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Protein kinase C epsilon type (EC 2.7.11.13) (nPKC-epsilon)

 KPCE_MOUSE              Reviewed;         737 AA.
P16054;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
20-DEC-2017, entry version 186.
RecName: Full=Protein kinase C epsilon type;
EC=2.7.11.13;
AltName: Full=nPKC-epsilon;
Name=Prkce; Synonyms=Pkce, Pkcea;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2917656; DOI=10.1016/0014-5793(89)80160-7;
Schaap D., Parker P.J., Bristol A., Kriz R., Knopf J.;
"Unique substrate specificity and regulatory properties of PKC-
epsilon: a rationale for diversity.";
FEBS Lett. 243:351-357(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=9467942; DOI=10.1038/sj.onc.1201507;
Wang Q.J., Acs P., Goodnight J., Blumberg P.M., Mischak H.,
Mushinski J.F.;
"The catalytic domain of PKC-epsilon, in reciprocal PKC-delta and
- epsilon chimeras, is responsible for conferring tumorgenicity to
NIH3T3 cells, whereas both regulatory and catalytic domains of PKC-
epsilon contribute to in vitro transformation.";
Oncogene 16:53-60(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Wheeler D.L.;
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[4]
FUNCTION, INTERACTION WITH ACTIN, AND ACTIN-BINDING MOTIF.
PubMed=11746497; DOI=10.1002/jcb.1246;
Hernandez R.M., Wescott G.G., Mayhew M.W., McJilton M.A.,
Terrian D.M.;
"Biochemical and morphogenic effects of the interaction between
protein kinase C-epsilon and actin in vitro and in cultured NIH3T3
cells.";
J. Cell. Biochem. 83:532-546(2001).
[5]
FUNCTION IN PHOSPHORYLATION OF PRKD1.
PubMed=12407104; DOI=10.1074/jbc.M208075200;
Waldron R.T., Rozengurt E.;
"Protein kinase C phosphorylates protein kinase D activation loop
Ser744 and Ser748 and releases autoinhibition by the pleckstrin
homology domain.";
J. Biol. Chem. 278:154-163(2003).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-710, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[7]
FUNCTION.
PubMed=15949469; DOI=10.1016/j.cardiores.2005.03.002;
Stawowy P., Margeta C., Blaschke F., Lindschau C., Spencer-Haensch C.,
Leitges M., Biagini G., Fleck E., Graf K.;
"Protein kinase C epsilon mediates angiotensin II-induced activation
of beta1-integrins in cardiac fibroblasts.";
Cardiovasc. Res. 67:50-59(2005).
[8]
FUNCTION IN PHOSPHORYLATION OF VIM.
PubMed=16270034; DOI=10.1038/sj.emboj.7600847;
Ivaska J., Vuoriluoto K., Huovinen T., Izawa I., Inagaki M.,
Parker P.J.;
"PKCepsilon-mediated phosphorylation of vimentin controls integrin
recycling and motility.";
EMBO J. 24:3834-3845(2005).
[9]
FUNCTION IN PHOSPHORYLATION OF TNNI3.
PubMed=16445938; DOI=10.1016/j.yjmcc.2005.12.009;
Scruggs S.B., Walker L.A., Lyu T., Geenen D.L., Solaro R.J.,
Buttrick P.M., Goldspink P.H.;
"Partial replacement of cardiac troponin I with a non-phosphorylatable
mutant at serines 43/45 attenuates the contractile dysfunction
associated with PKCepsilon phosphorylation.";
J. Mol. Cell. Cardiol. 40:465-473(2006).
[10]
FUNCTION IN PHOSPHORYLATION OF TICAM2/TRAM.
PubMed=16757566; DOI=10.1073/pnas.0600462103;
McGettrick A.F., Brint E.K., Palsson-McDermott E.M., Rowe D.C.,
Golenbock D.T., Gay N.J., Fitzgerald K.A., O'Neill L.A.J.;
"Trif-related adapter molecule is phosphorylated by PKCepsilon during
Toll-like receptor 4 signaling.";
Proc. Natl. Acad. Sci. U.S.A. 103:9196-9201(2006).
[11]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-729, AND MUTAGENESIS OF
SER-729.
PubMed=17611075; DOI=10.1016/j.cellsig.2007.05.009;
Xu T.R., He G., Dobson K., England K., Rumsby M.;
"Phosphorylation at Ser729 specifies a Golgi localisation for protein
kinase C epsilon (PKCepsilon) in 3T3 fibroblasts.";
Cell. Signal. 19:1986-1995(2007).
[12]
PHOSPHORYLATION AT SER-234; SER-316 AND SER-368.
PubMed=18237277; DOI=10.1042/bj20071348;
Durgan J., Cameron A.J., Saurin A.T., Hanrahan S., Totty N.,
Messing R.O., Parker P.J.;
"The identification and characterization of novel PKCepsilon
phosphorylation sites provide evidence for functional cross-talk
within the PKC superfamily.";
Biochem. J. 411:319-331(2008).
[13]
FUNCTION, INTERACTION WITH YWHAB, PHOSPHORYLATION AT SER-346; SER-350
AND SER-368, AND MUTAGENESIS OF SER-346 AND SER-368.
PubMed=18604201; DOI=10.1038/ncb1749;
Saurin A.T., Durgan J., Cameron A.J., Faisal A., Marber M.S.,
Parker P.J.;
"The regulated assembly of a PKCepsilon complex controls the
completion of cytokinesis.";
Nat. Cell Biol. 10:891-901(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-329; SER-337;
SER-346; THR-349 AND SER-388, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Brain, and Heart;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Calcium-independent, phospholipid- and diacylglycerol
(DAG)-dependent serine/threonine-protein kinase that plays
essential roles in the regulation of multiple cellular processes
linked to cytoskeletal proteins, such as cell adhesion, motility,
migration and cell cycle, functions in neuron growth and ion
channel regulation, and is involved in immune response, cancer
cell invasion and regulation of apoptosis. Mediates cell adhesion
to the extracellular matrix via integrin-dependent signaling, by
mediating angiotensin-2-induced activation of integrin beta-1
(ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which
phosphorylates and activates PTK2/FAK, leading to the spread of
cardiomyocytes. Involved in the control of the directional
transport of ITGB1 in mesenchymal cells by phosphorylating
vimentin (VIM), an intermediate filament (IF) protein. In
epithelial cells, associates with and phosphorylates keratin-8
(KRT8), which induces targeting of desmoplakin at desmosomes and
regulates cell-cell contact. Phosphorylates IQGAP1, which binds to
CDC42, mediating epithelial cell-cell detachment prior to
migration. During cytokinesis, forms a complex with YWHAB, which
is crucial for daughter cell separation, and facilitates
abscission by a mechanism which may implicate the regulation of
RHOA. In cardiac myocytes, regulates myofilament function and
excitation coupling at the Z-lines, where it is indirectly
associated with F-actin via interaction with COPB1. During
endothelin-induced cardiomyocyte hypertrophy, mediates activation
of PTK2/FAK, which is critical for cardiomyocyte survival and
regulation of sarcomere length. Plays a role in the pathogenesis
of dilated cardiomyopathy via persistent phosphorylation of
troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced
neurite outgrowth and neuron morphological change independently of
its kinase activity, by inhibition of RHOA pathway, activation of
CDC42 and cytoskeletal rearrangement. May be involved in
presynaptic facilitation by mediating phorbol ester-induced
synaptic potentiation. Phosphorylates gamma-aminobutyric acid
receptor subunit gamma-2 (GABRG2), which reduces the response of
GABA receptors to ethanol and benzodiazepines and may mediate
acute tolerance to the intoxicating effects of ethanol. Upon PMA
treatment, phosphorylates the capsaicin- and heat-activated cation
channel TRPV1, which is required for bradykinin-induced
sensitization of the heat response in nociceptive neurons. Is able
to form a complex with PDLIM5 and N-type calcium channel, and may
enhance channel activities and potentiates fast synaptic
transmission by phosphorylating the pore-forming alpha subunit
CACNA1B (CaV2.2). Downstream of TLR4, plays an important role in
the lipopolysaccharide (LPS)-induced immune response by
phosphorylating and activating TICAM2/TRAM, which in turn
activates the transcription factor IRF3 and subsequent cytokines
production. In differentiating erythroid progenitors, is regulated
by EPO and controls the protection against the TNFSF10/TRAIL-
mediated apoptosis, via BCL2. May be involved in the regulation of
the insulin-induced phosphorylation and activation of AKT1.
{ECO:0000269|PubMed:11746497, ECO:0000269|PubMed:12407104,
ECO:0000269|PubMed:15949469, ECO:0000269|PubMed:16270034,
ECO:0000269|PubMed:16445938, ECO:0000269|PubMed:16757566,
ECO:0000269|PubMed:18604201}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are
calcium-insensitive, but activated by diacylglycerol (DAG) and
phosphatidylserine. Three specific sites; Thr-566 (activation loop
of the kinase domain), Thr-710 (turn motif) and Ser-729
(hydrophobic region), need to be phosphorylated for its full
activation.
-!- SUBUNIT: Forms a ternary complex with TRIM63 and GN2BL1. Can form
a complex with PDLIM5 and N-type calcium channel. Interacts with
COPB1, DGKQ and STAT3 (By similarity). Interacts with YWHAB.
Interacts with HSP90AB1; promotes functional activation in a heat
shock-dependent manner (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:Q02156, ECO:0000269|PubMed:11746497,
ECO:0000269|PubMed:18604201}.
-!- INTERACTION:
P23242:Gja1; NbExp=3; IntAct=EBI-298451, EBI-298630;
Q9CQV8:Ywhab; NbExp=6; IntAct=EBI-298451, EBI-771608;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm,
cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}.
Cytoplasm, perinuclear region {ECO:0000269|PubMed:17611075}.
Nucleus {ECO:0000269|PubMed:17611075}. Note=Translocated to plasma
membrane in epithelial cells stimulated by HGF (By similarity).
Associated with the Golgi at the perinuclear site in pre-passage
fibroblasts. In passaging cells, translocated to the cell
periphery. Translocated to the nucleus in PMA-treated cells.
{ECO:0000250}.
-!- DOMAIN: The C1 domain, containing the phorbol ester/DAG-type
region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the
C2 domain is a non-calcium binding domain.
-!- PTM: Phosphorylation on Thr-566 by PDPK1 triggers
autophosphorylation on Ser-729 (By similarity). Phosphorylation in
the hinge domain at Ser-350 by MAPK11 or MAPK14, Ser-346 by GSK3B
and Ser-368 by autophosphorylation is required for interaction
with YWHAB. {ECO:0000250, ECO:0000269|PubMed:17611075,
ECO:0000269|PubMed:18237277, ECO:0000269|PubMed:18604201}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
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EMBL; AF028009; AAB84189.1; -; mRNA.
EMBL; AF325507; AAG53692.1; -; mRNA.
CCDS; CCDS29008.1; -.
PIR; S02270; KIMSCE.
RefSeq; NP_035234.1; NM_011104.3.
UniGene; Mm.24614; -.
ProteinModelPortal; P16054; -.
SMR; P16054; -.
BioGrid; 202198; 12.
DIP; DIP-31066N; -.
IntAct; P16054; 92.
MINT; MINT-98243; -.
STRING; 10090.ENSMUSP00000094873; -.
BindingDB; P16054; -.
ChEMBL; CHEMBL4366; -.
GuidetoPHARMACOLOGY; 1486; -.
iPTMnet; P16054; -.
PhosphoSitePlus; P16054; -.
MaxQB; P16054; -.
PaxDb; P16054; -.
PeptideAtlas; P16054; -.
PRIDE; P16054; -.
DNASU; 18754; -.
Ensembl; ENSMUST00000097274; ENSMUSP00000094873; ENSMUSG00000045038.
Ensembl; ENSMUST00000097275; ENSMUSP00000094874; ENSMUSG00000045038.
GeneID; 18754; -.
KEGG; mmu:18754; -.
UCSC; uc008dug.2; mouse.
CTD; 5581; -.
MGI; MGI:97599; Prkce.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00820000126964; -.
HOGENOM; HOG000233022; -.
HOVERGEN; HBG108317; -.
InParanoid; P16054; -.
KO; K18050; -.
OMA; PCDQELK; -.
OrthoDB; EOG091G0QRS; -.
PhylomeDB; P16054; -.
TreeFam; TF351133; -.
BRENDA; 2.7.11.13; 3474.
Reactome; R-MMU-114508; Effects of PIP2 hydrolysis.
Reactome; R-MMU-1489509; DAG and IP3 signaling.
Reactome; R-MMU-2029485; Role of phospholipids in phagocytosis.
ChiTaRS; Prkce; mouse.
PRO; PR:P16054; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000045038; -.
CleanEx; MM_PRKCE; -.
ExpressionAtlas; P16054; baseline and differential.
Genevisible; P16054; MM.
GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IDA:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0071889; F:14-3-3 protein binding; IPI:UniProtKB.
GO; GO:0003785; F:actin monomer binding; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004699; F:calcium-independent protein kinase C activity; IDA:MGI.
GO; GO:0008047; F:enzyme activator activity; ISO:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0035276; F:ethanol binding; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004697; F:protein kinase C activity; ISO:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:MGI.
GO; GO:0030546; F:receptor activator activity; IDA:MGI.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0071361; P:cellular response to ethanol; IGI:MGI.
GO; GO:0071456; P:cellular response to hypoxia; IDA:MGI.
GO; GO:0071380; P:cellular response to prostaglandin E stimulus; IDA:MGI.
GO; GO:0007635; P:chemosensory behavior; TAS:MGI.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0035641; P:locomotory exploration behavior; IGI:MGI.
GO; GO:0002281; P:macrophage activation involved in immune response; IMP:MGI.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IMP:ParkinsonsUK-UCL.
GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:UniProtKB.
GO; GO:0010811; P:positive regulation of cell-substrate adhesion; IMP:MGI.
GO; GO:2001031; P:positive regulation of cellular glucuronidation; ISO:MGI.
GO; GO:0032467; P:positive regulation of cytokinesis; ISS:UniProtKB.
GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:UniProtKB.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IMP:MGI.
GO; GO:0032024; P:positive regulation of insulin secretion; IMP:MGI.
GO; GO:0050996; P:positive regulation of lipid catabolic process; IMP:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; IDA:MGI.
GO; GO:0070257; P:positive regulation of mucus secretion; IMP:MGI.
GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IMP:MGI.
GO; GO:0090303; P:positive regulation of wound healing; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:MGI.
GO; GO:0019216; P:regulation of lipid metabolic process; IMP:MGI.
GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IDA:MGI.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IMP:MGI.
GO; GO:0043278; P:response to morphine; IMP:MGI.
GO; GO:0035669; P:TRAM-dependent toll-like receptor 4 signaling pathway; IMP:UniProtKB.
CDD; cd00029; C1; 2.
CDD; cd05591; STKc_nPKC_epsilon; 1.
Gene3D; 2.60.40.150; -; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR000008; C2_dom.
InterPro; IPR035892; C2_domain_sf.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR034669; nPKC_epsilon.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR027274; PKC_epsilon.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR014376; Prot_kin_PKC_delta.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00130; C1_1; 2.
Pfam; PF00168; C2; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000551; PKC_delta; 1.
PIRSF; PIRSF501106; Protein_kin_C_epsilon; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 2.
SMART; SM00239; C2; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF49562; SSF49562; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS50004; C2; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 2.
PROSITE; PS50081; ZF_DAG_PE_2; 2.
1: Evidence at protein level;
ATP-binding; Cell adhesion; Cell cycle; Cell division; Cell membrane;
Complete proteome; Cytoplasm; Cytoskeleton; Immunity; Kinase;
Membrane; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Transferase; Zinc; Zinc-finger.
CHAIN 1 737 Protein kinase C epsilon type.
/FTId=PRO_0000055698.
DOMAIN 1 99 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 408 668 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 669 737 AGC-kinase C-terminal.
ZN_FING 169 220 Phorbol-ester/DAG-type 1.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
ZN_FING 242 292 Phorbol-ester/DAG-type 2.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 414 422 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 223 228 Interaction with actin.
ACT_SITE 532 532 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 437 437 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 62 62 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 228 228 Phosphothreonine.
{ECO:0000250|UniProtKB:Q02156}.
MOD_RES 234 234 Phosphoserine.
{ECO:0000269|PubMed:18237277}.
MOD_RES 309 309 Phosphothreonine.
{ECO:0000250|UniProtKB:Q02156}.
MOD_RES 316 316 Phosphoserine.
{ECO:0000269|PubMed:18237277}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 346 346 Phosphoserine; by GSK3-beta.
{ECO:0000244|PubMed:21183079,
ECO:0000269|PubMed:18604201}.
MOD_RES 349 349 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 350 350 Phosphoserine; by MAPK11 and MAPK14.
{ECO:0000269|PubMed:18604201}.
MOD_RES 368 368 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:18237277,
ECO:0000269|PubMed:18604201}.
MOD_RES 388 388 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 566 566 Phosphothreonine; by PDPK1.
{ECO:0000250|UniProtKB:Q02156}.
MOD_RES 703 703 Phosphothreonine; by autocatalysis.
{ECO:0000255}.
MOD_RES 710 710 Phosphothreonine.
{ECO:0000244|PubMed:15345747}.
MOD_RES 729 729 Phosphoserine; by autocatalysis.
{ECO:0000305|PubMed:17611075}.
MUTAGEN 346 346 S->A: Loss of interaction with YWHAB and
defects in the completion of cytokinesis.
{ECO:0000269|PubMed:18604201}.
MUTAGEN 368 368 S->A: Loss of interaction with YWHAB and
defects in the completion of cytokinesis.
{ECO:0000269|PubMed:18604201}.
MUTAGEN 729 729 S->A,E,T: Loss of localization to the
perinuclear region. Loss of translocation
to the nucleus upon PMA stimulation.
{ECO:0000269|PubMed:17611075}.
SEQUENCE 737 AA; 83561 MW; 7AEBB8CC10C99F57 CRC64;
MVVFNGLLKI KICEAVSLKP TAWSLRHAVG PRPQTFLLDP YIALNVDDSR IGQTATKQKT
NSPAWHDEFV TDVCNGRKIE LAVFHDAPIG YDDFVANCTI QFEELLQNGS RHFEDWIDLE
PEGKVYVIID LSGSSGEAPK DNEERVFRER MRPRKRQGAV RRRVHQVNGH KFMATYLRQP
TYCSHCRDFI WGVIGKQGYQ CQVCTCVVHK RCHELIITKC AGLKKQETPD EVGSQRFSVN
MPHKFGIHNY KVPTFCDHCG SLLWGLLRQG LQCKVCKMNV HRRCETNVAP NCGVDARGIA
KVLADLGVTP DKITNSGQRR KKLAAGAESP QPASGNSPSE DDRSKSAPTS PCDQELKELE
NNIRKALSFD NRGEEHRASS ATDGQLASPG ENGEVRPGQA KRLGLDEFNF IKVLGKGSFG
KVMLAELKGK DEVYAVKVLK KDVILQDDDV DCTMTEKRIL ALARKHPYLT QLYCCFQTKD
RLFFVMEYVN GGDLMFQIQR SRKFDEPRSR FYAAEVTSAL MFLHQHGVIY RDLKLDNILL
DAEGHCKLAD FGMCKEGIMN GVTTTTFCGT PDYIAPEILQ ELEYGPSVDW WALGVLMYEM
MAGQPPFEAD NEDDLFESIL HDDVLYPVWL SKEAVSILKA FMTKNPHKRL GCVAAQNGED
AIKQHPFFKE IDWVLLEQKK IKPPFKPRIK TKRDVNNFDQ DFTREEPILT LVDEAIIKQI
NQEEFKGFSY FGEDLMP


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