ID F2Z400_MOUSE Unreviewed; 457 AA. AC F2Z400; DT 31-MAY-2011, integrated into UniProtKB/TrEMBL. DT 31-MAY-2011, sequence version 1. DT 16-OCT-2019, entry version 68. 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; Myomorpha; 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; DOI=10.1016/j.cell.2010.12.001; 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 -!- SIMILARITY: Belongs to the protein kinase superfamily. CC {ECO:0000256|RuleBase:RU000304}. 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 SMR; F2Z400; -. DR jPOST; F2Z400; -. DR MaxQB; F2Z400; -. DR PeptideAtlas; F2Z400; -. DR PRIDE; F2Z400; -. DR Ensembl; ENSMUST00000115407; ENSMUSP00000111066; ENSMUSG00000024122. DR MGI; MGI:1338068; Pdpk1. DR eggNOG; KOG0592; Eukaryota. DR eggNOG; ENOG410XRT8; LUCA. DR GeneTree; ENSGT00940000155267; -. DR OMA; QASGNPC; -. DR ChiTaRS; Pdpk1; mouse. DR Proteomes; UP000000589; Chromosome 17. DR Bgee; ENSMUSG00000024122; Expressed in 303 organ(s), highest expression level in rostral migratory stream. DR ExpressionAtlas; F2Z400; baseline and differential. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR Gene3D; 2.30.29.30; -; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR039046; PDPK1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24356:SF163; PTHR24356:SF163; 1. 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 Kinase {ECO:0000256|RuleBase:RU000304}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU000304}; KW Proteomics identification {ECO:0000213|EPD:F2Z400, KW ECO:0000213|MaxQB:F2Z400, ECO:0000213|PeptideAtlas:F2Z400}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Serine/threonine-protein kinase {ECO:0000256|RuleBase:RU000304}; KW Transferase {ECO:0000256|RuleBase:RU000304}. FT DOMAIN 85 345 Protein kinase. {ECO:0000259|PROSITE: FT PS50011}. FT REGION 25 83 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 25 69 Polar. {ECO:0000256|SAM:MobiDB-lite}. 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 //