dbPTM

KPCD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KPCD_HUMAN
UniProt AC	Q05655
Protein Name	Protein kinase C delta type
Gene Name	PRKCD
Organism	Homo sapiens (Human).
Sequence Length	676
Subcellular Localization	Cytoplasm . Cytoplasm, perinuclear region . Nucleus . Cell membrane Peripheral membrane protein .
Protein Description	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 as well as survival of several cancers, is required for oxygen radical production by NADPH oxidase and acts as positive or negative regulator in platelet functional responses. Negatively regulates B cell proliferation and also has an important function in self-antigen induced B cell tolerance induction. 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. Is highly expressed in a number of cancer cells and promotes cell survival and resistance against chemotherapeutic drugs by inducing cyclin D1 (CCND1) and hyperphosphorylation of RB1, and via several pro-survival pathways, including NF-kappa-B, AKT1 and MAPK1/3 (ERK1/2). 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. 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. The catalytic subunit phosphorylates 14-3-3 proteins (YWHAB, YWHAZ and YWHAH) in a sphingosine-dependent fashion (By similarity). Phosphorylates ELAVL1 in response to angiotensin-2 treatment. [PubMed: 18285462]
Protein Sequence	MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDVDCKQSMRSEDEAKFPTMNRRGAIKQAKIHYIKNHEFIATFFGQPTFCSVCKDFVWGLNKQGYKCRQCNAAIHKKCIDKIIGRCTGTAANSRDTIFQKERFNIDMPHRFKVHNYMSPTFCDHCGSLLWGLVKQGLKCEDCGMNVHHKCREKVANLCGINQKLLAEALNQVTQRASRRSDSASSEPVGIYQGFEKKTGVAGEDMQDNSGTYGKIWEGSSKCNINNFIFHKVLGKGSFGKVLLGELKGRGEYFAIKALKKDVVLIDDDVECTMVEKRVLTLAAENPFLTHLICTFQTKDHLFFVMEFLNGGDLMYHIQDKGRFELYRATFYAAEIMCGLQFLHSKGIIYRDLKLDNVLLDRDGHIKIADFGMCKENIFGESRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFEREPTKRLGVTGNIKIHPFFKTINWTLLEKRRLEPPFRPKVKSPRDYSNFDQEFLNEKARLSYSDKNLIDSMDQSAFAGFSFVNPKFEHLLED

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
37	Phosphorylation	VKMKEALSTERGKTL EEHHHHHCCCCCCCH	34.96	18691976
38	Phosphorylation	KMKEALSTERGKTLV EHHHHHCCCCCCCHH	30.47	29514088
43	Phosphorylation	LSTERGKTLVQKKPT HCCCCCCCHHCCCCC	34.68	28102081
50	Phosphorylation	TLVQKKPTMYPEWKS CHHCCCCCCCCCHHH	37.91	17192257
52	Phosphorylation	VQKKPTMYPEWKSTF HCCCCCCCCCHHHCE	10.65	26074081
58	Phosphorylation	MYPEWKSTFDAHIYE CCCCHHHCEEEEEEC	23.08	28152594
64	Phosphorylation	STFDAHIYEGRVIQI HCEEEEEECCCEEEE	11.49	27155012
113	Sumoylation	LDLQPQAKVLMSVQY EECCHHHHHHHHHHH	30.56	-
120	Phosphorylation	KVLMSVQYFLEDVDC HHHHHHHHHHHCCCH	14.15	18691976
130	Phosphorylation	EDVDCKQSMRSEDEA HCCCHHHHCCCCCHH	11.14	28674151
133	Phosphorylation	DCKQSMRSEDEAKFP CHHHHCCCCCHHCCC	40.53	17192257
138	Ubiquitination	MRSEDEAKFPTMNRR CCCCCHHCCCCCCCC	50.24	-
141	Phosphorylation	EDEAKFPTMNRRGAI CCHHCCCCCCCCCHH	30.15	23401153
155	Phosphorylation	IKQAKIHYIKNHEFI HHHHEEEEEECCCEE	19.64	22817900
184	Ubiquitination	DFVWGLNKQGYKCRQ HHHHCCCCCCCCCCC	50.58	21890473
187	Phosphorylation	WGLNKQGYKCRQCNA HCCCCCCCCCCCCCH	12.38	8824297
209	Phosphorylation	DKIIGRCTGTAANSR HHHHHHCCCCCCCCC	35.89	29514088
211	Phosphorylation	IIGRCTGTAANSRDT HHHHCCCCCCCCCCC	12.39	29514088
215	Phosphorylation	CTGTAANSRDTIFQK CCCCCCCCCCCCCCH	27.14	25159151
218	Phosphorylation	TAANSRDTIFQKERF CCCCCCCCCCCHHHC	23.68	19369195
222	Ubiquitination	SRDTIFQKERFNIDM CCCCCCCHHHCCCCC	39.86	21890473
271	Ubiquitination	CGMNVHHKCREKVAN CCCCHHHHHHHHHHH	21.80	-
295	Phosphorylation	AEALNQVTQRASRRS HHHHHHHHHHHHHCC	11.54	23401153
299	Phosphorylation	NQVTQRASRRSDSAS HHHHHHHHHCCCCCC	30.34	23927012
302	Phosphorylation	TQRASRRSDSASSEP HHHHHHCCCCCCCCC	34.50	23927012
304	Phosphorylation	RASRRSDSASSEPVG HHHHCCCCCCCCCCC	31.15	25159151
306	Phosphorylation	SRRSDSASSEPVGIY HHCCCCCCCCCCCEE	38.90	23927012
307	Phosphorylation	RRSDSASSEPVGIYQ HCCCCCCCCCCCEEE	45.71	23927012
313	Phosphorylation	SSEPVGIYQGFEKKT CCCCCCEEECCEECC	9.17	23927012
319	Ubiquitination	IYQGFEKKTGVAGED EEECCEECCCCCCCC	43.23	21890473
331	Phosphorylation	GEDMQDNSGTYGKIW CCCCCCCCCCCCCCC	40.58	25159151
333	Phosphorylation	DMQDNSGTYGKIWEG CCCCCCCCCCCCCCC	28.99	23927012
334	Phosphorylation	MQDNSGTYGKIWEGS CCCCCCCCCCCCCCC	21.68	22322096
336	Ubiquitination	DNSGTYGKIWEGSSK CCCCCCCCCCCCCCC	33.94	21890473
341	Phosphorylation	YGKIWEGSSKCNINN CCCCCCCCCCCEECC	18.34	19060867
342	Phosphorylation	GKIWEGSSKCNINNF CCCCCCCCCCEECCE	52.68	23312004
353	Acetylation	INNFIFHKVLGKGSF ECCEEEEEHHCCCCC	28.53	25953088
357	Ubiquitination	IFHKVLGKGSFGKVL EEEEHHCCCCCHHHH	47.42	-
359	Phosphorylation	HKVLGKGSFGKVLLG EEHHCCCCCHHHHHH	34.02	27067055
362	Ubiquitination	LGKGSFGKVLLGELK HCCCCCHHHHHHHHC	27.91	21890473
369	Ubiquitination	KVLLGELKGRGEYFA HHHHHHHCCCCCEEE	42.11	-
374	Phosphorylation	ELKGRGEYFAIKALK HHCCCCCEEEEEEEC	10.92	27273156
448	Phosphorylation	DKGRFELYRATFYAA CCCCEEEHHHHHHHH	7.33	-
451	Phosphorylation	RFELYRATFYAAEIM CEEEHHHHHHHHHHH	14.26	22817900
453	Phosphorylation	ELYRATFYAAEIMCG EEHHHHHHHHHHHHH	10.68	-
471	Phosphorylation	LHSKGIIYRDLKLDN HHHCCCEECCCCCCC	8.99	-
496	Ubiquitination	IADFGMCKENIFGES ECCCCCCHHHCCCCC	44.92	-
503	Phosphorylation	KENIFGESRASTFCG HHHCCCCCHHHHCCC	33.26	28355574
506	Phosphorylation	IFGESRASTFCGTPD CCCCCHHHHCCCCCC	22.39	20201521
507	Phosphorylation	FGESRASTFCGTPDY CCCCHHHHCCCCCCC	23.20	15949469
507	Dephosphorylation	FGESRASTFCGTPDY CCCCHHHHCCCCCCC	23.20	11959144
511	Phosphorylation	RASTFCGTPDYIAPE HHHHCCCCCCCCCHH	17.73	23401153
514	Phosphorylation	TFCGTPDYIAPEILQ HCCCCCCCCCHHHHC	10.53	30278072
525	Phosphorylation	EILQGLKYTFSVDWW HHHCCCCEEEECCHH	20.33	22817900
527 (in isoform 2)	Ubiquitination	-	6.42	-
559	Phosphorylation	DEDELFESIRVDTPH CHHHHHHHHCCCCCC	14.36	24719451
567	Phosphorylation	IRVDTPHYPRWITKE HCCCCCCCCCCCCHH	8.83	22817900
581	Ubiquitination	ESKDILEKLFEREPT HHHHHHHHHHHCCCC	55.84	-
594	Phosphorylation	PTKRLGVTGNIKIHP CCCCCCCCCCEEEEC	23.78	22817900
605	Phosphorylation	KIHPFFKTINWTLLE EEECCCEECCCHHHH	17.87	27499020
609	Phosphorylation	FFKTINWTLLEKRRL CCEECCCHHHHHCCC	19.58	-
613	Ubiquitination	INWTLLEKRRLEPPF CCCHHHHHCCCCCCC	42.67	21890473
626	Phosphorylation	PFRPKVKSPRDYSNF CCCCCCCCCCCCCCC	28.31	23898821
630	Phosphorylation	KVKSPRDYSNFDQEF CCCCCCCCCCCCHHH	13.54	20007894
631	Phosphorylation	VKSPRDYSNFDQEFL CCCCCCCCCCCHHHH	35.00	28152594
641	Ubiquitination	DQEFLNEKARLSYSD CHHHHCHHHCCCCCC	37.42	21890473
645	Phosphorylation	LNEKARLSYSDKNLI HCHHHCCCCCCHHHH	19.62	22322096
645	Dephosphorylation	LNEKARLSYSDKNLI HCHHHCCCCCCHHHH	19.62	11959144
646	Phosphorylation	NEKARLSYSDKNLID CHHHCCCCCCHHHHH	26.02	30266825
647	Phosphorylation	EKARLSYSDKNLIDS HHHCCCCCCHHHHHH	38.44	22322096
654	Phosphorylation	SDKNLIDSMDQSAFA CCHHHHHHCCHHHHC	19.77	30266825
658	Phosphorylation	LIDSMDQSAFAGFSF HHHHCCHHHHCCCCC	22.53	30266825
664	Phosphorylation	QSAFAGFSFVNPKFE HHHHCCCCCCCCCHH	27.63	22322096
664	Dephosphorylation	QSAFAGFSFVNPKFE HHHHCCCCCCCCCHH	27.63	11959144
672 (in isoform 2)	Ubiquitination	-	38.56	-

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
141	T	Phosphorylation	Kinase	PRKCD	Q05655	GPS
218	T	Phosphorylation	Kinase	PRKCD	Q05655	GPS
295	T	Phosphorylation	Kinase	PRKCD	Q05655	GPS
299	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
302	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
304	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
313	Y	Phosphorylation	Kinase	SRC	P12931	PSP
334	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
503	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
507	T	Phosphorylation	Kinase	PDK1	Q15118	GPS
507	T	Phosphorylation	Kinase	PDPK1	O15530	PhosphoELM
645	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
299	S	Phosphorylation	17603046
Autophosphorylated at Ser-299, Ser-302 and Ser-304.
302	S	Phosphorylation	17603046
Autophosphorylated at Ser-299, Ser-302 and Ser-304.
304	S	Phosphorylation	17603046
Autophosphorylated at Ser-299, Ser-302 and Ser-304.
507	T	Phosphorylation	11772397
Autophosphorylated and/or phosphorylated at Thr-507, within the activation loop; phosphorylation at Thr-507 is not a prerequisite for enzymatic activity.

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 KPCD_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GRP3_HUMAN	RASGRP3	physical	15213298
PLS3_HUMAN	PLSCR3	physical	12649167
1433G_HUMAN	YWHAG	physical	10433554
PDPK1_HUMAN	PDPK1	physical	11781095
GNA12_HUMAN	GNA12	physical	8824244
GNA13_HUMAN	GNA13	physical	8824244
MTOR_HUMAN	MTOR	physical	10698949
STAT1_HUMAN	STAT1	physical	12807916
FAK2_HUMAN	PTK2B	physical	11352632
PDP1_HUMAN	PDP1	physical	11577086
PDP2_HUMAN	PDP2	physical	11577086
IRS1_HUMAN	IRS1	physical	12031982
INSR_HUMAN	INSR	physical	12031982
PTN6_HUMAN	PTPN6	physical	11723252
TIAM1_HUMAN	TIAM1	physical	10212259
MUC1_HUMAN	MUC1	physical	11877440
IRS1_HUMAN	IRS1	physical	15516986
IKKB_HUMAN	IKBKB	physical	10022904
IKKA_HUMAN	CHUK	physical	10022904
SP1_HUMAN	SP1	physical	21159880
NF2L2_HUMAN	NFE2L2	physical	19920073
KPCD_HUMAN	PRKCD	physical	19920073
HDAC5_HUMAN	HDAC5	physical	21146494
STAT3_HUMAN	STAT3	physical	10446219
HSPB1_HUMAN	HSPB1	physical	15731106
KLF4_HUMAN	KLF4	physical	22282354
VHL_HUMAN	VHL	physical	16669786
H11_HUMAN	HIST1H1A	physical	16314418
P53_HUMAN	TP53	physical	16314418
IBTK_HUMAN	IBTK	physical	21482705
H15_HUMAN	HIST1H1B	physical	15978696
SYUA_HUMAN	SNCA	physical	15978696
NCF1_HUMAN	NCF1	physical	12056906
H11_HUMAN	HIST1H1A	physical	12056906
A4_HUMAN	APP	physical	21832049
STAT1_HUMAN	STAT1	physical	15322115
H15_HUMAN	HIST1H1B	physical	11839738
KPCD_HUMAN	PRKCD	physical	11839738
STAT1_HUMAN	STAT1	physical	11839738
MARCS_MOUSE	Marcks	physical	7588787
STAT1_HUMAN	STAT1	physical	12817007
ITB2_HUMAN	ITGB2	physical	11700305
TNR1A_HUMAN	TNFRSF1A	physical	11078718
GSK3A_HUMAN	GSK3A	physical	11884598
ELAV1_HUMAN	ELAVL1	physical	17392515
OCLN_MOUSE	Ocln	physical	11502742
KPCB_HUMAN	PRKCB	physical	23455922
KPCT_HUMAN	PRKCQ	physical	23455922
DYHC1_HUMAN	DYNC1H1	physical	20395553
HSP74_HUMAN	HSPA4	physical	20395553
HS90A_HUMAN	HSP90AA1	physical	20395553
ITPR1_HUMAN	ITPR1	physical	20395553
MACF1_HUMAN	MACF1	physical	20395553
NAR3_HUMAN	ART3	physical	20395553
TERA_HUMAN	VCP	physical	20395553
RBP10_HUMAN	RANBP10	physical	20395553
RANB9_HUMAN	RANBP9	physical	20395553
EP300_HUMAN	EP300	physical	11020388
FLI1_HUMAN	FLI1	physical	19158279
DBLOH_HUMAN	DIABLO	physical	22465666
TEBP_HUMAN	PTGES3	physical	26344197
DAB2_HUMAN	DAB2	physical	10542228
RL37A_HUMAN	RPL37A	physical	26496610
TKT_HUMAN	TKT	physical	26496610
ZN131_HUMAN	ZNF131	physical	26496610
FXR1_HUMAN	FXR1	physical	26496610
DHX16_HUMAN	DHX16	physical	26496610
PRP4B_HUMAN	PRPF4B	physical	26496610
PPRC1_HUMAN	PPRC1	physical	26496610
CWC15_HUMAN	CWC15	physical	26496610
TPC13_HUMAN	TRAPPC13	physical	26496610
F192A_HUMAN	FAM192A	physical	26496610
CHD9_HUMAN	CHD9	physical	26496610
BUD13_HUMAN	BUD13	physical	26496610
LYSM2_HUMAN	LYSMD2	physical	26496610
ACTBL_HUMAN	ACTBL2	physical	26496610
FYN_HUMAN	FYN	physical	25241761
GRM5_HUMAN	GRM5	physical	25241761
NOTC1_HUMAN	NOTCH1	physical	24662486
KPCD_HUMAN	PRKCD	physical	18285462
ELAV1_HUMAN	ELAVL1	physical	18285462
ELAV1_HUMAN	ELAVL1	physical	21310943
ELAV1_HUMAN	ELAVL1	physical	20086103
SP1_HUMAN	SP1	physical	19169273
P73_HUMAN	TP73	physical	12097319
MBP_HUMAN	MBP	physical	12097319
KPCD_HUMAN	PRKCD	physical	12097319
IL32_HUMAN	IL32	physical	29050245
VHL_HUMAN	VHL	physical	29050245
SPY2_HUMAN	SPRY2	physical	19458088

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615559	Autoimmune lymphoproliferative syndrome 3 (ALPS3)
Kegg Drug
D09671	Sotrastaurin (USAN/INN)
D09718	Sotrastaurin acetate (USAN)
DrugBank
DB05013	Ingenol Mebutate
DB00675	Tamoxifen

Regulatory Network of KPCD_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Regulation of TNF-induced oxygen radical production in humanneutrophils: role of delta-PKC."; Kilpatrick L.E., Sun S., Li H., Vary T.C., Korchak H.M.; J. Leukoc. Biol. 87:153-164(2010). Cited for: FUNCTION IN PHOSPHORYLATION OF NCF1, AND PHOSPHORYLATION AT THR-507AND SER-645.	19801500 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-313 AND SER-664, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"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-43; THR-218; THR-295;SER-299; SER-302; SER-304; TYR-313; TYR-334; SER-506; SER-645; SER-647AND SER-664, AND MASS SPECTROMETRY.	19369195 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-302; SER-304;SER-307 AND SER-664, AND MASS SPECTROMETRY.	18669648 [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 THR-43; THR-50; SER-299;SER-302; SER-307; TYR-313; TYR-334; SER-503; SER-647; SER-654; SER-658AND SER-664, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Novel phosphorylation site markers of protein kinase C deltaactivation."; Durgan J., Michael N., Totty N., Parker P.J.; FEBS Lett. 581:3377-3381(2007). Cited for: SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT SER-299;SER-302 AND SER-304, AND MUTAGENESIS OF SER-299.	17603046 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664, AND MASSSPECTROMETRY.	15302935 [Abstract]
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-313 AND TYR-374, ANDMASS SPECTROMETRY.	19534553 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-313; TYR-334 ANDTYR-374, AND MASS SPECTROMETRY.	18083107 [Abstract]
"Coincident regulation of PKCdelta in human platelets byphosphorylation of Tyr311 and Tyr565 and phospholipase C signalling."; Hall K.J., Jones M.L., Poole A.W.; Biochem. J. 406:501-509(2007). Cited for: PHOSPHORYLATION AT TYR-313 AND TYR-567.	17570831 [Abstract]
"Roles of tyrosine phosphorylation and cleavage of protein kinaseCdelta in its protective effect against tumor necrosis factor-relatedapoptosis inducing ligand-induced apoptosis."; Okhrimenko H., Lu W., Xiang C., Ju D., Blumberg P.M., Gomel R.,Kazimirsky G., Brodie C.; J. Biol. Chem. 280:23643-23652(2005). Cited for: FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYR-155.	15774464 [Abstract]

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