dbPTM

KPCT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KPCT_HUMAN
UniProt AC	Q04759
Protein Name	Protein kinase C theta type
Gene Name	PRKCQ
Organism	Homo sapiens (Human).
Sequence Length	706
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.
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	MSPFLRIGLSNFDCGSCQSCQGEAVNPYCAVLVKEYVESENGQMYIQKKPTMYPPWDSTFDAHINKGRVMQIIVKGKNVDLISETTVELYSLAERCRKNNGKTEIWLELKPQGRMLMNARYFLEMSDTKDMNEFETEGFFALHQRRGAIKQAKVHHVKCHEFTATFFPQPTFCSVCHEFVWGLNKQGYQCRQCNAAIHKKCIDKVIAKCTGSAINSRETMFHKERFKIDMPHRFKVYNYKSPTFCEHCGTLLWGLARQGLKCDACGMNVHHRCQTKVANLCGINQKLMAEALAMIESTQQARCLRDTEQIFREGPVEIGLPCSIKNEARPPCLPTPGKREPQGISWESPLDEVDKMCHLPEPELNKERPSLQIKLKIEDFILHKMLGKGSFGKVFLAEFKKTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTHMFCTFQTKENLFFVMEYLNGGDLMYHIQSCHKFDLSRATFYAAEIILGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAKTNTFCGTPDYIAPEILLGQKYNHSVDWWSFGVLLYEMLIGQSPFHGQDEEELFHSIRMDNPFYPRWLEKEAKDLLVKLFVREPEKRLGVRGDIRQHPLFREINWEELERKEIDPPFRPKVKSPFDCSNFDKEFLNEKPRLSFADRALINSMDQNMFRNFSFMNPGMERLIS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
28	Phosphorylation	QGEAVNPYCAVLVKE CCCCCCHHHHHHHHH	6.45	-
36	Phosphorylation	CAVLVKEYVESENGQ HHHHHHHHHHCCCCC	12.10	26552605
39	Phosphorylation	LVKEYVESENGQMYI HHHHHHHCCCCCEEE	26.73	26552605
41	Ubiquitination	KEYVESENGQMYIQK HHHHHCCCCCEEEEE	56.10	29967540
45	Phosphorylation	ESENGQMYIQKKPTM HCCCCCEEEEECCCC	7.72	26552605
48	Ubiquitination	NGQMYIQKKPTMYPP CCCEEEEECCCCCCC	51.68	29967540
49	Ubiquitination	GQMYIQKKPTMYPPW CCEEEEECCCCCCCC	29.37	29967540
51	Phosphorylation	MYIQKKPTMYPPWDS EEEEECCCCCCCCCC	37.91	-
66	Ubiquitination	TFDAHINKGRVMQII CEECEECCCCEEEEE	47.71	-
75	Ubiquitination	RVMQIIVKGKNVDLI CEEEEEECCCCCEEE	54.48	-
77	Ubiquitination	MQIIVKGKNVDLISE EEEEECCCCCEEEEC	48.34	29967540
79	Ubiquitination	IIVKGKNVDLISETT EEECCCCCEEEECHH	7.84	29967540
83	Ubiquitination	GKNVDLISETTVELY CCCCEEEECHHHHHH	35.87	-
83	Ubiquitination	GKNVDLISETTVELY CCCCEEEECHHHHHH	35.87	29967540
90	Phosphorylation	SETTVELYSLAERCR ECHHHHHHHHHHHHH	6.53	17548359
98	Ubiquitination	SLAERCRKNNGKTEI HHHHHHHHHCCCEEE	59.39	-
98	Ubiquitination	SLAERCRKNNGKTEI HHHHHHHHHCCCEEE	59.39	29967540
102	Ubiquitination	RCRKNNGKTEIWLEL HHHHHCCCEEEEEEE	45.14	-
102	Ubiquitination	RCRKNNGKTEIWLEL HHHHHCCCEEEEEEE	45.14	29967540
110	Ubiquitination	TEIWLELKPQGRMLM EEEEEEECHHHCEEE	26.39	-
110	Ubiquitination	TEIWLELKPQGRMLM EEEEEEECHHHCEEE	26.39	29967540
115	Ubiquitination	ELKPQGRMLMNARYF EECHHHCEEEEEEHH	5.50	-
121	Phosphorylation	RMLMNARYFLEMSDT CEEEEEEHHHHCCCC	15.31	-
151	Ubiquitination	QRRGAIKQAKVHHVK HHCCCCCCCEEEECC	40.06	-
151	Ubiquitination	QRRGAIKQAKVHHVK HHCCCCCCCEEEECC	40.06	29967540
161	Ubiquitination	VHHVKCHEFTATFFP EEECCCCCCEEECCC	54.91	-
168	Ubiquitination	EFTATFFPQPTFCSV CCEEECCCCCCCHHH	34.74	29967540
172	Ubiquitination	TFFPQPTFCSVCHEF ECCCCCCCHHHHHHH	3.58	29967540
187	Ubiquitination	VWGLNKQGYQCRQCN HHCCCCCCCCCCCCC	18.98	29967540
191	Ubiquitination	NKQGYQCRQCNAAIH CCCCCCCCCCCHHHH	28.67	29967540
199	Ubiquitination	QCNAAIHKKCIDKVI CCCHHHHHHHHHHHH	43.13	29967540
200	Ubiquitination	CNAAIHKKCIDKVIA CCHHHHHHHHHHHHH	23.43	-
200	Ubiquitination	CNAAIHKKCIDKVIA CCHHHHHHHHHHHHH	23.43	24816145
204	Ubiquitination	IHKKCIDKVIAKCTG HHHHHHHHHHHHHHC	18.67	29967540
208	Acetylation	CIDKVIAKCTGSAIN HHHHHHHHHHCCCHH	22.62	25953088
208	Ubiquitination	CIDKVIAKCTGSAIN HHHHHHHHHHCCCHH	22.62	29967540
212	Phosphorylation	VIAKCTGSAINSRET HHHHHHCCCHHCCCC	14.07	27080861
213	Ubiquitination	IAKCTGSAINSRETM HHHHHCCCHHCCCCC	13.31	29967540
216	Phosphorylation	CTGSAINSRETMFHK HHCCCHHCCCCCCCH	25.94	27080861
219	Phosphorylation	SAINSRETMFHKERF CCHHCCCCCCCHHHC	24.83	28060719
223	Ubiquitination	SRETMFHKERFKIDM CCCCCCCHHHCCCCC	39.04	29967540
227	Ubiquitination	MFHKERFKIDMPHRF CCCHHHCCCCCCCCE	43.98	29967540
230	Ubiquitination	KERFKIDMPHRFKVY HHHCCCCCCCCEEEC	3.24	29967540
235	Ubiquitination	IDMPHRFKVYNYKSP CCCCCCEEECCCCCC	43.71	29967540
240	Ubiquitination	RFKVYNYKSPTFCEH CEEECCCCCCCHHHH	46.45	29967540
249	Ubiquitination	PTFCEHCGTLLWGLA CCHHHHHHHHHHHHH	22.70	29967540
251	Ubiquitination	FCEHCGTLLWGLARQ HHHHHHHHHHHHHHC	1.99	-
251	Ubiquitination	FCEHCGTLLWGLARQ HHHHHHHHHHHHHHC	1.99	29967540
259	Ubiquitination	LWGLARQGLKCDACG HHHHHHCCCCCCCCC	22.88	-
259	Acetylation	LWGLARQGLKCDACG HHHHHHCCCCCCCCC	22.88	19608861
259	Ubiquitination	LWGLARQGLKCDACG HHHHHHCCCCCCCCC	22.88	29967540
263	Ubiquitination	ARQGLKCDACGMNVH HHCCCCCCCCCCCHH	43.22	-
263	Ubiquitination	ARQGLKCDACGMNVH HHCCCCCCCCCCCHH	43.22	29967540
275	Ubiquitination	NVHHRCQTKVANLCG CHHHHHHHHHHHHHC	30.98	-
275	Phosphorylation	NVHHRCQTKVANLCG CHHHHHHHHHHHHHC	30.98	-
275	Ubiquitination	NVHHRCQTKVANLCG CHHHHHHHHHHHHHC	30.98	29967540
276	Ubiquitination	VHHRCQTKVANLCGI HHHHHHHHHHHHHCC	17.30	-
276	Ubiquitination	VHHRCQTKVANLCGI HHHHHHHHHHHHHCC	17.30	29967540
284	Ubiquitination	VANLCGINQKLMAEA HHHHHCCCHHHHHHH	20.44	29967540
286	Ubiquitination	NLCGINQKLMAEALA HHHCCCHHHHHHHHH	35.42	-
289	Ubiquitination	GINQKLMAEALAMIE CCCHHHHHHHHHHHH	14.89	24816145
297	Phosphorylation	EALAMIESTQQARCL HHHHHHHHHHHHHHH	22.16	28857561
302	Ubiquitination	IESTQQARCLRDTEQ HHHHHHHHHHHCHHH	18.70	29967540
304	Ubiquitination	STQQARCLRDTEQIF HHHHHHHHHCHHHHH	4.65	-
307	Phosphorylation	QARCLRDTEQIFREG HHHHHHCHHHHHHHC	24.29	22322096
319	Ubiquitination	REGPVEIGLPCSIKN HHCCCEEECCCCCCC	15.29	29967540
323	Phosphorylation	VEIGLPCSIKNEARP CEEECCCCCCCCCCC	34.36	30266825
325	Ubiquitination	IGLPCSIKNEARPPC EECCCCCCCCCCCCC	32.23	24816145
338	Acetylation	PCLPTPGKREPQGIS CCCCCCCCCCCCCCC	55.58	25953088
338	Ubiquitination	PCLPTPGKREPQGIS CCCCCCCCCCCCCCC	55.58	29967540
340	Ubiquitination	LPTPGKREPQGISWE CCCCCCCCCCCCCCC	45.52	29967540
345	Phosphorylation	KREPQGISWESPLDE CCCCCCCCCCCCHHH	31.45	28122231
348	Acetylation	PQGISWESPLDEVDK CCCCCCCCCHHHHHH	25.22	19608861
348	Phosphorylation	PQGISWESPLDEVDK CCCCCCCCCHHHHHH	25.22	25159151
348	Ubiquitination	PQGISWESPLDEVDK CCCCCCCCCHHHHHH	25.22	29967540
352	Ubiquitination	SWESPLDEVDKMCHL CCCCCHHHHHHHHCC	61.37	29967540
355	Ubiquitination	SPLDEVDKMCHLPEP CCHHHHHHHHCCCCC	48.91	29967540
359	Ubiquitination	EVDKMCHLPEPELNK HHHHHHCCCCCHHCC	4.35	24816145
364	Ubiquitination	CHLPEPELNKERPSL HCCCCCHHCCCCCCC	19.00	29967540
365	Ubiquitination	HLPEPELNKERPSLQ CCCCCHHCCCCCCCE	42.34	29967540
370	Phosphorylation	ELNKERPSLQIKLKI HHCCCCCCCEEEEEH	38.84	26552605
373	Ubiquitination	KERPSLQIKLKIEDF CCCCCCEEEEEHHHH	7.37	29967540
374	Ubiquitination	ERPSLQIKLKIEDFI CCCCCEEEEEHHHHH	30.66	29967540
376	Ubiquitination	PSLQIKLKIEDFILH CCCEEEEEHHHHHHH	38.76	29967540
381	Ubiquitination	KLKIEDFILHKMLGK EEEHHHHHHHHHHCC	6.44	-
381	Ubiquitination	KLKIEDFILHKMLGK EEEHHHHHHHHHHCC	6.44	29967540
384	Acetylation	IEDFILHKMLGKGSF HHHHHHHHHHCCCCC	32.16	19608861
384	Ubiquitination	IEDFILHKMLGKGSF HHHHHHHHHHCCCCC	32.16	19608861
388	Ubiquitination	ILHKMLGKGSFGKVF HHHHHHCCCCCCHHH	47.63	29967540
389	Ubiquitination	LHKMLGKGSFGKVFL HHHHHCCCCCCHHHH	26.80	-
389	Ubiquitination	LHKMLGKGSFGKVFL HHHHHCCCCCCHHHH	26.80	29967540
400	Ubiquitination	KVFLAEFKKTNQFFA HHHHHHHHHHCCEEE	50.63	29967540
401	Ubiquitination	VFLAEFKKTNQFFAI HHHHHHHHHCCEEEE	59.01	29967540
402	Ubiquitination	FLAEFKKTNQFFAIK HHHHHHHHCCEEEEE	34.54	-
402	Ubiquitination	FLAEFKKTNQFFAIK HHHHHHHHCCEEEEE	34.54	22505724
409	Ubiquitination	TNQFFAIKALKKDVV HCCEEEEEECCCCEE	44.21	29967540
410	Ubiquitination	NQFFAIKALKKDVVL CCEEEEEECCCCEEE	20.64	-
410	Ubiquitination	NQFFAIKALKKDVVL CCEEEEEECCCCEEE	20.64	29967540
429	Ubiquitination	VECTMVEKRVLSLAW CEEEHHHHHHHHHHH	36.07	-
470	Ubiquitination	GGDLMYHIQSCHKFD CCCCEEEEHHHHCCC	1.45	29967540
478	Ubiquitination	QSCHKFDLSRATFYA HHHHCCCCHHHHHHH	4.14	29967540
479	Ubiquitination	SCHKFDLSRATFYAA HHHCCCCHHHHHHHH	23.01	-
482	Acetylation	KFDLSRATFYAAEII CCCCHHHHHHHHHHH	18.97	-
491	Ubiquitination	YAAEIILGLQFLHSK HHHHHHHHHHHHHHC	13.66	22505724
495	Ubiquitination	IILGLQFLHSKGIVY HHHHHHHHHHCCCEE	2.62	-
499	Ubiquitination	LQFLHSKGIVYRDLK HHHHHHCCCEECEEE	20.01	29967540
506	Ubiquitination	GIVYRDLKLDNILLD CCEECEEECCCEEEC	59.07	29967540
514	Ubiquitination	LDNILLDKDGHIKIA CCCEEECCCCCEEEC	66.63	29967540
520	Ubiquitination	DKDGHIKIADFGMCK CCCCCEEECCCCCCC	4.38	29967540
527	Ubiquitination	IADFGMCKENMLGDA ECCCCCCCCCCCCCC	43.14	22505724
529	Ubiquitination	DFGMCKENMLGDAKT CCCCCCCCCCCCCCC	19.24	29967540
531	Ubiquitination	GMCKENMLGDAKTNT CCCCCCCCCCCCCCC	9.41	29967540
535	Ubiquitination	ENMLGDAKTNTFCGT CCCCCCCCCCCCCCC	47.23	29967540
536	Phosphorylation	NMLGDAKTNTFCGTP CCCCCCCCCCCCCCC	41.01	23401153
538	Phosphorylation	LGDAKTNTFCGTPDY CCCCCCCCCCCCCCC	26.07	23401153
541	Ubiquitination	AKTNTFCGTPDYIAP CCCCCCCCCCCCCCH	35.77	29967540
542	Phosphorylation	KTNTFCGTPDYIAPE CCCCCCCCCCCCCHH	17.73	23898821
545	Phosphorylation	TFCGTPDYIAPEILL CCCCCCCCCCHHHHH	10.53	28122231
547	Ubiquitination	CGTPDYIAPEILLGQ CCCCCCCCHHHHHCC	6.88	-
547	Ubiquitination	CGTPDYIAPEILLGQ CCCCCCCCHHHHHCC	6.88	29967540
561	Ubiquitination	QKYNHSVDWWSFGVL CCCCCCCCHHHHHHH	44.11	22505724
582	Ubiquitination	GQSPFHGQDEEELFH CCCCCCCCCHHHHHH	46.50	29967540
591	Ubiquitination	EEELFHSIRMDNPFY HHHHHHHHHCCCCCC	2.95	29967540
593	Ubiquitination	ELFHSIRMDNPFYPR HHHHHHHCCCCCCHH	5.79	29967540
603	Ubiquitination	PFYPRWLEKEAKDLL CCCHHHHHHHHHHHH	41.72	29967540
604	Ubiquitination	FYPRWLEKEAKDLLV CCHHHHHHHHHHHHH	61.88	-
607	Acetylation	RWLEKEAKDLLVKLF HHHHHHHHHHHHHHH	50.42	23749302
609	Ubiquitination	LEKEAKDLLVKLFVR HHHHHHHHHHHHHCC	6.12	29967540
618	Ubiquitination	VKLFVREPEKRLGVR HHHHCCCHHHHHCCC	41.67	29967540
620	Ubiquitination	LFVREPEKRLGVRGD HHCCCHHHHHCCCCC	64.73	29967540
630	Ubiquitination	GVRGDIRQHPLFREI CCCCCHHHCHHHHCC	42.77	29967540
636	Ubiquitination	RQHPLFREINWEELE HHCHHHHCCCHHHHH	33.08	29967540
645	Ubiquitination	NWEELERKEIDPPFR CHHHHHHCCCCCCCC	50.04	29967540
654	Ubiquitination	IDPPFRPKVKSPFDC CCCCCCCCCCCCCCC	59.02	29967540
656	Ubiquitination	PPFRPKVKSPFDCSN CCCCCCCCCCCCCCC	59.54	29967540
657	Phosphorylation	PFRPKVKSPFDCSNF CCCCCCCCCCCCCCC	33.51	19369195
662	Phosphorylation	VKSPFDCSNFDKEFL CCCCCCCCCCCHHHH	42.23	-
666	Ubiquitination	FDCSNFDKEFLNEKP CCCCCCCHHHHCCCC	46.35	29967540
672	Ubiquitination	DKEFLNEKPRLSFAD CHHHHCCCCCCCHHH	34.07	29967540
676	Phosphorylation	LNEKPRLSFADRALI HCCCCCCCHHHHHHH	21.48	23401153
685	Phosphorylation	ADRALINSMDQNMFR HHHHHHHHCCHHHHH	19.42	30266825
695	Phosphorylation	QNMFRNFSFMNPGME HHHHHCCCCCCCCHH	27.43	25159151
706	Phosphorylation	PGMERLIS------- CCHHHHCC-------	38.47	26074081

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	P06239	Uniprot
219	T	Phosphorylation	Kinase	KPCT	Q04759	PhosphoELM
219	T	Phosphorylation	Kinase	PRKCQ	Q02111	GPS
538	T	Phosphorylation	Kinase	MAP4K3	Q8IVH8	GPS
538	T	Phosphorylation	Kinase	PDPK1	O15530	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
219	T	Phosphorylation	16252004
Autophosphorylation at Thr-219 is required for targeting to the TCR and cellular function of PRKCQ upon antigen receptor ligation.
685	S	Phosphorylation	18691976
Following TCR stimulation, phosphorylated at Tyr-90 and Ser-685.

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of KPCT_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VAV_HUMAN	VAV1	physical	10725744
FYN_HUMAN	FYN	physical	10383400
LCK_HUMAN	LCK	physical	10383400
TAL1_HUMAN	TAL1	physical	10383400
IKKB_HUMAN	IKBKB	physical	11120819
1433G_HUMAN	YWHAG	physical	10433554
AKT1_HUMAN	AKT1	physical	11410591
GLRX3_HUMAN	GLRX3	physical	10636891
PDPK1_HUMAN	PDPK1	physical	15802604
IKKA_HUMAN	CHUK	physical	15802604
IKKB_HUMAN	IKBKB	physical	15802604
NEMO_HUMAN	IKBKG	physical	15802604
JUND_HUMAN	JUND	physical	16264271
NF2L2_HUMAN	NFE2L2	physical	19920073
KPCT_HUMAN	PRKCQ	physical	19920073
IKKA_HUMAN	CHUK	physical	20164171
IKKB_HUMAN	IKBKB	physical	20164171
M3K7_HUMAN	MAP3K7	physical	20164171
FYB1_HUMAN	FYB	physical	20164171
CAR11_HUMAN	CARD11	physical	20164171
BCL10_HUMAN	BCL10	physical	20164171
1433T_HUMAN	YWHAQ	physical	8816492
CBL_HUMAN	CBL	physical	10358153
CAR11_HUMAN	CARD11	physical	16356855
GRP3_HUMAN	RASGRP3	physical	12730099
IKKB_HUMAN	IKBKB	physical	17363905
IKKA_HUMAN	CHUK	physical	17363905
MALT1_HUMAN	MALT1	physical	17363905
BCL10_HUMAN	BCL10	physical	17363905
M3K7_HUMAN	MAP3K7	physical	17363905
KPCT_HUMAN	PRKCQ	physical	11410591
C2C2L_HUMAN	C2CD2L	physical	28514442
ZNF24_HUMAN	ZNF24	physical	28514442
CAR11_HUMAN	CARD11	physical	19706536
KPCT_HUMAN	PRKCQ	physical	19706536

Drug and Disease Associations

Kegg Disease
H00408	Type I diabetes mellitus
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D09671	Sotrastaurin (USAN/INN)
D09718	Sotrastaurin acetate (USAN)
DrugBank
DB00675	Tamoxifen

Regulatory Network of KPCT_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-384, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-536; SER-657; SER-676;SER-685 AND SER-695, AND MASS SPECTROMETRY.	19369195 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-348; SER-676; SER-685AND SER-695, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry."; Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.; Mol. Cell. Proteomics 6:537-547(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-538; SER-685 ANDSER-695, AND MASS SPECTROMETRY.	17192257 [Abstract]
"Critical role of novel Thr-219 autophosphorylation for the cellularfunction of PKCtheta in T lymphocytes."; Thuille N., Heit I., Fresser F., Krumbock N., Bauer B.,Leuthaeusser S., Dammeier S., Graham C., Copeland T.D., Shaw S.,Baier G.; EMBO J. 24:3869-3880(2005). Cited for: FUNCTION, PHOSPHORYLATION AT THR-219; THR-538; SER-676 AND SER-695,AND MUTAGENESIS OF THR-219; THR-538; SER-676 AND SER-695.	16252004 [Abstract]
"Regulation of protein kinase Ctheta function during T cell activationby Lck-mediated tyrosine phosphorylation."; Liu Y., Witte S., Liu Y.C., Doyle M., Elly C., Altman A.; J. Biol. Chem. 275:3603-3609(2000). Cited for: PHOSPHORYLATION AT TYR-90, AND MUTAGENESIS OF TYR-90; ALA-148 ANDLYS-409.	10652356 [Abstract]

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