dbPTM

KPCD2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KPCD2_HUMAN
UniProt AC	Q9BZL6
Protein Name	Serine/threonine-protein kinase D2
Gene Name	PRKD2
Organism	Homo sapiens (Human).
Sequence Length	878
Subcellular Localization	Cytoplasm . Cell membrane . Nucleus . Golgi apparatus, trans-Golgi network . Translocation to the cell membrane is required for kinase activation. Accumulates in the nucleus upon CK1-mediated phosphorylation after activation of G-protein-coupled rece
Protein Description	Serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. [PubMed: 15604256]
Protein Sequence	MATAPSYPAGLPGSPGPGSPPPPGGLELQSPPPLLPQIPAPGSGVSFHIQIGLTREFVLLPAASELAHVKQLACSIVDQKFPECGFYGLYDKILLFKHDPTSANLLQLVRSSGDIQEGDLVEVVLSASATFEDFQIRPHALTVHSYRAPAFCDHCGEMLFGLVRQGLKCDGCGLNYHKRCAFSIPNNCSGARKRRLSSTSLASGHSVRLGTSESLPCTAEELSRSTTELLPRRPPSSSSSSSASSYTGRPIELDKMLLSKVKVPHTFLIHSYTRPTVCQACKKLLKGLFRQGLQCKDCKFNCHKRCATRVPNDCLGEALINGDVPMEEATDFSEADKSALMDESEDSGVIPGSHSENALHASEEEEGEGGKAQSSLGYIPLMRVVQSVRHTTRKSSTTLREGWVVHYSNKDTLRKRHYWRLDCKCITLFQNNTTNRYYKEIPLSEILTVESAQNFSLVPPGTNPHCFEIVTANATYFVGEMPGGTPGGPSGQGAEAARGWETAIRQALMPVILQDAPSAPGHAPHRQASLSISVSNSQIQENVDIATVYQIFPDEVLGSGQFGVVYGGKHRKTGRDVAVKVIDKLRFPTKQESQLRNEVAILQSLRHPGIVNLECMFETPEKVFVVMEKLHGDMLEMILSSEKGRLPERLTKFLITQILVALRHLHFKNIVHCDLKPENVLLASADPFPQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLLNQGYNRSLDMWSVGVIMYVSLSGTFPFNEDEDINDQIQNAAFMYPASPWSHISAGAIDLINNLLQVKMRKRYSVDKSLSHPWLQEYQTWLDLRELEGKMGERYITHESDDARWEQFAAEHPLPGSGLPTDRDLGGACPPQDHDMQGLAERISVL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
21	Ubiquitination	SPGPGSPPPPGGLEL CCCCCCCCCCCCCCC	49.79	29967540
30	Phosphorylation	PGGLELQSPPPLLPQ CCCCCCCCCCCCCCC	52.58	-
40	Phosphorylation	PLLPQIPAPGSGVSF CCCCCCCCCCCCCEE	23.79	32142685
41	Phosphorylation	LLPQIPAPGSGVSFH CCCCCCCCCCCCEEE	31.93	32645325
43	Phosphorylation	PQIPAPGSGVSFHIQ CCCCCCCCCCEEEEE	34.66	17192257
46	Phosphorylation	PAPGSGVSFHIQIGL CCCCCCCEEEEEECC	18.03	18669648
49	Phosphorylation	GSGVSFHIQIGLTRE CCCCEEEEEECCCCE	2.77	33259812
80	Ubiquitination	ACSIVDQKFPECGFY HHHHHCCCCCCCCEE	59.42	-
80	Ubiquitination	ACSIVDQKFPECGFY HHHHHCCCCCCCCEE	59.42	29967540
87	Phosphorylation	KFPECGFYGLYDKIL CCCCCCEEEEECEEE	7.48	-
92	Ubiquitination	GFYGLYDKILLFKHD CEEEEECEEEEEECC	23.00	-
97	Ubiquitination	YDKILLFKHDPTSAN ECEEEEEECCCCCCH	47.25	-
97	Ubiquitination	YDKILLFKHDPTSAN ECEEEEEECCCCCCH	47.25	-
98	Ubiquitination	DKILLFKHDPTSANL CEEEEEECCCCCCHH	38.66	29967540
101	Phosphorylation	LLFKHDPTSANLLQL EEEECCCCCCHHHHH	46.67	23312004
102	Phosphorylation	LFKHDPTSANLLQLV EEECCCCCCHHHHHH	22.13	23312004
103	Ubiquitination	FKHDPTSANLLQLVR EECCCCCCHHHHHHH	17.11	29967540
111	Phosphorylation	NLLQLVRSSGDIQEG HHHHHHHHCCCCCCC	31.06	26074081
112	Phosphorylation	LLQLVRSSGDIQEGD HHHHHHHCCCCCCCC	29.89	26074081
125	Ubiquitination	GDLVEVVLSASATFE CCEEEEEEEEECCCC	4.23	22817900
126	Ubiquitination	DLVEVVLSASATFED CEEEEEEEEECCCCC	14.47	22817900
129	Ubiquitination	EVVLSASATFEDFQI EEEEEEECCCCCCCC	18.94	21890473
129	Ubiquitination	EVVLSASATFEDFQI EEEEEEECCCCCCCC	18.94	21890473
178	Ubiquitination	GCGLNYHKRCAFSIP CCCCCCCCCCCEECC	38.52	29967540
183	Phosphorylation	YHKRCAFSIPNNCSG CCCCCCEECCCCCCC	20.72	30108239
189	Phosphorylation	FSIPNNCSGARKRRL EECCCCCCCCCCCCC	37.30	30108239
197	Phosphorylation	GARKRRLSSTSLASG CCCCCCCCCCCCCCC	29.74	29255136
198	Phosphorylation	ARKRRLSSTSLASGH CCCCCCCCCCCCCCC	26.97	29255136
199	Phosphorylation	RKRRLSSTSLASGHS CCCCCCCCCCCCCCC	25.12	29255136
200	Phosphorylation	KRRLSSTSLASGHSV CCCCCCCCCCCCCCE	24.72	29255136
203	Phosphorylation	LSSTSLASGHSVRLG CCCCCCCCCCCEEEC	42.19	23927012
206	Phosphorylation	TSLASGHSVRLGTSE CCCCCCCCEEECCCC	16.68	23927012
211	Phosphorylation	GHSVRLGTSESLPCT CCCEEECCCCCCCCC	33.63	30266825
212	Phosphorylation	HSVRLGTSESLPCTA CCEEECCCCCCCCCH	24.32	30266825
214	Phosphorylation	VRLGTSESLPCTAEE EEECCCCCCCCCHHH	37.06	29255136
218	Phosphorylation	TSESLPCTAEELSRS CCCCCCCCHHHHHHC	34.85	30266825
223	Phosphorylation	PCTAEELSRSTTELL CCCHHHHHHCCHHHC	27.71	30266825
225	Phosphorylation	TAEELSRSTTELLPR CHHHHHHCCHHHCCC	35.98	30266825
226	Phosphorylation	AEELSRSTTELLPRR HHHHHHCCHHHCCCC	24.15	30266825
227	Phosphorylation	EELSRSTTELLPRRP HHHHHCCHHHCCCCC	26.36	30266825
236	Phosphorylation	LLPRRPPSSSSSSSA HCCCCCCCCCCCCCC	45.60	21082442
237	Phosphorylation	LPRRPPSSSSSSSAS CCCCCCCCCCCCCCC	39.76	28450419
238	Phosphorylation	PRRPPSSSSSSSASS CCCCCCCCCCCCCCC	38.28	28450419
239	Phosphorylation	RRPPSSSSSSSASSY CCCCCCCCCCCCCCC	35.87	26657352
240	Phosphorylation	RPPSSSSSSSASSYT CCCCCCCCCCCCCCC	30.20	28450419
241	Phosphorylation	PPSSSSSSSASSYTG CCCCCCCCCCCCCCC	31.69	25394399
242	Phosphorylation	PSSSSSSSASSYTGR CCCCCCCCCCCCCCC	33.83	29496963
244	Phosphorylation	SSSSSSASSYTGRPI CCCCCCCCCCCCCCE	26.31	17962809
245	Phosphorylation	SSSSSASSYTGRPIE CCCCCCCCCCCCCEE	26.82	30576142
246	Phosphorylation	SSSSASSYTGRPIEL CCCCCCCCCCCCEEH	15.66	22817900
247	Phosphorylation	SSSASSYTGRPIELD CCCCCCCCCCCEEHH	28.76	27251275
255	Ubiquitination	GRPIELDKMLLSKVK CCCEEHHHHHHHCCC	44.03	29967540
260	Ubiquitination	LDKMLLSKVKVPHTF HHHHHHHCCCCCCEE	46.15	29967540
266	Phosphorylation	SKVKVPHTFLIHSYT HCCCCCCEEEEECCC	17.67	26074081
271	Phosphorylation	PHTFLIHSYTRPTVC CCEEEEECCCCHHHH	22.62	24719451
272	Phosphorylation	HTFLIHSYTRPTVCQ CEEEEECCCCHHHHH	7.81	26074081
273	Phosphorylation	TFLIHSYTRPTVCQA EEEEECCCCHHHHHH	32.94	26074081
276	Phosphorylation	IHSYTRPTVCQACKK EECCCCHHHHHHHHH	30.53	24719451
282	Ubiquitination	PTVCQACKKLLKGLF HHHHHHHHHHHHHHH	49.85	22817900
283	Ubiquitination	TVCQACKKLLKGLFR HHHHHHHHHHHHHHH	59.96	22817900
286	Ubiquitination	QACKKLLKGLFRQGL HHHHHHHHHHHHCCC	65.09	21890473
338	Phosphorylation	DFSEADKSALMDESE CCCHHHHHHHCCCCC	27.47	23312004
344	Phosphorylation	KSALMDESEDSGVIP HHHHCCCCCCCCCCC	42.30	23312004
347	Phosphorylation	LMDESEDSGVIPGSH HCCCCCCCCCCCCCC	30.79	23312004
353	Phosphorylation	DSGVIPGSHSENALH CCCCCCCCCCCCCCC	20.63	25159151
355	Phosphorylation	GVIPGSHSENALHAS CCCCCCCCCCCCCCC	33.95	25159151
362	Phosphorylation	SENALHASEEEEGEG CCCCCCCCHHHCCCC	34.49	25159151
374	Phosphorylation	GEGGKAQSSLGYIPL CCCCCCCCHHCHHHH	32.18	21945579
375	Phosphorylation	EGGKAQSSLGYIPLM CCCCCCCHHCHHHHH	17.46	21945579
378	Phosphorylation	KAQSSLGYIPLMRVV CCCCHHCHHHHHHHH	12.50	21945579
387	Phosphorylation	PLMRVVQSVRHTTRK HHHHHHHHHHCCCCC	14.98	26853621
391	Phosphorylation	VVQSVRHTTRKSSTT HHHHHHCCCCCCCCC	20.10	-
392	Phosphorylation	VQSVRHTTRKSSTTL HHHHHCCCCCCCCCC	29.94	28152594
395	Phosphorylation	VRHTTRKSSTTLREG HHCCCCCCCCCCCCE	29.62	27273156
396	Phosphorylation	RHTTRKSSTTLREGW HCCCCCCCCCCCCEE	28.57	27273156
397	Phosphorylation	HTTRKSSTTLREGWV CCCCCCCCCCCCEEE	36.62	30266825
398	Phosphorylation	TTRKSSTTLREGWVV CCCCCCCCCCCEEEE	26.26	30266825
407	Phosphorylation	REGWVVHYSNKDTLR CCEEEEEECCCHHCC	11.43	-
408	Phosphorylation	EGWVVHYSNKDTLRK CEEEEEECCCHHCCH	23.64	28857561
412	Phosphorylation	VHYSNKDTLRKRHYW EEECCCHHCCHHEEE	30.03	28857561
423	Ubiquitination	RHYWRLDCKCITLFQ HEEEEECCEEEEEEE	4.60	29967540
424	Ubiquitination	HYWRLDCKCITLFQN EEEEECCEEEEEEEC	28.48	-
424	Ubiquitination	HYWRLDCKCITLFQN EEEEECCEEEEEEEC	28.48	-
427	Phosphorylation	RLDCKCITLFQNNTT EECCEEEEEEECCCC	30.87	26074081
433	Phosphorylation	ITLFQNNTTNRYYKE EEEEECCCCCCEECC	32.75	26074081
433	Ubiquitination	ITLFQNNTTNRYYKE EEEEECCCCCCEECC	32.75	27667366
434	Phosphorylation	TLFQNNTTNRYYKEI EEEECCCCCCEECCC	21.59	26074081
437	Phosphorylation	QNNTTNRYYKEIPLS ECCCCCCEECCCCHH	22.43	26074081
438	Phosphorylation	NNTTNRYYKEIPLSE CCCCCCEECCCCHHH	10.02	26074081
518	Phosphorylation	VILQDAPSAPGHAPH HHHCCCCCCCCCCCC	49.14	21082442
519	Ubiquitination	ILQDAPSAPGHAPHR HHCCCCCCCCCCCCC	17.03	29967540
529	Phosphorylation	HAPHRQASLSISVSN CCCCCCEEEEEEECH	17.82	17001009
535	Ubiquitination	ASLSISVSNSQIQEN EEEEEEECHHHHHCC	24.79	29967540
548	Ubiquitination	ENVDIATVYQIFPDE CCCCEEEEEECCCHH	2.15	32142685
557	Phosphorylation	QIFPDEVLGSGQFGV ECCCHHHHCCCCCEE	4.20	32142685
572	Acetylation	VYGGKHRKTGRDVAV EECCCCCCCCCCHHH	55.86	30591367
580	Ubiquitination	TGRDVAVKVIDKLRF CCCCHHHHHHHHHCC	24.60	-
580	Acetylation	TGRDVAVKVIDKLRF CCCCHHHHHHHHHCC	24.60	30591373
580	Ubiquitination	TGRDVAVKVIDKLRF CCCCHHHHHHHHHCC	24.60	29967540
584	Acetylation	VAVKVIDKLRFPTKQ HHHHHHHHHCCCCHH	30.36	30591379
590	Ubiquitination	DKLRFPTKQESQLRN HHHCCCCHHHHHHHH	52.91	27667366
619	Phosphorylation	NLECMFETPEKVFVV EEEEEEECCCEEEEE	26.03	-
643	Ubiquitination	EMILSSEKGRLPERL HHHHHCCCCCCCHHH	51.80	-
676	Ubiquitination	NIVHCDLKPENVLLA CCCCCCCCHHHEEEE	36.71	29967540
684	Phosphorylation	PENVLLASADPFPQV HHHEEEEECCCCCCC	32.92	20068231
692	Ubiquitination	ADPFPQVKLCDFGFA CCCCCCCEECHHCCC	37.84	29967540
705	Ubiquitination	FARIIGEKSFRRSVV CCEECCCCCHHCCCC	50.08	32142685
706	Phosphorylation	ARIIGEKSFRRSVVG CEECCCCCHHCCCCC	21.49	23401153
710	Phosphorylation	GEKSFRRSVVGTPAY CCCCHHCCCCCCHHH	19.52	23927012
714	Phosphorylation	FRRSVVGTPAYLAPE HHCCCCCCHHHHCHH	7.98	21945579
717	Phosphorylation	SVVGTPAYLAPEVLL CCCCCHHHHCHHHHH	12.47	21945579
728	Phosphorylation	EVLLNQGYNRSLDMW HHHHCCCCCCCCCCC	9.53	21945579
731	Phosphorylation	LNQGYNRSLDMWSVG HCCCCCCCCCCCCEE	25.69	19369195
797	Phosphorylation	VKMRKRYSVDKSLSH HHHHHCCCCCCCCCC	28.07	19369195
876	Phosphorylation	QGLAERISVL----- HHHHHHHHCC-----	24.48	28674151

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
87	Y	Phosphorylation	Kinase	SRC	P12931	PSP
244	S	Phosphorylation	Kinase	CK1D	P48730	PSP
244	S	Phosphorylation	Kinase	CK1E	P49674	PSP
438	Y	Phosphorylation	Kinase	ABL-FAMILY	-	GPS
438	Y	Phosphorylation	Kinase	ABL1	P00519	Uniprot
706	S	Phosphorylation	Kinase	PRKCE	Q02156	GPS
706	S	Phosphorylation	Kinase	PKC	-	Uniprot
706	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
706	S	Phosphorylation	Kinase	PRKCH	P24723	GPS
706	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
710	S	Phosphorylation	Kinase	PRKCE	Q02156	GPS
710	S	Phosphorylation	Kinase	PRKCH	P24723	GPS
710	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
717	Y	Phosphorylation	Kinase	ABL1	P00519	Uniprot
876	S	Phosphorylation	Kinase	PRKCE	Q02156	GPS
876	S	Phosphorylation	Kinase	PRKCH	P24723	GPS
876	S	Phosphorylation	Kinase	PRKD2	Q9BZL6	PSP
876	S	Phosphorylation	Kinase	PKD2	Q13563	PhosphoELM
876	S	Phosphorylation	Kinase	PRKCA	P17252	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
244	S	Phosphorylation	17962809
Phosphorylation at Ser-244 by CSNK1D and CSNK1E promotes nuclear localization and substrate targeting.
244	S	Phosphorylation	17962809
Phosphorylation at Ser-244, Ser-706 and Ser-710 is required for nuclear localization.
706	S	Oxidation	12058027
Phosphorylated at Tyr-717 by ABL1 specifically in response to oxidative stress; requires prior phosphorylation at Ser-706 or/and Ser-710.
706	S	Phosphorylation	12058027
Phosphorylated at Tyr-717 by ABL1 specifically in response to oxidative stress; requires prior phosphorylation at Ser-706 or/and Ser-710.
706	S	Phosphorylation	12058027
Phosphorylation at Ser-244, Ser-706 and Ser-710 is required for nuclear localization.
706	S	Phosphorylation	12058027
Ser-706 or/and Ser-710 are probably phosphorylated by PKC.
710	S	Oxidation	12058027
Phosphorylated at Tyr-717 by ABL1 specifically in response to oxidative stress; requires prior phosphorylation at Ser-706 or/and Ser-710.
710	S	Phosphorylation	12058027
Phosphorylated at Tyr-717 by ABL1 specifically in response to oxidative stress; requires prior phosphorylation at Ser-706 or/and Ser-710.
710	S	Phosphorylation	12058027
Phosphorylation at Ser-244, Ser-706 and Ser-710 is required for nuclear localization.
710	S	Phosphorylation	12058027
Ser-706 or/and Ser-710 are probably phosphorylated by PKC.
876	S	Phosphorylation	11062248
Phosphorylation of Ser-876 correlates with the activation status of the kinase.

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 KPCD2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
INAR1_HUMAN	IFNAR1	physical	21173164
CSKP_HUMAN	CASK	physical	15231748
GLRX3_HUMAN	GLRX3	physical	15231748
RU17_HUMAN	SNRNP70	physical	15231748
RARB_HUMAN	RARB	physical	15231748
RXRA_HUMAN	RXRA	physical	15231748
DYST_HUMAN	DST	physical	15231748
PSG3_HUMAN	PSG3	physical	15231748
GORS1_HUMAN	GORASP1	physical	15231748
PDLI7_HUMAN	PDLIM7	physical	15231748
RRBP1_HUMAN	RRBP1	physical	15231748
GRIP1_HUMAN	GRIP1	physical	15231748
MTF2_HUMAN	MTF2	physical	15231748
HEY1_HUMAN	HEY1	physical	15231748
CDK10_HUMAN	CDK10	physical	26496610
1433T_HUMAN	YWHAQ	physical	26496610
S23IP_HUMAN	SEC23IP	physical	26496610
KPCD3_HUMAN	PRKD3	physical	26496610
NGDN_HUMAN	NGDN	physical	26496610
NGRN_HUMAN	NGRN	physical	26496610

Drug and Disease Associations

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

Regulatory Network of KPCD2_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-206 AND SER-710, 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 SER-189; SER-197; SER-198;THR-199; SER-200; SER-206; SER-214; SER-225; THR-227; SER-236;SER-237; SER-238; SER-338; SER-353; SER-355; SER-362; SER-374;SER-375; SER-518; SER-706; SER-710; TYR-717 AND SER-876, AND MASSSPECTROMETRY.	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-214, 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-197; SER-200; SER-203;SER-206; SER-214 AND SER-710, 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 SER-197; SER-214; SER-375;SER-396; SER-518; SER-706; SER-710 AND SER-876, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASSSPECTROMETRY.	19367720 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND MASSSPECTROMETRY.	18220336 [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 SER-197; SER-214 ANDSER-710, AND MASS SPECTROMETRY.	17192257 [Abstract]
"Phosphorylation at Ser244 by CK1 determines nuclear localization andsubstrate targeting of PKD2."; von Blume J., Knippschild U., Dequiedt F., Giamas G., Beck A.,Auer A., Van Lint J., Adler G., Seufferlein T.; EMBO J. 26:4619-4633(2007). Cited for: FUNCTION IN PHOSPHORYLATION OF HDAC7, ENZYME REGULATION, SUBCELLULARLOCATION, AND PHOSPHORYLATION AT SER-244.	17962809 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-198, ANDMASS SPECTROMETRY.	16083285 [Abstract]
"Mechanism of activation of protein kinase D2(PKD2) by theCCK(B)/gastrin receptor."; Sturany S., Van Lint J., Gilchrist A., Vandenheede J.R., Adler G.,Seufferlein T.; J. Biol. Chem. 277:29431-29436(2002). Cited for: ENZYME REGULATION, AND PHOSPHORYLATION AT SER-706; SER-710 ANDSER-876.	12058027 [Abstract]
"Molecular cloning and characterization of the human protein kinaseD2. A novel member of the protein kinase d family of serine threoninekinases."; Sturany S., Van Lint J., Mueller F., Wilda M., Hameister H.,Hoecker M., Brey A., Gern U., Vandenheede J., Gress T., Adler G.,Seufferlein T.; J. Biol. Chem. 276:3310-3318(2001). Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT SER-876, AND VARIANTALA-835.	11062248 [Abstract]
"Protein kinase D2 mediates activation of nuclear factor kappaB byBcr-Abl in Bcr-Abl+ human myeloid leukemia cells."; Mihailovic T., Marx M., Auer A., Van Lint J., Schmid M., Weber C.,Seufferlein T.; Cancer Res. 64:8939-8944(2004). Cited for: FUNCTION IN NF-KAPPA-B ACTIVATION, PHOSPHORYLATION AT TYR-438, ANDMUTAGENESIS OF TYR-438.	15604256 [Abstract]

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