KPCT_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KPCT_MOUSE
• UniProt AC: Q02111
• Protein Name: Protein kinase C theta type
• Gene Name: Prkcq
• Organism: Mus musculus (Mouse).
• Sequence Length: 707
• Subcellular Localization: Cytoplasm. Cell membrane; Peripheral membrane protein. In resting T-cells, mostly localized in cytoplasm. In response to TCR stimulation, associates with lipid rafts and then localizes in the immunological synapse (By similarity)..
• Protein Description: 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. 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..
• Protein Sequence: MSPFLRIGLSNFDCGTCQACQGEAVNPYCAVLVKEYVESENGQMYIQKKPTMYPPWDSTFDAHINKGRVMQIIVKGKNVDLISETTVELYSLAERCRKNNGRTEIWLELKPQGRMLMNARYFLEMSDTKDMSEFENEGFFALHQRRGAIKQAKVHHVKCHEFTATFFPQPTFCSVCHEFVWGLNKQGYQCRQCNAAIHKKCIDKVIAKCTGSAINSRETMFHKERFKIDMPHRFKVYNYKSPTFCEHCGTLLWGLARQGLKCDACGMNVHHRCQTKVANLCGINQKLMAEALAMIESTQQARSLRDSEHIFREGPVEIGLPCSTKNETRPPCVPTPGKREPQGISWDSPLDGSNKSAGPPEPEVSMRRTSLQLKLKIDDFILHKMLGKGSFGKVFLAEFKRTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTHMFCTFQTKENLFFVMEYLNGGDLMYHIQSCHKFDLSRATFYAAEVILGLQFLHSKGIVYRDLKLDNILLDRDGHIKIADFGMCKENMLGDAKTNTFCGTPDYIAPEILLGQKYNHSVDWWSFGVLVYEMLIGQSPFHGQDEEELFHSIRMDNPFYPRWLEREAKDLLVKLFVREPEKRLGVRGDIRQHPLFREINWEELERKEIDPPFRPKVKSPYDCSNFDKEFLSEKPRLSFADRALINSMDQNMFSNFSFINPGMETLICS

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
90	Phosphorylation	SETTVELYSLAERCR ECHHHHHHHHHHHHH	6.53	-
210	Phosphorylation	DKVIAKCTGSAINSR HHHHHHHHCCCHHCC	33.20	25266776
212	Phosphorylation	VIAKCTGSAINSRET HHHHHHCCCHHCCCC	14.07	25266776
219	Phosphorylation	SAINSRETMFHKERF CCHHCCCCCCCHHHC	24.83	25266776
303	Phosphorylation	ESTQQARSLRDSEHI HHHHHHHHCCCCCCH	30.67	25266776
307	Phosphorylation	QARSLRDSEHIFREG HHHHCCCCCCHHHCC	25.33	28978645
323	Phosphorylation	VEIGLPCSTKNETRP EEEECCCCCCCCCCC	40.24	25266776
324	Phosphorylation	EIGLPCSTKNETRPP EEECCCCCCCCCCCC	44.60	19060867
328	Phosphorylation	PCSTKNETRPPCVPT CCCCCCCCCCCCCCC	58.85	26239621
348	Phosphorylation	PQGISWDSPLDGSNK CCCCCCCCCCCCCCC	22.54	22210690
353	Phosphorylation	WDSPLDGSNKSAGPP CCCCCCCCCCCCCCC	40.53	22210690
365	Phosphorylation	GPPEPEVSMRRTSLQ CCCCCCHHHCHHHEE	12.62	25266776
369	Phosphorylation	PEVSMRRTSLQLKLK CCHHHCHHHEEEEEE	24.35	22817900
370	Phosphorylation	EVSMRRTSLQLKLKI CHHHCHHHEEEEEEH	16.59	29472430
536	Phosphorylation	NMLGDAKTNTFCGTP CCCCCCCCCCCCCCC	41.01	28833060
538	Phosphorylation	LGDAKTNTFCGTPDY CCCCCCCCCCCCCCC	26.07	28542873
542	Phosphorylation	KTNTFCGTPDYIAPE CCCCCCCCCCCCCHH	17.73	28833060
545	Phosphorylation	TFCGTPDYIAPEILL CCCCCCCCCCHHHHH	10.53	27566939
670	Phosphorylation	NFDKEFLSEKPRLSF CCCHHHHCCCCCCCH	49.23	25266776
676	Phosphorylation	LSEKPRLSFADRALI HCCCCCCCHHHHHHH	21.48	28542873
685	Phosphorylation	ADRALINSMDQNMFS HHHHHHHHCCCCCCC	19.42	-
692	Phosphorylation	SMDQNMFSNFSFINP HCCCCCCCCCCCCCC	26.62	27600695
695	Phosphorylation	QNMFSNFSFINPGME CCCCCCCCCCCCCCC	29.48	22817900
703	Phosphorylation	FINPGMETLICS--- CCCCCCCEECCC---	16.72	14725789

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
90	Y	Phosphorylation	Kinase	LCK	P06240	Uniprot
219	T	Phosphorylation	Kinase	PRKCQ	Q02111	GPS
538	T	Phosphorylation	Kinase	PDPK1	Q9Z2A0	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
219	T	Phosphorylation	Autophosphorylation at Thr-219 is required for targeting to the TCR and cellular function of PRKCQ upon antigen receptor ligation.	-
685	S	Phosphorylation	Following TCR stimulation, phosphorylated at Tyr-90 and Ser-685 (By similarity).	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of KPCT_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MP2K4_MOUSE	Map2k4	physical	22411628
MP2K7_MOUSE	Map2k7	physical	22411628
CISH_MOUSE	Cish	physical	12618484
DTX1_MOUSE	Dtx1	physical	25000980
CBLB_MOUSE	Cblb	physical	25000980

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.