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Q16654

- PDK4_HUMAN

UniProt

Q16654 - PDK4_HUMAN

Protein

[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 4, mitochondrial

Gene

PDK4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Serine/threonine kinase that plays a key role in 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 in response to prolonged fasting and starvation. Plays an important role in maintaining normal blood glucose levels under starvation, and is involved in the insulin signaling cascade. 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. In the fed state, mediates cellular responses to glucose levels and to a high-fat diet. Regulates both fatty acid oxidation and de novo fatty acid biosynthesis. Plays a role in the generation of reactive oxygen species. Protects detached epithelial cells against anoikis. Plays a role in cell proliferation via its role in regulating carbohydrate and fatty acid metabolism.4 Publications

    Catalytic activityi

    ATP + [pyruvate dehydrogenase (acetyl-transferring)] = ADP + [pyruvate dehydrogenase (acetyl-transferring)] phosphate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei157 – 1571Interaction with the other subunit in the homodimer
    Sitei161 – 1611Interaction with the other subunit in the homodimer
    Binding sitei293 – 2931ATP1 Publication
    Sitei395 – 3951Interaction with the other subunit in the homodimer

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi254 – 2618ATP1 Publication
    Nucleotide bindingi312 – 3132ATP1 Publication
    Nucleotide bindingi329 – 3346ATP1 Publication

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. protein kinase activity Source: UniProtKB
    3. protein serine/threonine kinase activity Source: UniProtKB-KW
    4. pyruvate dehydrogenase (acetyl-transferring) kinase activity Source: UniProtKB

    GO - Biological processi

    1. cellular metabolic process Source: Reactome
    2. cellular response to fatty acid Source: UniProtKB
    3. cellular response to starvation Source: UniProtKB
    4. glucose homeostasis Source: UniProtKB
    5. glucose metabolic process Source: UniProtKB-KW
    6. insulin receptor signaling pathway Source: UniProtKB
    7. negative regulation of anoikis Source: UniProtKB
    8. protein phosphorylation Source: GOC
    9. pyruvate metabolic process Source: Reactome
    10. reactive oxygen species metabolic process Source: UniProtKB
    11. regulation of acetyl-CoA biosynthetic process from pyruvate Source: UniProtKB
    12. regulation of bone resorption Source: Ensembl
    13. regulation of cellular ketone metabolic process Source: UniProtKB
    14. regulation of fatty acid biosynthetic process Source: UniProtKB
    15. regulation of fatty acid oxidation Source: UniProtKB
    16. regulation of glucose metabolic process Source: UniProtKB
    17. regulation of pH Source: UniProtKB
    18. response to starvation Source: UniProtKB
    19. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Carbohydrate metabolism, Glucose metabolism

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.2. 2681.
    ReactomeiREACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 4, mitochondrial (EC:2.7.11.2)
    Alternative name(s):
    Pyruvate dehydrogenase kinase isoform 4
    Gene namesi
    Name:PDK4
    Synonyms:PDHK4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:8812. PDK4.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial inner membrane Source: Ensembl
    2. mitochondrial matrix Source: Reactome
    3. mitochondrion Source: ProtInc

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi157 – 1571Y → F: Loss of activity. 1 Publication
    Mutagenesisi161 – 1611R → A: Loss of activity. 1 Publication
    Mutagenesisi394 – 3941D → A: Loss of activity; when associated with A-395. 1 Publication
    Mutagenesisi395 – 3951W → A: Loss of activity; when associated with A-394. 1 Publication

    Organism-specific databases

    PharmGKBiPA33157.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 411[Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 4, mitochondrialPRO_0000023445
    Transit peptidei1 – ?MitochondrionSequence Analysis

    Proteomic databases

    PaxDbiQ16654.
    PRIDEiQ16654.

    PTM databases

    PhosphoSiteiQ16654.

    Expressioni

    Tissue specificityi

    Ubiquitous; highest levels of expression in heart and skeletal muscle.2 Publications

    Inductioni

    Up-regulated by prolonged fasting, in glucose-deprived cells and in response to a high-fat diet. Down-regulated by insulin. Up-regulated by PPARD.5 Publications

    Gene expression databases

    ArrayExpressiQ16654.
    BgeeiQ16654.
    CleanExiHS_PDK4.
    GenevestigatoriQ16654.

    Organism-specific databases

    HPAiHPA056731.

    Interactioni

    Subunit structurei

    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).2 Publications

    Protein-protein interaction databases

    BioGridi111192. 2 interactions.
    IntActiQ16654. 1 interaction.
    STRINGi9606.ENSP00000005178.

    Structurei

    Secondary structure

    1
    411
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi22 – 276
    Helixi37 – 426
    Helixi50 – 7223
    Helixi77 – 804
    Helixi83 – 10018
    Beta strandi103 – 1053
    Helixi110 – 12718
    Helixi130 – 14213
    Turni149 – 1513
    Helixi153 – 18028
    Beta strandi194 – 1996
    Helixi200 – 21920
    Beta strandi225 – 23410
    Beta strandi240 – 2434
    Helixi245 – 26622
    Turni267 – 2693
    Beta strandi270 – 2723
    Beta strandi276 – 2827
    Beta strandi284 – 29310
    Helixi300 – 3023
    Helixi303 – 3064
    Beta strandi329 – 3313
    Helixi333 – 34311
    Beta strandi347 – 3537
    Turni354 – 3563
    Beta strandi357 – 36711
    Turni368 – 3703
    Helixi380 – 3856

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2E0AX-ray1.86A/B20-411[»]
    2ZDXX-ray2.54A/B20-411[»]
    2ZDYX-ray2.40A/B20-411[»]
    2ZKJX-ray2.00A/B20-411[»]
    3D2RX-ray2.03A/B20-411[»]
    ProteinModelPortaliQ16654.
    SMRiQ16654. Positions 20-386.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16654.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini138 – 368231Histidine kinasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PDK/BCKDK protein kinase family.Curated
    Contains 1 histidine kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0642.
    HOGENOMiHOG000164315.
    HOVERGENiHBG000511.
    InParanoidiQ16654.
    KOiK00898.
    OMAiPSREPKN.
    OrthoDBiEOG71VSSV.
    PhylomeDBiQ16654.
    TreeFamiTF314918.

    Family and domain databases

    Gene3Di1.20.140.20. 1 hit.
    3.30.565.10. 1 hit.
    InterProiIPR018955. BCDHK/PDK_N.
    IPR003594. HATPase_ATP-bd.
    IPR005467. Sig_transdc_His_kinase_core.
    [Graphical view]
    PfamiPF10436. BCDHK_Adom3. 1 hit.
    PF02518. HATPase_c. 1 hit.
    [Graphical view]
    SMARTiSM00387. HATPase_c. 1 hit.
    [Graphical view]
    SUPFAMiSSF55874. SSF55874. 1 hit.
    SSF69012. SSF69012. 1 hit.
    PROSITEiPS50109. HIS_KIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q16654-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKAARFVLRS AGSLNGAGLV PREVEHFSRY SPSPLSMKQL LDFGSENACE    50
    RTSFAFLRQE LPVRLANILK EIDILPTQLV NTSSVQLVKS WYIQSLMDLV 100
    EFHEKSPDDQ KALSDFVDTL IKVRNRHHNV VPTMAQGIIE YKDACTVDPV 150
    TNQNLQYFLD RFYMNRISTR MLMNQHILIF SDSQTGNPSH IGSIDPNCDV 200
    VAVVQDAFEC SRMLCDQYYL SSPELKLTQV NGKFPDQPIH IVYVPSHLHH 250
    MLFELFKNAM RATVEHQENQ PSLTPIEVIV VLGKEDLTIK ISDRGGGVPL 300
    RIIDRLFSYT YSTAPTPVMD NSRNAPLAGF GYGLPISRLY AKYFQGDLNL 350
    YSLSGYGTDA IIYLKALSSE SIEKLPVFNK SAFKHYQMSS EADDWCIPSR 400
    EPKNLAKEVA M 411
    Length:411
    Mass (Da):46,469
    Last modified:November 1, 1996 - v1
    Checksum:iC17B78B6057000E9
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171A → V.1 Publication
    Corresponds to variant rs56391840 [ dbSNP | Ensembl ].
    VAR_042298
    Natural varianti19 – 191L → M.1 Publication
    Corresponds to variant rs55761955 [ dbSNP | Ensembl ].
    VAR_042299
    Natural varianti109 – 1091D → G.1 Publication
    Corresponds to variant rs34898343 [ dbSNP | Ensembl ].
    VAR_042300

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U54628
    , U54618, U54619, U54620, U54621, U54622, U54623, U54624, U54625, U54626, U54627 Genomic DNA. Translation: AAC50670.1.
    U54617 mRNA. Translation: AAC50669.1.
    AC002451 Genomic DNA. Translation: AAB67048.1.
    BC040239 mRNA. Translation: AAH40239.1.
    CCDSiCCDS5643.1.
    RefSeqiNP_002603.1. NM_002612.3.
    UniGeneiHs.8364.

    Genome annotation databases

    EnsembliENST00000005178; ENSP00000005178; ENSG00000004799.
    GeneIDi5166.
    KEGGihsa:5166.
    UCSCiuc003uoa.3. human.

    Polymorphism databases

    DMDMi3183120.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U54628
    , U54618 , U54619 , U54620 , U54621 , U54622 , U54623 , U54624 , U54625 , U54626 , U54627 Genomic DNA. Translation: AAC50670.1 .
    U54617 mRNA. Translation: AAC50669.1 .
    AC002451 Genomic DNA. Translation: AAB67048.1 .
    BC040239 mRNA. Translation: AAH40239.1 .
    CCDSi CCDS5643.1.
    RefSeqi NP_002603.1. NM_002612.3.
    UniGenei Hs.8364.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2E0A X-ray 1.86 A/B 20-411 [» ]
    2ZDX X-ray 2.54 A/B 20-411 [» ]
    2ZDY X-ray 2.40 A/B 20-411 [» ]
    2ZKJ X-ray 2.00 A/B 20-411 [» ]
    3D2R X-ray 2.03 A/B 20-411 [» ]
    ProteinModelPortali Q16654.
    SMRi Q16654. Positions 20-386.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111192. 2 interactions.
    IntActi Q16654. 1 interaction.
    STRINGi 9606.ENSP00000005178.

    Chemistry

    BindingDBi Q16654.
    ChEMBLi CHEMBL2096665.

    PTM databases

    PhosphoSitei Q16654.

    Polymorphism databases

    DMDMi 3183120.

    Proteomic databases

    PaxDbi Q16654.
    PRIDEi Q16654.

    Protocols and materials databases

    DNASUi 5166.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000005178 ; ENSP00000005178 ; ENSG00000004799 .
    GeneIDi 5166.
    KEGGi hsa:5166.
    UCSCi uc003uoa.3. human.

    Organism-specific databases

    CTDi 5166.
    GeneCardsi GC07M095212.
    HGNCi HGNC:8812. PDK4.
    HPAi HPA056731.
    MIMi 602527. gene.
    neXtProti NX_Q16654.
    PharmGKBi PA33157.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0642.
    HOGENOMi HOG000164315.
    HOVERGENi HBG000511.
    InParanoidi Q16654.
    KOi K00898.
    OMAi PSREPKN.
    OrthoDBi EOG71VSSV.
    PhylomeDBi Q16654.
    TreeFami TF314918.

    Enzyme and pathway databases

    BRENDAi 2.7.11.2. 2681.
    Reactomei REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.

    Miscellaneous databases

    ChiTaRSi PDK4. human.
    EvolutionaryTracei Q16654.
    GeneWikii PDK4.
    GenomeRNAii 5166.
    NextBioi 19986.
    PROi Q16654.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16654.
    Bgeei Q16654.
    CleanExi HS_PDK4.
    Genevestigatori Q16654.

    Family and domain databases

    Gene3Di 1.20.140.20. 1 hit.
    3.30.565.10. 1 hit.
    InterProi IPR018955. BCDHK/PDK_N.
    IPR003594. HATPase_ATP-bd.
    IPR005467. Sig_transdc_His_kinase_core.
    [Graphical view ]
    Pfami PF10436. BCDHK_Adom3. 1 hit.
    PF02518. HATPase_c. 1 hit.
    [Graphical view ]
    SMARTi SM00387. HATPase_c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55874. SSF55874. 1 hit.
    SSF69012. SSF69012. 1 hit.
    PROSITEi PS50109. HIS_KIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of PDK4 on 7q21.3 encoding a fourth pyruvate dehydrogenase kinase isoenzyme in human."
      Rowles J., Scherer S.W., Xi T., Majer M., Nickle D.C., Rommens J.M., Popov K.M., Harris R.A., Riebow N.L., Xia J., Tsui L.-C., Bogardus C., Prochazka M.
      J. Biol. Chem. 271:22376-22382(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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].
      Tissue: Cervix.
    4. "Pyruvate dehydrogenase activation and kinase expression in human skeletal muscle during fasting."
      Spriet L.L., Tunstall R.J., Watt M.J., Mehan K.A., Hargreaves M., Cameron-Smith D.
      J. Appl. Physiol. 96:2082-2087(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INDUCTION.
    5. "Diverging regulation of pyruvate dehydrogenase kinase isoform gene expression in cultured human muscle cells."
      Abbot E.L., McCormack J.G., Reynet C., Hassall D.G., Buchan K.W., Yeaman S.J.
      FEBS J. 272:3004-3014(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.
    6. "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.
    7. "Erk regulation of pyruvate dehydrogenase flux through PDK4 modulates cell proliferation."
      Grassian A.R., Metallo C.M., Coloff J.L., Stephanopoulos G., Brugge J.S.
      Genes Dev. 25:1716-1733(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "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.
    9. "Mitochondrial regulators of fatty acid metabolism reflect metabolic dysfunction in type 2 diabetes mellitus."
      Kulkarni S.S., Salehzadeh F., Fritz T., Zierath J.R., Krook A., Osler M.E.
      Metabolism 61:175-185(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.
    10. "Pyruvate dehydrogenase kinase-4 structures reveal a metastable open conformation fostering robust core-free basal activity."
      Wynn R.M., Kato M., Chuang J.L., Tso S.C., Li J., Chuang D.T.
      J. Biol. Chem. 283:25305-25315(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 20-411 IN COMPLEX WITH ATP, FUNCTION, ENZYME REGULATION, SUBUNIT, MUTAGENESIS OF TYR-157; ARG-161; ASP-394 AND TRP-395.
    11. Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 20-411 IN COMPLEX WITH ATP ANALOG, CATALYTIC ACTIVITY, SUBUNIT.
    12. "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: VARIANTS [LARGE SCALE ANALYSIS] VAL-17; MET-19 AND GLY-109.

    Entry informationi

    Entry nameiPDK4_HUMAN
    AccessioniPrimary (citable) accession number: Q16654
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 138 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3