ID KAPCA_CRIGR Reviewed; 351 AA. AC P25321; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 11-DEC-2019, entry version 137. DE RecName: Full=cAMP-dependent protein kinase catalytic subunit alpha; DE Short=PKA C-alpha; DE EC=2.7.11.11; GN Name=PRKACA; OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; OC Cricetidae; Cricetinae; Cricetulus. OX NCBI_TaxID=10029; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=1645343; RA Howard P., Day K.H., Kim K.E., Richardson J., Thomas J., Abraham I., RA Fleischmann R.D., Gottesman M.M., Maurer R.A.; RT "Decreased catalytic subunit mRNA levels and altered catalytic subunit mRNA RT structure in a cAMP-resistant Chinese hamster ovary cell line."; RL J. Biol. Chem. 266:10189-10195(1991). CC -!- FUNCTION: Phosphorylates a large number of substrates in the cytoplasm CC and the nucleus. Regulates the abundance of compartmentalized pools of CC its regulatory subunits through phosphorylation of PJA2 which binds and CC ubiquitinates these subunits, leading to their subsequent proteolysis. CC Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA CC and VASP. RORA is activated by phosphorylation. Required for glucose- CC mediated adipogenic differentiation increase and osteogenic CC differentiation inhibition from osteoblasts. Involved in the regulation CC of platelets in response to thrombin and collagen; maintains CC circulating platelets in a resting state by phosphorylating proteins in CC numerous platelet inhibitory pathways when in complex with NF-kappa-B CC (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and CC collagen disrupt these complexes and free active PRKACA stimulates CC platelets and leads to platelet aggregation by phosphorylating VASP. CC Prevents the antiproliferative and anti-invasive effects of alpha- CC difluoromethylornithine in breast cancer cells when activated. RYR2 CC channel activity is potentiated by phosphorylation in presence of CC luminal Ca(2+), leading to reduced amplitude and increased frequency of CC store overload-induced Ca(2+) release (SOICR) characterized by an CC increased rate of Ca(2+) release and propagation velocity of CC spontaneous Ca(2+) waves, despite reduced wave amplitude and resting CC cytosolic Ca(2+). PSMC5/RPT6 activation by phosphorylation stimulates CC proteasome. Negatively regulates tight junctions (TJs) in ovarian CC cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes CC NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by CC down-regulating the Hedgehog (Hh) signaling pathway that determines CC embryo pattern formation and morphogenesis. Prevents meiosis resumption CC in prophase-arrested oocytes via CDC25B inactivation by CC phosphorylation. May also regulate rapid eye movement (REM) sleep in CC the pedunculopontine tegmental (PPT) (By similarity). Phosphorylates CC APOBEC3G and AICDA (By similarity). Phosphorylates HSF1; this CC phosphorylation promotes HSF1 nuclear localization and transcriptional CC activity upon heat shock (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:P17612}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.11.11; CC -!- ACTIVITY REGULATION: Allosterically activated by various compounds, CC including ATP. Activated by cAMP; the nucleotide acts as a dynamic and CC allosteric activator by coupling the two lobes of apo PKA, enhancing CC the enzyme dynamics synchronously and priming it for catalysis. CC -!- SUBUNIT: A number of inactive tetrameric holoenzymes are produced by CC the combination of homo- or heterodimers of the different regulatory CC subunits associated with two catalytic subunits. cAMP causes the CC dissociation of the inactive holoenzyme into a dimer of regulatory CC subunits bound to four cAMP and two free monomeric catalytic subunits. CC Activates cAMP-sensitive PKAI and PKAII holoenzymes by interacting with CC regulatory subunit (R) of PKA, PRKAR1A/PKR1 and PRKAR2A/PKR2, CC respectively. Interacts with NFKB1, NFKB2 and NFKBIA in platelets; CC these interactions are disrupted by thrombin and collagen. Binds to CC ABL1 in spermatozoa and with CDC25B in oocytes (By similarity). CC Interacts with APOBEC3G and AICDA (By similarity). Interacts with CC RAB13; downstream effector of RAB13 involved in tight junction assembly CC (By similarity). Found in a complex at least composed of MROH2B, PRKACA CC and TCP11 (By similarity). Interacts with MROH2B (By similarity). CC Interacts with TCP11 (By similarity). Interacts with HSF1 (By CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P05132, CC ECO:0000250|UniProtKB:P17612}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. CC Cell membrane {ECO:0000250}. Mitochondrion {ECO:0000250}. Membrane CC {ECO:0000250|UniProtKB:P17612}; Lipid-anchor CC {ECO:0000250|UniProtKB:P17612}. Cell projection, cilium, flagellum CC {ECO:0000250|UniProtKB:P05132}. Cytoplasmic vesicle, secretory vesicle, CC acrosome {ECO:0000250|UniProtKB:P05132}. Note=Translocates into the CC nucleus (monomeric catalytic subunit). The inactive holoenzyme is found CC in the cytoplasm. Distributed throughout the cytoplasm in meiotically CC incompetent oocytes. Associated to mitochondrion as meiotic competence CC is acquired. Aggregates around the germinal vesicles (GV) at the CC immature GV stage oocytes (By similarity). Expressed in the midpiece CC region of the sperm flagellum (By similarity). Colocalizes with MROH2B CC and TCP11 on the acrosome and tail regions in round spermatids and CC spermatozoa regardless of the capacitation status of the sperm (By CC similarity). Colocalizes with HSF1 in nuclear stress bodies (nSBs) upon CC heat shock (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P05132, CC ECO:0000250|UniProtKB:P17612}. CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in mammalian tissues. CC -!- PTM: Asn-3 is partially deaminated to Asp giving rise to 2 major CC isoelectric variants, called CB and CA respectively. {ECO:0000250}. CC -!- PTM: Autophosphorylated. Phosphorylation is enhanced by vitamin K(2). CC Phosphorylated on threonine and serine residues. Phosphorylation on CC Thr-198 is required for full activity (By similarity). {ECO:0000250}. CC -!- PTM: Phosphorylated at Tyr-331 by activated receptor tyrosine kinases CC EGFR and PDGFR; this increases catalytic efficiency. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr CC protein kinase family. cAMP subfamily. {ECO:0000305}. 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; M63311; AAA37010.1; -; mRNA. DR PIR; B40384; OKHYCA. DR PDB; 4WIH; X-ray; 1.14 A; A=1-351. DR PDB; 5LCP; X-ray; 1.43 A; A=1-351. DR PDB; 5LCQ; X-ray; 1.42 A; A=1-351. DR PDB; 5LCR; X-ray; 1.56 A; A=1-351. DR PDB; 5LCT; X-ray; 1.61 A; A=1-351. DR PDB; 5LCU; X-ray; 1.58 A; A=1-351. DR PDB; 5M0B; X-ray; 1.51 A; A=1-351. DR PDB; 5M0C; X-ray; 1.73 A; A=1-351. DR PDB; 5M0L; X-ray; 1.47 A; A=1-351. DR PDB; 5M0U; X-ray; 1.67 A; A=1-351. DR PDB; 5M6V; X-ray; 1.42 A; A=1-351. DR PDB; 5M6Y; X-ray; 1.37 A; A=1-351. DR PDB; 5M71; X-ray; 1.49 A; A=1-351. DR PDB; 5M75; X-ray; 1.54 A; A=1-351. DR PDB; 5MHI; X-ray; 1.49 A; A=1-351. DR PDB; 5N1D; X-ray; 1.61 A; A=1-351. DR PDB; 5N1E; X-ray; 1.53 A; A=1-351. DR PDB; 5N1F; X-ray; 1.12 A; A=1-351. DR PDB; 5N1G; X-ray; 1.14 A; A=1-351. DR PDB; 5N1H; X-ray; 1.18 A; A=1-351. DR PDB; 5N1K; X-ray; 1.80 A; A=1-351. DR PDB; 5N1L; X-ray; 1.49 A; A=1-351. DR PDB; 5N1M; X-ray; 1.44 A; A=1-351. DR PDB; 5N1N; X-ray; 1.41 A; A=1-351. DR PDB; 5N1O; X-ray; 1.80 A; A=1-351. DR PDB; 5N32; X-ray; 1.83 A; A=1-351. DR PDB; 5N33; X-ray; 1.43 A; A=1-351. DR PDB; 5N36; X-ray; 1.58 A; A=1-351. DR PDB; 5N37; X-ray; 1.59 A; A=1-351. DR PDB; 5N39; X-ray; 1.45 A; A=1-351. DR PDB; 5N3A; X-ray; 1.40 A; A=1-351. DR PDB; 5N3B; X-ray; 1.64 A; A=1-351. DR PDB; 5N3C; X-ray; 1.77 A; A=1-351. DR PDB; 5N3D; X-ray; 1.77 A; A=1-351. DR PDB; 5N3E; X-ray; 1.53 A; A=1-351. DR PDB; 5N3F; X-ray; 1.68 A; A=1-351. DR PDB; 5N3G; X-ray; 1.16 A; A=1-351. DR PDB; 5N3H; X-ray; 1.36 A; A=1-351. DR PDB; 5N3I; X-ray; 1.14 A; A=1-351. DR PDB; 5N3J; X-ray; 1.12 A; A=1-351. DR PDB; 5N3K; X-ray; 1.33 A; A=1-351. DR PDB; 5N3L; X-ray; 1.38 A; A=1-351. DR PDB; 5N3M; X-ray; 1.23 A; A=1-351. DR PDB; 5N3N; X-ray; 1.22 A; A=1-351. DR PDB; 5N3O; X-ray; 1.32 A; A=1-351. DR PDB; 5N3P; X-ray; 1.58 A; A=1-351. DR PDB; 5N3Q; X-ray; 1.31 A; A=1-351. DR PDB; 5N3R; X-ray; 1.36 A; A=1-351. DR PDB; 5N3S; X-ray; 1.14 A; A=1-351. DR PDB; 5N3T; X-ray; 1.21 A; A=1-351. DR PDB; 5N7P; X-ray; 1.50 A; A=1-351. DR PDB; 5N7U; X-ray; 1.37 A; A=1-351. DR PDB; 5NTJ; X-ray; 1.56 A; A=1-351. DR PDB; 5NW8; X-ray; 2.09 A; A=1-351. DR PDB; 5O0E; X-ray; 1.50 A; A=1-351. DR PDB; 5O5M; X-ray; 1.58 A; A=1-351. DR PDB; 5OK3; X-ray; 1.59 A; A=1-351. DR PDB; 5OL3; X-ray; 1.58 A; A=1-351. DR PDB; 5OT3; X-ray; 2.04 A; A=1-351. DR PDB; 5OTG; X-ray; 1.73 A; A=1-351. DR PDB; 5OUA; X-ray; 1.67 A; A=1-351. DR PDB; 5OUC; X-ray; 1.46 A; A=1-351. DR PDB; 5OUS; X-ray; 2.21 A; A=1-351. DR PDB; 6EGW; X-ray; 1.74 A; A=1-351. DR PDB; 6EH0; X-ray; 1.49 A; A=1-351. DR PDB; 6EH2; X-ray; 1.76 A; A=1-351. DR PDB; 6EH3; X-ray; 1.95 A; A=1-351. DR PDB; 6EM2; X-ray; 1.30 A; A=1-351. DR PDB; 6EM6; X-ray; 1.64 A; A=1-351. DR PDB; 6EM7; X-ray; 1.24 A; A=1-351. DR PDB; 6EMA; X-ray; 1.88 A; A=1-351. DR PDB; 6EMB; X-ray; 1.75 A; A=1-351. DR PDB; 6EMD; X-ray; 1.91 A; A=1-351. DR PDB; 6EME; X-ray; 1.68 A; A=1-351. DR PDB; 6ERS; X-ray; 1.82 A; A=1-351. DR PDB; 6ERT; X-ray; 1.80 A; A=1-351. DR PDB; 6ERU; X-ray; 2.15 A; A=1-351. DR PDB; 6ERV; X-ray; 2.06 A; A=1-351. DR PDB; 6ERW; X-ray; 1.89 A; A=1-351. DR PDB; 6ESA; X-ray; 1.31 A; A=1-351. DR PDB; 6F14; X-ray; 1.87 A; A=1-351. DR PDB; 6I2A; X-ray; 1.75 A; A=1-351. DR PDB; 6I2B; X-ray; 1.97 A; A=1-351. DR PDB; 6I2C; X-ray; 1.82 A; A=1-351. DR PDB; 6I2D; X-ray; 1.91 A; A=1-351. DR PDBsum; 4WIH; -. DR PDBsum; 5LCP; -. DR PDBsum; 5LCQ; -. DR PDBsum; 5LCR; -. DR PDBsum; 5LCT; -. DR PDBsum; 5LCU; -. DR PDBsum; 5M0B; -. DR PDBsum; 5M0C; -. DR PDBsum; 5M0L; -. DR PDBsum; 5M0U; -. DR PDBsum; 5M6V; -. DR PDBsum; 5M6Y; -. DR PDBsum; 5M71; -. DR PDBsum; 5M75; -. DR PDBsum; 5MHI; -. DR PDBsum; 5N1D; -. DR PDBsum; 5N1E; -. DR PDBsum; 5N1F; -. DR PDBsum; 5N1G; -. DR PDBsum; 5N1H; -. DR PDBsum; 5N1K; -. DR PDBsum; 5N1L; -. DR PDBsum; 5N1M; -. DR PDBsum; 5N1N; -. DR PDBsum; 5N1O; -. DR PDBsum; 5N32; -. DR PDBsum; 5N33; -. DR PDBsum; 5N36; -. DR PDBsum; 5N37; -. DR PDBsum; 5N39; -. DR PDBsum; 5N3A; -. DR PDBsum; 5N3B; -. DR PDBsum; 5N3C; -. DR PDBsum; 5N3D; -. DR PDBsum; 5N3E; -. DR PDBsum; 5N3F; -. DR PDBsum; 5N3G; -. DR PDBsum; 5N3H; -. DR PDBsum; 5N3I; -. DR PDBsum; 5N3J; -. DR PDBsum; 5N3K; -. DR PDBsum; 5N3L; -. DR PDBsum; 5N3M; -. DR PDBsum; 5N3N; -. DR PDBsum; 5N3O; -. DR PDBsum; 5N3P; -. DR PDBsum; 5N3Q; -. DR PDBsum; 5N3R; -. DR PDBsum; 5N3S; -. DR PDBsum; 5N3T; -. DR PDBsum; 5N7P; -. DR PDBsum; 5N7U; -. DR PDBsum; 5NTJ; -. DR PDBsum; 5NW8; -. DR PDBsum; 5O0E; -. DR PDBsum; 5O5M; -. DR PDBsum; 5OK3; -. DR PDBsum; 5OL3; -. DR PDBsum; 5OT3; -. DR PDBsum; 5OTG; -. DR PDBsum; 5OUA; -. DR PDBsum; 5OUC; -. DR PDBsum; 5OUS; -. DR PDBsum; 6EGW; -. DR PDBsum; 6EH0; -. DR PDBsum; 6EH2; -. DR PDBsum; 6EH3; -. DR PDBsum; 6EM2; -. DR PDBsum; 6EM6; -. DR PDBsum; 6EM7; -. DR PDBsum; 6EMA; -. DR PDBsum; 6EMB; -. DR PDBsum; 6EMD; -. DR PDBsum; 6EME; -. DR PDBsum; 6ERS; -. DR PDBsum; 6ERT; -. DR PDBsum; 6ERU; -. DR PDBsum; 6ERV; -. DR PDBsum; 6ERW; -. DR PDBsum; 6ESA; -. DR PDBsum; 6F14; -. DR PDBsum; 6I2A; -. DR PDBsum; 6I2B; -. DR PDBsum; 6I2C; -. DR PDBsum; 6I2D; -. DR SMR; P25321; -. DR STRING; 10029.XP_007612815.1; -. DR PRIDE; P25321; -. DR Ensembl; ENSCGRT00001021270; ENSCGRP00001017026; ENSCGRG00001017184. DR BRENDA; 2.7.11.11; 1309. DR GO; GO:0001669; C:acrosomal vesicle; ISS:UniProtKB. DR GO; GO:0005930; C:axoneme; IEA:Ensembl. DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IEA:Ensembl. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0005813; C:centrosome; IEA:Ensembl. DR GO; GO:0097546; C:ciliary base; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0043197; C:dendritic spine; IEA:Ensembl. DR GO; GO:0045171; C:intercellular bridge; IEA:Ensembl. DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. DR GO; GO:0031594; C:neuromuscular junction; IEA:Ensembl. DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0044853; C:plasma membrane raft; IEA:Ensembl. DR GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; ISS:UniProtKB. DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl. DR GO; GO:0030145; F:manganese ion binding; IEA:Ensembl. DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl. DR GO; GO:0034237; F:protein kinase A regulatory subunit binding; IEA:Ensembl. DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl. DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB. DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:Ensembl. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl. DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl. DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB. DR GO; GO:0071374; P:cellular response to parathyroid hormone stimulus; IEA:Ensembl. DR GO; GO:0001707; P:mesoderm formation; IEA:Ensembl. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl. DR GO; GO:0006397; P:mRNA processing; IEA:Ensembl. DR GO; GO:1901621; P:negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IEA:Ensembl. DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl. DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl. DR GO; GO:0071158; P:positive regulation of cell cycle arrest; IEA:Ensembl. DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:Ensembl. DR GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl. DR GO; GO:0010737; P:protein kinase A signaling; IEA:InterPro. DR GO; GO:2000810; P:regulation of bicellular tight junction assembly; IEA:Ensembl. DR GO; GO:0045667; P:regulation of osteoblast differentiation; IEA:Ensembl. DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IEA:Ensembl. DR GO; GO:0070613; P:regulation of protein processing; IEA:Ensembl. DR GO; GO:0048240; P:sperm capacitation; IEA:Ensembl. DR InterPro; IPR000961; AGC-kinase_C. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR039035; PKA_C-alpha. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24353:SF82; PTHR24353:SF82; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00133; S_TK_X; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS51285; AGC_KINASE_CTER; 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 3D-structure; ATP-binding; cAMP; Cell membrane; Cell projection; Cilium; KW Cytoplasm; Cytoplasmic vesicle; Flagellum; Kinase; Lipoprotein; Membrane; KW Mitochondrion; Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; KW Serine/threonine-protein kinase; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P00517" FT CHAIN 2..351 FT /note="cAMP-dependent protein kinase catalytic subunit FT alpha" FT /id="PRO_0000086051" FT DOMAIN 44..298 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT DOMAIN 299..351 FT /note="AGC-kinase C-terminal" FT NP_BIND 50..58 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT NP_BIND 122..128 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT NP_BIND 169..172 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT ACT_SITE 167 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 73 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 3 FT /note="Deamidated asparagine" FT /evidence="ECO:0000250" FT MOD_RES 11 FT /note="Phosphoserine; by autocatalysis" FT /evidence="ECO:0000250|UniProtKB:P05132" FT MOD_RES 49 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P17612" FT MOD_RES 140 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P05132" FT MOD_RES 196 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P17612" FT MOD_RES 198 FT /note="Phosphothreonine; by PDPK1" FT /evidence="ECO:0000250|UniProtKB:P00517" FT MOD_RES 331 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P05132" FT MOD_RES 339 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00517" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000250|UniProtKB:P17612" FT HELIX 14..32 FT /evidence="ECO:0000244|PDB:5N1F" FT HELIX 41..43 FT /evidence="ECO:0000244|PDB:5N1F" FT STRAND 44..52 FT /evidence="ECO:0000244|PDB:5N1F" FT STRAND 54..63 FT /evidence="ECO:0000244|PDB:5N1F" FT TURN 64..66 FT /evidence="ECO:0000244|PDB:5N1F" FT STRAND 69..76 FT /evidence="ECO:0000244|PDB:5N1F" FT HELIX 77..82 FT /evidence="ECO:0000244|PDB:5N1F" FT HELIX 86..98 FT /evidence="ECO:0000244|PDB:5N1F" FT STRAND 107..112 FT /evidence="ECO:0000244|PDB:5N1F" FT STRAND 114..122 FT /evidence="ECO:0000244|PDB:5N1F" FT HELIX 129..136 FT /evidence="ECO:0000244|PDB:5N1F" FT HELIX 141..160 FT /evidence="ECO:0000244|PDB:5N1F" FT HELIX 170..172 FT /evidence="ECO:0000244|PDB:5N1F" FT STRAND 173..175 FT /evidence="ECO:0000244|PDB:5N1F" FT STRAND 181..183 FT /evidence="ECO:0000244|PDB:5N1F" FT STRAND 199..201 FT /evidence="ECO:0000244|PDB:5M0U" FT HELIX 203..205 FT /evidence="ECO:0000244|PDB:5N1F" FT HELIX 208..211 FT /evidence="ECO:0000244|PDB:5N1F" FT STRAND 212..214 FT /evidence="ECO:0000244|PDB:5LCQ" FT HELIX 219..234 FT /evidence="ECO:0000244|PDB:5N1F" FT HELIX 244..252 FT /evidence="ECO:0000244|PDB:5N1F" FT HELIX 264..273 FT /evidence="ECO:0000244|PDB:5N1F" FT HELIX 278..280 FT /evidence="ECO:0000244|PDB:5N1F" FT TURN 286..289 FT /evidence="ECO:0000244|PDB:5N1F" FT HELIX 290..293 FT /evidence="ECO:0000244|PDB:5N1F" FT HELIX 296..298 FT /evidence="ECO:0000244|PDB:5N1F" FT HELIX 303..307 FT /evidence="ECO:0000244|PDB:5N1F" FT HELIX 325..327 FT /evidence="ECO:0000244|PDB:5OUS" FT TURN 345..350 FT /evidence="ECO:0000244|PDB:5N1F" SQ SEQUENCE 351 AA; 40620 MW; 84333CD0B439F356 CRC64; MGNAAAAKKG SEQESVKEFL AKAKEEFLKK WESPSQNTAQ LDHFDRIKTL GTGSFGRVML VKHKETGNHY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVKLEFS FKDNSNLYMV MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDQQGY IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVN DIKNHKWFAT TDWIAIYQRK VEAPFIPKFK GPGDTSNFDD YEEEEIRVSI NEKCGKEFTE F //