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Protein

3-phosphoinositide-dependent protein kinase 1

Gene

PDPK1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca2+ entry and Ca2+-activated K+ channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses. Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages. Isoform 3 is catalytically inactive.15 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Homodimerization regulates its activity by maintaining the kinase in an autoinhibitory conformation. NPRL2 down-regulates its activity by interfering with tyrosine phosphorylation at the Tyr-9, Tyr-373 and Tyr-376 residues. The 14-3-3 protein YWHAQ acts as a negative regulator by association with the residues surrounding the Ser-241 residue. STRAP positively regulates its activity by enhancing its autophosphorylation and by stimulating its dissociation from YWHAQ. SMAD2, SMAD3, SMAD4 and SMAD7 also positively regulate its activity by stimulating its dissociation from YWHAQ. Activated by phosphorylation on Tyr-9, Tyr-373 and Tyr-376 by INSR in response to insulin.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei111ATP3 Publications1
Binding sitei166ATP3 Publications1
Active sitei205Proton acceptorPROSITE-ProRule annotation1
Binding sitei209ATP; via carbonyl oxygen1 Publication1
Binding sitei223ATP3 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi92 – 94ATP3 Publications3
Nucleotide bindingi160 – 162ATP3 Publications3

GO - Molecular functioni

  • 3-phosphoinositide-dependent protein kinase activity Source: BHF-UCL
  • ATP binding Source: UniProtKB-KW
  • insulin receptor binding Source: Ensembl
  • kinase activity Source: Reactome
  • phospholipase activator activity Source: BHF-UCL
  • phospholipase binding Source: BHF-UCL
  • protein kinase binding Source: Ensembl
  • protein serine/threonine kinase activity Source: BHF-UCL

GO - Biological processi

  • actin cytoskeleton organization Source: ProtInc
  • activation of protein kinase B activity Source: BHF-UCL
  • calcium-mediated signaling Source: BHF-UCL
  • cell migration Source: BHF-UCL
  • cellular response to brain-derived neurotrophic factor stimulus Source: Ensembl
  • cellular response to epidermal growth factor stimulus Source: BHF-UCL
  • cellular response to insulin stimulus Source: BHF-UCL
  • epidermal growth factor receptor signaling pathway Source: BHF-UCL
  • extrinsic apoptotic signaling pathway Source: UniProtKB
  • Fc-epsilon receptor signaling pathway Source: Reactome
  • focal adhesion assembly Source: Ensembl
  • hyperosmotic response Source: Ensembl
  • intracellular signal transduction Source: MGI
  • negative regulation of cardiac muscle cell apoptotic process Source: Ensembl
  • negative regulation of endothelial cell apoptotic process Source: BHF-UCL
  • negative regulation of neuron apoptotic process Source: Ensembl
  • negative regulation of protein kinase activity Source: BHF-UCL
  • negative regulation of toll-like receptor signaling pathway Source: Ensembl
  • negative regulation of transforming growth factor beta receptor signaling pathway Source: UniProtKB
  • peptidyl-serine phosphorylation Source: GO_Central
  • peptidyl-threonine phosphorylation Source: BHF-UCL
  • platelet activation Source: Reactome
  • positive regulation of angiogenesis Source: BHF-UCL
  • positive regulation of blood vessel endothelial cell migration Source: BHF-UCL
  • positive regulation of phospholipase activity Source: BHF-UCL
  • positive regulation of protein localization to plasma membrane Source: BHF-UCL
  • positive regulation of release of sequestered calcium ion into cytosol Source: BHF-UCL
  • positive regulation of sprouting angiogenesis Source: BHF-UCL
  • positive regulation of vascular endothelial cell proliferation Source: BHF-UCL
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • regulation of mast cell degranulation Source: Ensembl
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • stimulatory C-type lectin receptor signaling pathway Source: Reactome
  • T cell costimulation Source: Reactome
  • T cell receptor signaling pathway Source: Reactome
  • transcription, DNA-templated Source: UniProtKB-KW
  • type B pancreatic cell development Source: Ensembl

Keywordsi

Molecular functionActivator, Kinase, Serine/threonine-protein kinase, Transferase
Biological processTranscription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1 2681
ReactomeiR-HSA-114604 GPVI-mediated activation cascade
R-HSA-1257604 PIP3 activates AKT signaling
R-HSA-165158 Activation of AKT2
R-HSA-202424 Downstream TCR signaling
R-HSA-2730905 Role of LAT2/NTAL/LAB on calcium mobilization
R-HSA-2871837 FCERI mediated NF-kB activation
R-HSA-354192 Integrin alphaIIb beta3 signaling
R-HSA-389357 CD28 dependent PI3K/Akt signaling
R-HSA-389513 CTLA4 inhibitory signaling
R-HSA-392451 G beta:gamma signalling through PI3Kgamma
R-HSA-444257 RSK activation
R-HSA-5218920 VEGFR2 mediated vascular permeability
R-HSA-5218921 VEGFR2 mediated cell proliferation
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5625740 RHO GTPases activate PKNs
R-HSA-5674400 Constitutive Signaling by AKT1 E17K in Cancer
R-HSA-6804757 Regulation of TP53 Degradation
SABIO-RKiO15530
SignaLinkiO15530
SIGNORiO15530

Names & Taxonomyi

Protein namesi
Recommended name:
3-phosphoinositide-dependent protein kinase 1 (EC:2.7.11.1)
Short name:
hPDK1
Gene namesi
Name:PDPK1
Synonyms:PDK1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

EuPathDBiHostDB:ENSG00000140992.18
HGNCiHGNC:8816 PDPK1
MIMi605213 gene
neXtProtiNX_O15530

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9Y → F: Slight reduction in pervanadate-stimulated tyrosine phosphorylation. 1 Publication1
Mutagenesisi25S → A: No effect. 1 Publication1
Mutagenesisi241S → A: No activation. 1 Publication1
Mutagenesisi277A → V: 3-fold increase in kinase activity. 1 Publication1
Mutagenesisi354T → A: Abolishes phosphorylation by MELK. 1 Publication1
Mutagenesisi373Y → F: Reduction in basal activity. 1 Publication1
Mutagenesisi376Y → F: Reduction in basal activity. 1 Publication1
Mutagenesisi393S → A: No effect. 1 Publication1
Mutagenesisi394S → A: Abolishes phosphorylation by MAP3K5; when associated with A-398. 1 Publication1
Mutagenesisi396S → A: No effect. 1 Publication1
Mutagenesisi398S → A: Abolishes phosphorylation by MAP3K5; when associated with A-394. 1 Publication1
Mutagenesisi410S → A: No effect. 1 Publication1
Mutagenesisi474R → A: No PDGF-dependent translocation to the membrane. 1 Publication1
Mutagenesisi513T → E: Enhanced kinase activity towards PKB. 1 Publication1

Organism-specific databases

DisGeNETi5170
OpenTargetsiENSG00000140992
PharmGKBiPA33160

Chemistry databases

ChEMBLiCHEMBL2534
DrugBankiDB07132 1-{2-OXO-3-[(1R)-1-(1H-PYRROL-2-YL)ETHYL]-2H-INDOL-5-YL}UREA
DB07033 5-HYDROXY-3-[(1R)-1-(1H-PYRROL-2-YL)ETHYL]-2H-INDOL-2-ONE
DB01933 7-Hydroxystaurosporine
DB00482 Celecoxib
DB04522 Phosphonoserine
DB03777 Rbt205 Inhibitor
DB02010 Staurosporine
GuidetoPHARMACOLOGYi1519

Polymorphism and mutation databases

BioMutaiPDPK1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000865001 – 5563-phosphoinositide-dependent protein kinase 1Add BLAST556

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9Phosphotyrosine; by SRC and INSR3 Publications1
Modified residuei25Phosphoserine1 Publication1
Modified residuei241Phosphoserine; by autocatalysis5 Publications1
Modified residuei304N6-acetyllysineBy similarity1
Modified residuei354Phosphothreonine; by MELK1 Publication1
Modified residuei373Phosphotyrosine; by SRC and INSR3 Publications1
Modified residuei376Phosphotyrosine; by SRC and INSR3 Publications1
Modified residuei393Phosphoserine1 Publication1
Modified residuei394Phosphoserine; by MAP3K51 Publication1
Modified residuei396Phosphoserine2 Publications1
Modified residuei398Phosphoserine; by MAP3K51 Publication1
Modified residuei410Phosphoserine1 Publication1
Modified residuei501Phosphoserine; by PKC/PRKCQBy similarity1
Modified residuei513Phosphothreonine; by autocatalysis1 Publication1
Modified residuei529Phosphoserine; by PKC/PRKCQBy similarity1

Post-translational modificationi

Phosphorylation on Ser-241 in the activation loop is required for full activity. PDPK1 itself can autophosphorylate Ser-241, leading to its own activation. Autophosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2 (By similarity). Tyr-9 phosphorylation is critical for stabilization of both PDPK1 and the PDPK1/SRC complex via HSP90-mediated protection of PDPK1 degradation. Angiotensin II stimulates the tyrosine phosphorylation of PDPK1 in vascular smooth muscle in a calcium- and SRC-dependent manner. Phosphorylated on Tyr-9, Tyr-373 and Tyr-376 by INSR in response to insulin. Palmitate negatively regulates autophosphorylation at Ser-241 and palmitate-induced phosphorylation at Ser-529 and Ser-501 by PKC/PRKCQ negatively regulates its ability to phosphorylate PKB/AKT1. Phosphorylation at Thr-354 by MELK partially inhibits kinase activity, the inhibition is cooperatively enhanced by phosphorylation at Ser-394 and Ser-398 by MAP3K5.By similarity8 Publications
Autophosphorylated; autophosphorylation is inhibited by the apoptotic C-terminus cleavage product of PKN2.By similarity
Monoubiquitinated in the kinase domain, deubiquitinated by USP4.

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO15530
MaxQBiO15530
PaxDbiO15530
PeptideAtlasiO15530
PRIDEiO15530

PTM databases

iPTMnetiO15530
PhosphoSitePlusiO15530

Expressioni

Tissue specificityi

Appears to be expressed ubiquitously. The Tyr-9 phosphorylated form is markedly increased in diseased tissue compared with normal tissue from lung, liver, colon and breast.1 Publication

Inductioni

Stimulated by insulin, and the oxidants hydrogen peroxide and peroxovanadate.

Gene expression databases

BgeeiENSG00000140992
CleanExiHS_PDK1
HS_PDPK1
ExpressionAtlasiO15530 baseline and differential
GenevisibleiO15530 HS

Organism-specific databases

HPAiCAB004272
HPA035199
HPA068961

Interactioni

Subunit structurei

Homodimer in its autoinhibited state. Active as monomer. Interacts with NPRL2, PPARG, PAK1, PTK2B, GRB14, PKN1 (via C-terminus), STRAP and IKKB. The Tyr-9 phosphorylated form interacts with SRC, RASA1 and CRK (via their SH2 domains). Interacts with SGK3 in a phosphorylation-dependent manner. The tyrosine-phosphorylated form interacts with PTPN6. The Ser-241 phosphorylated form interacts with YWHAH and YWHAQ. Binds INSR in response to insulin. Interacts (via PH domain) with SMAD3, SMAD4 and SMAD7. Interacts with PKN2; the interaction stimulates PDPK1 autophosphorylation, its PI(3,4,5)P3-dependent kinase activity toward 'Ser-473' of AKT1 but also activates its kinase activity toward PRKCD and PRKCZ.14 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • insulin receptor binding Source: Ensembl
  • phospholipase binding Source: BHF-UCL
  • protein kinase binding Source: Ensembl

Protein-protein interaction databases

BioGridi111196, 61 interactors
DIPiDIP-38372N
ELMiO15530
IntActiO15530, 59 interactors
MINTiO15530
STRINGi9606.ENSP00000344220

Chemistry databases

BindingDBiO15530

Structurei

Secondary structure

1556
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi79 – 81Combined sources3
Beta strandi82 – 90Combined sources9
Beta strandi95 – 101Combined sources7
Turni102 – 104Combined sources3
Beta strandi107 – 114Combined sources8
Helixi115 – 120Combined sources6
Helixi124 – 136Combined sources13
Beta strandi145 – 150Combined sources6
Beta strandi152 – 159Combined sources8
Beta strandi163 – 166Combined sources4
Helixi167 – 174Combined sources8
Helixi179 – 198Combined sources20
Helixi208 – 210Combined sources3
Beta strandi211 – 213Combined sources3
Beta strandi219 – 221Combined sources3
Helixi224 – 226Combined sources3
Turni232 – 235Combined sources4
Beta strandi238 – 240Combined sources3
Helixi246 – 248Combined sources3
Helixi251 – 256Combined sources6
Helixi261 – 277Combined sources17
Helixi287 – 295Combined sources9
Beta strandi303 – 305Combined sources3
Helixi307 – 316Combined sources10
Helixi321 – 323Combined sources3
Helixi328 – 330Combined sources3
Helixi333 – 337Combined sources5
Helixi340 – 342Combined sources3
Helixi347 – 352Combined sources6
Helixi412 – 415Combined sources4
Beta strandi416 – 420Combined sources5
Beta strandi423 – 426Combined sources4
Helixi432 – 445Combined sources14
Helixi449 – 451Combined sources3
Turni452 – 454Combined sources3
Beta strandi457 – 467Combined sources11
Beta strandi470 – 479Combined sources10
Turni480 – 482Combined sources3
Beta strandi483 – 488Combined sources6
Turni489 – 492Combined sources4
Beta strandi493 – 498Combined sources6
Beta strandi505 – 518Combined sources14
Beta strandi521 – 526Combined sources6
Helixi532 – 547Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1H1WX-ray2.00A71-359[»]
1OKYX-ray2.30A51-360[»]
1OKZX-ray2.51A51-360[»]
1UU3X-ray1.70A51-360[»]
1UU7X-ray1.90A51-360[»]
1UU8X-ray2.50A51-360[»]
1UU9X-ray1.95A72-357[»]
1UVRX-ray2.81A71-359[»]
1W1DX-ray1.50A409-556[»]
1W1GX-ray1.45A409-556[»]
1W1HX-ray1.45A/B/C/D409-556[»]
1Z5MX-ray2.17A74-359[»]
2BIYX-ray1.95A51-360[»]
2PE0X-ray2.35A74-359[»]
2PE1X-ray2.14A74-359[»]
2PE2X-ray2.13A74-359[»]
2R7BX-ray2.70A48-359[»]
2VKIX-ray1.80A409-556[»]
2XCHX-ray2.00A51-359[»]
2XCKX-ray2.30A51-359[»]
3H9OX-ray2.30A51-359[»]
3HRCX-ray1.91A50-359[»]
3HRFX-ray1.90A50-359[»]
3IONX-ray2.40A48-359[»]
3IOPX-ray2.20A48-359[»]
3NAXX-ray1.75A66-362[»]
3NAYX-ray2.60A/B66-362[»]
3NUNX-ray2.20A67-358[»]
3NUSX-ray2.75A73-358[»]
3NUUX-ray1.98A73-358[»]
3NUYX-ray2.10A73-358[»]
3ORXX-ray2.20A/B/C/D/E/F/G/H51-359[»]
3ORZX-ray2.00A/B/C/D51-359[»]
3OTUX-ray2.10A51-359[»]
3PWYX-ray3.50A51-359[»]
3QC4X-ray1.80A/B51-359[»]
3QCQX-ray2.50A48-359[»]
3QCSX-ray2.49A48-359[»]
3QCXX-ray2.30A48-359[»]
3QCYX-ray2.20A48-359[»]
3QD0X-ray1.99A48-359[»]
3QD3X-ray2.00A48-359[»]
3QD4X-ray2.30A48-359[»]
3RCJX-ray1.70A50-359[»]
3RWPX-ray1.92A51-359[»]
3RWQX-ray2.55A51-359[»]
3SC1X-ray2.70A50-359[»]
4A06X-ray2.00A50-359[»]
4A07X-ray1.85A50-359[»]
4AW0X-ray1.43A51-359[»]
4AW1X-ray1.68A51-359[»]
4CT1X-ray1.85A50-359[»]
4CT2X-ray1.25A50-359[»]
4RQKX-ray1.55A50-359[»]
4RQVX-ray1.50A50-359[»]
4RRVX-ray1.41A50-359[»]
4XX9X-ray1.40A50-359[»]
5ACKX-ray1.24A50-359[»]
5HKMX-ray2.10A51-359[»]
5HNGX-ray3.01A51-359[»]
5HO7X-ray3.00A51-359[»]
5HO8X-ray2.70A51-359[»]
5LVLX-ray1.40A50-359[»]
5LVMX-ray1.26A50-359[»]
5LVNX-ray1.38A50-359[»]
5LVOX-ray1.09A50-359[»]
5LVPX-ray2.50A/B/C/D50-359[»]
5MRDX-ray1.41A50-359[»]
ProteinModelPortaliO15530
SMRiO15530
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15530

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini82 – 342Protein kinasePROSITE-ProRule annotationAdd BLAST261
Domaini459 – 550PHAdd BLAST92

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni113 – 157PIF-pocket1 PublicationAdd BLAST45

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi389 – 398Poly-Ser10

Domaini

The PH domain plays a pivotal role in the localization and nuclear import of PDPK1 and is also essential for its homodimerization.
The PIF-pocket is a small lobe in the catalytic domain required by the enzyme for the binding to the hydrophobic motif of its substrates. It is an allosteric regulatory site that can accommodate small compounds acting as allosteric inhibitors.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0592 Eukaryota
ENOG410XRT8 LUCA
GeneTreeiENSGT00550000074819
HOGENOMiHOG000233026
HOVERGENiHBG098357
InParanoidiO15530
KOiK06276
OMAiIPWSLEL
OrthoDBiEOG091G06CX
PhylomeDBiO15530
TreeFamiTF105423

Family and domain databases

CDDicd01262 PH_PDK1, 1 hit
Gene3Di2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR033931 PDK1-typ_PH
IPR011993 PH-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF14593 PH_3, 1 hit
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O15530-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MARTTSQLYD AVPIQSSVVL CSCPSPSMVR TQTESSTPPG IPGGSRQGPA
60 70 80 90 100
MDGTAAEPRP GAGSLQHAQP PPQPRKKRPE DFKFGKILGE GSFSTVVLAR
110 120 130 140 150
ELATSREYAI KILEKRHIIK ENKVPYVTRE RDVMSRLDHP FFVKLYFTFQ
160 170 180 190 200
DDEKLYFGLS YAKNGELLKY IRKIGSFDET CTRFYTAEIV SALEYLHGKG
210 220 230 240 250
IIHRDLKPEN ILLNEDMHIQ ITDFGTAKVL SPESKQARAN SFVGTAQYVS
260 270 280 290 300
PELLTEKSAC KSSDLWALGC IIYQLVAGLP PFRAGNEYLI FQKIIKLEYD
310 320 330 340 350
FPEKFFPKAR DLVEKLLVLD ATKRLGCEEM EGYGPLKAHP FFESVTWENL
360 370 380 390 400
HQQTPPKLTA YLPAMSEDDE DCYGNYDNLL SQFGCMQVSS SSSSHSLSAS
410 420 430 440 450
DTGLPQRSGS NIEQYIHDLD SNSFELDLQF SEDEKRLLLE KQAGGNPWHQ
460 470 480 490 500
FVENNLILKM GPVDKRKGLF ARRRQLLLTE GPHLYYVDPV NKVLKGEIPW
510 520 530 540 550
SQELRPEAKN FKTFFVHTPN RTYYLMDPSG NAHKWCRKIQ EVWRQRYQSH

PDAAVQ
Length:556
Mass (Da):63,152
Last modified:January 1, 1998 - v1
Checksum:iED8C0306DC4D0653
GO
Isoform 2 (identifier: O15530-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-50: Missing.

Show »
Length:506
Mass (Da):58,035
Checksum:i22D376B8A13FD3F3
GO
Isoform 3 (identifier: O15530-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     238-263: Missing.

Show »
Length:530
Mass (Da):60,396
Checksum:iCEAF882CBD3EB1F2
GO
Isoform 4 (identifier: O15530-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     110-237: IKILEKRHII...KVLSPESKQA → T

Show »
Length:429
Mass (Da):48,201
Checksum:i860C8A8C06161CE1
GO
Isoform 5 (identifier: O15530-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     448-556: WHQFVENNLI...YQSHPDAAVQ → CLTGRII

Note: No experimental confirmation available.
Show »
Length:454
Mass (Da):50,838
Checksum:i8D812DCC8CED2998
GO

Sequence cautioni

The sequence BAD93072 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0048941 – 50Missing in isoform 2. CuratedAdd BLAST50
Alternative sequenceiVSP_041902110 – 237IKILE…ESKQA → T in isoform 4. 1 PublicationAdd BLAST128
Alternative sequenceiVSP_004895238 – 263Missing in isoform 3. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_044796448 – 556WHQFV…DAAVQ → CLTGRII in isoform 5. 1 PublicationAdd BLAST109

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF017995 mRNA Translation: AAC51825.1
Y15056 mRNA Translation: CAA75341.1
CR536517 mRNA Translation: CAG38755.1
AB209835 mRNA Translation: BAD93072.1 Different initiation.
AC093525 Genomic DNA No translation available.
AC141586 Genomic DNA No translation available.
BC006339 mRNA Translation: AAH06339.2
BC012103 mRNA Translation: AAH12103.1
BC033494 mRNA Translation: AAH33494.1
CCDSiCCDS10472.1 [O15530-1]
CCDS10473.1 [O15530-4]
CCDS58411.1 [O15530-5]
RefSeqiNP_001248745.1, NM_001261816.1 [O15530-5]
NP_002604.1, NM_002613.4 [O15530-1]
NP_112558.2, NM_031268.5 [O15530-4]
UniGeneiHs.459691

Genome annotation databases

EnsembliENST00000268673; ENSP00000268673; ENSG00000140992 [O15530-4]
ENST00000342085; ENSP00000344220; ENSG00000140992 [O15530-1]
ENST00000441549; ENSP00000395357; ENSG00000140992 [O15530-5]
GeneIDi5170
KEGGihsa:5170
UCSCiuc002cqs.5 human [O15530-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiPDPK1_HUMAN
AccessioniPrimary (citable) accession number: O15530
Secondary accession number(s): H0Y4Z0
, Q59EH6, Q6FI20, Q8IV52, Q9BRD5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 1, 1998
Last modified: April 25, 2018
This is version 207 of the entry and version 1 of the sequence. See 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, Direct protein sequencing, Reference proteome
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