dbPTM

KAPCA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KAPCA_HUMAN
UniProt AC	P17612
Protein Name	cAMP-dependent protein kinase catalytic subunit alpha
Gene Name	PRKACA
Organism	Homo sapiens (Human).
Sequence Length	351
Subcellular Localization	Cytoplasm. Cell membrane. Nucleus. Mitochondrion. Membrane Lipid-anchor . Translocates into the nucleus (monomeric catalytic subunit). The inactive holoenzyme is found in the cytoplasm. Distributed throughout the cytoplasm in meiotically incompeten
Protein Description	Phosphorylates a large number of substrates in the cytoplasm and the nucleus. Regulates the abundance of compartmentalized pools of its regulatory subunits through phosphorylation of PJA2 which binds and ubiquitinates these subunits, leading to their subsequent proteolysis. Phosphorylates CDC25B, ABL1, NFKB1, CLDN3, PSMC5/RPT6, PJA2, RYR2, RORA and VASP. RORA is activated by phosphorylation. Required for glucose-mediated adipogenic differentiation increase and osteogenic differentiation inhibition from osteoblasts. Involved in the regulation of platelets in response to thrombin and collagen; maintains circulating platelets in a resting state by phosphorylating proteins in numerous platelet inhibitory pathways when in complex with NF-kappa-B (NFKB1 and NFKB2) and I-kappa-B-alpha (NFKBIA), but thrombin and collagen disrupt these complexes and free active PRKACA stimulates platelets and leads to platelet aggregation by phosphorylating VASP. Prevents the antiproliferative and anti-invasive effects of alpha-difluoromethylornithine in breast cancer cells when activated. RYR2 channel activity is potentiated by phosphorylation in presence of luminal Ca(2+), leading to reduced amplitude and increased frequency of store overload-induced Ca(2+) release (SOICR) characterized by an increased rate of Ca(2+) release and propagation velocity of spontaneous Ca(2+) waves, despite reduced wave amplitude and resting cytosolic Ca(2+). PSMC5/RPT6 activation by phosphorylation stimulates proteasome. Negatively regulates tight junctions (TJs) in ovarian cancer cells via CLDN3 phosphorylation. NFKB1 phosphorylation promotes NF-kappa-B p50-p50 DNA binding. Involved in embryonic development by down-regulating the Hedgehog (Hh) signaling pathway that determines embryo pattern formation and morphogenesis. Prevents meiosis resumption in prophase-arrested oocytes via CDC25B inactivation by phosphorylation. May also regulate rapid eye movement (REM) sleep in the pedunculopontine tegmental (PPT). Phosphorylates APOBEC3G and AICDA. Isoform 2 phosphorylates and activates ABL1 in sperm flagellum to promote spermatozoa capacitation. Phosphorylates HSF1; this phosphorylation promotes HSF1 nuclear localization and transcriptional activity upon heat shock. [PubMed: 21085490]
Protein Sequence	MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWESPAQNTAHLDQFERIKTLGTGSFGRVMLVKHKETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Myristoylation	------MGNAAAAKK ------CCCHHHHHC	32.27	25807930
3	Deamidation	-----MGNAAAAKKG -----CCCHHHHHCC	25.71	-
3 (in isoform 2)	Phosphorylation	-	25.71	16964243
3	Deamidated asparagine	-----MGNAAAAKKG -----CCCHHHHHCC	25.71	-
11	Phosphorylation	AAAAKKGSEQESVKE HHHHHCCCCHHHHHH	45.01	12124936
15	Phosphorylation	KKGSEQESVKEFLAK HCCCCHHHHHHHHHH	37.88	21406692
16 (in isoform 2)	Ubiquitination	-	7.29	21906983
17	Ubiquitination	GSEQESVKEFLAKAK CCCHHHHHHHHHHHH	52.61	-
24 (in isoform 1)	Ubiquitination	-	58.05	21906983
24	Ubiquitination	KEFLAKAKEDFLKKW HHHHHHHHHHHHHHC	58.05	-
30	Ubiquitination	AKEDFLKKWESPAQN HHHHHHHHCCCCCCC	59.34	-
48	Ubiquitination	LDQFERIKTLGTGSF HHHHHHHHCCCCCCC	43.87	-
49	Phosphorylation	DQFERIKTLGTGSFG HHHHHHHCCCCCCCC	28.22	21082442
52	Phosphorylation	ERIKTLGTGSFGRVM HHHHCCCCCCCCEEE	32.53	23403867
54	Phosphorylation	IKTLGTGSFGRVMLV HHCCCCCCCCEEEEE	25.10	23403867
62	Acetylation	FGRVMLVKHKETGNH CCEEEEEEECCCCCC	45.02	25953088
70	Phosphorylation	HKETGNHYAMKILDK ECCCCCCEEEEECCH	16.64	-
76 (in isoform 2)	Ubiquitination	-	55.61	21906983
84	Ubiquitination	KQKVVKLKQIEHTLN HHHCEEHHHHEHHCC	43.44	-
84 (in isoform 1)	Ubiquitination	-	43.44	21906983
85 (in isoform 2)	Ubiquitination	-	57.65	21906983
89	Phosphorylation	KLKQIEHTLNEKRIL EHHHHEHHCCHHHHH	20.63	25159151
93	Ubiquitination	IEHTLNEKRILQAVN HEHHCCHHHHHHHHC	43.60	21906983
93 (in isoform 1)	Ubiquitination	-	43.60	21906983
110	Phosphorylation	FLVKLEFSFKDNSNL EEEEEEEEECCCCCE	23.24	24719451
140	Phosphorylation	LRRIGRFSEPHARFY HHHHCCCCCHHHHHH	49.19	12124936
157	Phosphorylation	QIVLTFEYLHSLDLI HHHHHHHHHHHHHHH	12.91	-
165	Phosphorylation	LHSLDLIYRDLKPEN HHHHHHHHCCCCHHH	12.84	-
190	Ubiquitination	VTDFGFAKRVKGRTW EECCCCEEECCCCEE	56.30	-
196	Phosphorylation	AKRVKGRTWTLCGTP EEECCCCEEEECCCH	31.32	22322096
198	Phosphorylation	RVKGRTWTLCGTPEY ECCCCEEEECCCHHH	16.14	22322096
200	Glutathionylation	KGRTWTLCGTPEYLA CCCEEEECCCHHHHC	4.45	12189155
202	Phosphorylation	RTWTLCGTPEYLAPE CEEEECCCHHHHCCH	16.38	22167270
205	Phosphorylation	TLCGTPEYLAPEIIL EECCCHHHHCCHHHH	14.90	27461979
213	Phosphorylation	LAPEIILSKGYNKAV HCCHHHHCCCCHHHH	17.39	23403867
214	Ubiquitination	APEIILSKGYNKAVD CCHHHHCCCCHHHHH	63.07	-
255	Ubiquitination	YEKIVSGKVRFPSHF HHHHHCCCCCCCCCC	23.80	-
259 (in isoform 2)	Ubiquitination	-	19.14	21906983
260	Phosphorylation	SGKVRFPSHFSSDLK CCCCCCCCCCCHHHH	34.16	26657352
263	Phosphorylation	VRFPSHFSSDLKDLL CCCCCCCCHHHHHHH	19.95	22673903
264	Phosphorylation	RFPSHFSSDLKDLLR CCCCCCCHHHHHHHH	46.12	26437602
267 (in isoform 1)	Ubiquitination	-	51.85	21906983
267	Ubiquitination	SHFSSDLKDLLRNLL CCCCHHHHHHHHHHH	51.85	-
267	Acetylation	SHFSSDLKDLLRNLL CCCCHHHHHHHHHHH	51.85	19608861
272 (in isoform 2)	Ubiquitination	-	45.10	21906983
278 (in isoform 2)	Ubiquitination	-	6.81	-
280 (in isoform 1)	Ubiquitination	-	53.69	21906983
280	Ubiquitination	LLQVDLTKRFGNLKN HHHHHHHHHHCCCCC	53.69	21906983
280	Acetylation	LLQVDLTKRFGNLKN HHHHHHHHHHCCCCC	53.69	25953088
286	Ubiquitination	TKRFGNLKNGVNDIK HHHHCCCCCCCCHHH	56.51	-
293	Ubiquitination	KNGVNDIKNHKWFAT CCCCCHHHCCCCEEE	56.73	-
310	Ubiquitination	WIAIYQRKVEAPFIP EEEEEECCCCCCCCC	28.97	-
312 (in isoform 2)	Ubiquitination	-	54.37	21906983
318	Acetylation	VEAPFIPKFKGPGDT CCCCCCCCCCCCCCC	55.69	25953088
318	Ubiquitination	VEAPFIPKFKGPGDT CCCCCCCCCCCCCCC	55.69	-
320 (in isoform 1)	Ubiquitination	-	71.03	21906983
320	Ubiquitination	APFIPKFKGPGDTSN CCCCCCCCCCCCCCC	71.03	2190698
325	Phosphorylation	KFKGPGDTSNFDDYE CCCCCCCCCCCCCCC	31.33	29978859
326	Phosphorylation	FKGPGDTSNFDDYEE CCCCCCCCCCCCCCH	39.99	29978859
331	Phosphorylation	DTSNFDDYEEEEIRV CCCCCCCCCHHHHHH	27.38	28102081
339	Phosphorylation	EEEEIRVSINEKCGK CHHHHHHCCHHHCCC	15.17	15481030
343	Ubiquitination	IRVSINEKCGKEFSE HHHCCHHHCCCCCCC	43.74	-
346	Ubiquitination	SINEKCGKEFSEF-- CCHHHCCCCCCCC--	66.12	-

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
11	S	Phosphorylation	Kinase	PRKACA	P17252	GPS
15	S	Phosphorylation	Kinase	PRKACA	P17252	GPS
49	T	Phosphorylation	Kinase	PRKACA	P17252	GPS
54	S	Phosphorylation	Kinase	PRKACA	P17252	GPS
70	Y	Phosphorylation	Kinase	FYN	P06241	PSP
140	S	Phosphorylation	Kinase	PRKACA	P17252	GPS
198	T	Phosphorylation	Kinase	PRKACA	P17612	GPS
198	T	Phosphorylation	Kinase	PDK1	O15530	PSP
213	S	Phosphorylation	Kinase	PRKACA	P17252	GPS
260	S	Phosphorylation	Kinase	PRKACA	P17252	GPS
326	S	Phosphorylation	Kinase	PRKACA	P17252	GPS
339	S	Phosphorylation	Kinase	PKACA	P17612	PSP
339	S	Phosphorylation	Kinase	PRKACA	P17252	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	STUB1	Q9UNE7	PMID:31189917

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
198	T	Phosphorylation		12372837
Phosphorylation on Thr-198 is required for full 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 KAPCA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GRP3_HUMAN	RASGRP3	physical	15213298
DCE2_HUMAN	GAD2	physical	15147202
DCE1_HUMAN	GAD1	physical	15147202
CIP4_HUMAN	TRIP10	physical	15047863
HAND1_HUMAN	HAND1	physical	14636580
HAND2_HUMAN	HAND2	physical	14636580
IQGA1_HUMAN	IQGAP1	physical	12938160
NIN_HUMAN	NIN	physical	12927815
MGMT_HUMAN	MGMT	physical	10667577
IRF2_HUMAN	IRF2	physical	9213219
RYR2_HUMAN	RYR2	physical	10830164
ASIC3_HUMAN	ASIC3	physical	12578970
ASIC1_HUMAN	ASIC1	physical	12578970
PP1R8_HUMAN	PPP1R8	physical	9407077
IPKA_HUMAN	PKIA	physical	8027074
KKCC2_HUMAN	CAMKK2	physical	10187789
BAD_HUMAN	BAD	physical	11500364
CREB1_HUMAN	CREB1	physical	11500364
ATU2_YEAST	CCC2	physical	18291109
CAV1_HUMAN	CAV1	physical	11546661
PDPK1_HUMAN	PDPK1	physical	10698939
ABC3G_HUMAN	APOBEC3G	physical	18836454
PO2F1_HUMAN	POU2F1	physical	1684878
CLH1_HUMAN	CLTC	physical	20936779
RANB9_HUMAN	RANBP9	physical	20936779
SIK3_HUMAN	SIK3	physical	20936779
GRDN_HUMAN	CCDC88A	physical	20936779
MEF2D_HUMAN	MEF2D	physical	18299387
HDAC1_HUMAN	HDAC1	physical	11327722
STP1_HUMAN	TNP1	physical	9837753
STP2_HUMAN	TNP2	physical	9837753
RGS13_HUMAN	RGS13	physical	20974683
HDAC1_HUMAN	HDAC1	physical	12082111
HDAC8_HUMAN	HDAC8	physical	12082111
CFTR_HUMAN	CFTR	physical	17272822
ITCH_HUMAN	ITCH	physical	17437719
UHRF1_HUMAN	UHRF1	physical	15178447
TF65_HUMAN	RELA	physical	20133937
TAU_HUMAN	MAPT	physical	9771888
TAU_HUMAN	MAPT	physical	10090741
PDE4D_HUMAN	PDE4D	physical	9639573
TAU_HUMAN	MAPT	physical	9546672
AKP13_HUMAN	AKAP13	physical	15383279
GSK3A_HUMAN	GSK3A	physical	11035810
GSK3B_HUMAN	GSK3B	physical	11035810
F261_HUMAN	PFKFB1	physical	15896703
TAU_HUMAN	MAPT	physical	21127069
KAPCB_HUMAN	PRKACB	physical	22939629
VTNC_HUMAN	VTN	physical	9030777
TAU_HUMAN	MAPT	physical	12435421
RAD_HUMAN	RRAD	physical	7876254
PP1RA_HUMAN	PPP1R10	physical	12574161
SIK1_HUMAN	SIK1	physical	23256157
TF65_HUMAN	RELA	physical	12628924
NOXA1_HUMAN	NOXA1	physical	20110267
RAD_HUMAN	RRAD	physical	9677319
ANXA7_HUMAN	ANXA7	physical	11278415
BAD_HUMAN	BAD	physical	19667065
CALD1_HUMAN	CALD1	physical	2050683
EGFR_HUMAN	EGFR	physical	12589790
PDE4D_HUMAN	PDE4D	physical	20196770
ITA2B_HUMAN	ITGA2B	physical	1650365
TA2R_HUMAN	TBXA2R	physical	14530262
GNA13_HUMAN	GNA13	physical	12399457
CP3A4_HUMAN	CYP3A4	physical	22101235
SMO_DROME	smo	physical	24244405
AASD1_HUMAN	AARSD1	physical	22863883
MARCS_HUMAN	MARCKS	physical	22863883
NASP_HUMAN	NASP	physical	22863883
SH3G1_HUMAN	SH3GL1	physical	22863883
UBQL2_HUMAN	UBQLN2	physical	22863883
UGDH_HUMAN	UGDH	physical	22863883
VAPB_HUMAN	VAPB	physical	23455922
HS90A_HUMAN	HSP90AA1	physical	23455922
HS90B_HUMAN	HSP90AB1	physical	23455922
KAP0_HUMAN	PRKAR1A	physical	23455922
KAP2_HUMAN	PRKAR2A	physical	23455922
KAPCG_HUMAN	PRKACG	physical	23455922
KAPCB_HUMAN	PRKACB	physical	23455922
AKAP5_HUMAN	AKAP5	physical	23455922
KAP1_HUMAN	PRKAR1B	physical	23455922
KAP3_HUMAN	PRKAR2B	physical	23455922
DCAF7_HUMAN	DCAF7	physical	23455922
DYL1_HUMAN	DYNLL1	physical	23455922
DYR1A_HUMAN	DYRK1A	physical	23455922
MARE1_HUMAN	MAPRE1	physical	23455922
MYOME_HUMAN	PDE4DIP	physical	23455922
NXPE4_HUMAN	NXPE4	physical	23455922
GP161_HUMAN	GPR161	physical	23455922
AKAP1_HUMAN	AKAP1	physical	23455922
CK5P2_HUMAN	CDK5RAP2	physical	23455922
AKAP9_HUMAN	AKAP9	physical	23455922
SMAKA_HUMAN	C2orf88	physical	23455922
VAPA_HUMAN	VAPA	physical	23455922
AKA7A_HUMAN	AKAP7	physical	23455922
AKA7G_HUMAN	AKAP7	physical	23455922
AKA11_HUMAN	AKAP11	physical	23455922
TAU_HUMAN	MAPT	physical	19014373
PDE3A_HUMAN	PDE3A	physical	17124499
TOM22_YEAST	TOM22	physical	24093680
KAP2_HUMAN	PRKAR2A	physical	26344197
RPE_HUMAN	RPE	physical	26344197
UBP20_HUMAN	USP20	physical	25666616
PSD11_HUMAN	PSMD11	physical	26669444
KLHL3_HUMAN	KLHL3	physical	26435498
FOXO1_HUMAN	FOXO1	physical	21177856
PTN7_HUMAN	PTPN7	physical	14613483
NFAT5_HUMAN	NFAT5	physical	12482947
DOCK1_HUMAN	DOCK1	physical	25468898
UBE2N_HUMAN	UBE2N	physical	27173435
DRD1_HUMAN	DRD1	physical	7609904
GLI1_HUMAN	GLI1	physical	16293631
1433Z_HUMAN	YWHAZ	physical	16376338
KAP0_HUMAN	PRKAR1A	physical	16376338
CDN1A_HUMAN	CDKN1A	physical	11463845
HNF4A_HUMAN	HNF4A	physical	11811951
MAVS_HUMAN	MAVS	physical	28934360

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
615830	Primary pigmented nodular adrenocortical disease 4 (PPNAD4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of KAPCA_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Mutants of protein kinase A that mimic the ATP-binding site of Aurorakinase."; Pflug A., de Oliveira T.M., Bossemeyer D., Engh R.A.; Biochem. J. 440:85-93(2011). Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH AURORA KINASEINHIBITORS, PHOSPHORYLATION AT SER-11; THR-198 AND SER-339, ANDMUTAGENESIS OF LYS-48; LEU-96; MET-121; VAL-124; GLN-182 AND THR-184.	21774789 [Abstract]
"Diversity of bisubstrate binding modes of adenosine analogue-oligoarginine conjugates in protein kinase a and implications forprotein substrate interactions."; Pflug A., Rogozina J., Lavogina D., Enkvist E., Uri A., Engh R.A.,Bossemeyer D.; J. Mol. Biol. 403:66-77(2010). Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH ADENOSINEANALOG, PHOSPHORYLATION AT SER-11; THR-198 AND SER-339, AND ENZYMEREGULATION.	20732331 [Abstract]
"Design of selective, ATP-competitive inhibitors of Akt."; Freeman-Cook K.D., Autry C., Borzillo G., Gordon D.,Barbacci-Tobin E., Bernardo V., Briere D., Clark T., Corbett M.,Jakubczak J., Kakar S., Knauth E., Lippa B., Luzzio M.J., Mansour M.,Martinelli G., Marx M., Nelson K., Pandit J., Rajamohan F.,Robinson S., Subramanyam C., Wei L., Wythes M., Morris J.; J. Med. Chem. 53:4615-4622(2010). Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS), PHOSPHORYLATION AT THR-198 ANDSER-339, AND ENZYME REGULATION.	20481595 [Abstract]
"Azole-based inhibitors of AKT/PKB for the treatment of cancer."; Zeng Q., Allen J.G., Bourbeau M.P., Wang X., Yao G., Tadesse S.,Rider J.T., Yuan C.C., Hong F.-T., Lee M.R., Zhang S., Lofgren J.A.,Freeman D.J., Yang S., Li C., Tominey E., Huang X., Hoffman D.,Yamane H.K., Fotsch C., Dominguez C., Hungate R., Zhang X.; Bioorg. Med. Chem. Lett. 20:1559-1564(2010). Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), PHOSPHORYLATION AT THR-198 ANDSER-339, AND ENZYME REGULATION.	20137943 [Abstract]
"Discovery of 2-pyrimidyl-5-amidothiophenes as potent inhibitors forAKT: synthesis and SAR studies."; Lin X., Murray J.M., Rico A.C., Wang M.X., Chu D.T., Zhou Y.,Del Rosario M., Kaufman S., Ma S., Fang E., Crawford K.,Jefferson A.B.; Bioorg. Med. Chem. Lett. 16:4163-4168(2006). Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 15-351, AND PHOSPHORYLATIONAT THR-198 AND SER-339.	16765046 [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 SER-339, AND MASSSPECTROMETRY.	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-196 AND SER-339, ANDMASS 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 THR-49; THR-196 AND SER-339,AND MASS SPECTROMETRY.	18691976 [Abstract]
"Phosphoproteome analysis of capacitated human sperm. Evidence oftyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation."; Ficarro S., Chertihin O., Westbrook V.A., White F., Jayes F.,Kalab P., Marto J.A., Shabanowitz J., Herr J.C., Hunt D.F.,Visconti P.E.; J. Biol. Chem. 278:11579-11589(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-339, AND MASSSPECTROMETRY.	12509440 [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-198, AND MASSSPECTROMETRY.	17192257 [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 THR-202, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Phosphorylation of the catalytic subunit of protein kinase A.Autophosphorylation versus phosphorylation by phosphoinositide-dependent kinase-1."; Moore M.J., Kanter J.R., Jones K.C., Taylor S.S.; J. Biol. Chem. 277:47878-47884(2002). Cited for: AUTOPHOSPHORYLATION, PHOSPHORYLATION AT THR-196, PHOSPHORYLATION ATTHR-198 BY PDK1, AND MUTAGENESIS OF ARG-195; GLY-201 AND THR-202.	12372837 [Abstract]

show