ID F2Z400_MOUSE Unreviewed; 457 AA. AC F2Z400; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 27-MAY-2015, entry version 28. DE SubName: Full=3-phosphoinositide-dependent protein kinase 1 {ECO:0000313|Ensembl:ENSMUSP00000111066}; GN Name=Pdpk1 {ECO:0000313|Ensembl:ENSMUSP00000111066, GN ECO:0000313|MGI:MGI:1338068}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000111066, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000213|PubMed:15345747} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200; RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; RT "Phosphoproteomic analysis of the developing mouse brain."; RL Mol. Cell. Proteomics 3:1093-1101(2004). RN [2] {ECO:0000213|PubMed:17242355} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000111066, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000111066, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] {ECO:0000213|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and RT expression."; RL Cell 143:1174-1189(2010). RN [5] {ECO:0000313|Ensembl:ENSMUSP00000111066} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000111066}; RG Ensembl; RL Submitted (MAY-2011) to UniProtKB. RN [6] {ECO:0000213|PubMed:23806337} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001; RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., RA Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.; RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic RT pathways."; RL Mol. Cell 50:919-930(2013). CC -!- CAUTION: The sequence shown here is derived from an Ensembl CC automatic analysis pipeline and should be considered as CC preliminary data. {ECO:0000313|Ensembl:ENSMUSP00000111066}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CT010502; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; F2Z400; -. DR SMR; F2Z400; 45-450. DR Ensembl; ENSMUST00000115407; ENSMUSP00000111066; ENSMUSG00000024122. DR MGI; MGI:1338068; Pdpk1. DR GeneTree; ENSGT00550000074819; -. DR ChiTaRS; Pdpk1; mouse. DR NextBio; 35556225; -. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; F2Z400; -. DR ExpressionAtlas; F2Z400; baseline and differential. DR GO; GO:0042995; C:cell projection; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IDA:MGI. DR GO; GO:0097481; C:neuronal postsynaptic density; IDA:MGI. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0004676; F:3-phosphoinositide-dependent protein kinase activity; IDA:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; ISO:MGI. DR GO; GO:0016004; F:phospholipase activator activity; ISO:MGI. DR GO; GO:0043274; F:phospholipase binding; ISO:MGI. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI. DR GO; GO:0032148; P:activation of protein kinase B activity; ISO:MGI. DR GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI. DR GO; GO:0016477; P:cell migration; ISO:MGI. DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISO:MGI. DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI. DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISO:MGI. DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:MGI. DR GO; GO:0006972; P:hyperosmotic response; IDA:MGI. DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISO:MGI. DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISO:MGI. DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; ISO:MGI. DR GO; GO:0090004; P:positive regulation of establishment of protein localization to plasma membrane; ISO:MGI. DR GO; GO:0010518; P:positive regulation of phospholipase activity; ISO:MGI. DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISO:MGI. DR GO; GO:0006468; P:protein phosphorylation; ISO:MGI. DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI. DR GO; GO:0007165; P:signal transduction; TAS:MGI. DR Gene3D; 2.30.29.30; -; 2. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR011993; PH_like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW ATP-binding {ECO:0000256|RuleBase:RU000304}; KW Complete proteome {ECO:0000313|Proteomes:UP000000589}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000304}; KW Proteomics identification {ECO:0000213|MaxQB:F2Z400, KW ECO:0000213|PeptideAtlas:F2Z400}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}. SQ SEQUENCE 457 AA; 51471 MW; E72F7240CED5C5A3 CRC64; MARTTSQLYD AVPIQSSVVL CSCPSPSMVR SQTEPGSSPG IPSGVSRQGS TMDGTTAEAR PSTNPLQQHP AQLPPQPRKK RPEDFKFGKI LGEGSFSTVV LARELATSRE YAIKILEKRH IIKENKVPYV TRERDVMSRL DHPFFVKLYF TFQDDEKLYF GLSYAKNGEL LKYIRKIGSF DETCTRFYTA EIVSALEYLH GKGIIHRDLK PENILLNEDM HIQITDFGTA KVLSPESKQA RANSFVGTAQ YVSPELLTEK SACKSSDLWA LGCIIYQLVA GLPPFRAGNE YLIFQKIIKL EYHFPEKFFP KARDLVEKLL VLDATKRLGC EEMEGYGPLK AHPFFETITW ENLHQQTPPK LTAYLPAMSE DDEDCYGNYD NLLSQFGFMQ VSSSSSSHSL STVETSLPQR SGSNIEQYIH DLDTNSFELD LQFSEDEKRL LLEKQAGGNP CLTGRTT //