dbPTM

MK14_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MK14_HUMAN
UniProt AC	Q16539
Protein Name	Mitogen-activated protein kinase 14
Gene Name	MAPK14
Organism	Homo sapiens (Human).
Sequence Length	360
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK14 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36 (tristetraprolin) and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. MAPK14 interacts also with casein kinase II, leading to its activation through autophosphorylation and further phosphorylation of TP53/p53. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. In a similar way, MAPK14 phosphorylates the ubiquitin ligase SIAH2, regulating its activity towards EGLN3. MAPK14 may also inhibit the lysosomal degradation pathway of autophagy by interfering with the intracellular trafficking of the transmembrane protein ATG9. Another function of MAPK14 is to regulate the endocytosis of membrane receptors by different mechanisms that impinge on the small GTPase RAB5A. In addition, clathrin-mediated EGFR internalization induced by inflammatory cytokines and UV irradiation depends on MAPK14-mediated phosphorylation of EGFR itself as well as of RAB5A effectors. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10' (H3S10ph) in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. Phosphorylates CDC25B and CDC25C which is required for binding to 14-3-3 proteins and leads to initiation of a G2 delay after ultraviolet radiation. Phosphorylates TIAR following DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA degradation. The p38 MAPKs may also have kinase-independent roles, which are thought to be due to the binding to targets in the absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by the OGT is regulated by MAPK14, and, although OGT does not seem to be phosphorylated by MAPK14, their interaction increases upon MAPK14 activation induced by glucose deprivation. This interaction may regulate OGT activity by recruiting it to specific targets such as neurofilament H, stimulating its O-Glc-N-acylation. Required in mid-fetal development for the growth of embryo-derived blood vessels in the labyrinth layer of the placenta. Also plays an essential role in developmental and stress-induced erythropoiesis, through regulation of EPO gene expression. Isoform MXI2 activation is stimulated by mitogens and oxidative stress and only poorly phosphorylates ELK1 and ATF2. Isoform EXIP may play a role in the early onset of apoptosis. Phosphorylates S100A9 at 'Thr-113'.; (Microbial infection) Activated by phosphorylation by M.tuberculosis EsxA in T-cells leading to inhibition of IFN-gamma production; phosphorylation is apparent within 15 minute and is inhibited by kinase-specific inhibitors SB203580 and siRNA. [PubMed: 21586573]
Protein Sequence	MSQERPTFYRQELNKTIWEVPERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFNDVYLVTHLMGADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAELLKKISSESARNYIQSLTQMPKMNFANVFIGANPLAVDLLEKMLVLDSDKRITAAQALAHAYFAQYHDPDDEPVADPYDQSFESRDLLIDEWKSLTYDEVISFVPPPLDQEEMES

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSQERPTFY ------CCCCCCCCC	40.52	23401153
2	Acetylation	------MSQERPTFY ------CCCCCCCCC	40.52	20068231
7	Phosphorylation	-MSQERPTFYRQELN -CCCCCCCCCHHHHH	39.25	23401153
9	Phosphorylation	SQERPTFYRQELNKT CCCCCCCCHHHHHHH	17.54	18691976
15 (in isoform 2)	Ubiquitination	-	54.75	21890473
15	Ubiquitination	FYRQELNKTIWEVPE CCHHHHHHHHHHCHH	54.75	21890473
15 (in isoform 1)	Ubiquitination	-	54.75	21890473
15 (in isoform 3)	Ubiquitination	-	54.75	21890473
15 (in isoform 4)	Ubiquitination	-	54.75	21890473
15	Ubiquitination	FYRQELNKTIWEVPE CCHHHHHHHHHHCHH	54.75	21890473
16	Phosphorylation	YRQELNKTIWEVPER CHHHHHHHHHHCHHH	30.19	17192257
24	Phosphorylation	IWEVPERYQNLSPVG HHHCHHHHCCCCCCC	10.49	27251275
28	Phosphorylation	PERYQNLSPVGSGAY HHHHCCCCCCCCCCC	25.70	25159151
32	Phosphorylation	QNLSPVGSGAYGSVC CCCCCCCCCCCCCCH	22.08	28152594
35	Phosphorylation	SPVGSGAYGSVCAAF CCCCCCCCCCCHHEE	17.29	27251275
37	Phosphorylation	VGSGAYGSVCAAFDT CCCCCCCCCHHEEEC	11.01	27251275
45	Ubiquitination	VCAAFDTKTGLRVAV CHHEEECCCCHHHHH	42.30	-
53	Acetylation	TGLRVAVKKLSRPFQ CCHHHHHHHCCCCHH	37.95	21444723
54	Ubiquitination	GLRVAVKKLSRPFQS CHHHHHHHCCCCHHH	45.13	-
56	Phosphorylation	RVAVKKLSRPFQSII HHHHHHCCCCHHHHH	46.95	-
61	Phosphorylation	KLSRPFQSIIHAKRT HCCCCHHHHHHHHHH	24.72	20873877
66	Ubiquitination	FQSIIHAKRTYRELR HHHHHHHHHHHHHHH	30.98	-
79	Ubiquitination	LRLLKHMKHENVIGL HHHHHHCCCCCCHHH	47.70	-
79	Sumoylation	LRLLKHMKHENVIGL HHHHHHCCCCCCHHH	47.70	-
79	Sumoylation	LRLLKHMKHENVIGL HHHHHHCCCCCCHHH	47.70	-
118	Ubiquitination	ADLNNIVKCQKLTDD CCCCCCCCCCCCCHH	27.44	-
121	Ubiquitination	NNIVKCQKLTDDHVQ CCCCCCCCCCHHHHH	63.93	-
123	Phosphorylation	IVKCQKLTDDHVQFL CCCCCCCCHHHHHHH	46.55	17055984
139 (in isoform 4)	Ubiquitination	-	45.01	21890473
139	Ubiquitination	YQILRGLKYIHSADI HHHHHHCCHHHHHCE	45.01	21890473
139	Ubiquitination	YQILRGLKYIHSADI HHHHHHCCHHHHHCE	45.01	21890473
139 (in isoform 1)	Ubiquitination	-	45.01	21890473
139 (in isoform 2)	Ubiquitination	-	45.01	21890473
139 (in isoform 3)	Ubiquitination	-	45.01	21890473
140	Phosphorylation	QILRGLKYIHSADII HHHHHCCHHHHHCEE	14.65	23312004
143	Phosphorylation	RGLKYIHSADIIHRD HHCCHHHHHCEECCC	20.34	23312004
152	Acetylation	DIIHRDLKPSNLAVN CEECCCCCHHHCCCC	51.17	21444723
152	Ubiquitination	DIIHRDLKPSNLAVN CEECCCCCHHHCCCC	51.17	21444723
162	Glutathionylation	NLAVNEDCELKILDF HCCCCCCCEEEEEEE	5.56	22555962
165	Ubiquitination	VNEDCELKILDFGLA CCCCCEEEEEEEEEC	20.94	-
175	Phosphorylation	DFGLARHTDDEMTGY EEEECCCCCCCHHHH	39.32	21945579
179	Sulfoxidation	ARHTDDEMTGYVATR CCCCCCCHHHHHHCC	4.54	30846556
180	Phosphorylation	RHTDDEMTGYVATRW CCCCCCHHHHHHCCC	24.26	19934253
182	Phosphorylation	TDDEMTGYVATRWYR CCCCHHHHHHCCCEE	4.26	19934253
185	Phosphorylation	EMTGYVATRWYRAPE CHHHHHHCCCEECCH	16.22	21945579
221	Phosphorylation	AELLTGRTLFPGTDH HHHHHCCCCCCCCCC	33.81	22985185
233	Ubiquitination	TDHIDQLKLILRLVG CCCHHHHHHHHHHHC	28.05	-
233	Acetylation	TDHIDQLKLILRLVG CCCHHHHHHHHHHHC	28.05	25953088
239 (in isoform 2)	Phosphorylation	-	6.93	20068231
241	Phosphorylation	LILRLVGTPGAELLK HHHHHHCCCHHHHHH	15.86	18691976
241 (in isoform 2)	Phosphorylation	-	15.86	17192257
245 (in isoform 2)	Phosphorylation	-	61.62	20068231
248 (in isoform 1)	Ubiquitination	-	61.76	21890473
248 (in isoform 3)	Ubiquitination	-	61.76	21890473
248	Ubiquitination	TPGAELLKKISSESA CCHHHHHHHHCCHHH	61.76	21890473
248 (in isoform 4)	Ubiquitination	-	61.76	21890473
248	Ubiquitination	TPGAELLKKISSESA CCHHHHHHHHCCHHH	61.76	21890473
249	Ubiquitination	PGAELLKKISSESAR CHHHHHHHHCCHHHH	48.03	-
252 (in isoform 2)	Phosphorylation	-	38.76	20068231
256	Methylation	KISSESARNYIQSLT HHCCHHHHHHHHHHH	45.85	115386679
258	Nitration	SSESARNYIQSLTQM CCHHHHHHHHHHHCC	8.52	-
258 (in isoform 2)	Phosphorylation	-	8.52	20068231
258	Phosphorylation	SSESARNYIQSLTQM CCHHHHHHHHHHHCC	8.52	27642862
261 (in isoform 2)	Phosphorylation	-	24.67	20068231
263 (in isoform 2)	Phosphorylation	-	28.24	20068231
263	Phosphorylation	RNYIQSLTQMPKMNF HHHHHHHHCCCCCCC	28.24	17525332
295	Ubiquitination	MLVLDSDKRITAAQA HHCCCCCCCHHHHHH	50.04	-
298	Phosphorylation	LDSDKRITAAQALAH CCCCCCHHHHHHHHH	21.70	18691976
323	Phosphorylation	DEPVADPYDQSFESR CCCCCCCCCCCHHHH	27.45	15284239
326	Phosphorylation	VADPYDQSFESRDLL CCCCCCCCHHHHCCH	28.25	25159151
338	Sumoylation	DLLIDEWKSLTYDEV CCHHHHHHHCCHHHH	33.27	-

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
123	T	Phosphorylation	Kinase	GRK2	P25098	PSP
180	T	Phosphorylation	Kinase	MAP2K_GROUP	-	PhosphoELM
180	T	Phosphorylation	Kinase	MAP2K-FAMILY	-	GPS
180	T	Phosphorylation	Kinase	MAP3K5	Q99683	GPS
180	T	Phosphorylation	Kinase	MAP3K6	O95382	GPS
180	T	Phosphorylation	Kinase	MAPK14	Q16539	GPS
180	T	Phosphorylation	Kinase	MKK3	P46734	PSP
180	T	Phosphorylation	Kinase	MKK4	P45985	PSP
180	T	Phosphorylation	Kinase	MP2K6	P52564	PhosphoELM
182	Y	Phosphorylation	Kinase	MKK3	P46734	PSP
182	Y	Phosphorylation	Kinase	MAP2K_GROUP	-	PhosphoELM
182	Y	Phosphorylation	Kinase	MAP2K-FAMILY	-	GPS
182	Y	Phosphorylation	Kinase	RET	P07949	PSP
182	Y	Phosphorylation	Kinase	MKK6	P52564	PSP
182	Y	Phosphorylation	Kinase	MKK4	P45985	PSP
182	Y	Phosphorylation	Kinase	MAPK14	Q16539	GPS
182	Y	Phosphorylation	Kinase	MAP3K6	O95382	GPS
182	Y	Phosphorylation	Kinase	MAP3K5	Q99683	GPS
323	Y	Phosphorylation	Kinase	ZAP70	P43403	Uniprot
323	Y	Phosphorylation	Kinase	LCK	P06239	PSP
323	Y	Phosphorylation	Kinase	FYN	P06241	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
53	K	Acetylation	7493921
Acetylated at Lys-53 and Lys-152 by KAT2B and EP300.
53	K	Acetylation	7493921
Acetylation at Lys-53 increases the affinity for ATP and enhances kinase activity.
53	K	Acetylation	7493921
Lys-53 and Lys-152 are deacetylated by HDAC3.
152	K	Acetylation	21444723
Acetylated at Lys-53 and Lys-152 by KAT2B and EP300.
152	K	Acetylation	21444723
Lys-53 and Lys-152 are deacetylated by HDAC3.
180	T	Phosphorylation	7535770
Dually phosphorylated on Thr-180 and Tyr-182 by the MAP2Ks MAP2K3/MKK3, MAP2K4/MKK4 and MAP2K6/MKK6 in response to inflammatory citokines, environmental stress or growth factors, which activates the enzyme.

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 MK14_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MPIP1_HUMAN	CDC25A	physical	12963847
S12A2_HUMAN	SLC12A2	physical	14563843
STK39_HUMAN	STK39	physical	14563843
MK01_HUMAN	MAPK1	physical	12697810
MK03_HUMAN	MAPK3	physical	12697810
SMAD7_HUMAN	SMAD7	physical	12589052
KS6A4_HUMAN	RPS6KA4	physical	9792677
AKT1_HUMAN	AKT1	physical	11042204
EGFR_HUMAN	EGFR	physical	7535770
ATF2_HUMAN	ATF2	physical	7535770
MEF2A_HUMAN	MEF2A	physical	9858528
KS6B1_MOUSE	Rps6kb1	physical	11279232
MEF2A_HUMAN	MEF2A	physical	10330143
DUS16_HUMAN	DUSP16	physical	11359773
DUS10_HUMAN	DUSP10	physical	11359773
DUS6_HUMAN	DUSP6	physical	11359773
DUS1_HUMAN	DUSP1	physical	11359773
CSK21_HUMAN	CSNK2A1	physical	10747897
DYR1B_HUMAN	DYRK1B	physical	10910078
MPIP2_HUMAN	CDC25B	physical	11333986
MPIP3_HUMAN	CDC25C	physical	11333986
GMFB_HUMAN	GMFB	physical	8798479
ETV1_HUMAN	ETV1	physical	11551945
MK01_HUMAN	MAPK1	physical	11157753
KS6A3_HUMAN	RPS6KA3	physical	11157753
KS6A5_HUMAN	RPS6KA5	physical	11157753
MKNK1_HUMAN	MKNK1	physical	11157753
DUS10_HUMAN	DUSP10	physical	11157753
MK14_HUMAN	MAPK14	physical	11847341
DUS1_HUMAN	DUSP1	physical	11278799
ATF2_HUMAN	ATF2	physical	11279118
MP2K7_HUMAN	MAP2K7	physical	9207092
DDIT3_HUMAN	DDIT3	physical	8650547
K2C8_HUMAN	KRT8	physical	11788583
AES_HUMAN	AES	physical	20936779
DUS1_HUMAN	DUSP1	physical	20936779
FLNA_HUMAN	FLNA	physical	20936779
MKNK2_HUMAN	MKNK2	physical	20936779
ZEP1_HUMAN	HIVEP1	physical	20936779
MEF2C_HUMAN	MEF2C	physical	20936779
MEF2D_HUMAN	MEF2D	physical	20936779
NKTR_HUMAN	NKTR	physical	20936779
ROBO1_HUMAN	ROBO1	physical	20936779
SPTB2_HUMAN	SPTBN1	physical	20936779
TCF20_HUMAN	TCF20	physical	20936779
ZN142_HUMAN	ZNF142	physical	20936779
MAPK5_HUMAN	MAPKAPK5	physical	20936779
MKNK1_HUMAN	MKNK1	physical	20936779
KS6A5_HUMAN	RPS6KA5	physical	20936779
DUS10_HUMAN	DUSP10	physical	20936779
YYAP1_HUMAN	YY1AP1	physical	20936779
SP20H_HUMAN	SUPT20H	physical	20936779
P4R3A_HUMAN	SMEK1	physical	20936779
KMT2C_HUMAN	KMT2C	physical	20936779
CCD14_HUMAN	CCDC14	physical	20936779
MOB3B_HUMAN	MOB3B	physical	20936779
DUS16_HUMAN	DUSP16	physical	20936779
CCD97_HUMAN	CCDC97	physical	20936779
EMSA1_HUMAN	ELMSAN1	physical	20936779
INT6L_HUMAN	DDX26B	physical	20936779
MUC12_HUMAN	MUC12	physical	20936779
P4K2B_HUMAN	PI4K2B	physical	16949365
TFCP2_HUMAN	TFCP2	physical	15857981
SP1_HUMAN	SP1	physical	18419748
CD4_HUMAN	CD4	physical	20530479
MP2K3_HUMAN	MAP2K3	physical	17255949
MP2K6_HUMAN	MAP2K6	physical	17255949
ZNHI1_HUMAN	ZNHIT1	physical	17380123
GDF15_HUMAN	GDF15	physical	18624398
SRSF5_HUMAN	SRSF5	physical	18624398
ZNHI1_HUMAN	ZNHIT1	physical	18624398
CENPC_HUMAN	CENPC	physical	18624398
CSN5_HUMAN	COPS5	physical	18624398
EF1A1_HUMAN	EEF1A1	physical	18624398
EPB42_HUMAN	EPB42	physical	18624398
RL22_HUMAN	RPL22	physical	18624398
RL41_HUMAN	RPL41	physical	18624398
SNAPN_HUMAN	SNAPIN	physical	18624398
IKBA_HUMAN	NFKBIA	physical	20797629
IKKB_HUMAN	IKBKB	physical	20797629
CSK2B_HUMAN	CSNK2B	physical	20797629
FBW1A_HUMAN	BTRC	physical	20797629
NCOA3_HUMAN	NCOA3	physical	15383283
KAT2B_HUMAN	KAT2B	physical	21444723
EP300_HUMAN	EP300	physical	21444723
HDAC3_HUMAN	HDAC3	physical	21444723
ATF2_HUMAN	ATF2	physical	21444723
ATF2_HUMAN	ATF2	physical	16456540
NCOA3_HUMAN	NCOA3	physical	16456540
MK01_HUMAN	MAPK1	physical	21675959
MK03_HUMAN	MAPK3	physical	21675959
PHC2_HUMAN	PHC2	physical	21675959
BMI1_HUMAN	BMI1	physical	21675959
SMRD3_HUMAN	SMARCD3	physical	22068056
TOLIP_HUMAN	TOLLIP	physical	15388348
IRAK1_HUMAN	IRAK1	physical	15388348
AKT1_HUMAN	AKT1	physical	16982329
RB_HUMAN	RB1	physical	20871633
CBL_HUMAN	CBL	physical	19635790
ATF2_HUMAN	ATF2	physical	9162092
SQSTM_HUMAN	SQSTM1	physical	10708586
ATF2_HUMAN	ATF2	physical	10708586
MBP_HUMAN	MBP	physical	10708586
4EBP1_HUMAN	EIF4EBP1	physical	20090955
MBP_HUMAN	MBP	physical	17906618
HTRA2_HUMAN	HTRA2	physical	17906618
SMAD7_HUMAN	SMAD7	physical	17172861
P53_HUMAN	TP53	physical	17172861
SQSTM_HUMAN	SQSTM1	physical	18296712
STAB2_HUMAN	STAB2	physical	18387958
ATF2_HUMAN	ATF2	physical	20213747
P53_HUMAN	TP53	physical	20213747
GORS2_HUMAN	GORASP2	physical	11408587
RHG09_HUMAN	ARHGAP9	physical	17284314
ATF2_HUMAN	ATF2	physical	11839738
TAB1_HUMAN	TAB1	physical	12429732
MBP_HUMAN	MBP	physical	12429732
ATF2_HUMAN	ATF2	physical	9235954
SH21A_HUMAN	SH2D1A	physical	9235954
TISB_HUMAN	ZFP36L1	physical	17030608
TSC1_HUMAN	TSC1	physical	20368287
ATF2_HUMAN	ATF2	physical	12697749
ATF2_HUMAN	ATF2	physical	14499342
LIMK1_HUMAN	LIMK1	physical	16456544
M3K10_HUMAN	MAP3K10	physical	11278395
CREB1_HUMAN	CREB1	physical	23532963
ACTS_HUMAN	ACTA1	physical	14676314
YYAP1_HUMAN	YY1AP1	physical	21988832
PLMN_HUMAN	PLG	physical	21988832
UDB10_HUMAN	UGT2B10	physical	21988832
MAPK2_HUMAN	MAPKAPK2	physical	21988832
CSCL2_HUMAN	TMEM63B	physical	21988832
RRP1B_HUMAN	RRP1B	physical	23602568
EF2_HUMAN	EEF2	physical	23602568
MK14_HUMAN	MAPK14	physical	23602568
MAPK2_HUMAN	MAPKAPK2	physical	23602568
MAPK3_HUMAN	MAPKAPK3	physical	23602568
OBSL1_HUMAN	OBSL1	physical	23602568
MAZ_HUMAN	MAZ	physical	23602568
MKNK1_HUMAN	MKNK1	physical	23602568
NEBU_HUMAN	NEB	physical	23602568
MP2K3_HUMAN	MAP2K3	physical	23602568
CCDC8_HUMAN	CCDC8	physical	23602568
KS6A4_HUMAN	RPS6KA4	physical	23602568
TCAL1_HUMAN	TCEAL1	physical	23602568
IQGA1_HUMAN	IQGAP1	physical	23602568
CNBP_HUMAN	CNBP	physical	23602568
MKNK2_HUMAN	MKNK2	physical	23602568
MRP_HUMAN	MARCKSL1	physical	23602568
UBP11_HUMAN	USP11	physical	23602568
DUS9_HUMAN	DUSP9	physical	23602568
PURA2_HUMAN	ADSS	physical	22863883
CH60_HUMAN	HSPD1	physical	22863883
NDKA_HUMAN	NME1	physical	22863883
SCOT1_HUMAN	OXCT1	physical	22863883
PTN11_HUMAN	PTPN11	physical	22863883
TYSY_HUMAN	TYMS	physical	22863883
WDR1_HUMAN	WDR1	physical	22863883
ATF6A_HUMAN	ATF6	physical	21131360
OBSL1_HUMAN	OBSL1	physical	23455922
MAPK2_HUMAN	MAPKAPK2	physical	23455922
CUL7_HUMAN	CUL7	physical	23455922
MAPK3_HUMAN	MAPKAPK3	physical	23455922
MKNK1_HUMAN	MKNK1	physical	23455922
CCDC8_HUMAN	CCDC8	physical	23455922
MAPK2_HUMAN	MAPKAPK2	physical	10581204
ATF2_HUMAN	ATF2	physical	17170118
SP20H_HUMAN	SUPT20H	physical	19893488
MAPK2_HUMAN	MAPKAPK2	physical	25852190
MAPK3_HUMAN	MAPKAPK3	physical	25852190
KS6A4_HUMAN	RPS6KA4	physical	25852190
JUN_HUMAN	JUN	physical	25483191
SLX4I_HUMAN	SLX4IP	physical	26186194
CUL7_HUMAN	CUL7	physical	26186194
HXB9_HUMAN	HOXB9	physical	26186194
HXB6_HUMAN	HOXB6	physical	26186194
HXA5_HUMAN	HOXA5	physical	26186194
HXA10_HUMAN	HOXA10	physical	26186194
HXC9_HUMAN	HOXC9	physical	26186194
UBP47_HUMAN	USP47	physical	26186194
LRRC1_HUMAN	LRRC1	physical	26186194
EMSA1_HUMAN	ELMSAN1	physical	26186194
FWCH2_HUMAN	FLYWCH2	physical	26186194
RICTR_HUMAN	RICTOR	physical	26186194
RHDF1_HUMAN	RHBDF1	physical	26186194
RECQ4_HUMAN	RECQL4	physical	26186194
IQGA1_HUMAN	IQGAP1	physical	26186194
KIF22_HUMAN	KIF22	physical	26186194
PPIL2_HUMAN	PPIL2	physical	26186194
OBSL1_HUMAN	OBSL1	physical	26186194
MAPK2_HUMAN	MAPKAPK2	physical	26186194
MAPK3_HUMAN	MAPKAPK3	physical	26186194
KS6A4_HUMAN	RPS6KA4	physical	26186194
KS6A5_HUMAN	RPS6KA5	physical	26186194
MKNK2_HUMAN	MKNK2	physical	26186194
MKNK1_HUMAN	MKNK1	physical	26186194
DCNL5_HUMAN	DCUN1D5	physical	26186194
DUS9_HUMAN	DUSP9	physical	26186194
DUS7_HUMAN	DUSP7	physical	26186194
AMERL_HUMAN	AMMECR1L	physical	26186194
CCDC8_HUMAN	CCDC8	physical	26186194
KKCC2_HUMAN	CAMKK2	physical	26186194
MYLK3_HUMAN	MYLK3	physical	26186194
DUS16_HUMAN	DUSP16	physical	26186194
MP2K3_HUMAN	MAP2K3	physical	26186194
FOXK1_HUMAN	FOXK1	physical	26186194
MEF2D_HUMAN	MEF2D	physical	26186194
FBXW8_HUMAN	FBXW8	physical	26186194
AR13B_HUMAN	ARL13B	physical	26186194
CIZ1_HUMAN	CIZ1	physical	26186194
TPX2_HUMAN	TPX2	physical	26186194
TRM1L_HUMAN	TRMT1L	physical	26186194
ERF_HUMAN	ERF	physical	26186194
RN138_HUMAN	RNF138	physical	26186194
KC1G2_HUMAN	CSNK1G2	physical	26186194
GATA3_HUMAN	GATA3	physical	24820417
HDAC1_HUMAN	HDAC1	physical	26344197
PPM1G_HUMAN	PPM1G	physical	26344197
CDT1_HUMAN	CDT1	physical	21930785
MAPK3_HUMAN	MAPKAPK3	physical	26496610
MAPK2_HUMAN	MAPKAPK2	physical	26496610
BCAR1_HUMAN	BCAR1	physical	26496610
DCAF1_HUMAN	VPRBP	physical	26496610
MAPK2_HUMAN	MAPKAPK2	physical	25241761
DUS1_HUMAN	DUSP1	physical	25241761
MKNK2_HUMAN	MKNK2	physical	25241761
TAB1_HUMAN	TAB1	physical	25241761
MAX_HUMAN	MAX	physical	25241761
MAPK3_HUMAN	MAPKAPK3	physical	25241761
EPS15_HUMAN	EPS15	physical	24269888
ATF2_HUMAN	ATF2	physical	26391660
TAB1_HUMAN	TAB1	physical	26391660
TAB2_HUMAN	TAB2	physical	26391660
ATF2_HUMAN	ATF2	physical	18695677
MK14_HUMAN	MAPK14	physical	18695677
ATF2_HUMAN	ATF2	physical	16998585
MBP_HUMAN	MBP	physical	10978313
ATF2_HUMAN	ATF2	physical	10978313
ATF2_HUMAN	ATF2	physical	9753474
ATF2_HUMAN	ATF2	physical	26987986
P53_HUMAN	TP53	physical	15642743
ATF2_HUMAN	ATF2	physical	25098452
S10A9_HUMAN	S100A9	physical	15331440
MAPK3_HUMAN	MAPKAPK3	physical	15331440
MAPK3_HUMAN	MAPKAPK3	physical	28514442
MKNK1_HUMAN	MKNK1	physical	28514442
MAPK2_HUMAN	MAPKAPK2	physical	28514442
DUS9_HUMAN	DUSP9	physical	28514442
KS6A4_HUMAN	RPS6KA4	physical	28514442
HXC9_HUMAN	HOXC9	physical	28514442
KS6A5_HUMAN	RPS6KA5	physical	28514442
MP2K3_HUMAN	MAP2K3	physical	28514442
DUS7_HUMAN	DUSP7	physical	28514442
CUL7_HUMAN	CUL7	physical	28514442
RHDF1_HUMAN	RHBDF1	physical	28514442
EMSA1_HUMAN	ELMSAN1	physical	28514442
FBXW8_HUMAN	FBXW8	physical	28514442
SLX4I_HUMAN	SLX4IP	physical	28514442
KKCC2_HUMAN	CAMKK2	physical	28514442
AMERL_HUMAN	AMMECR1L	physical	28514442
KIF22_HUMAN	KIF22	physical	28514442
HXB9_HUMAN	HOXB9	physical	28514442
MYLK3_HUMAN	MYLK3	physical	28514442
TPX2_HUMAN	TPX2	physical	28514442
OBSL1_HUMAN	OBSL1	physical	28514442
DUS16_HUMAN	DUSP16	physical	28514442
MKNK2_HUMAN	MKNK2	physical	28514442
HXB6_HUMAN	HOXB6	physical	28514442
MEF2D_HUMAN	MEF2D	physical	28514442
CCDC8_HUMAN	CCDC8	physical	28514442
DCNL5_HUMAN	DCUN1D5	physical	28514442
PPIL2_HUMAN	PPIL2	physical	28514442
HXA10_HUMAN	HOXA10	physical	28514442
LRRC1_HUMAN	LRRC1	physical	28514442
RN138_HUMAN	RNF138	physical	28514442
IQGA1_HUMAN	IQGAP1	physical	28514442
AR13B_HUMAN	ARL13B	physical	28514442
RECQ4_HUMAN	RECQL4	physical	28514442
FWCH2_HUMAN	FLYWCH2	physical	28514442
ERF_HUMAN	ERF	physical	28514442
CIZ1_HUMAN	CIZ1	physical	28514442
TRM1L_HUMAN	TRMT1L	physical	28514442
ALR_HUMAN	GFER	physical	28514442
RICTR_HUMAN	RICTOR	physical	28514442
KC1G2_HUMAN	CSNK1G2	physical	28514442
UBP47_HUMAN	USP47	physical	28514442
MK08_HUMAN	MAPK8	physical	18586681
MK01_HUMAN	MAPK1	physical	18586681
PAK1_HUMAN	PAK1	physical	18586681
PAK2_HUMAN	PAK2	physical	18586681
PAK3_HUMAN	PAK3	physical	18586681
B2CL1_HUMAN	BCL2L1	physical	22617334
ATF2_HUMAN	ATF2	physical	9596579
DUS9_HUMAN	DUSP9	physical	9596579
ATF2_HUMAN	ATF2	physical	12118074
HSPB1_HUMAN	HSPB1	physical	10908726
CDN1A_HUMAN	CDKN1A	physical	12058028
CASP3_HUMAN	CASP3	physical	14970175
CASP8_HUMAN	CASP8	physical	14970175

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 MK14_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Acetylation of a conserved lysine residue in the ATP binding pocketof p38 augments its kinase activity during hypertrophy ofcardiomyocytes."; Pillai V.B., Sundaresan N.R., Samant S.A., Wolfgeher D., Trivedi C.M.,Gupta M.P.; Mol. Cell. Biol. 31:2349-2363(2011). Cited for: ACETYLATION AT LYS-53 AND LYS-152 BY KAT2B/PCAF AND EP300, ANDDEACETYLATION BY HDAC3.	21444723 [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 SER-2; THR-180 AND TYR-182,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-2; THR-16; THR-180 ANDTYR-182, AND MASS SPECTROMETRY.	18691976 [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 THR-180 AND TYR-182, ANDMASS SPECTROMETRY.	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 THR-180 AND TYR-182, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-263, AND MASSSPECTROMETRY.	17525332 [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-180 AND TYR-182, ANDMASS SPECTROMETRY.	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-180 AND TYR-182, ANDMASS SPECTROMETRY.	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 THR-180 AND TYR-182, ANDMASS SPECTROMETRY.	16083285 [Abstract]
"Pro-inflammatory cytokines and environmental stress cause p38mitogen-activated protein kinase activation by dual phosphorylation ontyrosine and threonine."; Raingeaud J., Gupta S., Rogers J.S., Dickens M., Han J.,Ulevitch R.J., Davis R.J.; J. Biol. Chem. 270:7420-7426(1995). Cited for: PHOSPHORYLATION AT THR-180 AND TYR-182, ENZYME REGULATION, ANDSUBCELLULAR LOCATION.	7535770 [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-182, AND MASSSPECTROMETRY.	19534553 [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 TYR-182, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks."; Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.; Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-182, AND MASSSPECTROMETRY.	17389395 [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-182, AND MASSSPECTROMETRY.	18083107 [Abstract]
"Alternative p38 activation pathway mediated by T cell receptor-proximal tyrosine kinases."; Salvador J.M., Mittelstadt P.R., Guszczynski T., Copeland T.D.,Yamaguchi H., Appella E., Fornace A.J. Jr., Ashwell J.D.; Nat. Immunol. 6:390-395(2005). Cited for: PHOSPHORYLATION AT TYR-323, AND ENZYME REGULATION.	15735648 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-182, AND MASSSPECTROMETRY.	15592455 [Abstract]

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