CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-039513
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 3-phosphoinositide-dependent protein kinase 1 
Protein Synonyms/Alias
  
Gene Name
 Pdpk1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
233SPELLTEKSACKSSDubiquitination[1]
272LIFQKIIKLEYHFPEubiquitination[1]
280LEYHFPEKFFPKARDacetylation[2, 3, 4, 5]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [3] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [5] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337] 
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 532 AA 
Protein Sequence
MVRSQTEPGS SPGIPSGVSR QGSTMDGTTA EARPSTNPLQ QHPAQLPPQP RKKRPEDFKF 60
GKILGEGSFS TVVLARELAT SREYAIKILE KRHIIKENKV PYVTRERDVM SRLDHPFFVK 120
LYFTFQDDEK LYFGLSYAKN GELLKYIRKI GSFDETCTRF YTAEIVSALE YLHGKGIIHR 180
DLKPENILLN EDMHIQITDF GTAKVLSPES KQARANSFVG TAQYVSPELL TEKSACKSSD 240
LWALGCIIYQ LVAGLPPFRA GNEYLIFQKI IKLEYHFPEK FFPKARDLVE KLLVLDATKR 300
LGCEEMEGYG PLKAHPFFET ITWENLHQQT PPKLTAYLPA MSEDDEDCYG NYDNLLSQFG 360
FMQVSSSSSS HSLSTVETSL PQRSGSNIEQ YIHDLDTNSF ELDLQFSEDE KRLLLEKQAG 420
GNPWHQFVEN NLILKMGPVD KRKGLFARRR QLLLTEGPHL YYVDPVNKVL KGEIPWSQEL 480
RPEAKNFKTF FVHTPNRTYY LMDPSGNAHK WCRKIQEVWR QQYQSNPDAA VQ 532 
Gene Ontology
 GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0004676; F:3-phosphoinositide-dependent protein kinase activity; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0032148; P:activation of protein kinase B activity; IEA:Compara.
 GO:0032869; P:cellular response to insulin stimulus; IEA:Compara.
 GO:0048041; P:focal adhesion assembly; IEA:Compara.
 GO:0006972; P:hyperosmotic response; IDA:MGI.
 GO:0035556; P:intracellular signal transduction; IEA:Compara.
 GO:0006469; P:negative regulation of protein kinase activity; IEA:Compara.
 GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Compara.
 GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Compara.
 GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; IEA:Compara.
 GO:0042981; P:regulation of apoptotic process; IEA:Compara.
 GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB cascade; IEA:Compara.
 GO:0007165; P:signal transduction; TAS:MGI. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR011993; PH_like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00069; Pkinase 
SMART
 SM00220; S_TKc 
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS