Reviewed, UniProtKB/Swiss-Prot Q9Z2A0 (PDPK1_MOUSE)

Names and origin

Protein names

Recommended name:
    3-phosphoinositide-dependent protein kinase 1
      Short name=mPDK1
    EC=2.7.11.1

Gene names

Name:	Pdpk1
Synonyms:	Pdk1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	559 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Phosphorylates and activates not only PKB/AKT, but also PKA, PKC-zeta, RPS6KA1 and RPS6KB1. May play a general role in signaling processes and in development. Could also play a role in sex differentiation processes.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subcellular location	Cytoplasm. Membrane; Peripheral membrane protein. Note= Membrane-associated after cell stimulation leading to its translocation. Tyrosine phosphorylation seems to occur only at the plasma membrane.
Tissue specificity	Highly expressed in heart, brain, liver and testis, also expressed in embryonic cells.
Post-translational modification	Phosphorylated on tyrosine and serine/threonine. Phosphorylation on Ser-244 in the activation loop is required for full activity. PDK1 itself can autophosphorylate Ser-244, leading to its own activation By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PDK1 subfamily. Contains 1 PH domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	hyperosmotic response Inferred from direct assay. Source: MGI signal transduction Ref.1 Traceable author statement. Source: MGI
Cellular component	cytoplasmic membrane-bounded vesicle Inferred from direct assay. Source: MGI
Molecular function	3-phosphoinositide-dependent protein kinase activity Ref.1 Inferred from direct assay. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 559	559	3-phosphoinositide-dependent protein kinase 1
Regions
	Domain	85 – 345	261	Protein kinase
	Domain	462 – 553	92	PH
	Nucleotide binding	91 – 99	9	ATP By similarity
	Compositional bias	392 – 401	10	Poly-Ser
Sites
	Active site	208	1	Proton acceptor By similarity
	Binding site	114	1	ATP By similarity
Amino acid modifications
	Modified residue	9	1	Phosphotyrosine By similarity
	Modified residue	25	1	Phosphoserine By similarity
	Modified residue	244	1	Phosphoserine; by autocatalysis By similarity
	Modified residue	248	1	Phosphothreonine By similarity
	Modified residue	376	1	Phosphotyrosine By similarity
	Modified residue	379	1	Phosphotyrosine By similarity
	Modified residue	396	1	Phosphoserine By similarity
	Modified residue	399	1	Phosphoserine By similarity
	Modified residue	406	1	Phosphoserine By similarity
	Modified residue	413	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	84	1	D → N in AAC67544. Ref.1
	Sequence conflict	248	1	T → P in AAC96115. Ref.3
	Sequence conflict	285	1	F → S in AAC96115. Ref.3
	Sequence conflict	546	1	W → R in AAC96115. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9Z2A0-1 [UniParc]. Last modified October 18, 2001. Version 2. Checksum: F2A617A27460FAC9	FASTA	559	63,759
	10 20 30 40 50 60 MARTTSQLYD AVPIQSSVVL CSCPSPSMVR SQTEPGSSPG IPSGVSRQGS TMDGTTAEAR 70 80 90 100 110 120 PSTNPLQQHP AQLPPQPRKK RPEDFKFGKI LGEGSFSTVV LARELATSRE YAIKILEKRH 130 140 150 160 170 180 IIKENKVPYV TRERDVMSRL DHPFFVKLYF TFQDDEKLYF GLSYAKNGEL LKYIRKIGSF 190 200 210 220 230 240 DETCTRFYTA EIVSALEYLH GKGIIHRDLK PENILLNEDM HIQITDFGTA KVLSPESKQA 250 260 270 280 290 300 RANSFVGTAQ YVSPELLTEK SACKSSDLWA LGCIIYQLVA GLPPFRAGNE YLIFQKIIKL 310 320 330 340 350 360 EYHFPEKFFP KARDLVEKLL VLDATKRLGC EEMEGYGPLK AHPFFETITW ENLHQQTPPK 370 380 390 400 410 420 LTAYLPAMSE DDEDCYGNYD NLLSQFGFMQ VSSSSSSHSL STVETSLPQR SGSNIEQYIH 430 440 450 460 470 480 DLDTNSFELD LQFSEDEKRL LLEKQAGGNP WHQFVENNLI LKMGPVDKRK GLFARRRQLL 490 500 510 520 530 540 LTEGPHLYYV DPVNKVLKGE IPWSQELRPE AKNFKTFFVH TPNRTYYLMD PSGNAHKWCR 550 KIQEVWRQQY QSNPDAAVQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure, tissue distribution, and expression of mouse phosphoinositide-dependent protein kinase-1, a protein kinase that phosphorylates and activates protein kinase C zeta." Dong L.Q., Zhang R.-B., Langlais P., He H., Clark M., Zhu L., Liu F. J. Biol. Chem. 274:8117-8122(1999) [PubMed: 10075713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	"Mouse phosphoinositide-dependent protein kinase 1 (mPDK1)." Park J., Hemmings B.A. Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[3]	Xu P., Taylor S. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6.
[4]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, MASS SPECTROMETRY. Tissue: Brain cortex.
[5]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF086625 mRNA. Translation: AAC67544.1. AF126294 mRNA. Translation: AAD38505.1. AF079535 mRNA. Translation: AAC96115.1.
RefSeq	NP_035192.2.
UniGene	Mm.10504
3D structure databases
HSSP	HSSP built from PDB template 1H1W based on UniProtKB O15530.
SMR	Q9Z2A0. Positions 75-361, 412-559.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Z2A0.
PTM databases
PhosphoSite	Q9Z2A0.
Genome annotation databases
Ensembl	ENSMUSG00000024122. Mus musculus. [Contig view]
GeneID	18607.
Organism-specific databases
MGI	MGI:1338068. Pdpk1.
Phylogenomic databases
HOGENOM	Q9Z2A0.
HOVERGEN	Q9Z2A0.
Gene expression databases
ArrayExpress	Q9Z2A0.
CleanEx	MM_PDK1. MM_PDPK1.
GermOnline	ENSMUSG00000024122. Mus musculus.
Family and domain databases
InterPro	IPR001849. PH. IPR011993. PH_type. IPR015746. PK1_3-phosphoinositide. IPR000719. Prot_kinase_core. IPR017441. Protein_kinase_ATP_bd_CS. IPR017442. Se/Thr_pkinase-rel. IPR008271. Ser_thr_pkin_AS. IPR002290. Ser_thr_pkinase. [Graphical view]
Gene3D	G3DSA:2.30.29.30. PH_type. 1 hit.
PANTHER	PTHR22985:SF93. PK1_3-phosphoinositide. 1 hit.
Pfam	PF00069. Pkinase. 1 hit. [Graphical view]
ProDom	PD000001. Prot_kinase. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00220. S_TKc. 1 hit. [Graphical view]
PROSITE	PS50003. PH_DOMAIN. False negative. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
BLOCKS	Search...
Other Resources
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

PDPK1_MOUSE

Accession

Primary (citable) accession number: Q9Z2A0
Secondary accession number(s): Q9R1D8, Q9R215

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 18, 2001
Last sequence update:	October 18, 2001
Last modified:	July 22, 2008
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)