Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q15119 (PDK2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
[Pyruvate dehydrogenase (acetyl-transferring)] 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.12 Ref.13 Ref.14

Catalytic activity

ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate. Ref.1 Ref.8 Ref.9 Ref.12

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.12

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.12

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. Up-regulated by PPARD. Ref.6 Ref.8 Ref.9 Ref.11 Ref.12 Ref.13

Sequence similarities

Belongs to the PDK/BCKDK protein kinase family.

Contains 1 histidine kinase domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular metabolic process

Traceable author statement. Source: Reactome

cellular response to nutrient

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to reactive oxygen species

Inferred from mutant phenotype Ref.13. 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.14. Source: UniProtKB

protein phosphorylation

Inferred from direct assay Ref.12. Source: GOC

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 cellular ketone metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of gluconeogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of glucose metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of pH

Inferred from sequence or structural similarity. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrial pyruvate dehydrogenase complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionATP binding

Inferred from direct assay Ref.15. Source: UniProtKB

protein homodimerization activity

Inferred from physical interaction Ref.12. Source: UniProtKB

protein kinase activity

Traceable author statement PubMed 10748134Ref.1. Source: ProtInc

protein serine/threonine kinase activity

Inferred from electronic annotation. Source: UniProtKB-KW

pyruvate dehydrogenase (acetyl-transferring) kinase activity

Inferred from direct assay Ref.12. 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 407[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 2, mitochondrialPRO_0000023440

Regions

Domain135 – 364230Histidine kinase
Nucleotide binding251 – 2588ATP
Nucleotide binding309 – 3102ATP By similarity
Nucleotide binding325 – 3306ATP

Sites

Binding site2901ATP

Natural variations

Alternative sequence1 – 6464Missing in isoform 2.
VSP_042549
Natural variant3421G → R in a glioblastoma multiforme sample; somatic mutation. Ref.5 Ref.16
Corresponds to variant rs17855787 [ dbSNP | Ensembl ].
VAR_042296

Experimental info

Sequence conflict801S → T in AAC42010. Ref.1
Sequence conflict4071S → T in AAC42010. Ref.1

Secondary structure

................................................. 407
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 6, 2002. Version 2.
Checksum: 77DBA03EF922EF03

FASTA40746,154
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 27A955EC48BCA113
Show »

FASTA34338,864

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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]"Three members of the human pyruvate dehydrogenase kinase gene family are direct targets of the peroxisome proliferator-activated receptor beta/delta."
Degenhardt T., Saramaki A., Malinen M., Rieck M., Vaisanen S., Huotari A., Herzig K.H., Muller R., Carlberg C.
J. Mol. Biol. 372:341-355(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY PPARD.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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. expand/collapse author list , 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.
PIRI70159.
RefSeqNP_001186827.1. NM_001199898.1.
NP_001186828.1. NM_001199899.1.
NP_002602.2. NM_002611.4.
UniGeneHs.256667.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BTZX-ray2.20A16-407[»]
2BU2X-ray2.40A16-407[»]
2BU5X-ray2.35A16-407[»]
2BU6X-ray2.40A16-407[»]
2BU7X-ray2.40A16-407[»]
2BU8X-ray2.50A16-407[»]
4MP2X-ray1.75A9-407[»]
4MP7X-ray1.80A9-407[»]
4MPCX-ray1.70A9-407[»]
4MPEX-ray1.95A9-407[»]
4MPNX-ray1.75A9-407[»]
ProteinModelPortalQ15119.
SMRQ15119. Positions 16-383.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111190. 5 interactions.
IntActQ15119. 6 interactions.
MINTMINT-1379180.
STRING9606.ENSP00000007708.

Chemistry

BindingDBQ15119.
ChEMBLCHEMBL2096665.

Polymorphism databases

DMDM21431820.

Proteomic databases

PaxDbQ15119.
PRIDEQ15119.

Protocols and materials databases

DNASU5164.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000007708; ENSP00000007708; ENSG00000005882. [Q15119-2]
ENST00000503176; ENSP00000420927; ENSG00000005882. [Q15119-1]
GeneID5164.
KEGGhsa:5164.
UCSCuc002iqb.3. human. [Q15119-1]

Organism-specific databases

CTD5164.
GeneCardsGC17P048172.
HGNCHGNC:8810. PDK2.
HPAHPA008287.
MIM602525. gene.
neXtProtNX_Q15119.
PharmGKBPA33155.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0642.
HOGENOMHOG000164315.
HOVERGENHBG000511.
InParanoidQ15119.
KOK00898.
OMANLFSYMY.
OrthoDBEOG71VSSV.
PhylomeDBQ15119.
TreeFamTF314918.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SignaLinkQ15119.

Gene expression databases

ArrayExpressQ15119.
BgeeQ15119.
CleanExHS_PDK2.
GenevestigatorQ15119.

Family and domain databases

Gene3D1.20.140.20. 1 hit.
3.30.565.10. 1 hit.
InterProIPR018955. BCDHK/PDK_N.
IPR003594. HATPase_ATP-bd.
IPR005467. Sig_transdc_His_kinase_core.
[Graphical view]
PfamPF10436. BCDHK_Adom3. 1 hit.
PF02518. HATPase_c. 1 hit.
[Graphical view]
SMARTSM00387. HATPase_c. 1 hit.
[Graphical view]
SUPFAMSSF55874. SSF55874. 1 hit.
SSF69012. SSF69012. 1 hit.
PROSITEPS50109. HIS_KIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPDK2. human.
EvolutionaryTraceQ15119.
GeneWikiPDK2.
GenomeRNAi5164.
NextBio19978.
PROQ15119.
SOURCESearch...

Entry information

Entry namePDK2_HUMAN
AccessionPrimary (citable) accession number: Q15119
Secondary accession number(s): A8K3A7 expand/collapse secondary AC list , B3KNW0, Q6P515, Q9BS05
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: June 6, 2002
Last modified: April 16, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM