dbPTM

IF4A3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IF4A3_HUMAN
UniProt AC	P38919
Protein Name	Eukaryotic initiation factor 4A-III
Gene Name	EIF4A3
Organism	Homo sapiens (Human).
Sequence Length	411
Subcellular Localization	Nucleus . Nucleus speckle . Cytoplasm . Nucleocytoplasmic shuttling protein. Travels to the cytoplasm as part of the exon junction complex (EJC) bound to mRNA. Detected in dendritic layer as well as the nuclear and cytoplasmic (somatic) compartments
Protein Description	ATP-dependent RNA helicase. [PubMed: 16170325 Involved in pre-mRNA splicing as component of the spliceosome]
Protein Sequence	MATTATMATSGSARKRLLKEEDMTKVEFETSEEVDVTPTFDTMGLREDLLRGIYAYGFEKPSAIQQRAIKQIIKGRDVIAQSQSGTGKTATFSISVLQCLDIQVRETQALILAPTRELAVQIQKGLLALGDYMNVQCHACIGGTNVGEDIRKLDYGQHVVAGTPGRVFDMIRRRSLRTRAIKMLVLDEADEMLNKGFKEQIYDVYRYLPPATQVVLISATLPHEILEMTNKFMTDPIRILVKRDELTLEGIKQFFVAVEREEWKFDTLCDLYDTLTITQAVIFCNTKRKVDWLTEKMREANFTVSSMHGDMPQKERESIMKEFRSGASRVLISTDVWARGLDVPQVSLIINYDLPNNRELYIHRIGRSGRYGRKGVAINFVKNDDIRILRDIEQYYSTQIDEMPMNVADLI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MATTATMA -------CCCCHHHC	7.25	21406692
2	Acetylation	------MATTATMAT ------CCCCHHHCC	17.41	20068231
3	Phosphorylation	-----MATTATMATS -----CCCCHHHCCC	18.70	21955146
4	Phosphorylation	----MATTATMATSG ----CCCCHHHCCCH	15.59	25159151
6	Phosphorylation	--MATTATMATSGSA --CCCCHHHCCCHHH	12.78	25159151
9	Phosphorylation	ATTATMATSGSARKR CCCHHHCCCHHHHHH	23.85	29255136
10	Phosphorylation	TTATMATSGSARKRL CCHHHCCCHHHHHHH	22.63	29255136
12	Phosphorylation	ATMATSGSARKRLLK HHHCCCHHHHHHHHC	25.35	29255136
14	Methylation	MATSGSARKRLLKEE HCCCHHHHHHHHCHH	26.73	-
19	Acetylation	SARKRLLKEEDMTKV HHHHHHHCHHHCCCE	64.74	25953088
19	2-Hydroxyisobutyrylation	SARKRLLKEEDMTKV HHHHHHHCHHHCCCE	64.74	-
19	Ubiquitination	SARKRLLKEEDMTKV HHHHHHHCHHHCCCE	64.74	-
19	Sumoylation	SARKRLLKEEDMTKV HHHHHHHCHHHCCCE	64.74	28112733
19	Sumoylation	SARKRLLKEEDMTKV HHHHHHHCHHHCCCE	64.74	-
31	Phosphorylation	TKVEFETSEEVDVTP CCEEEECCCCEECCC	25.27	-
54	Phosphorylation	EDLLRGIYAYGFEKP HHHHHHHHHHCCCCC	9.15	28152594
56	Phosphorylation	LLRGIYAYGFEKPSA HHHHHHHHCCCCCHH	12.84	28152594
60	Sumoylation	IYAYGFEKPSAIQQR HHHHCCCCCHHHHHH	41.85	-
60	2-Hydroxyisobutyrylation	IYAYGFEKPSAIQQR HHHHCCCCCHHHHHH	41.85	-
60	Acetylation	IYAYGFEKPSAIQQR HHHHCCCCCHHHHHH	41.85	23954790
60	Malonylation	IYAYGFEKPSAIQQR HHHHCCCCCHHHHHH	41.85	26320211
60	Ubiquitination	IYAYGFEKPSAIQQR HHHHCCCCCHHHHHH	41.85	21890473
60	Sumoylation	IYAYGFEKPSAIQQR HHHHCCCCCHHHHHH	41.85	-
60	Methylation	IYAYGFEKPSAIQQR HHHHCCCCCHHHHHH	41.85	-
62	Phosphorylation	AYGFEKPSAIQQRAI HHCCCCCHHHHHHHH	49.42	28152594
70	Acetylation	AIQQRAIKQIIKGRD HHHHHHHHHHHCCCC	34.16	25953088
70	2-Hydroxyisobutyrylation	AIQQRAIKQIIKGRD HHHHHHHHHHHCCCC	34.16	-
70	Methylation	AIQQRAIKQIIKGRD HHHHHHHHHHHCCCC	34.16	23748837
70	Ubiquitination	AIQQRAIKQIIKGRD HHHHHHHHHHHCCCC	34.16	-
82	Phosphorylation	GRDVIAQSQSGTGKT CCCEEEECCCCCCCE	19.79	27282143
84	Phosphorylation	DVIAQSQSGTGKTAT CEEEECCCCCCCEEE	43.50	25159151
86	Phosphorylation	IAQSQSGTGKTATFS EEECCCCCCCEEEEE	40.53	27732954
124	Acetylation	ELAVQIQKGLLALGD HHHHHHHHHHHHHCC	53.83	-
132	Phosphorylation	GLLALGDYMNVQCHA HHHHHCCCCCCEECE	6.70	-
152	2-Hydroxyisobutyrylation	NVGEDIRKLDYGQHV CCCHHHHHCCCCCEE	46.15	-
152	Acetylation	NVGEDIRKLDYGQHV CCCHHHHHCCCCCEE	46.15	26051181
152	Malonylation	NVGEDIRKLDYGQHV CCCHHHHHCCCCCEE	46.15	26320211
152	Ubiquitination	NVGEDIRKLDYGQHV CCCHHHHHCCCCCEE	46.15	-
155	Phosphorylation	EDIRKLDYGQHVVAG HHHHHCCCCCEEECC	29.17	27273156
163	Phosphorylation	GQHVVAGTPGRVFDM CCEEECCCCCHHHHH	16.91	22167270
182	2-Hydroxyisobutyrylation	SLRTRAIKMLVLDEA HHHHHHHHHHHCHHH	25.79	-
182	Ubiquitination	SLRTRAIKMLVLDEA HHHHHHHHHHHCHHH	25.79	21906983
182	Acetylation	SLRTRAIKMLVLDEA HHHHHHHHHHHCHHH	25.79	25953088
195	Ubiquitination	EADEMLNKGFKEQIY HHHHHHHHHHHHHHH	62.86	21906983
195	2-Hydroxyisobutyrylation	EADEMLNKGFKEQIY HHHHHHHHHHHHHHH	62.86	-
195	Acetylation	EADEMLNKGFKEQIY HHHHHHHHHHHHHHH	62.86	25953088
198	Ubiquitination	EMLNKGFKEQIYDVY HHHHHHHHHHHHHHH	58.33	21890473
198	Acetylation	EMLNKGFKEQIYDVY HHHHHHHHHHHHHHH	58.33	25825284
198	Malonylation	EMLNKGFKEQIYDVY HHHHHHHHHHHHHHH	58.33	26320211
202	Phosphorylation	KGFKEQIYDVYRYLP HHHHHHHHHHHHHCC	10.07	27273156
205	Phosphorylation	KEQIYDVYRYLPPAT HHHHHHHHHHCCCCC	7.22	28152594
218	Phosphorylation	ATQVVLISATLPHEI CCEEEEEECCCCHHH	15.84	-
242	Acetylation	DPIRILVKRDELTLE CCEEEEECCCCCCHH	51.16	26051181
247	Phosphorylation	LVKRDELTLEGIKQF EECCCCCCHHHHHHH	22.25	-
264	Ubiquitination	AVEREEWKFDTLCDL EEECCCCCHHHHHHH	36.32	-
276	O-linked_Glycosylation	CDLYDTLTITQAVIF HHHHHHEEEEEEHHH	24.87	32119511
278	O-linked_Glycosylation	LYDTLTITQAVIFCN HHHHEEEEEEHHHCC	12.77	32119511
287	Ubiquitination	AVIFCNTKRKVDWLT EHHHCCCCCCHHHHH	35.91	-
289	Malonylation	IFCNTKRKVDWLTEK HHCCCCCCHHHHHHH	46.21	26320211
289	Acetylation	IFCNTKRKVDWLTEK HHCCCCCCHHHHHHH	46.21	27452117
289	2-Hydroxyisobutyrylation	IFCNTKRKVDWLTEK HHCCCCCCHHHHHHH	46.21	-
289	Ubiquitination	IFCNTKRKVDWLTEK HHCCCCCCHHHHHHH	46.21	-
296	Acetylation	KVDWLTEKMREANFT CHHHHHHHHHHCCCE	37.71	19608861
296	2-Hydroxyisobutyrylation	KVDWLTEKMREANFT CHHHHHHHHHHCCCE	37.71	-
296	Ubiquitination	KVDWLTEKMREANFT CHHHHHHHHHHCCCE	37.71	19608861
303	Phosphorylation	KMREANFTVSSMHGD HHHHCCCEEEECCCC	21.20	28509920
306	Phosphorylation	EANFTVSSMHGDMPQ HCCCEEEECCCCCCH	15.51	28509920
314	2-Hydroxyisobutyrylation	MHGDMPQKERESIMK CCCCCCHHHHHHHHH	53.52	-
314	Sumoylation	MHGDMPQKERESIMK CCCCCCHHHHHHHHH	53.52	28112733
314	Acetylation	MHGDMPQKERESIMK CCCCCCHHHHHHHHH	53.52	25953088
314	Ubiquitination	MHGDMPQKERESIMK CCCCCCHHHHHHHHH	53.52	21906983
321	Ubiquitination	KERESIMKEFRSGAS HHHHHHHHHHHHCCC	52.62	21906983
321	Acetylation	KERESIMKEFRSGAS HHHHHHHHHHHHCCC	52.62	19608861
321	2-Hydroxyisobutyrylation	KERESIMKEFRSGAS HHHHHHHHHHHHCCC	52.62	-
333	Phosphorylation	GASRVLISTDVWARG CCCEEEEECCHHHCC	17.88	29978859
334	Phosphorylation	ASRVLISTDVWARGL CCEEEEECCHHHCCC	27.81	29978859
347	Phosphorylation	GLDVPQVSLIINYDL CCCCCEEEEEEEEEC	14.49	29978859
352	Phosphorylation	QVSLIINYDLPNNRE EEEEEEEEECCCCCE	14.40	29978859
374	Ubiquitination	RSGRYGRKGVAINFV CCCCCCCCCEEEEEE	54.06	21906983
374	Methylation	RSGRYGRKGVAINFV CCCCCCCCCEEEEEE	54.06	23748837
374	Acetylation	RSGRYGRKGVAINFV CCCCCCCCCEEEEEE	54.06	26051181
382	Ubiquitination	GVAINFVKNDDIRIL CEEEEEECCCCCCHH	50.99	21890473
382	Acetylation	GVAINFVKNDDIRIL CEEEEEECCCCCCHH	50.99	23749302
382	2-Hydroxyisobutyrylation	GVAINFVKNDDIRIL CEEEEEECCCCCCHH	50.99	-
382	Succinylation	GVAINFVKNDDIRIL CEEEEEECCCCCCHH	50.99	23954790
382	Sumoylation	GVAINFVKNDDIRIL CEEEEEECCCCCCHH	50.99	28112733

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
163	T	Phosphorylation	Kinase	CDK1	P06493	PSP
163	T	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IF4A3_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 IF4A3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CC174_HUMAN	CCDC174	physical	16189514
NXF1_HUMAN	NXF1	physical	14730019
STF1_HUMAN	NR5A1	physical	17190602
SMAD4_HUMAN	SMAD4	physical	17190602
RNPS1_HUMAN	RNPS1	physical	22939629
SRRM2_HUMAN	SRRM2	physical	22939629
ILF2_HUMAN	ILF2	physical	22939629
RL37A_HUMAN	RPL37A	physical	22939629
RL31_HUMAN	RPL31	physical	22939629
PRP6_HUMAN	PRPF6	physical	22939629
RU2B_HUMAN	SNRPB2	physical	22939629
SRSF5_HUMAN	SRSF5	physical	22939629
SNUT1_HUMAN	SART1	physical	22939629
SRSF1_HUMAN	SRSF1	physical	22939629
PRPF3_HUMAN	PRPF3	physical	22939629
SRSF3_HUMAN	SRSF3	physical	22939629
PR40A_HUMAN	PRPF40A	physical	22939629
RS11_HUMAN	RPS11	physical	22939629
WDR18_HUMAN	WDR18	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
SRP19_HUMAN	SRP19	physical	22939629
S10A9_HUMAN	S100A9	physical	22939629
WIPF2_HUMAN	WIPF2	physical	22939629
SMCA5_HUMAN	SMARCA5	physical	22939629
NUP62_HUMAN	NUP62	physical	22939629
SNF5_HUMAN	SMARCB1	physical	22939629
SRS10_HUMAN	SRSF10	physical	22939629
ROA0_HUMAN	HNRNPA0	physical	22939629
LBR_HUMAN	LBR	physical	22939629
MIRO2_HUMAN	RHOT2	physical	22939629
PSIP1_HUMAN	PSIP1	physical	22939629
HBB_HUMAN	HBB	physical	21145460
MGN_HUMAN	MAGOH	physical	23084401
IF4A3_HUMAN	EIF4A3	physical	23084401
RBM8A_HUMAN	RBM8A	physical	23084401
CASC3_HUMAN	CASC3	physical	23084401
ACINU_HUMAN	ACIN1	physical	23084401
PININ_HUMAN	PNN	physical	23084401
RNPS1_HUMAN	RNPS1	physical	23084401
SAP18_HUMAN	SAP18	physical	23084401
THOC4_HUMAN	ALYREF	physical	23084401
UIF_HUMAN	FYTTD1	physical	23084401
SRS10_HUMAN	SRSF10	physical	23084401
SRSF5_HUMAN	SRSF5	physical	23084401
SRSF1_HUMAN	SRSF1	physical	23084401
SRSF2_HUMAN	SRSF2	physical	23084401
SRSF3_HUMAN	SRSF3	physical	23084401
SRSF4_HUMAN	SRSF4	physical	23084401
SRSF6_HUMAN	SRSF6	physical	23084401
SRSF7_HUMAN	SRSF7	physical	23084401
SRSF9_HUMAN	SRSF9	physical	23084401
SON_HUMAN	SON	physical	23084401
TRA2A_HUMAN	TRA2A	physical	23084401
TRA2B_HUMAN	TRA2B	physical	23084401
SRRM1_HUMAN	SRRM1	physical	23084401
SRRM2_HUMAN	SRRM2	physical	23084401
TR150_HUMAN	THRAP3	physical	23084401
FMR1_HUMAN	FMR1	physical	23084401
ILF3_HUMAN	ILF3	physical	23084401
ILF2_HUMAN	ILF2	physical	23084401
MATR3_HUMAN	MATR3	physical	23084401
HNRPC_HUMAN	HNRNPC	physical	23084401
CCDC9_HUMAN	CCDC9	physical	23084401
TSN_HUMAN	TSN	physical	23084401
ERH_HUMAN	ERH	physical	23084401
PGAM5_HUMAN	PGAM5	physical	23084401
RU17_HUMAN	SNRNP70	physical	23084401
SF3A1_HUMAN	SF3A1	physical	23084401
SF3B1_HUMAN	SF3B1	physical	23084401
SF3B2_HUMAN	SF3B2	physical	23084401
SF3B3_HUMAN	SF3B3	physical	23084401
PRP8_HUMAN	PRPF8	physical	23084401
SNR40_HUMAN	SNRNP40	physical	23084401
U520_HUMAN	SNRNP200	physical	23084401
U5S1_HUMAN	EFTUD2	physical	23084401
CDC5L_HUMAN	CDC5L	physical	23084401
CRNL1_HUMAN	CRNKL1	physical	23084401
PLRG1_HUMAN	PLRG1	physical	23084401
PPIE_HUMAN	PPIE	physical	23084401
PRP19_HUMAN	PRPF19	physical	23084401
SPF27_HUMAN	BCAS2	physical	23084401
SYF1_HUMAN	XAB2	physical	23084401
RBM22_HUMAN	RBM22	physical	23084401
SNW1_HUMAN	SNW1	physical	23084401
AQR_HUMAN	AQR	physical	23084401
CWC15_HUMAN	CWC15	physical	23084401
DHX15_HUMAN	DHX15	physical	23084401
PRP17_HUMAN	CDC40	physical	23084401
ACTB_HUMAN	ACTB	physical	23084401
ACTC_HUMAN	ACTC1	physical	23084401
CAPZB_HUMAN	CAPZB	physical	23084401
CAZA1_HUMAN	CAPZA1	physical	23084401
E41L3_HUMAN	EPB41L3	physical	23084401
K1C10_HUMAN	KRT10	physical	23084401
K1C14_HUMAN	KRT14	physical	23084401
K1C16_HUMAN	KRT16	physical	23084401
K1C19_HUMAN	KRT19	physical	23084401
K1C9_HUMAN	KRT9	physical	23084401
K22E_HUMAN	KRT2	physical	23084401
K2C1_HUMAN	KRT1	physical	23084401
K2C5_HUMAN	KRT5	physical	23084401
K2C6B_HUMAN	KRT6B	physical	23084401
K2C71_HUMAN	KRT71	physical	23084401
K2C75_HUMAN	KRT75	physical	23084401
MAP1B_HUMAN	MAP1B	physical	23084401
SPI2A_HUMAN	SPIN2A	physical	23084401
SPIN1_HUMAN	SPIN1	physical	23084401
SPTN1_HUMAN	SPTAN1	physical	23084401
SPTB2_HUMAN	SPTBN1	physical	23084401
VIME_HUMAN	VIM	physical	23084401
MYH10_HUMAN	MYH10	physical	23084401
MYH9_HUMAN	MYH9	physical	23084401
POTEJ_HUMAN	POTEJ	physical	23084401
H2A1A_HUMAN	HIST1H2AA	physical	23084401
H2A1D_HUMAN	HIST1H2AD	physical	23084401
H31T_HUMAN	HIST3H3	physical	23084401
HNRH2_HUMAN	HNRNPH2	physical	23084401
HNRPF_HUMAN	HNRNPF	physical	23084401
RBMX_HUMAN	RBMX	physical	23084401
HNRPK_HUMAN	HNRNPK	physical	23084401
HNRPL_HUMAN	HNRNPL	physical	23084401
HNRPM_HUMAN	HNRNPM	physical	23084401
HNRPU_HUMAN	HNRNPU	physical	23084401
HNRH1_HUMAN	HNRNPH1	physical	23084401
ANM1_HUMAN	PRMT1	physical	23084401
CHTOP_HUMAN	CHTOP	physical	23084401
ANM5_HUMAN	PRMT5	physical	23084401
ICLN_HUMAN	CLNS1A	physical	23084401
MEP50_HUMAN	WDR77	physical	23084401
ADT2_HUMAN	SLC25A5	physical	23084401
BLM_HUMAN	BLM	physical	23084401
BOLA2_HUMAN	BOLA2	physical	23084401
DOCK4_HUMAN	DOCK4	physical	23084401
F263_HUMAN	PFKFB3	physical	23084401
FAS_HUMAN	FASN	physical	23084401
GRP75_HUMAN	HSPA9	physical	23084401
HSP7C_HUMAN	HSPA8	physical	23084401
JAK1_HUMAN	JAK1	physical	23084401
MOB2_HUMAN	MOB2	physical	23084401
PPM1B_HUMAN	PPM1B	physical	23084401
PRDX1_HUMAN	PRDX1	physical	23084401
RAN_HUMAN	RAN	physical	23084401
REST_HUMAN	REST	physical	23084401
RIOK1_HUMAN	RIOK1	physical	23084401
ST38L_HUMAN	STK38L	physical	23084401
STK38_HUMAN	STK38	physical	23084401
DDX17_HUMAN	DDX17	physical	23084401
YBOX1_HUMAN	YBX1	physical	23084401
ZC3HD_HUMAN	ZC3H13	physical	23084401
DDX3X_HUMAN	DDX3X	physical	23084401
FBRL_HUMAN	FBL	physical	23084401
YBOX3_HUMAN	YBX3	physical	23084401
RL4_HUMAN	RPL4	physical	23084401
RL10_HUMAN	RPL10	physical	23084401
RL13_HUMAN	RPL13	physical	23084401
RL13A_HUMAN	RPL13A	physical	23084401
RL15_HUMAN	RPL15	physical	23084401
RL17_HUMAN	RPL17	physical	23084401
RL18_HUMAN	RPL18	physical	23084401
RL19_HUMAN	RPL19	physical	23084401
RL21_HUMAN	RPL21	physical	23084401
RL24_HUMAN	RPL24	physical	23084401
RL26_HUMAN	RPL26	physical	23084401
RL27A_HUMAN	RPL27A	physical	23084401
RL28_HUMAN	RPL28	physical	23084401
RL3_HUMAN	RPL3	physical	23084401
RL6_HUMAN	RPL6	physical	23084401
RL7_HUMAN	RPL7	physical	23084401
RL7A_HUMAN	RPL7A	physical	23084401
RL8_HUMAN	RPL8	physical	23084401
RS6_HUMAN	RPS6	physical	23084401
RS8_HUMAN	RPS8	physical	23084401
RS11_HUMAN	RPS11	physical	23084401
RS2_HUMAN	RPS2	physical	23084401
RS24_HUMAN	RPS24	physical	23084401
RS9_HUMAN	RPS9	physical	23084401
RSMB_HUMAN	SNRPB	physical	23084401
SMD1_HUMAN	SNRPD1	physical	23084401
SMD2_HUMAN	SNRPD2	physical	23084401
SMD3_HUMAN	SNRPD3	physical	23084401
RBM10_HUMAN	RBM10	physical	23084401
SCYL2_HUMAN	SCYL2	physical	23084401
YTDC1_HUMAN	YTHDC1	physical	23084401
EF1A1_HUMAN	EEF1A1	physical	23084401
IF4B_HUMAN	EIF4B	physical	23084401
REN3B_HUMAN	UPF3B	physical	23084401
PDIP3_HUMAN	POLDIP3	physical	23084401
CWC22_HUMAN	CWC22	physical	22365833
RD23B_HUMAN	RAD23B	physical	22863883
PDCD4_HUMAN	PDCD4	physical	25416956
CDA7L_HUMAN	CDCA7L	physical	25416956
CWC22_HUMAN	CWC22	physical	22961380
PRP19_HUMAN	PRPF19	physical	22961380
CASC3_HUMAN	CASC3	physical	22961380
RBM8A_HUMAN	RBM8A	physical	22961380
MGN_HUMAN	MAGOH	physical	22961380
KCRM_HUMAN	CKM	physical	26344197
PP6R3_HUMAN	PPP6R3	physical	26344197
RRS1_HUMAN	RRS1	physical	26344197
STK25_HUMAN	STK25	physical	26344197
TIPRL_HUMAN	TIPRL	physical	26344197
LZTR1_HUMAN	LZTR1	physical	28514442
CASC3_HUMAN	CASC3	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
268305	Richieri-Costa-Pereira syndrome (RCPS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of IF4A3_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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-10 AND SER-12, 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-60; LYS-296 AND LYS-321, ANDMASS SPECTROMETRY.	19608861 [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-12, 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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-10 AND SER-12, AND MASS SPECTROMETRY.	19413330 [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-12, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASSSPECTROMETRY.	19007248 [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-163, AND MASSSPECTROMETRY.	18669648 [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 THR-163, AND MASSSPECTROMETRY.	18220336 [Abstract]