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

 KPCZ_RAT                Reviewed;         592 AA.
P09217;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 2.
22-NOV-2017, entry version 178.
RecName: Full=Protein kinase C zeta type;
EC=2.7.11.13;
AltName: Full=nPKC-zeta;
Name=Prkcz; Synonyms=Pkcz;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=2470089; DOI=10.1073/pnas.86.9.3099;
Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y.;
"Protein kinase C zeta subspecies from rat brain: its structure,
expression, and properties.";
Proc. Natl. Acad. Sci. U.S.A. 86:3099-3103(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 101-592.
TISSUE=Brain;
PubMed=2834397;
Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y.;
"The structure, expression, and properties of additional members of
the protein kinase C family.";
J. Biol. Chem. 263:6927-6932(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 101-180.
PubMed=3691811; DOI=10.1016/0014-5793(87)80564-1;
Ono Y., Fujii T., Ogita K., Kikkawa U., Igarashi K., Nishizuka Y.;
"Identification of three additional members of rat protein kinase C
family: delta-, epsilon- and zeta-subspecies.";
FEBS Lett. 226:125-128(1987).
[4]
FUNCTION IN LONG-TERM POTENTIATION.
PubMed=8378304; DOI=10.1073/pnas.90.18.8342;
Sacktor T.C., Osten P., Valsamis H., Jiang X., Naik M.U., Sublette E.;
"Persistent activation of the zeta isoform of protein kinase C in the
maintenance of long-term potentiation.";
Proc. Natl. Acad. Sci. U.S.A. 90:8342-8346(1993).
[5]
FUNCTION IN ACTIVATION OF MAP2K1/MEK1 AND MAPK3/ERK1.
PubMed=8557035;
Berra E., Diaz-Meco M.T., Lozano J., Frutos S., Municio M.M.,
Sanchez P., Sanz L., Moscat J.;
"Evidence for a role of MEK and MAPK during signal transduction by
protein kinase C zeta.";
EMBO J. 14:6157-6163(1995).
[6]
FUNCTION.
PubMed=9374484; DOI=10.1074/jbc.272.48.30075;
Standaert M.L., Galloway L., Karnam P., Bandyopadhyay G., Moscat J.,
Farese R.V.;
"Protein kinase C-zeta as a downstream effector of
phosphatidylinositol 3-kinase during insulin stimulation in rat
adipocytes. Potential role in glucose transport.";
J. Biol. Chem. 272:30075-30082(1997).
[7]
FUNCTION, INTERACTION WITH SQSTM1, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=9177193; DOI=10.1073/pnas.94.12.6191;
Puls A., Schmidt S., Grawe F., Stabel S.;
"Interaction of protein kinase C zeta with ZIP, a novel protein kinase
C-binding protein.";
Proc. Natl. Acad. Sci. U.S.A. 94:6191-6196(1997).
[8]
FUNCTION IN NF-KAPPA-B ACTIVATION.
PubMed=10022904; DOI=10.1128/MCB.19.3.2180;
Lallena M.J., Diaz-Meco M.T., Bren G., Paya C.V., Moscat J.;
"Activation of IkappaB kinase beta by protein kinase C isoforms.";
Mol. Cell. Biol. 19:2180-2188(1999).
[9]
FUNCTION IN NF-KAPPA-B ACTIVATION.
PubMed=10747026; DOI=10.1093/emboj/19.7.1576;
Sanz L., Diaz-Meco M.T., Nakano H., Moscat J.;
"The atypical PKC-interacting protein p62 channels NF-kappaB
activation by the IL-1-TRAF6 pathway.";
EMBO J. 19:1576-1586(2000).
[10]
FUNCTION IN CELL POLARITY.
PubMed=11525734; DOI=10.1016/S0092-8674(01)00471-8;
Etienne-Manneville S., Hall A.;
"Integrin-mediated activation of Cdc42 controls cell polarity in
migrating astrocytes through PKCzeta.";
Cell 106:489-498(2001).
[11]
FUNCTION IN ACTIVATION OF MAP2K5/MEK5 AND MAPK7/ERK5.
PubMed=11158308; DOI=10.1128/MCB.21.4.1218-1227.2001;
Diaz-Meco M.T., Moscat J.;
"MEK5, a new target of the atypical protein kinase C isoforms in
mitogenic signaling.";
Mol. Cell. Biol. 21:1218-1227(2001).
[12]
FUNCTION IN LONG-TERM POTENTIATION.
PubMed=11914719; DOI=10.1038/nn829;
Ling D.S., Benardo L.S., Serrano P.A., Blace N., Kelly M.T.,
Crary J.F., Sacktor T.C.;
"Protein kinase Mzeta is necessary and sufficient for LTP
maintenance.";
Nat. Neurosci. 5:295-296(2002).
[13]
INTERACTION WITH SQSTM1 AND GABRR3, AND SUBCELLULAR LOCATION.
PubMed=12431995; DOI=10.1074/jbc.M205162200;
Croci C., Brandstaetter J.H., Enz R.;
"ZIP3, a new splice variant of the PKC-zeta-interacting protein
family, binds to GABAC receptors, PKC-zeta, and Kv beta 2.";
J. Biol. Chem. 278:6128-6135(2003).
[14]
INTERACTION WITH SQSTM1 AND MAP2K5, AND MUTAGENESIS OF ASP-62.
PubMed=12813044; DOI=10.1074/jbc.M303221200;
Lamark T., Perander M., Outzen H., Kristiansen K., Oevervatn A.,
Michaelsen E., Bjoerkoey G., Johansen T.;
"Interaction codes within the family of mammalian Phox and Bem1p
domain-containing proteins.";
J. Biol. Chem. 278:34568-34581(2003).
[15]
PHOSPHORYLATION AT THR-410 AND THR-560.
PubMed=14580237; DOI=10.1042/BJ20031194;
Le Good J.A., Brindley D.N.;
"Molecular mechanisms regulating protein kinase Czeta turnover and
cellular transformation.";
Biochem. J. 378:83-92(2004).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-560 AND SER-591, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Calcium- and diacylglycerol-independent
serine/threonine-protein kinase that functions in
phosphatidylinositol 3-kinase (PI3K) pathway and mitogen-activated
protein (MAP) kinase cascade, and is involved in NF-kappa-B
activation, mitogenic signaling, cell proliferation, cell
polarity, inflammatory response and maintenance of long-term
potentiation (LTP). Upon lipopolysaccharide (LPS) treatment in
macrophages, or following mitogenic stimuli, functions downstream
of PI3K to activate MAP2K1/MEK1-MAPK1/ERK2 signaling cascade
independently of RAF1 activation. Required for insulin-dependent
activation of AKT3, but may function as an adapter rather than a
direct activator. Upon insulin treatment may act as a downstream
effector of PI3K and contribute to the activation of translocation
of the glucose transporter SLC2A4/GLUT4 and subsequent glucose
transport in adipocytes. In EGF-induced cells, binds and activates
MAP2K5/MEK5-MAPK7/ERK5 independently of its kinase activity and
can activate JUN promoter through MEF2C. Through binding with
SQSTM1/p62, functions in interleukin-1 signaling and activation of
NF-kappa-B with the specific adapters RIPK1 and TRAF6.
Participates in TNF-dependent transactivation of NF-kappa-B by
phosphorylating and activating IKBKB kinase, which in turn leads
to the degradation of NF-kappa-B inhibitors. In migrating
astrocytes, forms a cytoplasmic complex with PARD6A and is
recruited by CDC42 to function in the establishment of cell
polarity along with the microtubule motor and dynein. In
association with FEZ1, stimulates neuronal differentiation in PC12
cells. In the inflammatory response, is required for the T-helper
2 (Th2) differentiation process, including interleukin production,
efficient activation of JAK1 and the subsequent phosphorylation
and nuclear translocation of STAT6. May be involved in development
of allergic airway inflammation (asthma), a process dependent on
Th2 immune response. In the NF-kappa-B-mediated inflammatory
response, can relieve SETD6-dependent repression of NF-kappa-B
target genes by phosphorylating the RELA subunit at 'Ser-311'.
Necessary and sufficient for LTP maintenance in hippocampal CA1
pyramidal cells. In vein endothelial cells treated with the
oxidant peroxynitrite, phosphorylates STK11 leading to nuclear
export of STK11, subsequent inhibition of PI3K/Akt signaling, and
increased apoptosis. Phosphorylates VAMP2 in vitro (By
similarity). {ECO:0000250|UniProtKB:Q05513,
ECO:0000269|PubMed:10022904, ECO:0000269|PubMed:10747026,
ECO:0000269|PubMed:11158308, ECO:0000269|PubMed:11525734,
ECO:0000269|PubMed:11914719, ECO:0000269|PubMed:8378304,
ECO:0000269|PubMed:8557035, ECO:0000269|PubMed:9177193,
ECO:0000269|PubMed:9374484}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Atypical PKCs (PRKCI and PRKCZ) exhibit an
elevated basal enzymatic activity (that may be due to the
interaction with SMG1 or SQSTM1) and are not regulated by
diacylglycerol, phosphatidylserine, phorbol esters or calcium
ions. Two specific sites, Thr-410 (activation loop of the kinase
domain) and Thr-560 (turn motif), need to be phosphorylated for
its full activation. Phosphatidylinositol 3,4,5-trisphosphate
might be a physiological activator (By similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts with PARD6A, PARD6B and PARD6G. Part of a
complex with PARD3, PARD6A or PARD6B or PARD6G and CDC42 or RAC1.
Interacts with ADAP1/CENTA1 (By similarity). Forms a ternary
complex with SQSTM1 and KCNAB2. Forms another ternary complex with
SQSTM1 and GABRR3. Forms a complex with SQSTM1 and MAP2K5.
Interacts (via the protein kinase domain) with WWC1. Forms a
tripartite complex with WWC1 and DDR1, but predominantly in the
absence of collagen. Component of the Par polarity complex,
composed of at least phosphorylated PRKCZ, PARD3 and TIAM1.
Interacts with PDPK1 (via N-terminal region). Interacts with WDFY2
(via WD repeats 1-3) (By similarity). Interacts with VAMP2 (By
similarity). Forms a complex with WDFY2 and VAMP2 (By similarity).
{ECO:0000250|UniProtKB:Q05513, ECO:0000269|PubMed:12431995,
ECO:0000269|PubMed:12813044, ECO:0000269|PubMed:9177193}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12431995,
ECO:0000269|PubMed:9177193}. Endosome
{ECO:0000250|UniProtKB:Q05513}. Cell junction
{ECO:0000250|UniProtKB:Q05513}. Note=In the retina, localizes in
the terminals of the rod bipolar cells. Associated with endosomes.
Presence of KRIT1, CDH5 and RAP1B is required for its localization
to the cell junction. Colocalizes with VAMP2 and WDFY2 in
intracellular vesicles. {ECO:0000250|UniProtKB:Q05513}.
-!- DOMAIN: The PB1 domain mediate mutually exclusive interactions
with SQSTM1 and PARD6B. {ECO:0000250}.
-!- DOMAIN: The C1 domain does not bind the diacylglycerol (DAG).
{ECO:0000269|PubMed:9177193}.
-!- PTM: CDH5 is required for its phosphorylation at Thr-410.
Phosphorylated by protein kinase PDPK1; phosphorylation is
inhibited by the apoptotic C-terminal cleavage product of PKN2.
Phosphorylation at Thr-410 by PI3K activates the kinase (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. PKC subfamily. {ECO:0000305}.
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EMBL; J04532; AAA41934.1; -; mRNA.
EMBL; M18332; AAA41878.1; -; mRNA.
PIR; A30314; A30314.
RefSeq; NP_071952.1; NM_022507.1.
UniGene; Rn.1109; -.
PDB; 4MJS; X-ray; 2.50 A; A/C/E/G/I/K/M/O/Q/S/U/W=15-101.
PDBsum; 4MJS; -.
ProteinModelPortal; P09217; -.
SMR; P09217; -.
BioGrid; 247554; 16.
CORUM; P09217; -.
DIP; DIP-40867N; -.
IntAct; P09217; 5.
MINT; MINT-125335; -.
STRING; 10116.ENSRNOP00000021285; -.
ChEMBL; CHEMBL2094266; -.
iPTMnet; P09217; -.
PhosphoSitePlus; P09217; -.
PaxDb; P09217; -.
PRIDE; P09217; -.
Ensembl; ENSRNOT00000021285; ENSRNOP00000021285; ENSRNOG00000015480.
GeneID; 25522; -.
KEGG; rno:25522; -.
CTD; 5590; -.
RGD; 3399; Prkcz.
eggNOG; KOG0695; Eukaryota.
eggNOG; ENOG410ZMG2; LUCA.
GeneTree; ENSGT00820000126964; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; P09217; -.
KO; K18952; -.
OMA; RCHVLVP; -.
OrthoDB; EOG091G03Q9; -.
PhylomeDB; P09217; -.
BRENDA; 2.7.11.13; 5301.
Reactome; R-RNO-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
Reactome; R-RNO-5218921; VEGFR2 mediated cell proliferation.
PRO; PR:P09217; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000015480; -.
Genevisible; P09217; RN.
GO; GO:0045179; C:apical cortex; ISO:RGD.
GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
GO; GO:0043203; C:axon hillock; ISO:RGD.
GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
GO; GO:0005938; C:cell cortex; ISO:RGD.
GO; GO:0031252; C:cell leading edge; IDA:RGD.
GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0005815; C:microtubule organizing center; ISO:RGD.
GO; GO:0035748; C:myelin sheath abaxonal region; ISO:RGD.
GO; GO:0005635; C:nuclear envelope; ISO:RGD.
GO; GO:0016363; C:nuclear matrix; ISO:RGD.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0031982; C:vesicle; ISO:RGD.
GO; GO:0071889; F:14-3-3 protein binding; IPI:RGD.
GO; GO:0005524; F:ATP binding; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043274; F:phospholipase binding; IPI:RGD.
GO; GO:0015459; F:potassium channel regulator activity; IMP:RGD.
GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
GO; GO:0004672; F:protein kinase activity; ISO:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0004697; F:protein kinase C activity; IDA:RGD.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:RGD.
GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:RGD.
GO; GO:0031584; P:activation of phospholipase D activity; IMP:RGD.
GO; GO:0032148; P:activation of protein kinase B activity; IMP:RGD.
GO; GO:0016477; P:cell migration; IMP:RGD.
GO; GO:0007166; P:cell surface receptor signaling pathway; IMP:RGD.
GO; GO:0034613; P:cellular protein localization; IMP:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; IMP:RGD.
GO; GO:0030010; P:establishment of cell polarity; IMP:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0008286; P:insulin receptor signaling pathway; IMP:RGD.
GO; GO:0035556; P:intracellular signal transduction; IDA:RGD.
GO; GO:0007616; P:long-term memory; IMP:RGD.
GO; GO:0060291; P:long-term synaptic potentiation; IMP:UniProtKB.
GO; GO:0051899; P:membrane depolarization; IMP:RGD.
GO; GO:0060081; P:membrane hyperpolarization; IMP:RGD.
GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:RGD.
GO; GO:0051346; P:negative regulation of hydrolase activity; IDA:RGD.
GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISO:RGD.
GO; GO:0050732; P:negative regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
GO; GO:0031333; P:negative regulation of protein complex assembly; ISO:RGD.
GO; GO:1990138; P:neuron projection extension; ISO:RGD.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:RGD.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:RGD.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IMP:RGD.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IDA:UniProtKB.
GO; GO:0046326; P:positive regulation of glucose import; IMP:RGD.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IMP:UniProtKB.
GO; GO:2001181; P:positive regulation of interleukin-10 secretion; ISS:UniProtKB.
GO; GO:2000667; P:positive regulation of interleukin-13 secretion; ISS:UniProtKB.
GO; GO:0032753; P:positive regulation of interleukin-4 production; ISS:UniProtKB.
GO; GO:2000664; P:positive regulation of interleukin-5 secretion; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0051222; P:positive regulation of protein transport; IMP:RGD.
GO; GO:0050806; P:positive regulation of synaptic transmission; IMP:RGD.
GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; ISS:UniProtKB.
GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; ISS:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; IPI:RGD.
GO; GO:0070528; P:protein kinase C signaling; IMP:RGD.
GO; GO:0072659; P:protein localization to plasma membrane; ISO:RGD.
GO; GO:0006468; P:protein phosphorylation; IDA:RGD.
GO; GO:0007165; P:signal transduction; IDA:RGD.
GO; GO:0047496; P:vesicle transport along microtubule; IMP:RGD.
CDD; cd00029; C1; 1.
CDD; cd06404; PB1_aPKC; 1.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR020454; DAG/PE-bd.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR034877; PB1_aPKC.
InterPro; IPR000270; PB1_dom.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR012233; PKC.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00130; C1_1; 1.
Pfam; PF00564; PB1; 1.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000554; PKC_zeta; 1.
PRINTS; PR00008; DAGPEDOMAIN.
SMART; SM00109; C1; 1.
SMART; SM00666; PB1; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS51745; PB1; 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; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Cell junction; Complete proteome;
Cytoplasm; Endosome; Inflammatory response; Kinase; Metal-binding;
Nucleotide-binding; Phosphoprotein; Reference proteome;
Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger.
CHAIN 1 592 Protein kinase C zeta type.
/FTId=PRO_0000055704.
DOMAIN 15 98 PB1. {ECO:0000255|PROSITE-
ProRule:PRU01081}.
DOMAIN 252 518 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 519 590 AGC-kinase C-terminal.
ZN_FING 130 180 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
NP_BIND 258 266 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 79 145 Interaction with SQSTM1.
ACT_SITE 376 376 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 281 281 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 410 410 Phosphothreonine; by PDPK1 and PI3K.
{ECO:0000250|UniProtKB:Q05513}.
MOD_RES 560 560 Phosphothreonine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:14580237}.
MOD_RES 591 591 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MUTAGEN 62 62 D->A: Loss of interaction with SQSTM1.
{ECO:0000269|PubMed:12813044}.
CONFLICT 102 112 QPGMPCPGEDK -> FRAEEAAEKAE (in Ref. 2;
AAA41878 and 3; no nucleotide entry).
{ECO:0000305}.
STRAND 15 22 {ECO:0000244|PDB:4MJS}.
STRAND 25 31 {ECO:0000244|PDB:4MJS}.
HELIX 37 47 {ECO:0000244|PDB:4MJS}.
STRAND 56 61 {ECO:0000244|PDB:4MJS}.
STRAND 67 70 {ECO:0000244|PDB:4MJS}.
HELIX 73 85 {ECO:0000244|PDB:4MJS}.
STRAND 89 97 {ECO:0000244|PDB:4MJS}.
SEQUENCE 592 AA; 67733 MW; 5A3021171C2FD7C7 CRC64;
MPSRTDPKMD RSGGRVRLKA HYGGDILITS VDPTTTFQDL CEEVRDMCGL HQQHPLTLKW
VDSEGDPCTV SSQMELEEAF RLACQGRDEV LIIHVFPSIP EQPGMPCPGE DKSIYRRGAR
RWRKLYRANG HLFQAKRFNR RAYCGQCSER IWGLARQGYR CINCKLLVHK RCHVLVPLTC
RRHMDSVMPS QEPPVDDKND GVDLPSEETD GIAYISSSRK HDNIKDDSED LKPVIDGVDG
IKISQGLGLQ DFDLIRVIGR GSYAKVLLVR LKKNDQIYAM KVVKKELVHD DEDIDWVQTE
KHVFEQASSN PFLVGLHSCF QTTSRLFLVI EYVNGGDLMF HMQRQRKLPE EHARFYAAEI
CIALNFLHER GIIYRDLKLD NVLLDADGHI KLTDYGMCKE GLGPGDTTST FCGTPNYIAP
EILRGEEYGF SVDWWALGVL MFEMMAGRSP FDIITDNPDM NTEDYLFQVI LEKPIRIPRF
LSVKASHVLK GFLNKDPKER LGCRPQTGFS DIKSHAFFRS IDWDLLEKKQ TLPPFQPQIT
DDYGLDNFDT QFTSEPVQLT PDDEDVIKRI DQSEFEGFEY INPLLLSAEE SV


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10-782-55107 Protein kinase C zeta type - EC 2.7.11.13; nPKC-zeta N_A 0.02 mg
10-782-55107 Protein kinase C zeta type - EC 2.7.11.13; nPKC-zeta N_A 0.005 mg
EIAAB11076 DAG kinase zeta,DAGK6,DGKZ,DGK-zeta,Diacylglycerol kinase zeta,Diglyceride kinase zeta,Homo sapiens,Human
EIAAB11077 DAG kinase zeta,Dgkz,DGK-zeta,Diacylglycerol kinase zeta,Diglyceride kinase zeta,Mouse,Mus musculus
EIAAB11078 104 kDa diacylglycerol kinase,DAG kinase zeta,Dagk6,DGK-IV,Dgkz,DGK-zeta,Diacylglycerol kinase zeta,Diglyceride kinase zeta,Rat,Rattus norvegicus
EIAAB41779 Bos taurus,Bovine,CCT6A,CCT-zeta,CCT-zeta-1,T-complex protein 1 subunit zeta,TCP-1-zeta
EIAAB41778 CCT6B,CCT-zeta-2,CCT-zeta-like,Homo sapiens,Human,T-complex protein 1 subunit zeta-2,TCP-1-zeta-2,TCP-1-zeta-like,Testis-specific protein TSA303,Testis-specific Tcp20
EIAAB31476 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase zeta-1,Homo sapiens,Human,Phosphoinositide phospholipase C-zeta-1,Phospholipase C-zeta-1,PLCZ1,PLC-zeta-1,Testis-development protein NYD-SP27
SCH-7864-0307 RABBIT ANTI RAT PROTEIN KINASE C ZETA, Product Type Polyclonal Antibody, Specificity PROTEIN KINASE C ZETA, Target Species Rat, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Application 0.25 ml
7864-0307 RABBIT ANTI RAT PROTEIN KINASE C ZETA, Product Type Polyclonal Antibody, Specificity PROTEIN KINASE C ZETA, Target Species Rat, Host Rabbit, Format Purified, Isotypes Polyclonal IgG, Application 0.25 ml
SCH-AHP1111 RABBIT ANTI HUMAN PROTEIN KINASE C ZETA (N_TERMINAL), Product Type Polyclonal Antibody, Specificity PROTEIN KINASE C ZETA , Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclona 50 µg
AHP1111 RABBIT ANTI HUMAN PROTEIN KINASE C ZETA (N_TERMINAL), Product Type Polyclonal Antibody, Specificity PROTEIN KINASE C ZETA , Target Species Human, Host Rabbit, Format Purified, Isotypes Polyclona 50 µg
EIAAB08629 Coatomer subunit zeta-2,COPZ2,Homo sapiens,Human,Zeta-2 COP,Zeta-2-coat protein
EIAAB08627 Coatomer subunit zeta-1,Copz,Copz1,Mouse,Mus musculus,Zeta-1 COP,Zeta-1-coat protein
EIAAB08626 Bos taurus,Bovine,Coatomer subunit zeta-1,COPZ,COPZ1,Zeta-1 COP,Zeta-1-coat protein
EIAAB41776 Cct6b,Cctz-2,CCT-zeta-2,Mouse,Mus musculus,T-complex protein 1 subunit zeta-2,TCP-1-zeta-2
EIAAB08630 Coatomer subunit zeta-2,Copz2,Mouse,Mus musculus,Zeta-2 COP,Zeta-2-coat protein
EIAAB41780 CCT6,CCT-zeta,Oryctolagus cuniculus,Rabbit,T-complex protein 1 subunit zeta,TCP-1-zeta
EIAAB41782 Cct6,Cct6a,Cctz,Cctz1,CCT-zeta-1,Mouse,Mus musculus,T-complex protein 1 subunit zeta,TCP-1-zeta
EIAAB41777 Bos taurus,Bovine,CCT6B,CCT-zeta-2,T-complex protein 1 subunit zeta-2,TCP-1-zeta-2
EIAAB41784 CCT6,CCTZ,CCT-zeta,Pig,Sus scrofa,T-complex protein 1 subunit zeta,TCP-1-zeta
EIAAB08628 CGI-120,Coatomer subunit zeta-1,COPZ,COPZ1,Homo sapiens,HSPC181,Human,Zeta-1 COP,Zeta-1-coat protein
EIAAB41783 Acute morphine dependence-related protein 2,CCT6,CCT6A,CCTZ,CCT-zeta-1,Homo sapiens,HTR3,Human,T-complex protein 1 subunit zeta,TCP-1-zeta,Tcp20


 

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