dbPTM

KPCA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KPCA_HUMAN
UniProt AC	P17252
Protein Name	Protein kinase C alpha type
Gene Name	PRKCA
Organism	Homo sapiens (Human).
Sequence Length	672
Subcellular Localization	Cytoplasm . Cell membrane Peripheral membrane protein . Mitochondrion membrane Peripheral membrane protein . Nucleus .
Protein Description	Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, tumorigenesis, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly phosphorylating targets such as RAF1, BCL2, CSPG4, TNNT2/CTNT, or activating signaling cascade involving MAPK1/3 (ERK1/2) and RAP1GAP. Involved in cell proliferation and cell growth arrest by positive and negative regulation of the cell cycle. Can promote cell growth by phosphorylating and activating RAF1, which mediates the activation of the MAPK/ERK signaling cascade, and/or by up-regulating CDKN1A, which facilitates active cyclin-dependent kinase (CDK) complex formation in glioma cells. In intestinal cells stimulated by the phorbol ester PMA, can trigger a cell cycle arrest program which is associated with the accumulation of the hyper-phosphorylated growth-suppressive form of RB1 and induction of the CDK inhibitors CDKN1A and CDKN1B. Exhibits anti-apoptotic function in glioma cells and protects them from apoptosis by suppressing the p53/TP53-mediated activation of IGFBP3, and in leukemia cells mediates anti-apoptotic action by phosphorylating BCL2. During macrophage differentiation induced by macrophage colony-stimulating factor (CSF1), is translocated to the nucleus and is associated with macrophage development. After wounding, translocates from focal contacts to lamellipodia and participates in the modulation of desmosomal adhesion. Plays a role in cell motility by phosphorylating CSPG4, which induces association of CSPG4 with extensive lamellipodia at the cell periphery and polarization of the cell accompanied by increases in cell motility. During chemokine-induced CD4(+) T cell migration, phosphorylates CDC42-guanine exchange factor DOCK8 resulting in its dissociation from LRCH1 and the activation of GTPase CDC42. [PubMed: 28028151 Is highly expressed in a number of cancer cells where it can act as a tumor promoter and is implicated in malignant phenotypes of several tumors such as gliomas and breast cancers. Negatively regulates myocardial contractility and positively regulates angiogenesis, platelet aggregation and thrombus formation in arteries. Mediates hypertrophic growth of neonatal cardiomyocytes, in part through a MAPK1/3 (ERK1/2)-dependent signaling pathway, and upon PMA treatment, is required to induce cardiomyocyte hypertrophy up to heart failure and death, by increasing protein synthesis, protein-DNA ratio and cell surface area. Regulates cardiomyocyte function by phosphorylating cardiac troponin T (TNNT2/CTNT), which induces significant reduction in actomyosin ATPase activity, myofilament calcium sensitivity and myocardial contractility. In angiogenesis, is required for full endothelial cell migration, adhesion to vitronectin (VTN), and vascular endothelial growth factor A (VEGFA)-dependent regulation of kinase activation and vascular tube formation. Involved in the stabilization of VEGFA mRNA at post-transcriptional level and mediates VEGFA-induced cell proliferation. In the regulation of calcium-induced platelet aggregation, mediates signals from the CD36/GP4 receptor for granule release, and activates the integrin heterodimer ITGA2B-ITGB3 through the RAP1GAP pathway for adhesion. During response to lipopolysaccharides (LPS), may regulate selective LPS-induced macrophage functions involved in host defense and inflammation. But in some inflammatory responses, may negatively regulate NF-kappa-B-induced genes, through IL1A-dependent induction of NF-kappa-B inhibitor alpha (NFKBIA/IKBA Upon stimulation with 12-O-tetradecanoylphorbol-13-acetate (TPA), phosphorylates EIF4G1, which modulates EIF4G1 binding to MKNK1 and may be involved in the regulation of EIF4E phosphorylation. Phosphorylates KIT, leading to inhibition of KIT activity. Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription.]
Protein Sequence	MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNMELRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKGTEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSVCKGLMTKHPAKRLGCGPEGERDVREHAFFRRIDWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVNPQFVHPILQSAV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADVFPGND ------CCCCCCCCC	22.98	22814378
10	Phosphorylation	DVFPGNDSTASQDVA CCCCCCCCCHHHHHH	29.85	28355574
11	Phosphorylation	VFPGNDSTASQDVAN CCCCCCCCHHHHHHH	32.94	25159151
13	Phosphorylation	PGNDSTASQDVANRF CCCCCCHHHHHHHHH	27.31	28464451
38	Ubiquitination	VHEVKDHKFIARFFK HHHHCCCHHHHHHHC	48.91	-
48	Phosphorylation	ARFFKQPTFCSHCTD HHHHCCCCCCHHHHH	34.48	30108239
51	Phosphorylation	FKQPTFCSHCTDFIW HCCCCCCHHHHHCHH	19.87	30108239
54	Phosphorylation	PTFCSHCTDFIWGFG CCCCHHHHHCHHCCC	28.64	28450419
76	Ubiquitination	VCCFVVHKRCHEFVT EEEEEEECCCCEEEE	45.14	-
91	Ubiquitination	FSCPGADKGPDTDDP EECCCCCCCCCCCCC	72.33	-
100	Phosphorylation	PDTDDPRSKHKFKIH CCCCCCCCCCCEEEE	44.49	28857561
105	Acetylation	PRSKHKFKIHTYGSP CCCCCCEEEEECCCC	38.08	7662335
108	Phosphorylation	KHKFKIHTYGSPTFC CCCEEEEECCCCCCH	32.81	27080861
109	Phosphorylation	HKFKIHTYGSPTFCD CCEEEEECCCCCCHH	11.05	27080861
111	Phosphorylation	FKIHTYGSPTFCDHC EEEEECCCCCCHHHH	15.45	27080861
113	Phosphorylation	IHTYGSPTFCDHCGS EEECCCCCCHHHHHH	38.30	27080861
120	Phosphorylation	TFCDHCGSLLYGLIH CCHHHHHHHHHHHHH	22.16	27080861
123	Phosphorylation	DHCGSLLYGLIHQGM HHHHHHHHHHHHCCC	18.38	20873877
134	Phosphorylation	HQGMKCDTCDMNVHK HCCCCCCCCCCCEEC	21.63	28857561
149	Phosphorylation	QCVINVPSLCGMDHT CCEECCHHHCCCCCC	31.82	27080861
156	Phosphorylation	SLCGMDHTEKRGRIY HHCCCCCCCCCCCEE	38.65	27080861
158	Acetylation	CGMDHTEKRGRIYLK CCCCCCCCCCCEEEE	62.40	25953088
158	Ubiquitination	CGMDHTEKRGRIYLK CCCCCCCCCCCEEEE	62.40	-
165	Ubiquitination	KRGRIYLKAEVADEK CCCCEEEEEEECCCE	26.06	-
172	Malonylation	KAEVADEKLHVTVRD EEEECCCEECEEEEH	44.43	26320211
172	Ubiquitination	KAEVADEKLHVTVRD EEEECCCEECEEEEH	44.43	-
172	2-Hydroxyisobutyrylation	KAEVADEKLHVTVRD EEEECCCEECEEEEH	44.43	-
172	Acetylation	KAEVADEKLHVTVRD EEEECCCEECEEEEH	44.43	23749302
176	Phosphorylation	ADEKLHVTVRDAKNL CCCEECEEEEHHHHC	10.08	-
176	O-linked_Glycosylation	ADEKLHVTVRDAKNL CCCEECEEEEHHHHC	10.08	30379171
192	Phosphorylation	PMDPNGLSDPYVKLK CCCCCCCCCCCEEEE	37.63	28102081
195	Phosphorylation	PNGLSDPYVKLKLIP CCCCCCCCEEEEECC	18.40	21082442
197	Acetylation	GLSDPYVKLKLIPDP CCCCCCEEEEECCCC	33.78	22637133
197	Ubiquitination	GLSDPYVKLKLIPDP CCCCCCEEEEECCCC	33.78	-
199	Ubiquitination	SDPYVKLKLIPDPKN CCCCEEEEECCCCCC	38.36	-
205	Ubiquitination	LKLIPDPKNESKQKT EEECCCCCCCCCCCC	79.37	-
208	Phosphorylation	IPDPKNESKQKTKTI CCCCCCCCCCCCCHH	50.18	17192257
214	Phosphorylation	ESKQKTKTIRSTLNP CCCCCCCHHHHHCCC	27.18	22468782
217	Phosphorylation	QKTKTIRSTLNPQWN CCCCHHHHHCCCCCC	33.14	26329039
218	Phosphorylation	KTKTIRSTLNPQWNE CCCHHHHHCCCCCCC	22.24	26329039
226	Phosphorylation	LNPQWNESFTFKLKP CCCCCCCEEEEECCC	26.77	22167270
228	Phosphorylation	PQWNESFTFKLKPSD CCCCCEEEEECCCCC	29.19	30266825
230	Ubiquitination	WNESFTFKLKPSDKD CCCEEEEECCCCCCC	53.17	-
234	Phosphorylation	FTFKLKPSDKDRRLS EEEECCCCCCCCCEE	56.56	23401153
236	2-Hydroxyisobutyrylation	FKLKPSDKDRRLSVE EECCCCCCCCCEEEE	58.43	-
241	Phosphorylation	SDKDRRLSVEIWDWD CCCCCCEEEEEEECC	18.85	28450419
250	Phosphorylation	EIWDWDRTTRNDFMG EEEECCCCCCHHHHC	27.86	-
258	Phosphorylation	TRNDFMGSLSFGVSE CCHHHHCHHHHCHHH	14.73	22210691
260	Phosphorylation	NDFMGSLSFGVSELM HHHHCHHHHCHHHHH	22.96	22210691
272	Phosphorylation	ELMKMPASGWYKLLN HHHCCCCCCHHHHHC	24.80	22210691
285	Phosphorylation	LNQEEGEYYNVPIPE HCCCCCCEEECCCCC	15.93	28796482
286	Phosphorylation	NQEEGEYYNVPIPEG CCCCCCEEECCCCCC	12.84	28796482
299	Sulfoxidation	EGDEEGNMELRQKFE CCCCCCCHHHHHHHH	8.25	30846556
309	Ubiquitination	RQKFEKAKLGPAGNK HHHHHHHCCCCCCCC	66.11	-
316	Ubiquitination	KLGPAGNKVISPSED CCCCCCCCCCCCCCC	39.77	-
316	Acetylation	KLGPAGNKVISPSED CCCCCCCCCCCCCCC	39.77	25953088
319	Phosphorylation	PAGNKVISPSEDRKQ CCCCCCCCCCCCCCC	25.92	29255136
321	Phosphorylation	GNKVISPSEDRKQPS CCCCCCCCCCCCCCC	45.39	30266825
325	Ubiquitination	ISPSEDRKQPSNNLD CCCCCCCCCCCCCCC	78.03	-
328	Phosphorylation	SEDRKQPSNNLDRVK CCCCCCCCCCCCCEE	35.54	23186163
337	Phosphorylation	NLDRVKLTDFNFLMV CCCCEEECCCCEEEE	32.59	-
347	Ubiquitination	NFLMVLGKGSFGKVM CEEEEECCCCCCCEE	47.42	-
349	Phosphorylation	LMVLGKGSFGKVMLA EEEECCCCCCCEEEC	34.02	28348404
352	Ubiquitination	LGKGSFGKVMLADRK ECCCCCCCEEECCCC	23.59	-
359	Ubiquitination	KVMLADRKGTEELYA CEEECCCCCCHHEEE	71.39	-
361	Phosphorylation	MLADRKGTEELYAIK EECCCCCCHHEEEEE	29.35	-
365	Phosphorylation	RKGTEELYAIKILKK CCCCHHEEEEEEECC	15.01	25147952
368	Ubiquitination	TEELYAIKILKKDVV CHHEEEEEEECCCEE	33.54	-
388	Ubiquitination	VECTMVEKRVLALLD CEEEEEEHHHHHHHC	36.07	-
465	Ubiquitination	GIIYRDLKLDNVMLD CEEECCCCCCCEEEC	59.07	-
473	Phosphorylation	LDNVMLDSEGHIKIA CCCEEECCCCCEEEC	41.33	-
478	Ubiquitination	LDSEGHIKIADFGMC ECCCCCEEECCCCCC	26.60	-
486	Ubiquitination	IADFGMCKEHMMDGV ECCCCCCHHHCCCCC	41.59	-
494	Phosphorylation	EHMMDGVTTRTFCGT HHCCCCCCHHCCCCC	18.98	22322096
495	Phosphorylation	HMMDGVTTRTFCGTP HCCCCCCHHCCCCCC	25.88	22322096
497	Phosphorylation	MDGVTTRTFCGTPDY CCCCCHHCCCCCCCC	22.61	22322096
499	Glutathionylation	GVTTRTFCGTPDYIA CCCHHCCCCCCCCCC	6.16	12189155
501	Phosphorylation	TTRTFCGTPDYIAPE CHHCCCCCCCCCCCH	17.73	22322096
504	Phosphorylation	TFCGTPDYIAPEIIA CCCCCCCCCCCHHHE	10.53	25463755
512	Phosphorylation	IAPEIIAYQPYGKSV CCCHHHEECCCCCCH	10.30	23898821
515	Phosphorylation	EIIAYQPYGKSVDWW HHHEECCCCCCHHHH	22.97	23403867
556	Phosphorylation	SIMEHNVSYPKSLSK HHHHCCCCCCCCCCH	40.82	24719451
570	Acetylation	KEAVSVCKGLMTKHP HHHHHHHHHHHHCCH	53.58	19608861
575	Ubiquitination	VCKGLMTKHPAKRLG HHHHHHHCCHHHHCC	33.36	-
575	Acetylation	VCKGLMTKHPAKRLG HHHHHHHCCHHHHCC	33.36	25953088
604	Ubiquitination	FRRIDWEKLENREIQ HHCCCHHHHHCCCCC	57.77	19608861
604	Acetylation	FRRIDWEKLENREIQ HHCCCHHHHHCCCCC	57.77	19608861
615	Ubiquitination	REIQPPFKPKVCGKG CCCCCCCCCCCCCCC	50.10	-
617	Malonylation	IQPPFKPKVCGKGAE CCCCCCCCCCCCCCC	51.23	26320211
617	Ubiquitination	IQPPFKPKVCGKGAE CCCCCCCCCCCCCCC	51.23	-
621	Ubiquitination	FKPKVCGKGAENFDK CCCCCCCCCCCCHHH	50.23	-
628	Acetylation	KGAENFDKFFTRGQP CCCCCHHHHHCCCCC	37.94	19608861
628	Ubiquitination	KGAENFDKFFTRGQP CCCCCHHHHHCCCCC	37.94	21890473
628	Ubiquitination	KGAENFDKFFTRGQP CCCCCHHHHHCCCCC	37.94	21890473
631	Phosphorylation	ENFDKFFTRGQPVLT CCHHHHHCCCCCCCC	36.70	26074081
638	Phosphorylation	TRGQPVLTPPDQLVI CCCCCCCCCCCCEEE	32.77	17591920
651	Phosphorylation	VIANIDQSDFEGFSY EEEECCHHHCCCCCC	40.28	30177828
657	Phosphorylation	QSDFEGFSYVNPQFV HHHCCCCCCCCHHHH	38.74	15949469
658	Phosphorylation	SDFEGFSYVNPQFVH HHCCCCCCCCHHHHH	11.28	30177828
670	Phosphorylation	FVHPILQSAV----- HHHHHHHHCC-----	27.79	20068231

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
226	S	Phosphorylation	Kinase	STK3	Q13188	GPS
228	T	Phosphorylation	Kinase	STK3	Q13188	GPS
250	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
497	T	Phosphorylation	Kinase	PDPK1	O15530	Uniprot
638	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
657	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
658	Y	Phosphorylation	Kinase	SYK	P43405	Uniprot
658	Y	Phosphorylation	Kinase	SYK	Q15046	PhosphoELM
-	K	Ubiquitination	E3 ubiquitin ligase	RBCK1	Q9BYM8	PMID:25118570
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:20804422
-	K	Ubiquitination	E3 ubiquitin ligase	RNF31	Q96EP0	PMID:17069764

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KPCA_HUMAN !!

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 KPCA_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AT1A1_HUMAN	ATP1A1	physical	15069082
HABP4_HUMAN	HABP4	physical	14699138
HAND1_HUMAN	HAND1	physical	14636580
HAND2_HUMAN	HAND2	physical	14636580
FSCN1_HUMAN	FSCN1	physical	14532112
EGFR_HUMAN	EGFR	physical	12878187
PLD1_HUMAN	PLD1	physical	12839565
KLF5_HUMAN	KLF5	physical	12682370
MGMT_HUMAN	MGMT	physical	10667577
PICK1_HUMAN	PICK1	physical	11007882
GRM7_HUMAN	GRM7	physical	11007882
CXA1_HUMAN	GJA1	physical	11273731
1433G_HUMAN	YWHAG	physical	10433554
V1AR_HUMAN	AVPR1A	physical	10858434
V1BR_HUMAN	AVPR1B	physical	10858434
GSK3B_HUMAN	GSK3B	physical	1324914
RGS2_HUMAN	RGS2	physical	11063746
OGG1_HUMAN	OGG1	physical	12034821
TIAM1_HUMAN	TIAM1	physical	10212259
RACK1_HUMAN	GNB2L1	physical	12435334
ITB1_HUMAN	ITGB1	physical	12138200
LMNA_HUMAN	LMNA	physical	12112001
HMGA1_HUMAN	HMGA1	physical	10889043
HMGA2_HUMAN	HMGA2	physical	10889043
STP1_HUMAN	TNP1	physical	9837753
STP2_HUMAN	TNP2	physical	9837753
H31_HUMAN	HIST1H3A	physical	20228790
IKKB_HUMAN	IKBKB	physical	10022904
IKKA_HUMAN	CHUK	physical	10022904
NF2L2_HUMAN	NFE2L2	physical	19920073
KPCA_HUMAN	PRKCA	physical	19920073
TRPV6_HUMAN	TRPV6	physical	11248124
DDX58_HUMAN	DDX58	physical	22114345
H11_HUMAN	HIST1H1A	physical	15927069
H15_HUMAN	HIST1H1B	physical	15927069
H12_HUMAN	HIST1H1C	physical	15927069
H13_HUMAN	HIST1H1D	physical	15927069
H14_HUMAN	HIST1H1E	physical	15927069
H1T_HUMAN	HIST1H1T	physical	15927069
4EBP1_HUMAN	EIF4EBP1	physical	15927069
MBP_HUMAN	MBP	physical	15927069
HDAC6_HUMAN	HDAC6	physical	21952047
HDAC6_HUMAN	HDAC6	physical	21949397
CTNB1_HUMAN	CTNNB1	physical	21949397
NR1H2_HUMAN	NR1H2	physical	18372238
H31T_HUMAN	HIST3H3	physical	9716497
ANXA6_HUMAN	ANXA6	physical	9480874
H11_HUMAN	HIST1H1A	physical	16314418
GLI3_HUMAN	GLI3	physical	16371461
IBTK_HUMAN	IBTK	physical	21482705
SCRIB_HUMAN	SCRIB	physical	20622900
CBL_HUMAN	CBL	physical	10358153
TOP2A_HUMAN	TOP2A	physical	7499337
LYAM1_HUMAN	SELL	physical	15192100
F261_HUMAN	PFKFB1	physical	15896703
NCF1_HUMAN	NCF1	physical	12056906
H11_HUMAN	HIST1H1A	physical	12056906
RBP1_HUMAN	RALBP1	physical	16087181
PP14A_HUMAN	PPP1R14A	physical	15003508
VTNC_HUMAN	VTN	physical	9030777
MARCS_MOUSE	Marcks	physical	7588787
SDC2_HUMAN	SDC2	physical	9244383
ITB2_HUMAN	ITGB2	physical	11700305
GSK3A_HUMAN	GSK3A	physical	11884598
ELAV1_HUMAN	ELAVL1	physical	17392515
NMDZ1_HUMAN	GRIN1	physical	9670010
NMDE2_HUMAN	GRIN2B	physical	9670010
CASR_HUMAN	CASR	physical	9694886
RAD_HUMAN	RRAD	physical	9677319
IKBA_HUMAN	NFKBIA	physical	10398585
KPCA_HUMAN	PRKCA	physical	10398585
H15_HUMAN	HIST1H1B	physical	8663071
HMGN1_HUMAN	HMGN1	physical	11438671
HMGN2_HUMAN	HMGN2	physical	11438671
NUMB_HUMAN	NUMB	physical	17203073
NUMB_DROME	numb	physical	17203073
PSB4_HUMAN	PSMB4	physical	21988832
SAC1_HUMAN	SACM1L	physical	21988832
PI2R_HUMAN	PTGIR	physical	9722557
TA2R_HUMAN	TBXA2R	physical	11504827
TA2R_HUMAN	TBXA2R	physical	12370102
CP3A4_HUMAN	CYP3A4	physical	22101235
HOIL1_HUMAN	RBCK1	physical	25118570
EP300_HUMAN	EP300	physical	11020388
PPARG_HUMAN	PPARG	physical	17325208
IF2A_HUMAN	EIF2S1	physical	21368187
WWC2_HUMAN	WWC2	physical	24682284
WWC3_HUMAN	WWC3	physical	24682284
KIBRA_HUMAN	WWC1	physical	24682284
MK07_HUMAN	MAPK7	physical	26344197
NOXA1_HUMAN	NOXA1	physical	20110267
GRM5_HUMAN	GRM5	physical	23152621
KPCA_HUMAN	PRKCA	physical	8375396
STXB1_HUMAN	STXBP1	physical	12519779
SPAG1_HUMAN	SPAG1	physical	11517287
PICK1_RAT	Pick1	physical	11237868
BTG2_HUMAN	BTG2	physical	11237868
NF2L2_HUMAN	NFE2L2	physical	12947090
GRM5_RAT	Grm5	physical	15894802
CYBP_HUMAN	CACYBP	physical	11927578
MERL_HUMAN	NF2	physical	21750658
PA24A_HUMAN	PLA2G4A	physical	16963226
KPCB_HUMAN	PRKCB	physical	28514442
KPCG_HUMAN	PRKCG	physical	28514442
KPCL_HUMAN	PRKCH	physical	28514442
PI51A_HUMAN	PIP5K1A	physical	28514442
SHCBP_HUMAN	SHCBP1	physical	28514442
GSH0_HUMAN	GCLM	physical	28514442
STAR7_HUMAN	STARD7	physical	28514442
FGD4_HUMAN	FGD4	physical	28514442
DUS11_HUMAN	DUSP11	physical	28514442
FBX21_HUMAN	FBXO21	physical	28514442
HAIR_HUMAN	HR	physical	27355563
KC1D_RAT	Csnk1d	physical	17594292

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
D02970	Aprinocarsen sodium (USAN); Affinitak (TN)
D04014	Enzastaurin hydrochloride (JAN/USAN)
D05029	Midostaurin (USAN/INN)
DrugBank
DB05013	Ingenol Mebutate
DB00144	Phosphatidylserine
DB00675	Tamoxifen
DB00163	Vitamin E

Regulatory Network of KPCA_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-604 AND LYS-628, AND MASSSPECTROMETRY.	19608861 [Abstract]
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-226, AND MASSSPECTROMETRY.	19690332 [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-226, AND MASSSPECTROMETRY.	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-208; SER-226; SER-319AND THR-497, 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-319, AND MASSSPECTROMETRY.	18088087 [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-226; THR-497; THR-501;THR-638 AND TYR-658, AND MASS SPECTROMETRY.	17192257 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND MASSSPECTROMETRY.	16964243 [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-226 AND SER-319, ANDMASS SPECTROMETRY.	17081983 [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-195, AND MASSSPECTROMETRY.	18083107 [Abstract]