2." Contractor T., Harris C.R. Cancer Res. 72:560-567(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"Regulatory roles of the N-terminal domain based on crystal structures of human pyruvate dehydrogenase kinase 2 containing physiological and synthetic ligands." Knoechel T.R., Tucker A.D., Robinson C.M., Phillips C., Taylor W., Bungay P.J., Kasten S.A., Roche T.E., Brown D.G. Biochemistry 45:402-415(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 16-407 IN COMPLEX WITH ATP AND THE INHIBITORS AZD7545; NOV3R; PFZ3 AND DICHLOROACETATE.
[15]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-342.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L42451 mRNA. Translation: AAC42010.1.
AK055119 mRNA. Translation: BAG51472.1.
AK290522 mRNA. Translation: BAF83211.1.
AC002401 Genomic DNA. No translation available.
CH471109 Genomic DNA. Translation: EAW94642.1.
CH471109 Genomic DNA. Translation: EAW94644.1.
BC005811 mRNA. Translation: AAH05811.1.
BC040478 mRNA. Translation: AAH40478.1.
BC063137 mRNA. Translation: AAH63137.1.

IPI

IPI00966638.
IPI01011342.

PIR

I70159.

RefSeq

NP_001186827.1. NM_001199898.1.
NP_001186828.1. NM_001199899.1.
NP_002602.2. NM_002611.4.

UniGene

Hs.256667.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2BTZ	X-ray	2.20	A	16-407	[»]
2BU2	X-ray	2.40	A	16-407	[»]
2BU5	X-ray	2.35	A	16-407	[»]
2BU6	X-ray	2.40	A	16-407	[»]
2BU7	X-ray	2.40	A	16-407	[»]
2BU8	X-ray	2.50	A	16-407	[»]

ProteinModelPortal

Q15119.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15119. 4 interactions.

MINT

MINT-1379180.

STRING

9606.ENSP00000007708.

Polymorphism databases

DMDM

21431820.

Proteomic databases

PaxDb

Q15119.

PRIDE

Q15119.

Protocols and materials databases

DNASU

5164.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000007708; ENSP00000007708; ENSG00000005882.
ENST00000503176; ENSP00000420927; ENSG00000005882.

GeneID

5164.

KEGG

hsa:5164.

UCSC

uc002iqb.3. human.

Organism-specific databases

CTD

5164.

GeneCards

GC17P048172.

HGNC

HGNC:8810. PDK2.

HPA

HPA008287.

MIM

602525. gene.

neXtProt

NX_Q15119.

PharmGKB

PA33155.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0642.

HOGENOM

HOG000164315.

HOVERGEN

HBG000511.

InParanoid

Q15119.

KO

K00898.

OMA

NLFSYMY.

PhylomeDB

Q15119.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

Q15119.

Bgee

Q15119.

CleanEx

HS_PDK2.

Genevestigator

Q15119.

GermOnline

ENSG00000005882. Homo sapiens.

Family and domain databases

Gene3D

1.20.140.20. 1 hit.
3.30.565.10. 1 hit.

InterPro

IPR018955. BCDHK/PDK_N.
IPR003594. HATPase_ATP-bd.
IPR005467. Sig_transdc_His_kinase_core.
[Graphical view]

Pfam

PF10436. BCDHK_Adom3. 1 hit.
PF02518. HATPase_c. 1 hit.
[Graphical view]

SMART

SM00387. HATPase_c. 1 hit.
[Graphical view]

SUPFAM

SSF55874. ATP_bd_ATPase. 1 hit.
SSF69012. BCDHK/PDK_N. 1 hit.

PROSITE

PS50109. HIS_KIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q15119.

ChEMBL

CHEMBL3861.

ChiTaRS

PDK2. human.

EvolutionaryTrace

Q15119.

GenomeRNAi

5164.

NextBio

19978.

SOURCE

Search...

Entry information

Entry name

PDK2_HUMAN

Accession

Primary (citable) accession number: Q15119
Secondary accession number(s): A8K3A7 , B3KNW0, Q6P515, Q9BS05

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	June 6, 2002
Last modified:	May 1, 2013
This is version 130 of the entry and version 2 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.