PAK1_BOVIN
ID PAK1_BOVIN Reviewed; 544 AA.
AC Q08E52;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Serine/threonine-protein kinase PAK 1 {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000250|UniProtKB:Q13153};
DE AltName: Full=Alpha-PAK {ECO:0000250|UniProtKB:Q13153};
DE AltName: Full=p21-activated kinase 1 {ECO:0000250|UniProtKB:Q13153};
DE Short=PAK-1;
DE AltName: Full=p65-PAK {ECO:0000250|UniProtKB:P35465};
GN Name=PAK1 {ECO:0000250|UniProtKB:Q13153};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION IN PHOSPHORYLATION OF MYL9/MLC2.
RX PubMed=21457715; DOI=10.1016/j.febslet.2011.03.054;
RA Tan I., Lai J., Yong J., Li S.F., Leung T.;
RT "Chelerythrine perturbs lamellar actomyosin filaments by selective
RT inhibition of myotonic dystrophy kinase-related Cdc42-binding kinase.";
RL FEBS Lett. 585:1260-1268(2011).
CC -!- FUNCTION: Protein kinase involved in intracellular signaling pathways
CC downstream of integrins and receptor-type kinases that plays an
CC important role in cytoskeleton dynamics, in cell adhesion, migration,
CC proliferation, apoptosis, mitosis, and in vesicle-mediated transport
CC processes. Can directly phosphorylate BAD and protects cells against
CC apoptosis. Activated by interaction with CDC42 and RAC1. Functions as
CC GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to
CC the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and
CC thereby mediates activation of downstream MAP kinases. Involved in the
CC reorganization of the actin cytoskeleton, actin stress fibers and of
CC focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and
CC thereby plays a role in the regulation of microtubule biogenesis and
CC organization of the tubulin cytoskeleton. Plays a role in the
CC regulation of insulin secretion in response to elevated glucose levels.
CC Part of a ternary complex that contains PAK1, DVL1 and MUSK that is
CC important for MUSK-dependent regulation of AChR clustering during the
CC formation of the neuromuscular junction (NMJ). Activity is inhibited in
CC cells undergoing apoptosis, potentially due to binding of CDC2L1 and
CC CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and
CC 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1
CC translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1
CC binding to BCL2. Phosphorylates SNAI1 at 'Ser-246' promoting its
CC transcriptional repressor activity by increasing its accumulation in
CC the nucleus. In podocytes, promotes NR3C2 nuclear localization.
CC Required for atypical chemokine receptor ACKR2-induced phosphorylation
CC of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from
CC endosomal compartment to cell membrane, increasing its efficiency in
CC chemokine uptake and degradation. In synapses, seems to mediate the
CC regulation of F-actin cluster formation performed by SHANK3, maybe
CC through CFL1 phosphorylation and inactivation. Plays a role in RUFY3-
CC mediated facilitating gastric cancer cells migration and invasion. In
CC response to DNA damage, phosphorylates MORC2 which activates its ATPase
CC activity and facilitates chromatin remodeling (By similarity). In
CC neurons, plays a crucial role in regulating GABA(A) receptor synaptic
CC stability and hence GABAergic inhibitory synaptic transmission through
CC its role in F-actin stabilization (By similarity). In hippocampal
CC neurons, necessary for the formation of dendritic spines and excitatory
CC synapses; this function is dependent on kinase activity and may be
CC exerted by the regulation of actomyosin contractility through the
CC phosphorylation of myosin II regulatory light chain (MLC) (By
CC similarity). Along with GIT1, positively regulates microtubule
CC nucleation during interphase (By similarity).
CC {ECO:0000250|UniProtKB:O88643, ECO:0000250|UniProtKB:P35465,
CC ECO:0000250|UniProtKB:Q13153, ECO:0000269|PubMed:21457715}.
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=2.7.11.1;
CC Evidence={ECO:0000250|UniProtKB:P35465,
CC ECO:0000250|UniProtKB:Q13153};
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=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P35465,
CC ECO:0000250|UniProtKB:Q13153};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Phosphorylation of Thr-84 by OXSR1 inhibits
CC activation (By similarity). Activated by binding small G proteins.
CC Binding of GTP-bound CDC42 or RAC1 to the autoregulatory region
CC releases monomers from the autoinhibited dimer, and enables activation
CC by phosphorylation of Thr-422 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer in its autoinhibited state. Active as monomer.
CC Interacts with GIT1 (By similarity). Component of cytoplasmic
CC complexes, which also contains PXN, ARHGEF7 and GIT1. Interacts with
CC NISCH (By similarity). Interacts with DVL1; mediates the formation of a
CC DVL1, MUSK and PAK1 ternary complex involved in AChR clustering (By
CC similarity). Binds to the caspase-cleaved p110 isoform of CDC2L1 and
CC CDC2L2, p110C, but not the full-length proteins (By similarity).
CC Interacts with ARHGEF7 (By similarity). Interacts tightly with GTP-
CC bound but not GDP-bound CDC42/P21 and RAC1. Probably found in a ternary
CC complex composed of DSCAM, PAK1 and RAC1. Interacts with DSCAM (via
CC cytoplasmic domain); the interaction is direct and enhanced in presence
CC of RAC1. Interacts with SCRIB (By similarity). Interacts with PDPK1 (By
CC similarity). Interacts (via kinase domain) with RAF1 (By similarity).
CC Interacts with NCK1 and NCK2 (By similarity). Interacts with TBCB (By
CC similarity). Interacts with BRSK2 (By similarity). Interacts with SNAI1
CC (By similarity). Interacts with CIB1 (via N-terminal region); the
CC interaction is direct, promotes PAK1 activity and occurs in a calcium-
CC dependent manner. Interacts with INPP5K (By similarity). Interacts with
CC gamma-tubulin (By similarity). {ECO:0000250|UniProtKB:P35465,
CC ECO:0000250|UniProtKB:Q13153}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q13153}. Cell
CC junction, focal adhesion {ECO:0000250|UniProtKB:Q13153}. Cell
CC projection, lamellipodium {ECO:0000250|UniProtKB:Q13153}. Cell membrane
CC {ECO:0000250|UniProtKB:Q13153}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:Q13153}. Cell projection, invadopodium
CC {ECO:0000250|UniProtKB:Q13153}. Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q13153}. Chromosome
CC {ECO:0000250|UniProtKB:Q13153}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q13153}.
CC Note=Recruited to the cell membrane by interaction with CDC42 and RAC1.
CC Recruited to focal adhesions upon activation. Colocalized with CIB1
CC within membrane ruffles during cell spreading upon readhesion to
CC fibronectin. Colocalizes with RUFY3, F-actin and other core migration
CC components in invadopodia at the cell periphery (By similarity). Upon
CC DNA damage, translocates to the nucleoplasm when phosphorylated at Thr-
CC 212 where is co-recruited with MORC2 on damaged chromatin (By
CC similarity). Localization to the centrosome does not depend upon the
CC presence of gamma-tubulin (By similarity). Localization of the active,
CC but not inactive, protein to the adhesions and edge of lamellipodia is
CC mediated by interaction with GIT1 (By similarity).
CC {ECO:0000250|UniProtKB:P35465, ECO:0000250|UniProtKB:Q13153}.
CC -!- PTM: Autophosphorylated in trans, meaning that in a dimer, one kinase
CC molecule phosphorylates the other one. Activated by autophosphorylation
CC at Thr-422 in response to a conformation change, triggered by
CC interaction with GTP-bound CDC42 or RAC1. Activated by phosphorylation
CC at Thr-422 by BRSK2 and by PDPK1. Phosphorylated by JAK2 in response to
CC PRL; this increases PAK1 kinase activity. Phosphorylated at Ser-21 by
CC PKB/AKT; this reduces interaction with NCK1 and association with focal
CC adhesion sites (By similarity). Upon DNA damage, phosphorylated at Thr-
CC 211 and translocates to the nucleoplasm (By similarity). Phosphorylated
CC at tyrosine residues, which can be enhanced by NTN1 (By similarity).
CC {ECO:0000250|UniProtKB:O88643, ECO:0000250|UniProtKB:P35465,
CC ECO:0000250|UniProtKB:Q13153}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; BC123416; AAI23417.1; -; mRNA.
DR RefSeq; NP_001070366.1; NM_001076898.1.
DR RefSeq; XP_010819137.1; XM_010820835.1.
DR RefSeq; XP_010819138.1; XM_010820836.2.
DR RefSeq; XP_010819139.1; XM_010820837.1.
DR RefSeq; XP_015316619.1; XM_015461133.1.
DR AlphaFoldDB; Q08E52; -.
DR SMR; Q08E52; -.
DR IntAct; Q08E52; 1.
DR MINT; Q08E52; -.
DR STRING; 9913.ENSBTAP00000013448; -.
DR PaxDb; Q08E52; -.
DR PeptideAtlas; Q08E52; -.
DR PRIDE; Q08E52; -.
DR Ensembl; ENSBTAT00000013448; ENSBTAP00000013448; ENSBTAG00000010191.
DR Ensembl; ENSBTAT00000072179; ENSBTAP00000063089; ENSBTAG00000010191.
DR Ensembl; ENSBTAT00000078859; ENSBTAP00000069557; ENSBTAG00000010191.
DR Ensembl; ENSBTAT00000079360; ENSBTAP00000062047; ENSBTAG00000010191.
DR Ensembl; ENSBTAT00000080749; ENSBTAP00000071646; ENSBTAG00000010191.
DR GeneID; 533729; -.
DR KEGG; bta:533729; -.
DR CTD; 5058; -.
DR VEuPathDB; HostDB:ENSBTAG00000010191; -.
DR VGNC; VGNC:53657; PAK1.
DR eggNOG; KOG0578; Eukaryota.
DR GeneTree; ENSGT00950000182988; -.
DR HOGENOM; CLU_000288_26_6_1; -.
DR InParanoid; Q08E52; -.
DR OMA; IEISTPY; -.
DR OrthoDB; 757766at2759; -.
DR TreeFam; TF105351; -.
DR Reactome; R-BTA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-BTA-3928664; Ephrin signaling.
DR Reactome; R-BTA-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-BTA-5627123; RHO GTPases activate PAKs.
DR Reactome; R-BTA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-BTA-8964616; G beta:gamma signalling through CDC42.
DR Reactome; R-BTA-9013404; RAC2 GTPase cycle.
DR Reactome; R-BTA-9013406; RHOQ GTPase cycle.
DR Reactome; R-BTA-9013420; RHOU GTPase cycle.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000010191; Expressed in prefrontal cortex and 103 other tissues.
DR GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005518; F:collagen binding; ISS:UniProtKB.
DR GO; GO:0043015; F:gamma-tubulin binding; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0060244; P:negative regulation of cell proliferation involved in contact inhibition; ISS:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; ISS:UniProtKB.
DR GO; GO:0090063; P:positive regulation of microtubule nucleation; ISS:UniProtKB.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0050770; P:regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR GO; GO:0042060; P:wound healing; ISS:UniProtKB.
DR CDD; cd01093; CRIB_PAK_like; 1.
DR Gene3D; 3.90.810.10; -; 1.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR036936; CRIB_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR033923; PAK_BD.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00786; PBD; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50108; CRIB; 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 Acetylation; Allosteric enzyme; Apoptosis; ATP-binding; Cell junction;
KW Cell membrane; Cell projection; Chromosome; Cytoplasm; Cytoskeleton;
KW Exocytosis; Kinase; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT CHAIN 2..544
FT /note="Serine/threonine-protein kinase PAK 1"
FT /id="PRO_0000286350"
FT DOMAIN 75..88
FT /note="CRIB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057"
FT DOMAIN 269..520
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..140
FT /note="Autoregulatory region"
FT /evidence="ECO:0000250"
FT REGION 70..105
FT /note="GTPase-binding"
FT /evidence="ECO:0000250"
FT REGION 161..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 388
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 275..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT MOD_RES 21
FT /note="Phosphoserine; by PKB and autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT MOD_RES 84
FT /note="Phosphothreonine; by OXSR1"
FT /evidence="ECO:0000250|UniProtKB:P35465"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT MOD_RES 131
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT MOD_RES 142
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT MOD_RES 144
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P35465"
FT MOD_RES 149
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P35465"
FT MOD_RES 153
FT /note="Phosphotyrosine; by JAK2"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT MOD_RES 184
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT MOD_RES 198
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P35465"
FT MOD_RES 200
FT /note="Phosphotyrosine; by JAK2"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT MOD_RES 203
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P35465"
FT MOD_RES 211
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT MOD_RES 218
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT MOD_RES 224
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88643"
FT MOD_RES 228
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88643"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT MOD_RES 284
FT /note="Phosphotyrosine; by JAK2"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
FT MOD_RES 422
FT /note="Phosphothreonine; by autocatalysis, BRSK2 and PDPK1"
FT /evidence="ECO:0000250|UniProtKB:Q13153"
SQ SEQUENCE 544 AA; 60546 MW; 92A385B77CD46DBF CRC64;
MSNNGLDIQD KPPAPPMRNT STMIGAGSKD AGTLNHGSKP LPPNPEEKKK KDRFYRAILP
GDKTNKKKEK ERPEISLPSD FEHTIHVGFD AVTGEFTGMP EQWARLLQTS NITKSEQKKN
PQAVLDVLEF YNSKKTSNSQ KYMSFTDKSA EDYNSSNTLN VKAVSETPAV PPVSEDEDDD
DDGTPPPVIA PRPEHTKSVY TRSVIEPLPI TPTRDVATSP ISPTENNTTP PDALTRNTEK
QKKKPKMSDE EILEKLRSIV SVGDPKKKYT RFEKIGQGAS GTVYTAMDVA TGQEVAIKQM
NLQQQPKKEL IINEILVMRE NKNPNIVNYL DSYLVGDELW VVMEYLAGGS LTDVVTETCM
DEGQIAAVCR ECLQALEFLH SNQVIHRDIK SDNILLGMDG SVKLTDFGFC AQITPEQSKR
STMVGTPYWM APEVVTRKAY GPKVDIWSLG IMAIEMIEGE PPYLNENPLR ALYLIATNGT
PELQNPEKLS AIFRDFLNRC LEMDVEKRGS AKELLQHQFL KIAKPLSSLT PLIAAAKEAT
KNNH
