dbPTM

FOXK2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	FOXK2_HUMAN
UniProt AC	Q01167
Protein Name	Forkhead box protein K2
Gene Name	FOXK2
Organism	Homo sapiens (Human).
Sequence Length	660
Subcellular Localization	Nucleus .
Protein Description	Transcriptional regulator that recognizes the core sequence 5'-TAAACA-3'. Binds to NFAT-like motifs (purine-rich) in the IL2 promoter. [PubMed: 1339390 Positively regulates WNT/beta-catenin signaling by translocating DVL proteins into the nucleus]
Protein Sequence	MAAAAAALSGAGTPPAGGGAGGGGAGGGGSPPGGWAVARLEGREFEYLMKKRSVTIGRNSSQGSVDVSMGHSSFISRRHLEIFTPPGGGGHGGAAPELPPAQPRPDAGGDFYLRCLGKNGVFVDGVFQRRGAPPLQLPRVCTFRFPSTNIKITFTALSSEKREKQEASESPVKAVQPHISPLTINIPDTMAHLISPLPSPTGTISAANSCPSSPRGAGSSGYKVGRVMPSDLNLMADNSQPENEKEASGGDSPKDDSKPPYSYAQLIVQAITMAPDKQLTLNGIYTHITKNYPYYRTADKGWQNSIRHNLSLNRYFIKVPRSQEEPGKGSFWRIDPASESKLIEQAFRKRRPRGVPCFRTPLGPLSSRSAPASPNHAGVLSAHSSGAQTPESLSREGSPAPLEPEPGAAQPKLAVIQEARFAQSAPGSPLSSQPVLITVQRQLPQAIKPVTYTVATPVTTSTSQPPVVQTVHVVHQIPAVSVTSVAGLAPANTYTVSGQAVVTPAAVLAPPKAEAQENGDHREVKVKVEPIPAIGHATLGTASRIIQTAQTTPVQTVTIVQQAPLGQHQLPIKTVTQNGTHVASVPTAVHGQVNNAAASPLHMLATHASASASLPTKRHNGDQPEQPELKRIKTEDGEGIVIALSVDTPPAAVREKGVQN

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAAAAALS ------CHHHHHHHH	13.05	20068231
9	Phosphorylation	AAAAAALSGAGTPPA HHHHHHHHCCCCCCC	23.13	28348404
13 (in isoform 1)	Phosphorylation	-	26.09	-
13	Phosphorylation	AALSGAGTPPAGGGA HHHHCCCCCCCCCCC	26.09	25159151
13 (in isoform 3)	Phosphorylation	-	26.09	-
30 (in isoform 1)	Phosphorylation	-	31.06	-
30	Phosphorylation	GGAGGGGSPPGGWAV CCCCCCCCCCCCEEE	31.06	28355574
30 (in isoform 3)	Phosphorylation	-	31.06	-
55	Phosphorylation	LMKKRSVTIGRNSSQ HEECCEEEECCCCCC	20.96	24719451
60	Phosphorylation	SVTIGRNSSQGSVDV EEEECCCCCCCEEEE	23.76	27273156
61 (in isoform 1)	Phosphorylation	-	41.95	-
61	Phosphorylation	VTIGRNSSQGSVDVS EEECCCCCCCEEEEE	41.95	17525332
61 (in isoform 3)	Phosphorylation	-	41.95	-
64	Phosphorylation	GRNSSQGSVDVSMGH CCCCCCCEEEEECCC	13.91	24732914
68	Phosphorylation	SQGSVDVSMGHSSFI CCCEEEEECCCCCCC	18.00	27273156
72	Phosphorylation	VDVSMGHSSFISRRH EEEECCCCCCCCCCE	22.63	24732914
73	Phosphorylation	DVSMGHSSFISRRHL EEECCCCCCCCCCEE	22.41	24732914
76	Phosphorylation	MGHSSFISRRHLEIF CCCCCCCCCCEEEEE	22.66	24719451
118	Ubiquitination	FYLRCLGKNGVFVDG EEEEEEECCCEEECC	37.26	-
130	Methylation	VDGVFQRRGAPPLQL ECCCCCCCCCCCCCC	34.54	-
144	Methylation	LPRVCTFRFPSTNIK CCCEEEEECCCCCEE	25.14	24129315
155	O-linked_Glycosylation	TNIKITFTALSSEKR CCEEEEEEEECHHHH	20.31	30059200
158	O-linked_Glycosylation	KITFTALSSEKREKQ EEEEEEECHHHHHHH	33.71	30059200
158	Phosphorylation	KITFTALSSEKREKQ EEEEEEECHHHHHHH	33.71	26074081
159	O-linked_Glycosylation	ITFTALSSEKREKQE EEEEEECHHHHHHHH	48.24	30059200
159	Phosphorylation	ITFTALSSEKREKQE EEEEEECHHHHHHHH	48.24	26074081
161	Sumoylation	FTALSSEKREKQEAS EEEECHHHHHHHHHC	68.74	-
161	Sumoylation	FTALSSEKREKQEAS EEEECHHHHHHHHHC	68.74	28112733
161	Ubiquitination	FTALSSEKREKQEAS EEEECHHHHHHHHHC	68.74	33845483
164	Sumoylation	LSSEKREKQEASESP ECHHHHHHHHHCCCC	58.43	28112733
168	Phosphorylation	KREKQEASESPVKAV HHHHHHHCCCCCCCC	37.54	30266825
170 (in isoform 1)	Phosphorylation	-	32.28	-
170	Phosphorylation	EKQEASESPVKAVQP HHHHHCCCCCCCCCC	32.28	23401153
170 (in isoform 3)	Phosphorylation	-	32.28	-
180 (in isoform 1)	Phosphorylation	-	15.72	-
180	Phosphorylation	KAVQPHISPLTINIP CCCCCCCCCEEECCC	15.72	20068231
180 (in isoform 3)	Phosphorylation	-	15.72	-
183 (in isoform 1)	Phosphorylation	-	18.50	-
183	Phosphorylation	QPHISPLTINIPDTM CCCCCCEEECCCCHH	18.50	20068231
183 (in isoform 3)	Phosphorylation	-	18.50	-
189	Phosphorylation	LTINIPDTMAHLISP EEECCCCHHHHHHCC	15.76	30108239
195	Phosphorylation	DTMAHLISPLPSPTG CHHHHHHCCCCCCCC	27.09	25159151
199	Phosphorylation	HLISPLPSPTGTISA HHHCCCCCCCCCEEE	42.66	25159151
201 (in isoform 1)	Phosphorylation	-	51.82	-
201	Phosphorylation	ISPLPSPTGTISAAN HCCCCCCCCCEEECC	51.82	30108239
201 (in isoform 3)	Phosphorylation	-	51.82	-
203	Phosphorylation	PLPSPTGTISAANSC CCCCCCCCEEECCCC	17.78	30108239
205 (in isoform 1)	Phosphorylation	-	22.59	-
205	Phosphorylation	PSPTGTISAANSCPS CCCCCCEEECCCCCC	22.59	30108239
205 (in isoform 3)	Phosphorylation	-	22.59	-
209 (in isoform 1)	Phosphorylation	-	23.76	-
209	Phosphorylation	GTISAANSCPSSPRG CCEEECCCCCCCCCC	23.76	30108239
209 (in isoform 3)	Phosphorylation	-	23.76	-
212	Phosphorylation	SAANSCPSSPRGAGS EECCCCCCCCCCCCC	58.25	30108239
213	Phosphorylation	AANSCPSSPRGAGSS ECCCCCCCCCCCCCC	12.08	25159151
219	Phosphorylation	SSPRGAGSSGYKVGR CCCCCCCCCCCEEEC	21.76	26074081
220	Phosphorylation	SPRGAGSSGYKVGRV CCCCCCCCCCEEECC	45.27	26074081
222 (in isoform 1)	Phosphorylation	-	12.40	-
222	Phosphorylation	RGAGSSGYKVGRVMP CCCCCCCCEEECCCH	12.40	26074081
222 (in isoform 3)	Phosphorylation	-	12.40	-
223	Acetylation	GAGSSGYKVGRVMPS CCCCCCCEEECCCHH	41.56	25953088
223	Ubiquitination	GAGSSGYKVGRVMPS CCCCCCCEEECCCHH	41.56	27667366
230	Phosphorylation	KVGRVMPSDLNLMAD EEECCCHHHHCCCCC	36.31	20068231
239 (in isoform 1)	Phosphorylation	-	47.89	-
239	Phosphorylation	LNLMADNSQPENEKE HCCCCCCCCCCCCCC	47.89	17525332
239 (in isoform 3)	Phosphorylation	-	47.89	-
248	Phosphorylation	PENEKEASGGDSPKD CCCCCCCCCCCCCCC	44.38	22617229
252	Phosphorylation	KEASGGDSPKDDSKP CCCCCCCCCCCCCCC	36.80	27362937
257	Phosphorylation	GDSPKDDSKPPYSYA CCCCCCCCCCCCCHH	58.14	20873877
261	Phosphorylation	KDDSKPPYSYAQLIV CCCCCCCCCHHHHHH	23.88	20873877
262	Phosphorylation	DDSKPPYSYAQLIVQ CCCCCCCCHHHHHHH	21.55	20873877
263	Phosphorylation	DSKPPYSYAQLIVQA CCCCCCCHHHHHHHH	7.79	20873877
272	Phosphorylation	QLIVQAITMAPDKQL HHHHHHHHCCCCCCE	15.42	20873877
295	Phosphorylation	ITKNYPYYRTADKGW HHCCCCCEECCCHHH	9.29	-
300	Ubiquitination	PYYRTADKGWQNSIR CCEECCCHHHHHHHH	60.63	-
305	Phosphorylation	ADKGWQNSIRHNLSL CCHHHHHHHHHCCEE	13.10	27067055
314	Methylation	RHNLSLNRYFIKVPR HHCCEECCEEEECCC	32.79	-
318	Ubiquitination	SLNRYFIKVPRSQEE EECCEEEECCCCCCC	35.97	33845483
328	Sumoylation	RSQEEPGKGSFWRID CCCCCCCCCCCEECC	63.20	-
328	Acetylation	RSQEEPGKGSFWRID CCCCCCCCCCCEECC	63.20	30588845
328	Sumoylation	RSQEEPGKGSFWRID CCCCCCCCCCCEECC	63.20	-
328	Ubiquitination	RSQEEPGKGSFWRID CCCCCCCCCCCEECC	63.20	32015554
330	Phosphorylation	QEEPGKGSFWRIDPA CCCCCCCCCEECCCC	25.73	23186163
338	Phosphorylation	FWRIDPASESKLIEQ CEECCCCCHHHHHHH	48.03	22817901
340	Phosphorylation	RIDPASESKLIEQAF ECCCCCHHHHHHHHH	30.21	22817901
341	Ubiquitination	IDPASESKLIEQAFR CCCCCHHHHHHHHHH	49.81	29967540
360	Phosphorylation	RGVPCFRTPLGPLSS CCCCCCCCCCCCCCC	11.56	28985074
366	Phosphorylation	RTPLGPLSSRSAPAS CCCCCCCCCCCCCCC	27.17	20860994
367	Phosphorylation	TPLGPLSSRSAPASP CCCCCCCCCCCCCCC	37.63	30576142
369	Phosphorylation	LGPLSSRSAPASPNH CCCCCCCCCCCCCCC	40.32	23927012
373 (in isoform 1)	Phosphorylation	-	25.77	-
373	Phosphorylation	SSRSAPASPNHAGVL CCCCCCCCCCCCCCE	25.77	23927012
381	Phosphorylation	PNHAGVLSAHSSGAQ CCCCCCEECCCCCCC	22.87	30266825
384	Phosphorylation	AGVLSAHSSGAQTPE CCCEECCCCCCCCCH	30.13	30266825
385	Phosphorylation	GVLSAHSSGAQTPES CCEECCCCCCCCCHH	28.42	30266825
389 (in isoform 1)	Phosphorylation	-	28.61	-
389	Phosphorylation	AHSSGAQTPESLSRE CCCCCCCCCHHHCCC	28.61	23401153
392	Phosphorylation	SGAQTPESLSREGSP CCCCCCHHHCCCCCC	32.61	30266825
394 (in isoform 1)	Phosphorylation	-	37.25	-
394	Phosphorylation	AQTPESLSREGSPAP CCCCHHHCCCCCCCC	37.25	30266825
398 (in isoform 1)	Phosphorylation	-	17.09	-
398	Phosphorylation	ESLSREGSPAPLEPE HHHCCCCCCCCCCCC	17.09	19664994
424 (in isoform 1)	Phosphorylation	-	32.76	-
424	O-linked_Glycosylation	QEARFAQSAPGSPLS EEHHHHHCCCCCCCC	32.76	30059200
424	Phosphorylation	QEARFAQSAPGSPLS EEHHHHHCCCCCCCC	32.76	29255136
428 (in isoform 1)	Phosphorylation	-	22.93	-
428	Phosphorylation	FAQSAPGSPLSSQPV HHHCCCCCCCCCCCE	22.93	29255136
431	Phosphorylation	SAPGSPLSSQPVLIT CCCCCCCCCCCEEEE	30.25	30266825
432	Phosphorylation	APGSPLSSQPVLITV CCCCCCCCCCEEEEE	46.30	22167270
438	Phosphorylation	SSQPVLITVQRQLPQ CCCCEEEEEEECCCC	13.36	23927012
527	Sumoylation	DHREVKVKVEPIPAI CCCEEEEEEEECCCC	34.85	-
527	Acetylation	DHREVKVKVEPIPAI CCCEEEEEEEECCCC	34.85	26051181
527	Sumoylation	DHREVKVKVEPIPAI CCCEEEEEEEECCCC	34.85	28112733
548	Phosphorylation	TASRIIQTAQTTPVQ HHHHHHHHCCCCCCE	15.43	26074081
551	Phosphorylation	RIIQTAQTTPVQTVT HHHHHCCCCCCEEEE	30.51	25159151
552	Phosphorylation	IIQTAQTTPVQTVTI HHHHCCCCCCEEEEE	14.91	29978859
556	Phosphorylation	AQTTPVQTVTIVQQA CCCCCCEEEEEEEEC	21.61	29978859
558	Phosphorylation	TTPVQTVTIVQQAPL CCCCEEEEEEEECCC	20.86	29978859
584	Phosphorylation	QNGTHVASVPTAVHG ECCEEEEECCCEECC	27.78	-
587	Phosphorylation	THVASVPTAVHGQVN EEEEECCCEECCCCC	38.87	-
599	Phosphorylation	QVNNAAASPLHMLAT CCCCCCCCHHHHHHH	24.22	25159151
606	Phosphorylation	SPLHMLATHASASAS CHHHHHHHHHHHHCC	17.64	27251275
609	Phosphorylation	HMLATHASASASLPT HHHHHHHHHHCCCCC	18.36	27251275
611	Phosphorylation	LATHASASASLPTKR HHHHHHHHCCCCCCC	18.85	27251275
613	Phosphorylation	THASASASLPTKRHN HHHHHHCCCCCCCCC	32.17	25332170
616	Phosphorylation	SASASLPTKRHNGDQ HHHCCCCCCCCCCCC	46.10	25332170
617	Acetylation	ASASLPTKRHNGDQP HHCCCCCCCCCCCCC	50.12	26051181
630	Acetylation	QPEQPELKRIKTEDG CCCCCCCEEEECCCC	50.87	25953088
633	Sumoylation	QPELKRIKTEDGEGI CCCCEEEECCCCCEE	50.31	-
633	Sumoylation	QPELKRIKTEDGEGI CCCCEEEECCCCCEE	50.31	28112733
634	Phosphorylation	PELKRIKTEDGEGIV CCCEEEECCCCCEEE	36.62	27273156
645	Phosphorylation	EGIVIALSVDTPPAA CEEEEEEEECCCCHH	14.66	27794612
648	Phosphorylation	VIALSVDTPPAAVRE EEEEEECCCCHHHHH	29.08	27251275

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
373	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
373	S	Phosphorylation	Kinase	CDK2	P24941	Uniprot
428	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
428	S	Phosphorylation	Kinase	CDK2	P24941	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
373	S	Phosphorylation	20810654
Phosphorylation at Ser-373 and Ser-428 affects stability by promoting degradation.
428	S	Phosphorylation	18220336
Phosphorylation at Ser-373 and Ser-428 affects stability by promoting degradation.

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 FOXK2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMU1_HUMAN	SMU1	physical	26344197
TEAD1_HUMAN	TEAD1	physical	26344197
ESR1_HUMAN	ESR1	physical	25740706
BARD1_HUMAN	BARD1	physical	25740706
BAP1_HUMAN	BAP1	physical	25451922
HCFC1_HUMAN	HCFC1	physical	25451922
SIN3A_HUMAN	SIN3A	physical	25609649
ARI4B_HUMAN	ARID4B	physical	25609649
BPTF_HUMAN	BPTF	physical	25609649
NCOR1_HUMAN	NCOR1	physical	25609649
ARI4A_HUMAN	ARID4A	physical	25609649
SMCA5_HUMAN	SMARCA5	physical	25609649
BAP1_HUMAN	BAP1	physical	25609649
TFAP4_HUMAN	TFAP4	physical	25609649
MNT_HUMAN	MNT	physical	25609649
SP130_HUMAN	SAP130	physical	25609649
SDS3_HUMAN	SUDS3	physical	25609649
SMCA1_HUMAN	SMARCA1	physical	25609649
ZBT10_HUMAN	ZBTB10	physical	25609649
BRM1L_HUMAN	BRMS1L	physical	25609649
HCFC1_HUMAN	HCFC1	physical	25609649
KANL1_HUMAN	KANSL1	physical	25609649
SAP30_HUMAN	SAP30	physical	25609649
TBL1R_HUMAN	TBL1XR1	physical	25609649
ASXL2_HUMAN	ASXL2	physical	25609649
BRMS1_HUMAN	BRMS1	physical	25609649
MAP1B_HUMAN	MAP1B	physical	25609649
MAX_HUMAN	MAX	physical	25609649
TPR_HUMAN	TPR	physical	25609649
CIC_HUMAN	CIC	physical	25609649
IRF2_HUMAN	IRF2	physical	25609649
BAP18_HUMAN	C17orf49	physical	25609649
DNLI3_HUMAN	LIG3	physical	25609649
KMT2D_HUMAN	KMT2D	physical	25609649
ASXL1_HUMAN	ASXL1	physical	25609649
CHD4_HUMAN	CHD4	physical	25609649
HDAC2_HUMAN	HDAC2	physical	25609649
ING2_HUMAN	ING2	physical	25609649
MCRS1_HUMAN	MCRS1	physical	25609649
PRD10_HUMAN	PRDM10	physical	25609649
RB_HUMAN	RB1	physical	25609649
RBBP5_HUMAN	RBBP5	physical	25609649
TBP_HUMAN	TBP	physical	25609649
KDM1B_HUMAN	KDM1B	physical	25609649
DVL2_HUMAN	DVL2	physical	25609649
ING1_HUMAN	ING1	physical	25609649
KDM5A_HUMAN	KDM5A	physical	25609649
KANL3_HUMAN	KANSL3	physical	25609649
P20L1_HUMAN	PHF20L1	physical	25609649
CUX1_HUMAN	CUX1	physical	25609649
CASP_HUMAN	CUX1	physical	25609649
DMAP1_HUMAN	DMAP1	physical	25609649
NC2A_HUMAN	DRAP1	physical	25609649
HIRA_HUMAN	HIRA	physical	25609649
HMGX4_HUMAN	HMGXB4	physical	25609649
HXD13_HUMAN	HOXD13	physical	25609649
NCOR2_HUMAN	NCOR2	physical	25609649
SATB2_HUMAN	SATB2	physical	25609649
SIN3B_HUMAN	SIN3B	physical	25609649
TBL1X_HUMAN	TBL1X	physical	25609649
TBL1Y_HUMAN	TBL1Y	physical	25609649
ADNP_HUMAN	ADNP	physical	25609649
EMSY_HUMAN	C11orf30	physical	25609649
KANL2_HUMAN	KANSL2	physical	25609649
DPY30_HUMAN	DPY30	physical	25609649
TF3C3_HUMAN	GTF3C3	physical	25609649
H2AY_HUMAN	H2AFY	physical	25609649
HXB9_HUMAN	HOXB9	physical	25609649
NFYC_HUMAN	NFYC	physical	25609649
NRF1_HUMAN	NRF1	physical	25609649
NU107_HUMAN	NUP107	physical	25609649
PSIP1_HUMAN	PSIP1	physical	25609649
SP30L_HUMAN	SAP30L	physical	25609649
SF3B1_HUMAN	SF3B1	physical	25609649
TP53B_HUMAN	TP53BP1	physical	25609649
SNX9_HUMAN	SNX9	physical	25609649
UBR4_HUMAN	UBR4	physical	25609649
RBM26_HUMAN	RBM26	physical	25609649
PUF60_HUMAN	PUF60	physical	25609649
ANR52_HUMAN	ANKRD52	physical	25609649
E2AK3_HUMAN	EIF2AK3	physical	25609649
CHK2_HUMAN	CHEK2	physical	25609649
PRC2C_HUMAN	PRRC2C	physical	25609649
URFB1_HUMAN	UHRF1BP1	physical	25609649
ANR28_HUMAN	ANKRD28	physical	25609649
SRPK2_HUMAN	SRPK2	physical	25609649
CD11A_HUMAN	CDK11A	physical	25609649
K0513_HUMAN	KIAA0513	physical	25609649
PER1_HUMAN	PER1	physical	25609649
UBP47_HUMAN	USP47	physical	25609649
TMF1_HUMAN	TMF1	physical	25609649
ABHDA_HUMAN	ABHD10	physical	25609649
IF2P_HUMAN	EIF5B	physical	25609649
KANK2_HUMAN	KANK2	physical	25609649
RSRC2_HUMAN	RSRC2	physical	25609649
F120A_HUMAN	FAM120A	physical	25609649
NHP2_HUMAN	NHP2	physical	25609649
PHF23_HUMAN	PHF23	physical	25609649
U520_HUMAN	SNRNP200	physical	25609649
TR150_HUMAN	THRAP3	physical	25609649
P53_HUMAN	TP53	physical	25609649
YTDC1_HUMAN	YTHDC1	physical	25609649
HDAC1_HUMAN	HDAC1	physical	24748658
BAP1_HUMAN	BAP1	physical	24748658
SIN3A_HUMAN	SIN3A	physical	24748658
ASXL2_HUMAN	ASXL2	physical	24748658
HCFC1_HUMAN	HCFC1	physical	24748658

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 FOXK2_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 THR-13; SER-30; SER-398 AND SER-428, AND MASSSPECTROMETRY.	19413330 [Abstract]
Phosphorylation
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 THR-13; SER-30; SER-398 AND SER-428, 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-398, 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 SER-428, AND MASSSPECTROMETRY.	18220336 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND MASSSPECTROMETRY.	18187866 [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 SER-61 AND SER-239, AND MASSSPECTROMETRY.	17525332 [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-398, AND MASSSPECTROMETRY.	16964243 [Abstract]

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