Proteína quinase C tipo delta

PRKCD
Estruturas disponíveis
PDB	Pesquisa Human UniProt: PDBe RCSB
Lista de códigos id do PDB
	2YUU, 1YRK
Identificadores
Nomes alternativos	PRKCD
IDs externos	OMIM: 176977 HomoloGene: 55963 GeneCards: PRKCD
Número EC	2.7.11.13 2.7.10.2, 2.7.11.13
Doenças Geneticamente Relacionadas
	autoimmune lymphoproliferative syndrome type 3
Targeted by Drug
	mebutato de ingenol, balanol, enzastaurin, ruboxistaurin
Ontologia genética
Função molecular	• kinase activity; • ATP binding; • protein kinase activity; • non-membrane spanning protein tyrosine kinase activity; • metal ion binding; • kinase binding; • enzyme binding; • insulin receptor substrate binding; • transferase activity; • GO:0001948, GO:0016582 ligação a proteínas plasmáticas; • calcium-independent protein kinase C activity; • protein kinase binding; • nucleotide binding; • GO:0010577 enzyme activator activity; • protein serine/threonine kinase activity; • protein kinase C activity;
Componente celular	• citoplasma; • citosol; • membrane; • cell-cell junction; • perinuclear region of cytoplasm; • núcleo celular; • matriz nuclear; • retículo endoplasmático; • Exossoma; • membrana plasmática; • cariolinfa; • extracellular region; • azurophil granule lumen;
Processo biológico	• intrinsic apoptotic signaling pathway in response to oxidative stress; • termination of signal transduction; • interferon-gamma-mediated signaling pathway; • negative regulation of protein binding; • positive regulation of endodeoxyribonuclease activity; • platelet activation; • protein phosphorylation; • senescência celular; • GO:1903105 negative regulation of insulin receptor signaling pathway; • positive regulation of sphingomyelin catabolic process; • cell chemotaxis; • ciclo celular; • negative regulation of inflammatory response; • positive regulation of protein dephosphorylation; • Fc-gamma receptor signaling pathway involved in phagocytosis; • positive regulation of apoptotic signaling pathway; • stimulatory C-type lectin receptor signaling pathway; • cellular response to hydroperoxide; • negative regulation of peptidyl-tyrosine phosphorylation; • defense response to bacterium; • negative regulation of MAP kinase activity; • positive regulation of response to DNA damage stimulus; • positive regulation of protein import into nucleus; • interleukin-10 production; • regulation of actin cytoskeleton organization; • negative regulation of actin filament polymerization; • regulation of mRNA stability; • fosforilação; • protein stabilization; • regulation of signaling receptor activity; • negative regulation of filopodium assembly; • cellular response to angiotensin; • interleukin-12 production; • peptidyl-threonine phosphorylation; • positive regulation of ceramide biosynthetic process; • neutrophil activation; • GO:0007243 intracellular signal transduction; • negative regulation of glial cell apoptotic process; • negative regulation of platelet aggregation; • positive regulation of phospholipid scramblase activity; • B cell proliferation; • immunoglobulin mediated immune response; • positive regulation of glucosylceramide catabolic process; • peptidyl-tyrosine phosphorylation; • positive regulation of superoxide anion generation; • activation of protein kinase activity; • GO:0072468 transdução de sinal; • cellular response to hydrogen peroxide; • GO:0035404 peptidyl-serine phosphorylation; • GO:0097285 apoptose; • neutrophil degranulation; • execution phase of apoptosis;
	Sources:Amigo / QuickGO
Padrão de expressão RNA
	Mais dados de referência de expressão
Ortólogos
	5580
	n/a
	ENSG00000163932
	n/a
	Q05655
	n/a
NM_006254; NM_212539; NM_001316327; NM_001354676; NM_001354678;
	NM_001354679; NM_001354680
	n/a
NP_001303256; NP_006245; NP_997704; NP_001341605; NP_001341607;
	NP_001341608; NP_001341609
	n/a
	Wikidata
Ver/Editar Humano

Proteína quinase C tipo delta (ou PKC-δ) é uma enzima que em humanos é codificada pelo gene PRKCD.

Função

Proteína quinase C (PKC) é uma família de serina- e treonina-específicas proteína quinases [en] que podem ser ativadas pelo segundo mensageiro diacilglicerol. Os membros da família PKC fosforilam uma grande variedade de proteínas-alvo e são conhecidos por estarem envolvidos em diversas vias de sinalização celular. Os membros da família PKC também servem como receptores principais para ésteres de forbol, uma classe de promotores de tumor. Cada membro da família PKC tem um perfil de expressão específico e acredita-se que desempenhe papéis distintos nas células. A proteína codificada por este gene é um dos membros da família PKC. Estudos em humanos e camundongos demonstram que esta quinase está envolvida na sinalização de célula B e na regulação do crescimento, apoptose e diferenciação de uma variedade de tipos celulares. A proteína quinase C delta também é regulada por fosforilação em vários resíduos de serina/treonina (por exemplo, T50, T141, S304, T451, T505, S506, T507, S643, S664) e tirosina, incluindo Y311 (pelo SRC [en]).

Interações

PRKCD demonstrou interagir com:

Referências

↑ «Doenças geneticamente associadas a PRKCD ver/editar referências no wikidata»
↑ «Drogas que interagem fisicamente com Protein kinase C delta ver/editar referências no wikidata»
↑ «Human PubMed Reference:»
↑ Huppi K, Siwarski D, Goodnight J, Mischak H (Junho de 1994). «Assignment of the protein kinase C delta polypeptide gene (PRKCD) to human chromosome 3 and mouse chromosome 14». Genomics. 19 (1): 161–2. PMID 8188219. doi:10.1006/geno.1994.1028
↑ Kikkawa, Ushio (2002). «Protein Kinase Cδ (PKCδ): Activaton Mechanisms and Functions». The Journal of Biochemistry. 132 (6): 831–839. PMID 12473183. doi:10.1093/oxfordjournals.jbchem.a003294. Consultado em 30 de junho de 2008
↑ «Entrez Gene: PRKCD protein kinase C, delta»
↑ Welman A, Griffiths JR, Whetton AD, Dive C (Dezembro de 2007). «Protein kinase C delta is phosphorylated on five novel Ser/Thr sites following inducible overexpression in human colorectal cancer cells». Protein Sci. 16 (12): 2711–5. PMC 2222818. PMID 17965192. doi:10.1110/ps.072874607
↑ Blake RA, Garcia-Paramio P, Parker PJ, Courtneidge SA (Abril de 1999). «Src promotes PKCdelta degradation». Cell Growth Differ. 10 (4): 231–41. PMID 10319993
↑ Storz P, Hausser A, Link G, Dedio J, Ghebrehiwet B, Pfizenmaier K, Johannes FJ (Agosto de 2000). «Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32». J. Biol. Chem. 275 (32): 24601–7. PMID 10831594. doi:10.1074/jbc.M002964200
↑ Keshamouni, V. G. (17 de abril de 2002). «Mechanism of 17-beta -Estradiol-induced Erk1/2 Activation in Breast Cancer Cells. A ROLE FOR HER2 AND PKC-delta». Journal of Biological Chemistry. 277 (25): 22558–22565. PMID 11960991. doi:10.1074/jbc.M202351200
↑ Braiman L, Alt A, Kuroki T, Ohba M, Bak A, Tennenbaum T, Sampson SR (Abril de 2001). «Insulin induces specific interaction between insulin receptor and protein kinase C delta in primary cultured skeletal muscle». Mol. Endocrinol. 15 (4): 565–74. PMID 11266508. doi:10.1210/mend.15.4.0612
↑ Rosenzweig T, Braiman L, Bak A, Alt A, Kuroki T, Sampson SR (Junho de 2002). «Differential effects of tumor necrosis factor-alpha on protein kinase C isoforms alpha and delta mediate inhibition of insulin receptor signaling». Diabetes. 51 (6): 1921–30. PMID 12031982. doi:10.2337/diabetes.51.6.1921
↑ Ren J, Li Y, Kufe D (Maio de 2002). «Protein kinase C delta regulates function of the DF3/MUC1 carcinoma antigen in beta-catenin signaling». J. Biol. Chem. 277 (20): 17616–22. PMID 11877440. doi:10.1074/jbc.M200436200
↑ Kumar V, Pandey P, Sabatini D, Kumar M, Majumder PK, Bharti A, Carmichael G, Kufe D, Kharbanda S (Março de 2000). «Functional interaction between RAFT1/FRAP/mTOR and protein kinase cdelta in the regulation of cap-dependent initiation of translation». EMBO J. 19 (5): 1087–97. PMC 305647. PMID 10698949. doi:10.1093/emboj/19.5.1087
↑ Han JM, Kim JH, Lee BD, Lee SD, Kim Y, Jung YW, Lee S, Cho W, Ohba M, Kuroki T, Suh PG, Ryu SH (Março de 2002). «Phosphorylation-dependent regulation of phospholipase D2 by protein kinase C delta in rat Pheochromocytoma PC12 cells». J. Biol. Chem. 277 (10): 8290–7. PMID 11744693. doi:10.1074/jbc.M108343200
↑ Yoshida K, Kufe D (Dezembro de 2001). «Negative regulation of the SHPTP1 protein tyrosine phosphatase by protein kinase C delta in response to DNA damage». Mol. Pharmacol. 60 (6): 1431–8. PMID 11723252. doi:10.1124/mol.60.6.1431
↑ Phillips-Mason PJ, Kaur H, Burden-Gulley SM, Craig SE, Brady-Kalnay SM (2011). «Identification of phospholipase C gamma1 as a protein tyrosine phosphatase mu substrate that regulates cell migration». J. Cell. Biochem. 112 (1): 39–48. PMC 3031780. PMID 20506511. doi:10.1002/jcb.22710
↑ Hodgkinson CP, Sale GJ (Janeiro de 2002). «Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment». Biochemistry. 41 (2): 561–9. PMID 11781095. doi:10.1021/bi010719z
↑ Brodie C, Steinhart R, Kazimirsky G, Rubinfeld H, Hyman T, Ayres JN, Hur GM, Toth A, Yang D, Garfield SH, Stone JC, Blumberg PM (Julho de 2004). «PKCdelta associates with and is involved in the phosphorylation of RasGRP3 in response to phorbol esters». Mol. Pharmacol. 66 (1): 76–84. PMID 15213298. doi:10.1124/mol.66.1.76
↑ Leitges M, Gimborn K, Elis W, Kalesnikoff J, Hughes MR, Krystal G, Huber M (Junho de 2002). «Protein kinase C-delta is a negative regulator of antigen-induced mast cell degranulation». Mol. Cell. Biol. 22 (12): 3970–80. PMC 133855. PMID 12024011. doi:10.1128/mcb.22.12.3970-3980.2002
↑ Kristof AS, Marks-Konczalik J, Billings E, Moss J (Setembro de 2003). «Stimulation of signal transducer and activator of transcription-1 (STAT1)-dependent gene transcription by lipopolysaccharide and interferon-gamma is regulated by mammalian target of rapamycin». J. Biol. Chem. 278 (36): 33637–44. PMID 12807916. doi:10.1074/jbc.M301053200

Leitura adicional

Ali A, Hoeflich KP, Woodgett JR (2002). «Glycogen synthase kinase-3: properties, functions, and regulation». Chem. Rev. 101 (8): 2527–40. PMID 11749387. doi:10.1021/cr000110o
Slater SJ, Ho C, Stubbs CD (2003). «The use of fluorescent phorbol esters in studies of protein kinase C-membrane interactions». Chem. Phys. Lipids. 116 (1–2): 75–91. PMID 12093536. doi:10.1016/S0009-3084(02)00021-X
Brodie C, Blumberg PM (2003). «Regulation of cell apoptosis by protein kinase c delta». Apoptosis. 8 (1): 19–27. PMID 12510148. doi:10.1023/A:1021640817208

[1] «Doenças geneticamente associadas a PRKCD ver/editar referências no wikidata»

[2] «Drogas que interagem fisicamente com Protein kinase C delta ver/editar referências no wikidata»

[3] «Human PubMed Reference:»

[pmid8188219-4] Huppi K, Siwarski D, Goodnight J, Mischak H (Junho de 1994). «Assignment of the protein kinase C delta polypeptide gene (PRKCD) to human chromosome 3 and mouse chromosome 14». Genomics. 19 (1): 161–2. PMID 8188219. doi:10.1006/geno.1994.1028

[5] Kikkawa, Ushio (2002). «Protein Kinase Cδ (PKCδ): Activaton Mechanisms and Functions». The Journal of Biochemistry. 132 (6): 831–839. PMID 12473183. doi:10.1093/oxfordjournals.jbchem.a003294. Consultado em 30 de junho de 2008

[6] «Entrez Gene: PRKCD protein kinase C, delta»

[pmid17965192-7] Welman A, Griffiths JR, Whetton AD, Dive C (Dezembro de 2007). «Protein kinase C delta is phosphorylated on five novel Ser/Thr sites following inducible overexpression in human colorectal cancer cells». Protein Sci. 16 (12): 2711–5. PMC 2222818. PMID 17965192. doi:10.1110/ps.072874607

[pmid10319993-8] Blake RA, Garcia-Paramio P, Parker PJ, Courtneidge SA (Abril de 1999). «Src promotes PKCdelta degradation». Cell Growth Differ. 10 (4): 231–41. PMID 10319993

[pmid10831594-9] Storz P, Hausser A, Link G, Dedio J, Ghebrehiwet B, Pfizenmaier K, Johannes FJ (Agosto de 2000). «Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32». J. Biol. Chem. 275 (32): 24601–7. PMID 10831594. doi:10.1074/jbc.M002964200

[10] Keshamouni, V. G. (17 de abril de 2002). «Mechanism of 17-beta -Estradiol-induced Erk1/2 Activation in Breast Cancer Cells. A ROLE FOR HER2 AND PKC-delta». Journal of Biological Chemistry. 277 (25): 22558–22565. PMID 11960991. doi:10.1074/jbc.M202351200

[pmid11266508-11] Braiman L, Alt A, Kuroki T, Ohba M, Bak A, Tennenbaum T, Sampson SR (Abril de 2001). «Insulin induces specific interaction between insulin receptor and protein kinase C delta in primary cultured skeletal muscle». Mol. Endocrinol. 15 (4): 565–74. PMID 11266508. doi:10.1210/mend.15.4.0612

[pmid12031982-12] Rosenzweig T, Braiman L, Bak A, Alt A, Kuroki T, Sampson SR (Junho de 2002). «Differential effects of tumor necrosis factor-alpha on protein kinase C isoforms alpha and delta mediate inhibition of insulin receptor signaling». Diabetes. 51 (6): 1921–30. PMID 12031982. doi:10.2337/diabetes.51.6.1921

[pmid11877440-13] Ren J, Li Y, Kufe D (Maio de 2002). «Protein kinase C delta regulates function of the DF3/MUC1 carcinoma antigen in beta-catenin signaling». J. Biol. Chem. 277 (20): 17616–22. PMID 11877440. doi:10.1074/jbc.M200436200

[pmid10698949-14] Kumar V, Pandey P, Sabatini D, Kumar M, Majumder PK, Bharti A, Carmichael G, Kufe D, Kharbanda S (Março de 2000). «Functional interaction between RAFT1/FRAP/mTOR and protein kinase cdelta in the regulation of cap-dependent initiation of translation». EMBO J. 19 (5): 1087–97. PMC 305647. PMID 10698949. doi:10.1093/emboj/19.5.1087

[pmid11744693-15] Han JM, Kim JH, Lee BD, Lee SD, Kim Y, Jung YW, Lee S, Cho W, Ohba M, Kuroki T, Suh PG, Ryu SH (Março de 2002). «Phosphorylation-dependent regulation of phospholipase D2 by protein kinase C delta in rat Pheochromocytoma PC12 cells». J. Biol. Chem. 277 (10): 8290–7. PMID 11744693. doi:10.1074/jbc.M108343200

[pmid11723252-16] Yoshida K, Kufe D (Dezembro de 2001). «Negative regulation of the SHPTP1 protein tyrosine phosphatase by protein kinase C delta in response to DNA damage». Mol. Pharmacol. 60 (6): 1431–8. PMID 11723252. doi:10.1124/mol.60.6.1431

[pmid20506511-17] Phillips-Mason PJ, Kaur H, Burden-Gulley SM, Craig SE, Brady-Kalnay SM (2011). «Identification of phospholipase C gamma1 as a protein tyrosine phosphatase mu substrate that regulates cell migration». J. Cell. Biochem. 112 (1): 39–48. PMC 3031780. PMID 20506511. doi:10.1002/jcb.22710

[pmid11781095-18] Hodgkinson CP, Sale GJ (Janeiro de 2002). «Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment». Biochemistry. 41 (2): 561–9. PMID 11781095. doi:10.1021/bi010719z

[pmid15213298-19] Brodie C, Steinhart R, Kazimirsky G, Rubinfeld H, Hyman T, Ayres JN, Hur GM, Toth A, Yang D, Garfield SH, Stone JC, Blumberg PM (Julho de 2004). «PKCdelta associates with and is involved in the phosphorylation of RasGRP3 in response to phorbol esters». Mol. Pharmacol. 66 (1): 76–84. PMID 15213298. doi:10.1124/mol.66.1.76

[pmid12024011-20] Leitges M, Gimborn K, Elis W, Kalesnikoff J, Hughes MR, Krystal G, Huber M (Junho de 2002). «Protein kinase C-delta is a negative regulator of antigen-induced mast cell degranulation». Mol. Cell. Biol. 22 (12): 3970–80. PMC 133855. PMID 12024011. doi:10.1128/mcb.22.12.3970-3980.2002

[pmid12807916-21] Kristof AS, Marks-Konczalik J, Billings E, Moss J (Setembro de 2003). «Stimulation of signal transducer and activator of transcription-1 (STAT1)-dependent gene transcription by lipopolysaccharide and interferon-gamma is regulated by mammalian target of rapamycin». J. Biol. Chem. 278 (36): 33637–44. PMID 12807916. doi:10.1074/jbc.M301053200

v d e Enzimas
Atividade	Sítio ativo Sítio de ligação Co-enzima Cofator Catálise enzimática
Controle	Inibição enzimática Ativador enzimático
Classificação	Número EC Superfamília enzimática Família de enzimas
Cinética	Cinética enzimática Diagrama de Lineweaver-Burke Cinética de Michaelis-Menten
Tipos	EC1 Oxirredutases EC2 Transferases EC3 Hidrolases EC4 Liases EC5 Isomerases EC6 Ligases