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Q15120 (PDK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. 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 3, mitochondrial

EC=2.7.11.2
Alternative name(s):
Pyruvate dehydrogenase kinase isoform 3
Gene names
Name:PDK3
Synonyms:PDHK3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length406 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Inhibits pyruvate dehydrogenase activity by phosphorylation of the E1 subunit PDHA1, and thereby regulates glucose metabolism and aerobic respiration. Can also phosphorylate PDHA2. Decreases glucose utilization and increases fat metabolism in response to prolonged fasting, and as adaptation to a high-fat diet. Plays a role in glucose homeostasis and in maintaining normal blood glucose levels in function of nutrient levels and under starvation. Plays a role in the generation of reactive oxygen species. Ref.5 Ref.6 Ref.8 Ref.10 Ref.13 Ref.14 Ref.16

Catalytic activity

ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate. Ref.5 Ref.6 Ref.8

Enzyme regulation

Activated by interaction with DLAT. Inhibited by AZD7545, dichloroacetate and radicicol. Ref.5 Ref.16

Subunit structure

Homodimer. 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.5 Ref.7 Ref.14 Ref.15 Ref.16

Subcellular location

Mitochondrion matrix.

Tissue specificity

Expressed in heart, skeletal muscle, spinal cord, as well as fetal and adult brain. Ref.18

Induction

Up-regulated in response to hypoxia. Up-regulated in response to fatty acids. Up-regulated by PPARD. Ref.5 Ref.9 Ref.10 Ref.11 Ref.16

Involvement in disease

Charcot-Marie-Tooth disease, X-linked dominant, 6 (CMTX6) [MIM:300905]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies characterized by severely reduced motor nerve conduction velocities (NCVs) (less than 38m/s) and segmental demyelination and remyelination, and primary peripheral axonal neuropathies characterized by normal or mildly reduced NCVs and chronic axonal degeneration and regeneration on nerve biopsy.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18

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
   DiseaseCharcot-Marie-Tooth disease
Disease mutation
Neurodegeneration
Neuropathy
   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 fatty acid

Inferred from mutant phenotype Ref.11. Source: UniProtKB

cellular response to glucose stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

glucose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

hypoxia-inducible factor-1alpha signaling pathway

Inferred from mutant phenotype Ref.10. Source: UniProtKB

peptidyl-serine phosphorylation

Inferred from direct assay Ref.6. Source: UniProtKB

peroxisome proliferator activated receptor signaling pathway

Inferred from mutant phenotype Ref.9. Source: UniProtKB

pyruvate metabolic process

Traceable author statement. Source: Reactome

regulation of acetyl-CoA biosynthetic process from pyruvate

Inferred from mutant phenotype Ref.13. Source: UniProtKB

regulation of glucose metabolic process

Inferred from mutant phenotype Ref.13. Source: UniProtKB

regulation of reactive oxygen species metabolic process

Inferred from mutant phenotype Ref.13. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionATP binding

Inferred from direct assay Ref.14. Source: UniProtKB

protein kinase activity

Inferred from direct assay Ref.14. Source: UniProtKB

protein serine/threonine kinase activity

Inferred from direct assay Ref.6. Source: UniProtKB

pyruvate dehydrogenase (acetyl-transferring) kinase activity

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15120-1)

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: Q15120-2)

The sequence of this isoform differs from the canonical sequence as follows:
     406-406: Q → QDKIKTNRTF
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – ?Mitochondrion Potential
Chain? – 406[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 3, mitochondrialPRO_0000023443

Regions

Domain131 – 362232Histidine kinase
Nucleotide binding247 – 2548ATP
Nucleotide binding306 – 3072ATP
Nucleotide binding323 – 3286ATP

Sites

Binding site2871ATP

Amino acid modifications

Modified residue2781N6-succinyllysine By similarity

Natural variations

Alternative sequence4061Q → QDKIKTNRTF in isoform 2.
VSP_043365
Natural variant1141K → T. Ref.18
Corresponds to variant rs146331370 [ dbSNP | Ensembl ].
VAR_070081
Natural variant1581R → H in CMTX6; gain of function; results in a 5-fold increase in kinase activity, decreased sensitivity to pyruvate inhibition, reduced affinity for nucleotides and increased affinity for pyruvate dehydrogenase complex component E2 (PDC-E2), leading to PDC hyperphosphorylation and increased inactivation. Ref.18
VAR_070082
Natural variant2191E → A in a head & neck squamous cell carcinoma sample; somatic mutation. Ref.17
VAR_042297
Natural variant3341Y → S. Ref.18
VAR_070083

Experimental info

Mutagenesis1201N → H: No effect on kinase activity; when associated with N-121. Ref.18
Mutagenesis1211D → N: No effect on kinase activity; when associated with H-120. Ref.18

Secondary structure

..................................................... 406
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: EF2415D3F9D8D61E

FASTA40646,939
        10         20         30         40         50         60 
MRLFRWLLKQ PVPKQIERYS RFSPSPLSIK QFLDFGRDNA CEKTSYMFLR KELPVRLANT 

        70         80         90        100        110        120 
MREVNLLPDN LLNRPSVGLV QSWYMQSFLE LLEYENKSPE DPQVLDNFLQ VLIKVRNRHN 

       130        140        150        160        170        180 
DVVPTMAQGV IEYKEKFGFD PFISTNIQYF LDRFYTNRIS FRMLINQHTL LFGGDTNPVH 

       190        200        210        220        230        240 
PKHIGSIDPT CNVADVVKDA YETAKMLCEQ YYLVAPELEV EEFNAKAPDK PIQVVYVPSH 

       250        260        270        280        290        300 
LFHMLFELFK NSMRATVELY EDRKEGYPAV KTLVTLGKED LSIKISDLGG GVPLRKIDRL 

       310        320        330        340        350        360 
FNYMYSTAPR PSLEPTRAAP LAGFGYGLPI SRLYARYFQG DLKLYSMEGV GTDAVIYLKA 

       370        380        390        400 
LSSESFERLP VFNKSAWRHY KTTPEADDWS NPSSEPRDAS KYKAKQ 

« Hide

Isoform 2 [UniParc].

Checksum: BDE814D88CE6A279
Show »

FASTA41548,043

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).
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] (ISOFORM 2).
Tissue: Testis.
[3]Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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).
Tissue: Skin.
[5]"Marked differences between two isoforms of human pyruvate dehydrogenase kinase."
Baker J.C., Yan X., Peng T., Kasten S., Roche T.E.
J. Biol. Chem. 275:15773-15781(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION, INTERACTION WITH DLAT, ENZYME REGULATION.
[6]"Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase."
Korotchkina L.G., Patel M.S.
J. Biol. Chem. 276:37223-37229(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION.
[7]"Interaction between the individual isoenzymes of pyruvate dehydrogenase kinase and the inner lipoyl-bearing domain of transacetylase component of pyruvate dehydrogenase complex."
Tuganova A., Boulatnikov I., Popov K.M.
Biochem. J. 366:129-136(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DLAT.
[8]"Characterization of testis-specific isoenzyme of human pyruvate dehydrogenase."
Korotchkina L.G., Sidhu S., Patel M.S.
J. Biol. Chem. 281:9688-9696(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, FUNCTION.
[9]"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.
[10]"Induction of pyruvate dehydrogenase kinase-3 by hypoxia-inducible factor-1 promotes metabolic switch and drug resistance."
Lu C.W., Lin S.C., Chen K.F., Lai Y.Y., Tsai S.J.
J. Biol. Chem. 283:28106-28114(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION.
[11]"Butyrate elicits a metabolic switch in human colon cancer cells by targeting the pyruvate dehydrogenase complex."
Blouin J.M., Penot G., Collinet M., Nacfer M., Forest C., Laurent-Puig P., Coumoul X., Barouki R., Benelli C., Bortoli S.
Int. J. Cancer 128:2591-2601(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Inactivation of the HIF-1alpha/PDK3 signaling axis drives melanoma toward mitochondrial oxidative metabolism and potentiates the therapeutic activity of pro-oxidants."
Kluza J., Corazao-Rozas P., Touil Y., Jendoubi M., Maire C., Guerreschi P., Jonneaux A., Ballot C., Balayssac S., Valable S., Corroyer-Dulmont A., Bernaudin M., Malet-Martino M., de Lassalle E.M., Maboudou P., Formstecher P., Polakowska R., Mortier L., Marchetti P.
Cancer Res. 72:5035-5047(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex."
Kato M., Chuang J.L., Tso S.C., Wynn R.M., Chuang D.T.
EMBO J. 24:1763-1774(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.48 ANGSTROMS) OF 9-406 IN COMPLEX WITH ATP, FUNCTION, INTERACTION WITH DLAT.
[15]"Crystal structure of an asymmetric complex of pyruvate dehydrogenase kinase 3 with lipoyl domain 2 and its biological implications."
Devedjiev Y., Steussy C.N., Vassylyev D.G.
J. Mol. Biol. 370:407-416(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 9-406, INTERACTION WITH DLAT.
[16]"Distinct structural mechanisms for inhibition of pyruvate dehydrogenase kinase isoforms by AZD7545, dichloroacetate, and radicicol."
Kato M., Li J., Chuang J.L., Chuang D.T.
Structure 15:992-1004(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 9-406 IN COMPLEX WITH THE INHIBITOR RADICICOL, FUNCTION, ENZYME REGULATION, INTERACTION WITH DLAT.
[17]"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] ALA-219.
[18]"A new locus for X-linked dominant Charcot-Marie-Tooth disease (CMTX6) is caused by mutations in the pyruvate dehydrogenase kinase isoenzyme 3 (PDK3) gene."
Kennerson M.L., Yiu E.M., Chuang D.T., Kidambi A., Tso S.C., Ly C., Chaudhry R., Drew A.P., Rance G., Delatycki M.B., Zuchner S., Ryan M.M., Nicholson G.A.
Hum. Mol. Genet. 22:1404-1416(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMTX6 HIS-158, VARIANTS THR-114 AND SER-334, CHARACTERIZATION OF VARIANT CMTX6 HIS-158, TISSUE SPECIFICITY, MUTAGENESIS OF ASN-120 AND ASP-121.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42452 mRNA. Translation: AAC42011.1.
AK301965 mRNA. Translation: BAG63378.1.
CH471074 Genomic DNA. Translation: EAW99019.1.
BC015948 mRNA. Translation: AAH15948.1.
PIRI70160.
RefSeqNP_001135858.1. NM_001142386.2.
NP_005382.1. NM_005391.4.
UniGeneHs.296031.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y8NX-ray2.60A9-406[»]
1Y8OX-ray2.48A9-406[»]
1Y8PX-ray2.63A9-406[»]
2PNRX-ray2.50A/B/E/F9-406[»]
2Q8IX-ray2.60A9-406[»]
ProteinModelPortalQ15120.
SMRQ15120. Positions 12-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111191. 8 interactions.
DIPDIP-29498N.
IntActQ15120. 2 interactions.
STRING9606.ENSP00000387536.

Chemistry

BindingDBQ15120.
ChEMBLCHEMBL2096665.

PTM databases

PhosphoSiteQ15120.

Polymorphism databases

DMDM3183119.

Proteomic databases

PaxDbQ15120.
PRIDEQ15120.

Protocols and materials databases

DNASU5165.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379162; ENSP00000368460; ENSG00000067992. [Q15120-1]
ENST00000441463; ENSP00000387536; ENSG00000067992. [Q15120-2]
GeneID5165.
KEGGhsa:5165.
UCSCuc004dbg.3. human. [Q15120-1]
uc004dbh.3. human. [Q15120-2]

Organism-specific databases

CTD5165.
GeneCardsGC0XP024393.
HGNCHGNC:8811. PDK3.
HPAHPA046583.
MIM300905. phenotype.
300906. gene.
neXtProtNX_Q15120.
Orphanet352675. X-linked Charcot-Marie-Tooth disease type 6.
PharmGKBPA33156.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0642.
HOGENOMHOG000164315.
HOVERGENHBG000511.
InParanoidQ15120.
KOK00898.
OMAPTGDWSN.
OrthoDBEOG71VSSV.
PhylomeDBQ15120.
TreeFamTF314918.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeQ15120.
CleanExHS_PDK3.
GenevestigatorQ15120.

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

EvolutionaryTraceQ15120.
GeneWikiPDK3.
GenomeRNAi5165.
NextBio19982.
PROQ15120.
SOURCESearch...

Entry information

Entry namePDK3_HUMAN
AccessionPrimary (citable) accession number: Q15120
Secondary accession number(s): B4DXG6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 143 of the entry and version 1 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 X

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