Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 KPCE_RABIT              Reviewed;         736 AA.
P10830;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
05-DEC-2018, entry version 146.
RecName: Full=Protein kinase C epsilon type;
EC=2.7.11.13;
AltName: Full=nPKC-epsilon;
Name=PRKCE;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3370672; DOI=10.1016/0092-8674(88)90091-8;
Ohno S., Akita Y., Konno Y., Imajoh S., Suzuki K.;
"A novel phorbol ester receptor/protein kinase, nPKC, distantly
related to the protein kinase C family.";
Cell 53:731-741(1988).
-!- 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 (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
EC=2.7.11.13;
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
EC=2.7.11.13;
-!- ACTIVITY REGULATION: Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ)
are calcium-insensitive, but activated by diacylglycerol (DAG) and
phosphatidylserine. Three specific sites; Thr-565 (activation loop
of the kinase domain), Thr-709 (turn motif) and Ser-728
(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, STAT3 and YWHAB (By similarity). Interacts with
HSP90AB1; promotes functional activation in a heat shock-dependent
manner (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:Q02156}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm,
cytoskeleton {ECO:0000250}. Cell membrane {ECO:0000250}.
Cytoplasm, perinuclear region {ECO:0000250}. Nucleus
{ECO:0000250}. Note=Translocated to plasma membrane in epithelial
cells stimulated by HGF. 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 (By similarity). {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-565 by PDPK1 triggers
autophosphorylation on Ser-728. 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
(By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; M20014; AAA31426.1; -; mRNA.
PIR; A29880; KIRBCE.
RefSeq; NP_001075743.1; NM_001082274.1.
UniGene; Ocu.1940; -.
ProteinModelPortal; P10830; -.
SMR; P10830; -.
STRING; 9986.ENSOCUP00000011861; -.
GeneID; 100009103; -.
KEGG; ocu:100009103; -.
CTD; 5581; -.
eggNOG; KOG0694; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
HOGENOM; HOG000233022; -.
HOVERGEN; HBG108317; -.
InParanoid; P10830; -.
KO; K18050; -.
BRENDA; 2.7.11.13; 1749.
Proteomes; UP000001811; Unplaced.
GO; GO:0071944; C:cell periphery; ISS:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0003785; F:actin monomer binding; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004699; F:calcium-independent protein kinase C activity; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:UniProtKB.
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; ISS:UniProtKB.
GO; GO:0090303; P:positive regulation of wound healing; ISS:UniProtKB.
GO; GO:0035669; P:TRAM-dependent toll-like receptor 4 signaling pathway; ISS: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; 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; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 2.
2: Evidence at transcript 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 1 736 Protein kinase C epsilon type.
/FTId=PRO_0000055699.
DOMAIN 1 99 C2. {ECO:0000255|PROSITE-
ProRule:PRU00041}.
DOMAIN 407 667 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 668 736 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 413 421 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 531 531 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 436 436 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 62 62 Phosphoserine.
{ECO:0000250|UniProtKB:P16054}.
MOD_RES 228 228 Phosphothreonine.
{ECO:0000250|UniProtKB:Q02156}.
MOD_RES 234 234 Phosphoserine.
{ECO:0000250|UniProtKB:P16054}.
MOD_RES 309 309 Phosphothreonine.
{ECO:0000250|UniProtKB:Q02156}.
MOD_RES 316 316 Phosphoserine.
{ECO:0000250|UniProtKB:Q02156}.
MOD_RES 329 329 Phosphoserine.
{ECO:0000250|UniProtKB:Q02156}.
MOD_RES 337 337 Phosphoserine.
{ECO:0000250|UniProtKB:P16054}.
MOD_RES 346 346 Phosphoserine; by GSK3-beta.
{ECO:0000250|UniProtKB:Q02156}.
MOD_RES 349 349 Phosphothreonine.
{ECO:0000250|UniProtKB:P16054}.
MOD_RES 350 350 Phosphoserine; by MAPK11 and MAPK14.
{ECO:0000250|UniProtKB:P16054}.
MOD_RES 368 368 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q02156}.
MOD_RES 388 388 Phosphoserine.
{ECO:0000250|UniProtKB:Q02156}.
MOD_RES 565 565 Phosphothreonine; by PDPK1.
{ECO:0000250|UniProtKB:Q02156}.
MOD_RES 702 702 Phosphothreonine; by autocatalysis.
{ECO:0000255}.
MOD_RES 709 709 Phosphothreonine; by autocatalysis.
{ECO:0000250|UniProtKB:Q02156,
ECO:0000255}.
MOD_RES 728 728 Phosphoserine; by autocatalysis.
{ECO:0000250|UniProtKB:Q02156}.
SEQUENCE 736 AA; 83516 MW; 261C4FEE59E9BFEB CRC64;
MVVFNGLLKI KICEAVSLKP TAWSLRHAVG PRPQTFLLDP YIALNVDDSR IGQTATKQKT
NSPAWHDEFV TDVCNGRKIE LAVFHDAPIG YDDFVANCTI QFEELLQNGS RHFEDWIDLE
PEGKVYVIID LSGSSGEAPK DNEERVFRER MRPRKRQGAV RRRVHQVNGH KFMATYLRQP
TYCSHCRDFI WGVIGKQGYQ CQVCTCVVHK RCHELIITKV AGLKKQETPD EVGSQRFSVN
MPHKFGIHNY KVPTFCDHCG SLLWGLLRQG LQCKVCKMNV HRRCETNVAP NCGVDARGIA
KVLADLGVTP DKITNSGQRR KKLIGGAESP QPTSGSSPSE EDRSKSAPTS PCDQELKELE
NNIRKALSFD NRGEEHRAAS STDGQLGSPE NGEVRQGQAK RLGLDEFNFI KVLGKGSFGK
VMLAELKGKD EVYAVKVLKK DVILQDDDVD CTMTEKRILA LARKHPYLTQ LYCCFQTKDR
LFFVMEYVNG GDLMFQIQRS RKFDEPRSRF YAAEVTSALM FLHQHGVIYR DLKLDNILLD
AEGHCKLADF GMCKEGILNG VTTTTFCGTP DYIAPEILQE LEYGPSVDWW ALGVLMYEMM
AGQPPFEADN EDDLFESILH DDVLYPVWLS KEAVSILKAF MTKNPHKRLG CVAAQNGEDA
IKQHPFFKEI DWVLLEQKKI KPPFKPRIKT KRDVNNFDQD FTREEPVLTL VDEAIVKQIN
QEEFKGFSYF GEDLMP


Related products :

Catalog number Product name Quantity
10-782-55101 Protein kinase C epsilon type - EC 2.7.11.13; nPKC-epsilon N_A 0.02 mg
10-782-55101 Protein kinase C epsilon type - EC 2.7.11.13; nPKC-epsilon N_A 0.01 mg
10-782-55101 Protein kinase C epsilon type - EC 2.7.11.13; nPKC-epsilon N_A 0.005 mg
10-782-55101 Protein kinase C epsilon type - EC 2.7.11.13; nPKC-epsilon N_A 0.001 mg
10-663-45565 Protein Kinase C epsilon (PKC-e) Human - EC 2.7.11.13; nPKC-epsilon N_A 0.01 mg
10-663-45565 Protein Kinase C epsilon (PKC-e) Human - EC 2.7.11.13; nPKC-epsilon N_A 0.002 mg
10-663-45565 Protein Kinase C epsilon (PKC-e) Human - EC 2.7.11.13; nPKC-epsilon N_A 1 mg
EIAAB11066 DAG kinase epsilon,DAGK5,DGKE,DGK-epsilon,Diacylglycerol kinase epsilon,Diglyceride kinase epsilon,Homo sapiens,Human
EIAAB11067 DAG kinase epsilon,Dgke,DGK-epsilon,Diacylglycerol kinase epsilon,Diglyceride kinase epsilon,Mouse,Mus musculus
SCH-MCA1574 MOUSE ANTI PROTEIN KINASE C EPSILON, Product Type Monoclonal Antibody, Specificity PROTEIN KINASE C EPSILON, Target Species , Host Mouse, Format S_N, Isotypes IgG2a, Applications C, WB, Clone 2 ml
MCA1574 MOUSE ANTI PROTEIN KINASE C EPSILON, Product Type Monoclonal Antibody, Specificity PROTEIN KINASE C EPSILON, Target Species , Host Mouse, Format S_N, Isotypes IgG2a, Applications C, WB, Clone 2 ml
18-661-15102 Inhibitor of nuclear factor kappa-B kinase epsilon subunit - EC 2.7.11.1; I kappa-B kinase epsilon; IkBKE; IKK-epsilon; IKK-E; Inducible I kappa-B kinase; IKK-i Polyclonal 0.1 mg
Z8050093 Rabbit Polyclonal Anti-Protein Kinase C Epsilon (PKC-epsilon) 100
EIAAB08609 Bos taurus,Bovine,Coatomer subunit epsilon,COPE,COPE1,Epsilon-coat protein,Epsilon-COP
EIAAB41754 Cct5,Ccte,CCT-epsilon,Kiaa0098,Mouse,Mus musculus,T-complex protein 1 subunit epsilon,TCP-1-epsilon
EIAAB08606 Coatomer subunit epsilon,Cope,Cope1,Epsilon-coat protein,Epsilon-COP,Mouse,Mus musculus
EIAAB08607 Coatomer subunit epsilon,COPE,Epsilon-coat protein,Epsilon-COP,Homo sapiens,Human
18-003-44146 Transcription factor AP-2 epsilon - AP2-epsilon; Activating enhancer-binding protein 2 epsilon Polyclonal 0.1 mg Protein A
EIAAB41756 CCT5,CCTE,CCT-epsilon,Homo sapiens,Human,KIAA0098,T-complex protein 1 subunit epsilon,TCP-1-epsilon
EIAAB41755 Cct5,CCT-epsilon,Rat,Rattus norvegicus,T-complex protein 1 subunit epsilon,TCP-1-epsilon
GTX25811 Protein Kinase C epsilon (PKC epsilon) pSer729 50 µl
GTX25811 Protein Kinase C epsilon (PKC epsilon) pSer729 50 µl
EIAAB33081 Mouse,Mus musculus,Protein-tyrosine phosphatase epsilon,Ptpe,Ptpre,Receptor-type tyrosine-protein phosphatase epsilon,R-PTP-epsilon
EIAAB33083 Protein-tyrosine phosphatase epsilon,Ptpe,Ptpre,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase epsilon,R-PTP-epsilon
EIAAB33082 Homo sapiens,Human,Protein-tyrosine phosphatase epsilon,PTPRE,Receptor-type tyrosine-protein phosphatase epsilon,R-PTP-epsilon


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur