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Q16654

- PDK4_HUMAN

UniProt

Q16654 - PDK4_HUMAN

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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

Functioni

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
Complete GO annotation...

Keywords - Molecular functioni

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
Complete GO annotation...

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

BgeeiQ16654.
CleanExiHS_PDK4.
ExpressionAtlasiQ16654. baseline and differential.
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 – 276Combined sources
Helixi37 – 426Combined sources
Helixi50 – 7223Combined sources
Helixi77 – 804Combined sources
Helixi83 – 10018Combined sources
Beta strandi103 – 1053Combined sources
Helixi110 – 12718Combined sources
Helixi130 – 14213Combined sources
Turni149 – 1513Combined sources
Helixi153 – 18028Combined sources
Beta strandi194 – 1996Combined sources
Helixi200 – 21920Combined sources
Beta strandi225 – 23410Combined sources
Beta strandi240 – 2434Combined sources
Helixi245 – 26622Combined sources
Turni267 – 2693Combined sources
Beta strandi270 – 2723Combined sources
Beta strandi276 – 2827Combined sources
Beta strandi284 – 29310Combined sources
Helixi300 – 3023Combined sources
Helixi303 – 3064Combined sources
Beta strandi329 – 3313Combined sources
Helixi333 – 34311Combined sources
Beta strandi347 – 3537Combined sources
Turni354 – 3563Combined sources
Beta strandi357 – 36711Combined sources
Turni368 – 3703Combined sources
Helixi380 – 3856Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00550000074574.
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_C.
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

        10         20         30         40         50
MKAARFVLRS AGSLNGAGLV PREVEHFSRY SPSPLSMKQL LDFGSENACE
60 70 80 90 100
RTSFAFLRQE LPVRLANILK EIDILPTQLV NTSSVQLVKS WYIQSLMDLV
110 120 130 140 150
EFHEKSPDDQ KALSDFVDTL IKVRNRHHNV VPTMAQGIIE YKDACTVDPV
160 170 180 190 200
TNQNLQYFLD RFYMNRISTR MLMNQHILIF SDSQTGNPSH IGSIDPNCDV
210 220 230 240 250
VAVVQDAFEC SRMLCDQYYL SSPELKLTQV NGKFPDQPIH IVYVPSHLHH
260 270 280 290 300
MLFELFKNAM RATVEHQENQ PSLTPIEVIV VLGKEDLTIK ISDRGGGVPL
310 320 330 340 350
RIIDRLFSYT YSTAPTPVMD NSRNAPLAGF GYGLPISRLY AKYFQGDLNL
360 370 380 390 400
YSLSGYGTDA IIYLKALSSE SIEKLPVFNK SAFKHYQMSS EADDWCIPSR
410
EPKNLAKEVA M
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00550000074574.
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

Bgeei Q16654.
CleanExi HS_PDK4.
ExpressionAtlasi Q16654. baseline and differential.
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_C.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 140 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