CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-033674
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
123RHIIKENKVPYVTREubiquitination[1]
280LEYDFPEKFFPKARDacetylation[1, 2, 3]
280LEYDFPEKFFPKARDubiquitination[4]
299LLVLDATKRLGCEEMubiquitination[5]
417EKRLLLEKQAGGNPWubiquitination[5]
Reference
 [1] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [2] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [3] 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]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961
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
MARTTSQLYD AVPIQSSVVL CSCPSPSMVR TQTESSTPPG IPGGSRQGPA MDGTAAEPRP 60
GAGSLQHAQP PPQPRKKRPE DFKFGKILGE GSFSTVVLAR ELATSREYAI KILEKRHIIK 120
ENKVPYVTRE RDVMSRLDHP FFVKLYFTFQ DDEKLYFGLS YAKNGELLKY IRKIGSFDET 180
CTRFYTAEIV SALEYLHGKG IIHRDLKPEN ILLNEDMHIQ ITDFGTAKVL SPESKQGVSD 240
LWALGCIIYQ LVAGLPPFRA GNEYLIFQKI IKLEYDFPEK FFPKARDLVE KLLVLDATKR 300
LGCEEMEGYG PLKAHPFFES VTWENLHQQT PPKLTAYLPA MSEDDEDCYG NYDNLLSQFG 360
CMQVSSSSSS HSLSASDTGL PQRSGSNIEQ YIHDLDSNSF ELDLQFSEDE KRLLLEKQAG 420
GNPWHQFVEN NLILKMGPVD KRKGLFARRR QLLLTEGPHL YYVDPVNKVL KGEIPWSQEL 480
RPEAKNFKTF FVHTPNRTYY LMDPSGNAHK WCRKIQEVWR QRYQSHPDAA VQ 532 
Gene Ontology
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro. 
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