PRKCQ
entrez
5588
canonical
uniprot
Q04759
canonical
ensembl
ENSG00000065675
resolver
ensp
ENSP00000263125
resolver
ensp
ENSP00000380361
resolver
ensp
ENSP00000441752
resolver
ensp
ENSP00000536256
resolver
ensp
ENSP00000625487
resolver
ensp
ENSP00000785374
resolver
ensp
ENSP00000785375
resolver
genesymbol
PRKCQ
resolver
genesymbol_syn
PRKCT
resolver
hgnc
HGNC:9410
resolver
uniprot
B4DF52
resolver
uniprot
Q14DH6
resolver
uniprot
Q3MJF1
resolver
uniprot
Q64FY5
resolver
uniprot
Q9H508
resolver
uniprot
Q9H549
resolver
uniprot_entry
KPCT_HUMAN
resolver
uniprot_sec
B4DF52
resolver
uniprot_sec
Q14DH6
resolver
uniprot_sec
Q3MJF1
resolver
uniprot_sec
Q64FY5
resolver
uniprot_sec
Q9H508
resolver
uniprot_sec
Q9H549
resolver
activity_regulation
ACTIVITY REGULATION: Novel PKCs (PRKCD, PRKCE, PRKCH and PRKCQ) are calcium-insensitive, but activated by diacylglycerol (DAG) and phosphatidylserine. Three specific sites; Thr-538 (activation loop of the kinase domain), Ser-676 (turn motif) and Ser-695 (hydrophobic region), need to be phosphorylated for its full activation. Inhibited by PRKCH upstream open reading frame 2 (PubMed:34593629). {ECO:0000269|PubMed:34593629}.
uniprot
proteins
amino_acid_sequence
MSPFLRIGLSNFDCGSCQSCQGEAVNPYCAVLVKEYVESENGQMYIQKKPTMYPPWDSTFDAHINKGRVMQIIVKGKNVDLISETTVELYSLAERCRKNNGKTEIWLELKPQGRMLMNARYFLEMSDTKDMNEFETEGFFALHQRRGAIKQAKVHHVKCHEFTATFFPQPTFCSVCHEFVWGLNKQGYQCRQCNAAIHKKCIDKVIAKCTGSAINSRETMFHKERFKIDMPHRFKVYNYKSPTFCEHCGTLLWGLARQGLKCDACGMNVHHRCQTKVANLCGINQKLMAEALAMIESTQQARCLRDTEQIFREGPVEIGLPCSIKNEARPPCLPTPGKREPQGISWESPLDEVDKMCHLPEPELNKERPSLQIKLKIEDFILHKMLGKGSFGKVFLAEFKKTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTHMFCTFQTKENLFFVMEYLNGGDLMYHIQSCHKFDLSRATFYAAEIILGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAKTNTFCGTPDYIAPEILLGQKYNHSVDWWSFGVLLYEMLIGQSPFHGQDEEELFHSIRMDNPFYPRWLEKEAKDLLVKLFVREPEKRLGVRGDIRQHPLFREINWEELERKEIDPPFRPKVKSPFDCSNFDKEFLNEKPRLSFADRALINSMDQNMFRNFSFMNPGMERLIS
uniprot
proteins
ec_number
2.7.11.13
uniprot
proteins
function
FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that mediates non-redundant functions in T-cell receptor (TCR) signaling, including T-cells activation, proliferation, differentiation and survival, by mediating activation of multiple transcription factors such as NF-kappa-B, JUN, NFATC1 and NFATC2. In TCR-CD3/CD28-co-stimulated T-cells, is required for the activation of NF-kappa-B and JUN, which in turn are essential for IL2 production, and participates in the calcium-dependent NFATC1 and NFATC2 transactivation (PubMed:21964608). Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on several serine residues, inducing CARD11 association with lipid rafts and recruitment of the BCL10-MALT1 complex, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. May also play an indirect role in activation of the non-canonical NF-kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN activation, acts by phosphorylating the mediator STK39/SPAK and may not act through MAP kinases signaling. Plays a critical role in TCR/CD28-induced NFATC1 and NFATC2 transactivation by participating in the regulation of reduced inositol 1,4,5-trisphosphate generation and intracellular calcium mobilization. After costimulation of T-cells through CD28 can phosphorylate CBLB and is required for the ubiquitination and subsequent degradation of CBLB, which is a prerequisite for the activation of TCR. During T-cells differentiation, plays an important role in the development of T-helper 2 (Th2) cells following immune and inflammatory responses, and, in the development of inflammatory autoimmune diseases, is necessary for the activation of IL17-producing Th17 cells. May play a minor role in Th1 response. Upon TCR stimulation, mediates T-cell protective survival signal by phosphorylating BAD, thus protecting T-cells from BAD-induced apoptosis, and by up-regulating BCL-X(L)/BCL2L1 levels through NF-kappa-B and JUN pathways. In platelets, regulates signal transduction downstream of the ITGA2B, CD36/GP4, F2R/PAR1 and F2RL3/PAR4 receptors, playing a positive role in 'outside-in' signaling and granule secretion signal transduction. May relay signals from the activated ITGA2B receptor by regulating the uncoupling of WASP and WIPF1, thereby permitting the regulation of actin filament nucleation and branching activity of the Arp2/3 complex. May mediate inhibitory effects of free fatty acids on insulin signaling by phosphorylating IRS1, which in turn blocks IRS1 tyrosine phosphorylation and downstream activation of the PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of phosphatidylglycerol or phosphatidylinositol. Phosphorylates PDPK1 at 'Ser-504' and 'Ser-532' and negatively regulates its ability to phosphorylate PKB/AKT1. Phosphorylates CCDC88A/GIV and inhibits its guanine nucleotide exchange factor activity (PubMed:23509302). Phosphorylates and activates LRRK1, which phosphorylates RAB proteins involved in intracellular trafficking (PubMed:36040231). {ECO:0000269|PubMed:11342610, ECO:0000269|PubMed:14988727, ECO:0000269|PubMed:15364919, ECO:0000269|PubMed:16252004, ECO:0000269|PubMed:16356855, ECO:0000269|PubMed:16709830, ECO:0000269|PubMed:19549985, ECO:0000269|PubMed:21964608, ECO:0000269|PubMed:23509302, ECO:0000269|PubMed:36040231, ECO:0000269|PubMed:8657160}.
uniprot
proteins
mass_dalton
81865
uniprot
proteins
mutagenesis
MUTAGEN 90; /note="Y->F: Loss of function in T-cells proliferation. No effect on kinase activity."; /evidence="ECO:0000269|PubMed:10652356"; MUTAGEN 148; /note="A->E: Constitutively active form."; /evidence="ECO:0000269|PubMed:10652356"; MUTAGEN 219; /note="T->A: Loss of transactivation of the IL2 promoter and translocation to the plasma membrane. No effect on kinase activity."; /evidence="ECO:0000269|PubMed:16252004"; MUTAGEN 409; /note="K->A,E: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:10652356"; MUTAGEN 538; /note="T->A: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:11772397, ECO:0000269|PubMed:16252004"; MUTAGEN 676; /note="S->A: Reduction in kinase activity."; /evidence="ECO:0000269|PubMed:16252004"; MUTAGEN 695; /note="S->A: Reduction in kinase activity."; /evidence="ECO:0000269|PubMed:11772397, ECO:0000269|PubMed:16252004
uniprot
proteins
post_translational_modification
PTM: Autophosphorylation at Thr-219 is required for targeting to the TCR and cellular function of PRKCQ upon antigen receptor ligation. Following TCR stimulation, phosphorylated at Tyr-90 and Ser-685. {ECO:0000269|PubMed:10652356, ECO:0000269|PubMed:11772397, ECO:0000269|PubMed:15364937, ECO:0000269|PubMed:16252004, ECO:0000269|Ref.40}.; PTM: Monoubiquitinated in a DTX1-dependent manner, leading to degradation via endosome-lysosome pathway. {ECO:0000269|PubMed:25000980}.
uniprot
proteins
protein_family
AGC Ser/Thr protein kinase family
uniprot
proteins
protein_family
PKC subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
pubmed
10636891
uniprot
proteins
pubmed
10652356
uniprot
proteins
pubmed
11342610
uniprot
proteins
pubmed
11772397
uniprot
proteins
pubmed
11861617
uniprot
proteins
pubmed
12473184
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14988727
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15254234
uniprot
proteins
pubmed
15282562
uniprot
proteins
pubmed
15364919
uniprot
proteins
pubmed
15364937
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16252004
uniprot
proteins
pubmed
16356855
uniprot
proteins
pubmed
16709830
uniprot
proteins
pubmed
16978534
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17544292
uniprot
proteins
pubmed
18328786
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19549985
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21944869
uniprot
proteins
pubmed
21964608
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23509302
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25000980
uniprot
proteins
pubmed
34593629
uniprot
proteins
pubmed
36040231
uniprot
proteins
pubmed
7686153
uniprot
proteins
pubmed
7983077
uniprot
proteins
pubmed
8444877
uniprot
proteins
pubmed
8657160
uniprot
proteins
sequence_length
706
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25000980}. Cell membrane; Peripheral membrane protein. Note=In resting T-cells, mostly localized in cytoplasm. In response to TCR stimulation, associates with lipid rafts and then localizes in the immunological synapse.
uniprot
proteins