UniProtKB - P09215 (KPCD_RAT)
Protein kinase C delta type
Prkcd
Functioni
Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays contrasting roles in cell death and cell survival by functioning as a pro-apoptotic protein during DNA damage-induced apoptosis, but acting as an anti-apoptotic protein during cytokine receptor-initiated cell death, is involved in tumor suppression, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Upon DNA damage, activates the promoter of the death-promoting transcription factor BCLAF1/Btf to trigger BCLAF1-mediated p53/TP53 gene transcription and apoptosis. In response to oxidative stress, interact with and activate CHUK/IKKA in the nucleus, causing the phosphorylation of p53/TP53. In the case of ER stress or DNA damage-induced apoptosis, can form a complex with the tyrosine-protein kinase ABL1 which trigger apoptosis independently of p53/TP53. In cytosol can trigger apoptosis by activating MAPK11 or MAPK14, inhibiting AKT1 and decreasing the level of X-linked inhibitor of apoptosis protein (XIAP), whereas in nucleus induces apoptosis via the activation of MAPK8 or MAPK9. Upon ionizing radiation treatment, is required for the activation of the apoptosis regulators BAX and BAK, which trigger the mitochondrial cell death pathway. Can phosphorylate MCL1 and target it for degradation which is sufficient to trigger for BAX activation and apoptosis. Is required for the control of cell cycle progression both at G1/S and G2/M phases. Mediates phorbol 12-myristate 13-acetate (PMA)-induced inhibition of cell cycle progression at G1/S phase by up-regulating the CDK inhibitor CDKN1A/p21 and inhibiting the cyclin CCNA2 promoter activity. In response to UV irradiation can phosphorylate CDK1, which is important for the G2/M DNA damage checkpoint activation. Can protect glioma cells from the apoptosis induced by TNFSF10/TRAIL, probably by inducing increased phosphorylation and subsequent activation of AKT1. Can also act as tumor suppressor upon mitogenic stimulation with PMA or TPA. In N-formyl-methionyl-leucyl-phenylalanine (fMLP)-treated cells, is required for NCF1 (p47-phox) phosphorylation and activation of NADPH oxidase activity, and regulates TNF-elicited superoxide anion production in neutrophils, by direct phosphorylation and activation of NCF1 or indirectly through MAPK1/3 (ERK1/2) signaling pathways. Involved in antifungal immunity by mediating phosphorylation and activation of CARD9 downstream of C-type lectin receptors activation, promoting interaction between CARD9 and BCL10, followed by activation of NF-kappa-B and MAP kinase p38 pathways (By similarity).
May also play a role in the regulation of NADPH oxidase activity in eosinophil after stimulation with IL5, leukotriene B4 or PMA. In collagen-induced platelet aggregation, acts a negative regulator of filopodia formation and actin polymerization by interacting with and negatively regulating VASP phosphorylation. Downstream of PAR1, PAR4 and CD36/GP4 receptors, regulates differentially platelet dense granule secretion; acts as a positive regulator in PAR-mediated granule secretion, whereas it negatively regulates CD36/GP4-mediated granule release. Phosphorylates MUC1 in the C-terminal and regulates the interaction between MUC1 and beta-catenin (By similarity).
The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion. Phosphorylates ELAVL1 in response to angiotensin-2 treatment (By similarity).
Phosphorylates mitochondrial phospholipid scramblase 3 (PLSCR3), resulting in increased cardiolipin expression on the mitochondrial outer membrane which facilitates apoptosis (By similarity).
Phosphorylates SMPD1 which induces SMPD1 secretion (By similarity).
By similarityTruncated isoform 2 is inactive.
Catalytic activityi
Activity regulationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 376 | ATPPROSITE-ProRule annotation | 1 | |
Active sitei | 471 | Proton acceptorPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 158 – 208 | Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST | 51 | |
Zinc fingeri | 230 – 280 | Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST | 51 | |
Nucleotide bindingi | 353 – 361 | ATPPROSITE-ProRule annotation | 9 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- calcium-dependent protein kinase C activity Source: UniProtKB-EC
- calcium-independent protein kinase C activity Source: RGD
- enzyme activator activity Source: RGD
- enzyme binding Source: RGD
- insulin receptor substrate binding Source: RGD
- kinase binding Source: RGD
- metal ion binding Source: UniProtKB-KW
- protein kinase activity Source: RGD
- protein kinase binding Source: RGD
- protein kinase C activity Source: Reactome
- protein serine/threonine/tyrosine kinase activity Source: RHEA
- protein serine/threonine kinase activity Source: RGD
- protein serine kinase activity Source: UniProtKB
- protein tyrosine kinase activity Source: RHEA
- TIR domain binding Source: BHF-UCL
GO - Biological processi
- activation of protein kinase activity Source: RGD
- aging Source: RGD
- apoptotic process Source: CACAO
- B cell proliferation Source: RGD
- cell chemotaxis Source: RGD
- cell cycle Source: UniProtKB-KW
- cellular response to angiotensin Source: UniProtKB
- cellular response to glucose starvation Source: RGD
- cellular response to hydrogen peroxide Source: RGD
- cellular response to hydroperoxide Source: RGD
- cellular response to insulin stimulus Source: RGD
- cellular response to oxidative stress Source: CACAO
- cellular response to UV Source: UniProtKB
- cellular senescence Source: RGD
- collagen metabolic process Source: RGD
- D-aspartate import across plasma membrane Source: RGD
- defense response to bacterium Source: UniProtKB
- histone phosphorylation Source: RGD
- immunoglobulin mediated immune response Source: RGD
- intracellular signal transduction Source: RGD
- negative regulation of actin filament polymerization Source: UniProtKB
- negative regulation of filopodium assembly Source: UniProtKB
- negative regulation of glial cell apoptotic process Source: UniProtKB
- negative regulation of insulin receptor signaling pathway Source: RGD
- negative regulation of MAP kinase activity Source: RGD
- negative regulation of peptidyl-tyrosine phosphorylation Source: RGD
- negative regulation of platelet aggregation Source: UniProtKB
- neutrophil activation Source: RGD
- peptidyl-serine phosphorylation Source: UniProtKB
- peptidyl-threonine phosphorylation Source: RGD
- positive regulation of apoptotic process Source: RGD
- positive regulation of apoptotic signaling pathway Source: RGD
- positive regulation of ceramide biosynthetic process Source: RGD
- positive regulation of endodeoxyribonuclease activity Source: RGD
- positive regulation of glucose import Source: RGD
- positive regulation of glucosylceramide catabolic process Source: RGD
- positive regulation of MAPK cascade Source: RGD
- positive regulation of MAP kinase activity Source: RGD
- positive regulation of phospholipid scramblase activity Source: RGD
- positive regulation of protein dephosphorylation Source: RGD
- positive regulation of protein import into nucleus Source: RGD
- positive regulation of response to DNA damage stimulus Source: RGD
- positive regulation of sphingomyelin catabolic process Source: RGD
- positive regulation of superoxide anion generation Source: UniProtKB
- protein autophosphorylation Source: RGD
- protein phosphorylation Source: RGD
- regulation of actin cytoskeleton organization Source: RGD
- regulation of ceramide biosynthetic process Source: UniProtKB
- regulation of phosphorylation Source: CACAO
- response to amino acid Source: RGD
- response to ethanol Source: RGD
- response to glucose Source: RGD
- response to heat Source: RGD
- response to hydrogen peroxide Source: RGD
- response to hypoxia Source: RGD
- response to mechanical stimulus Source: RGD
- response to organic cyclic compound Source: RGD
- response to organonitrogen compound Source: RGD
- response to oxidative stress Source: RGD
- response to xenobiotic stimulus Source: RGD
- termination of signal transduction Source: RGD
Keywordsi
Molecular function | Kinase, Serine/threonine-protein kinase, Transferase |
Biological process | Apoptosis, Cell cycle |
Ligand | ATP-binding, Metal-binding, Nucleotide-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 2.7.11.13, 5301 |
Reactomei | R-RNO-111465, Apoptotic cleavage of cellular proteins R-RNO-111933, Calmodulin induced events R-RNO-114508, Effects of PIP2 hydrolysis R-RNO-1250196, SHC1 events in ERBB2 signaling R-RNO-1489509, DAG and IP3 signaling R-RNO-2029485, Role of phospholipids in phagocytosis R-RNO-450520, HuR (ELAVL1) binds and stabilizes mRNA R-RNO-5218921, VEGFR2 mediated cell proliferation R-RNO-5607764, CLEC7A (Dectin-1) signaling R-RNO-5668599, RHO GTPases Activate NADPH Oxidases R-RNO-6798695, Neutrophil degranulation R-RNO-877300, Interferon gamma signaling |
Names & Taxonomyi
Protein namesi | Recommended name: Protein kinase C delta typeCurated (EC:2.7.11.13By similarity)Alternative name(s): nPKC-delta Cleaved into the following 2 chains: Alternative name(s): Sphingosine-dependent protein kinase-1 Short name: SDK1 |
Gene namesi | |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 67383, Prkcd |
Subcellular locationi
Nucleus
- Nucleus 1 Publication
Plasma membrane
- Cell membrane By similarity; Peripheral membrane protein By similarity
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Mitochondrion
- Mitochondrion By similarity
Other locations
- perinuclear region 1 Publication
- Endomembrane system By similarity
Note: Translocates to the mitochondria upon apoptotic stimulation. Upon activation, translocates to the plasma membrane followed by partial location to the endolysosomes.By similarity
Cytosol
- cytosol Source: RGD
- postsynaptic cytosol Source: SynGO
Endoplasmic reticulum
- endoplasmic reticulum Source: UniProtKB
Endosome
- endolysosome Source: UniProtKB
Lysosome
- endolysosome Source: UniProtKB
Mitochondrion
- mitochondrion Source: RGD
Nucleus
- nuclear matrix Source: RGD
- nucleus Source: RGD
Plasma Membrane
- plasma membrane Source: RGD
Other locations
- cell-cell junction Source: RGD
- cytoplasm Source: RGD
- membrane Source: RGD
- perinuclear region of cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
Cell membrane, Cytoplasm, Membrane, Mitochondrion, NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 505 | T → A: Decrease in the phosphorylation level. 1 Publication | 1 |
Keywords - Diseasei
Tumor suppressorChemistry databases
ChEMBLi | CHEMBL3633 |
DrugCentrali | P09215 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000055696 | 1 – 673 | Protein kinase C delta typeAdd BLAST | 673 | |
ChainiPRO_0000421671 | 1 – 327 | Protein kinase C delta type regulatory subunitAdd BLAST | 327 | |
ChainiPRO_0000421672 | 328 – 673 | Protein kinase C delta type catalytic subunitAdd BLAST | 346 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 43 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 50 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 64 | Phosphotyrosine1 Publication | 1 | |
Modified residuei | 130 | PhosphoserineBy similarity | 1 | |
Modified residuei | 141 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 155 | Phosphotyrosine1 Publication | 1 | |
Modified residuei | 218 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 299 | Phosphoserine; by autocatalysisBy similarity | 1 | |
Modified residuei | 311 | Phosphotyrosine; by SRCCombined sources1 Publication | 1 | |
Modified residuei | 332 | Phosphotyrosine; by SRC1 Publication | 1 | |
Modified residuei | 372 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 449 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 504 | PhosphoserineBy similarity | 1 | |
Modified residuei | 505 | Phosphothreonine; by autocatalysis3 Publications | 1 | |
Modified residuei | 565 | PhosphotyrosineBy similarity | 1 | |
Modified residuei | 643 | PhosphoserineCombined sources | 1 | |
Modified residuei | 652 | PhosphoserineBy similarity | 1 | |
Modified residuei | 662 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 327 – 328 | Cleavage; by caspase-3Curated | 2 |
Keywords - PTMi
PhosphoproteinProteomic databases
jPOSTi | P09215 |
PaxDbi | P09215 |
PTM databases
iPTMneti | P09215 |
PhosphoSitePlusi | P09215 |
Interactioni
Subunit structurei
Interacts with PDPK1 (via N-terminal region).
Interacts with RAD9A (By similarity).
Interacts with CDCP1.
Interacts with MUC1.
Interacts with VASP.
Interacts with CAVIN3.
Interacts with PRKD2 (via N-terminus and zing-finger domain 1 and 2) in response to oxidative stress; the interaction is independent of PRKD2 tyrosine phosphorylation (By similarity).
Interacts with PLSC3; interaction is enhanced by UV irradiation (By similarity).
By similaritySites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 48 | Interaction with phosphotyrosine-containing peptideBy similarity | 1 | |
Sitei | 62 | Interaction with phosphotyrosine-containing peptideBy similarity | 1 | |
Sitei | 67 | Interaction with phosphotyrosine-containing peptideBy similarity | 1 | |
Sitei | 123 | Interaction with phosphotyrosine-containing peptideBy similarity | 1 |
GO - Molecular functioni
- enzyme binding Source: RGD
- insulin receptor substrate binding Source: RGD
- kinase binding Source: RGD
- protein kinase binding Source: RGD
- TIR domain binding Source: BHF-UCL
Protein-protein interaction databases
BioGRIDi | 250924, 10 interactors |
IntActi | P09215, 6 interactors |
STRINGi | 10116.ENSRNOP00000025858 |
Chemistry databases
BindingDBi | P09215 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P09215 |
SMRi | P09215 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P09215 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1 – 106 | C2PROSITE-ProRule annotationAdd BLAST | 106 | |
Domaini | 347 – 601 | Protein kinasePROSITE-ProRule annotationAdd BLAST | 255 | |
Domaini | 602 – 673 | AGC-kinase C-terminalPROSITE-ProRule annotationAdd BLAST | 72 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 158 – 208 | Phorbol-ester/DAG-type 1PROSITE-ProRule annotationAdd BLAST | 51 | |
Zinc fingeri | 230 – 280 | Phorbol-ester/DAG-type 2PROSITE-ProRule annotationAdd BLAST | 51 |
Keywords - Domaini
Repeat, Zinc-fingerPhylogenomic databases
eggNOGi | KOG0694, Eukaryota |
InParanoidi | P09215 |
OrthoDBi | 222529at2759 |
PhylomeDBi | P09215 |
Family and domain databases
CDDi | cd00029, C1, 2 hits |
Gene3Di | 2.60.40.150, 1 hit |
InterProi | View protein in InterPro IPR000961, AGC-kinase_C IPR046349, C1-like_sf IPR000008, C2_dom IPR035892, C2_domain_sf IPR020454, DAG/PE-bd IPR011009, Kinase-like_dom_sf IPR002219, PE/DAG-bd IPR027436, PKC_delta IPR017892, Pkinase_C IPR014376, Prot_kin_PKC_delta IPR000719, Prot_kinase_dom IPR017441, Protein_kinase_ATP_BS IPR008271, Ser/Thr_kinase_AS |
Pfami | View protein in Pfam PF00130, C1_1, 2 hits PF00069, Pkinase, 1 hit PF00433, Pkinase_C, 1 hit |
PIRSFi | PIRSF000551, PKC_delta, 1 hit PIRSF501104, Protein_kin_C_delta, 1 hit |
PRINTSi | PR00008, DAGPEDOMAIN |
SMARTi | View protein in SMART SM00109, C1, 2 hits SM00133, S_TK_X, 1 hit SM00220, S_TKc, 1 hit |
SUPFAMi | SSF49562, SSF49562, 1 hit SSF56112, SSF56112, 1 hit SSF57889, SSF57889, 2 hits |
PROSITEi | View protein in PROSITE PS51285, AGC_KINASE_CTER, 1 hit PS50004, C2, 1 hit PS00107, PROTEIN_KINASE_ATP, 1 hit PS50011, PROTEIN_KINASE_DOM, 1 hit PS00108, PROTEIN_KINASE_ST, 1 hit PS00479, ZF_DAG_PE_1, 2 hits PS50081, ZF_DAG_PE_2, 2 hits |
s (2+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MAPFLRISFN SYELGSLQAE DDASQPFCAV KMKEALTTDR GKTLVQKKPT
60 70 80 90 100
MYPEWKSTFD AHIYEGRVIQ IVLMRAAEDP MSEVTVGVSV LAERCKKNNG
110 120 130 140 150
KAEFWLDLQP QAKVLMCVQY FLEDGDCKQS MRSEEEAMFP TMNRRGAIKQ
160 170 180 190 200
AKIHYIKNHE FIATFFGQPT FCSVCKEFVW GLNKQGYKCR QCNAAIHKKC
210 220 230 240 250
IDKIIGRCTG TATNSRDTIF QKERFNIDMP HRFKVYNYMS PTFCDHCGTL
260 270 280 290 300
LWGLVKQGLK CEDCGMNVHH KCREKVANLC GINQKLLAEA LNQVTQKASR
310 320 330 340 350
KPETPETVGI YQGFEKKTAV SGNDIPDNNG TYGKIWEGSN RCRLENFTFQ
360 370 380 390 400
KVLGKGSFGK VLLAELKGKE RYFAIKYLKK DVVLIDDDVE CTMVEKRVLA
410 420 430 440 450
LAWENPFLTH LICTFQTKDH LFFVMEFLNG GDLMFHIQDK GRFELYRATF
460 470 480 490 500
YAAEIICGLQ FLHGKGIIYR DLKLDNVMLD KDGHIKIADF GMCKENIFGE
510 520 530 540 550
NRASTFCGTP DYIAPEILQG LKYSFSVDWW SFGVLLYEML IGQSPFHGDD
560 570 580 590 600
EDELFESIRV DTPHYPRWIT KESKDIMEKL FERDPAKRLG VTGNIRLHPF
610 620 630 640 650
FKTINWNLLE KRKVEPPFKP KVKSPSDYSN FDPEFLNEKP QLSFSDKNLI
660 670
DSMDQTAFKG FSFVNPKYEQ FLE
Computationally mapped potential isoform sequencesi
There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A140UHX0 | A0A140UHX0_RAT | Protein kinase C delta type | Prkcd rCG_42255 | 673 | Annotation score: | ||
D4A0U0 | D4A0U0_RAT | Protein kinase C | Prkcd | 569 | Annotation score: | ||
A0A8I5ZVA4 | A0A8I5ZVA4_RAT | Protein kinase C delta type | Prkcd | 682 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 147 | A → S AA sequence (PubMed:1915352).Curated | 1 | |
Sequence conflicti | 249 | T → S in CAB75578 (PubMed:10721703).Curated | 1 | |
Sequence conflicti | 249 | T → S in AAH76505 (PubMed:15489334).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_004742 | 327 – 673 | DNNGT…EQFLE → GESGSHIPLKLPFPDRAREK NSSETWDKTTTGPMARSGRG ATGAALRTSPSRKYLAKAAL ARYCLQN in isoform 2. 1 PublicationAdd BLAST | 347 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M18330 mRNA Translation: AAA41871.1 AJ230617 , AJ230618, AJ230619, AJ230620, AJ230621, AJ230622, AJ230623, AJ230624, AJ230625, AJ230626, AJ230627, AJ230628, AJ230629, AJ230630, AJ230631, AJ230632, AJ230633 Genomic DNA Translation: CAB75578.1 AF219629 mRNA Translation: AAF32345.1 BC076505 mRNA Translation: AAH76505.1 |
PIRi | A28163, KIRTCD |
RefSeqi | NP_579841.1, NM_133307.1 [P09215-1] |
Genome annotation databases
GeneIDi | 170538 |
KEGGi | rno:170538 |
UCSCi | RGD:67383, rat [P09215-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M18330 mRNA Translation: AAA41871.1 AJ230617 , AJ230618, AJ230619, AJ230620, AJ230621, AJ230622, AJ230623, AJ230624, AJ230625, AJ230626, AJ230627, AJ230628, AJ230629, AJ230630, AJ230631, AJ230632, AJ230633 Genomic DNA Translation: CAB75578.1 AF219629 mRNA Translation: AAF32345.1 BC076505 mRNA Translation: AAH76505.1 |
PIRi | A28163, KIRTCD |
RefSeqi | NP_579841.1, NM_133307.1 [P09215-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1BDY | X-ray | 2.20 | A/B | 1-123 | [»] | |
AlphaFoldDBi | P09215 | |||||
SMRi | P09215 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 250924, 10 interactors |
IntActi | P09215, 6 interactors |
STRINGi | 10116.ENSRNOP00000025858 |
Chemistry databases
BindingDBi | P09215 |
ChEMBLi | CHEMBL3633 |
DrugCentrali | P09215 |
PTM databases
iPTMneti | P09215 |
PhosphoSitePlusi | P09215 |
Proteomic databases
jPOSTi | P09215 |
PaxDbi | P09215 |
Genome annotation databases
GeneIDi | 170538 |
KEGGi | rno:170538 |
UCSCi | RGD:67383, rat [P09215-1] |
Organism-specific databases
CTDi | 5580 |
RGDi | 67383, Prkcd |
Phylogenomic databases
eggNOGi | KOG0694, Eukaryota |
InParanoidi | P09215 |
OrthoDBi | 222529at2759 |
PhylomeDBi | P09215 |
Enzyme and pathway databases
BRENDAi | 2.7.11.13, 5301 |
Reactomei | R-RNO-111465, Apoptotic cleavage of cellular proteins R-RNO-111933, Calmodulin induced events R-RNO-114508, Effects of PIP2 hydrolysis R-RNO-1250196, SHC1 events in ERBB2 signaling R-RNO-1489509, DAG and IP3 signaling R-RNO-2029485, Role of phospholipids in phagocytosis R-RNO-450520, HuR (ELAVL1) binds and stabilizes mRNA R-RNO-5218921, VEGFR2 mediated cell proliferation R-RNO-5607764, CLEC7A (Dectin-1) signaling R-RNO-5668599, RHO GTPases Activate NADPH Oxidases R-RNO-6798695, Neutrophil degranulation R-RNO-877300, Interferon gamma signaling |
Miscellaneous databases
EvolutionaryTracei | P09215 |
PROi | PR:P09215 |
Family and domain databases
CDDi | cd00029, C1, 2 hits |
Gene3Di | 2.60.40.150, 1 hit |
InterProi | View protein in InterPro IPR000961, AGC-kinase_C IPR046349, C1-like_sf IPR000008, C2_dom IPR035892, C2_domain_sf IPR020454, DAG/PE-bd IPR011009, Kinase-like_dom_sf IPR002219, PE/DAG-bd IPR027436, PKC_delta IPR017892, Pkinase_C IPR014376, Prot_kin_PKC_delta IPR000719, Prot_kinase_dom IPR017441, Protein_kinase_ATP_BS IPR008271, Ser/Thr_kinase_AS |
Pfami | View protein in Pfam PF00130, C1_1, 2 hits PF00069, Pkinase, 1 hit PF00433, Pkinase_C, 1 hit |
PIRSFi | PIRSF000551, PKC_delta, 1 hit PIRSF501104, Protein_kin_C_delta, 1 hit |
PRINTSi | PR00008, DAGPEDOMAIN |
SMARTi | View protein in SMART SM00109, C1, 2 hits SM00133, S_TK_X, 1 hit SM00220, S_TKc, 1 hit |
SUPFAMi | SSF49562, SSF49562, 1 hit SSF56112, SSF56112, 1 hit SSF57889, SSF57889, 2 hits |
PROSITEi | View protein in PROSITE PS51285, AGC_KINASE_CTER, 1 hit PS50004, C2, 1 hit PS00107, PROTEIN_KINASE_ATP, 1 hit PS50011, PROTEIN_KINASE_DOM, 1 hit PS00108, PROTEIN_KINASE_ST, 1 hit PS00479, ZF_DAG_PE_1, 2 hits PS50081, ZF_DAG_PE_2, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | KPCD_RAT | |
Accessioni | P09215Primary (citable) accession number: P09215 Secondary accession number(s): Q6DG48, Q9JK29, Q9JL03 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | July 1, 1989 | |
Last modified: | May 25, 2022 | |
This is version 214 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families