dbPTM

COF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	COF1_HUMAN
UniProt AC	P23528
Protein Name	Cofilin-1
Gene Name	CFL1
Organism	Homo sapiens (Human).
Sequence Length	166
Subcellular Localization	Nucleus matrix . Cytoplasm, cytoskeleton . Cell projection, ruffle membrane Peripheral membrane protein Cytoplasmic side . Cell projection, lamellipodium membrane Peripheral membrane protein Cytoplasmic side . Cell projection, lamellipodium . Note
Protein Description	Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. [PubMed: 11812157]
Protein Sequence	MASGVAVSDGVIKVFNDMKVRKSSTPEEVKKRKKAVLFCLSEDKKNIILEEGKEILVGDVGQTVDDPYATFVKMLPDKDCRYALYDATYETKESKKEDLVFIFWAPESAPLKSKMIYASSKDAIKKKLTGIKHELQANCYEEVKDRCTLAEKLGGSAVISLEGKPL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASGVAVSD ------CCCCEEECC	18.26	20068231
3	Phosphorylation	-----MASGVAVSDG -----CCCCEEECCC	32.28	29255136
8	O-linked_Glycosylation	MASGVAVSDGVIKVF CCCCEEECCCEEEEE	20.93	23301498
8	Phosphorylation	MASGVAVSDGVIKVF CCCCEEECCCEEEEE	20.93	30266825
13	Sumoylation	AVSDGVIKVFNDMKV EECCCEEEEECCCCC	38.07	-
13	Acetylation	AVSDGVIKVFNDMKV EECCCEEEEECCCCC	38.07	19608861
13	Sumoylation	AVSDGVIKVFNDMKV EECCCEEEEECCCCC	38.07	19608861
13	Ubiquitination	AVSDGVIKVFNDMKV EECCCEEEEECCCCC	38.07	21890473
19	Sumoylation	IKVFNDMKVRKSSTP EEEECCCCCCCCCCH	41.57	-
19	2-Hydroxyisobutyrylation	IKVFNDMKVRKSSTP EEEECCCCCCCCCCH	41.57	-
19	Acetylation	IKVFNDMKVRKSSTP EEEECCCCCCCCCCH	41.57	25825284
19	Malonylation	IKVFNDMKVRKSSTP EEEECCCCCCCCCCH	41.57	26320211
19	Methylation	IKVFNDMKVRKSSTP EEEECCCCCCCCCCH	41.57	19608861
19	Sumoylation	IKVFNDMKVRKSSTP EEEECCCCCCCCCCH	41.57	19608861
19	Ubiquitination	IKVFNDMKVRKSSTP EEEECCCCCCCCCCH	41.57	21890473
22	Acetylation	FNDMKVRKSSTPEEV ECCCCCCCCCCHHHH	52.31	27178108
22	Ubiquitination	FNDMKVRKSSTPEEV ECCCCCCCCCCHHHH	52.31	-
23	Phosphorylation	NDMKVRKSSTPEEVK CCCCCCCCCCHHHHH	28.96	30278072
24	Phosphorylation	DMKVRKSSTPEEVKK CCCCCCCCCHHHHHH	51.52	29255136
25	Phosphorylation	MKVRKSSTPEEVKKR CCCCCCCCHHHHHHH	41.64	29255136
30	Sumoylation	SSTPEEVKKRKKAVL CCCHHHHHHHHCEEE	50.57	-
30	2-Hydroxyisobutyrylation	SSTPEEVKKRKKAVL CCCHHHHHHHHCEEE	50.57	-
30	Acetylation	SSTPEEVKKRKKAVL CCCHHHHHHHHCEEE	50.57	21339330
30	Sumoylation	SSTPEEVKKRKKAVL CCCHHHHHHHHCEEE	50.57	-
30	Ubiquitination	SSTPEEVKKRKKAVL CCCHHHHHHHHCEEE	50.57	-
31	Acetylation	STPEEVKKRKKAVLF CCHHHHHHHHCEEEE	74.71	11923949
33	Acetylation	PEEVKKRKKAVLFCL HHHHHHHHCEEEEEC	54.70	7616599
33	Ubiquitination	PEEVKKRKKAVLFCL HHHHHHHHCEEEEEC	54.70	-
34	Sumoylation	EEVKKRKKAVLFCLS HHHHHHHCEEEEECC	48.00	-
34	2-Hydroxyisobutyrylation	EEVKKRKKAVLFCLS HHHHHHHCEEEEECC	48.00	-
34	Acetylation	EEVKKRKKAVLFCLS HHHHHHHCEEEEECC	48.00	26051181
34	Sumoylation	EEVKKRKKAVLFCLS HHHHHHHCEEEEECC	48.00	-
34	Ubiquitination	EEVKKRKKAVLFCLS HHHHHHHCEEEEECC	48.00	-
39	Glutathionylation	RKKAVLFCLSEDKKN HHCEEEEECCCCCCE	3.41	22555962
39	S-nitrosylation	RKKAVLFCLSEDKKN HHCEEEEECCCCCCE	3.41	24105792
39	S-palmitoylation	RKKAVLFCLSEDKKN HHCEEEEECCCCCCE	3.41	29575903
41	Phosphorylation	KAVLFCLSEDKKNII CEEEEECCCCCCEEE	44.95	23401153
44	Sumoylation	LFCLSEDKKNIILEE EEECCCCCCEEEECC	43.60	-
44	Acetylation	LFCLSEDKKNIILEE EEECCCCCCEEEECC	43.60	23954790
44	Malonylation	LFCLSEDKKNIILEE EEECCCCCCEEEECC	43.60	26320211
44	Sumoylation	LFCLSEDKKNIILEE EEECCCCCCEEEECC	43.60	-
44	Ubiquitination	LFCLSEDKKNIILEE EEECCCCCCEEEECC	43.60	-
45	Sumoylation	FCLSEDKKNIILEEG EECCCCCCEEEECCC	66.74	-
45	Acetylation	FCLSEDKKNIILEEG EECCCCCCEEEECCC	66.74	27452117
45	Malonylation	FCLSEDKKNIILEEG EECCCCCCEEEECCC	66.74	26320211
45	Sumoylation	FCLSEDKKNIILEEG EECCCCCCEEEECCC	66.74	-
45	Ubiquitination	FCLSEDKKNIILEEG EECCCCCCEEEECCC	66.74	-
53	Sumoylation	NIILEEGKEILVGDV EEEECCCCEEEECCC	44.88	-
53	Acetylation	NIILEEGKEILVGDV EEEECCCCEEEECCC	44.88	26822725
53	Sumoylation	NIILEEGKEILVGDV EEEECCCCEEEECCC	44.88	-
53	Ubiquitination	NIILEEGKEILVGDV EEEECCCCEEEECCC	44.88	21906983
63	Phosphorylation	LVGDVGQTVDDPYAT EECCCCCCCCCCHHH	21.70	28450419
68	Nitration	GQTVDDPYATFVKML CCCCCCCHHHHHCCC	25.85	-
68	Phosphorylation	GQTVDDPYATFVKML CCCCCCCHHHHHCCC	25.85	27273156
70	Phosphorylation	TVDDPYATFVKMLPD CCCCCHHHHHCCCCC	24.10	25159151
73	Acetylation	DPYATFVKMLPDKDC CCHHHHHCCCCCCCC	30.45	19608861
73	Sumoylation	DPYATFVKMLPDKDC CCHHHHHCCCCCCCC	30.45	19608861
73	Ubiquitination	DPYATFVKMLPDKDC CCHHHHHCCCCCCCC	30.45	73
74	Sulfoxidation	PYATFVKMLPDKDCR CHHHHHCCCCCCCCC	5.73	30846556
78	Acetylation	FVKMLPDKDCRYALY HHCCCCCCCCCHHEE	57.71	23749302
78	Malonylation	FVKMLPDKDCRYALY HHCCCCCCCCCHHEE	57.71	26320211
78	Ubiquitination	FVKMLPDKDCRYALY HHCCCCCCCCCHHEE	57.71	-
80	Glutathionylation	KMLPDKDCRYALYDA CCCCCCCCCHHEEEC	4.40	22555962
80	S-nitrosylation	KMLPDKDCRYALYDA CCCCCCCCCHHEEEC	4.40	24105792
82	Phosphorylation	LPDKDCRYALYDATY CCCCCCCHHEEECCC	13.80	30550596
85	Phosphorylation	KDCRYALYDATYETK CCCCHHEEECCCCCC	8.72	27273156
88	Phosphorylation	RYALYDATYETKESK CHHEEECCCCCCCCC	20.99	27273156
89	Phosphorylation	YALYDATYETKESKK HHEEECCCCCCCCCC	24.26	25159151
91	Phosphorylation	LYDATYETKESKKED EEECCCCCCCCCCCC	29.69	27273156
92	2-Hydroxyisobutyrylation	YDATYETKESKKEDL EECCCCCCCCCCCCE	48.31	-
92	Acetylation	YDATYETKESKKEDL EECCCCCCCCCCCCE	48.31	23954790
92	Malonylation	YDATYETKESKKEDL EECCCCCCCCCCCCE	48.31	26320211
92	Ubiquitination	YDATYETKESKKEDL EECCCCCCCCCCCCE	48.31	19608861
94	Phosphorylation	ATYETKESKKEDLVF CCCCCCCCCCCCEEE	51.05	26356563
95	Ubiquitination	TYETKESKKEDLVFI CCCCCCCCCCCEEEE	62.36	-
96	Trimethylation	YETKESKKEDLVFIF CCCCCCCCCCEEEEE	66.78	-
96	2-Hydroxyisobutyrylation	YETKESKKEDLVFIF CCCCCCCCCCEEEEE	66.78	-
96	Acetylation	YETKESKKEDLVFIF CCCCCCCCCCEEEEE	66.78	129419
96	Methylation	YETKESKKEDLVFIF CCCCCCCCCCEEEEE	66.78	-
96	Ubiquitination	YETKESKKEDLVFIF CCCCCCCCCCEEEEE	66.78	21890473
108	O-linked_Glycosylation	FIFWAPESAPLKSKM EEEECCCCCCCCCCE	33.84	23301498
108	Phosphorylation	FIFWAPESAPLKSKM EEEECCCCCCCCCCE	33.84	28450419
112	Sumoylation	APESAPLKSKMIYAS CCCCCCCCCCEEEEC	47.15	-
112	2-Hydroxyisobutyrylation	APESAPLKSKMIYAS CCCCCCCCCCEEEEC	47.15	-
112	Acetylation	APESAPLKSKMIYAS CCCCCCCCCCEEEEC	47.15	25953088
112	Sumoylation	APESAPLKSKMIYAS CCCCCCCCCCEEEEC	47.15	-
112	Ubiquitination	APESAPLKSKMIYAS CCCCCCCCCCEEEEC	47.15	21906983
113	Phosphorylation	PESAPLKSKMIYASS CCCCCCCCCEEEECC	34.83	28270605
114	Sumoylation	ESAPLKSKMIYASSK CCCCCCCCEEEECCH	27.94	-
114	2-Hydroxyisobutyrylation	ESAPLKSKMIYASSK CCCCCCCCEEEECCH	27.94	-
114	Acetylation	ESAPLKSKMIYASSK CCCCCCCCEEEECCH	27.94	19608861
114	Methylation	ESAPLKSKMIYASSK CCCCCCCCEEEECCH	27.94	24129315
114	Succinylation	ESAPLKSKMIYASSK CCCCCCCCEEEECCH	27.94	23954790
114	Sumoylation	ESAPLKSKMIYASSK CCCCCCCCEEEECCH	27.94	19608861
114	Ubiquitination	ESAPLKSKMIYASSK CCCCCCCCEEEECCH	27.94	21890473
115	Sulfoxidation	SAPLKSKMIYASSKD CCCCCCCEEEECCHH	3.50	25058340
117	Phosphorylation	PLKSKMIYASSKDAI CCCCCEEEECCHHHH	9.27	27273156
119	Phosphorylation	KSKMIYASSKDAIKK CCCEEEECCHHHHHH	22.43	26356563
120	Phosphorylation	SKMIYASSKDAIKKK CCEEEECCHHHHHHH	26.78	26356563
121	Sumoylation	KMIYASSKDAIKKKL CEEEECCHHHHHHHH	49.00	-
121	Acetylation	KMIYASSKDAIKKKL CEEEECCHHHHHHHH	49.00	23954790
121	Malonylation	KMIYASSKDAIKKKL CEEEECCHHHHHHHH	49.00	26320211
121	Sumoylation	KMIYASSKDAIKKKL CEEEECCHHHHHHHH	49.00	19608861
121	Ubiquitination	KMIYASSKDAIKKKL CEEEECCHHHHHHHH	49.00	19608861
125	Acetylation	ASSKDAIKKKLTGIK ECCHHHHHHHHHCCC	45.64	8273235
126	Acetylation	SSKDAIKKKLTGIKH CCHHHHHHHHHCCCH	47.07	70231
127	Acetylation	SKDAIKKKLTGIKHE CHHHHHHHHHCCCHH	46.40	70235
127	Ubiquitination	SKDAIKKKLTGIKHE CHHHHHHHHHCCCHH	46.40	21890473
129	Phosphorylation	DAIKKKLTGIKHELQ HHHHHHHHCCCHHHH	45.82	29496963
132	Sumoylation	KKKLTGIKHELQANC HHHHHCCCHHHHHCH	32.16	-
132	2-Hydroxyisobutyrylation	KKKLTGIKHELQANC HHHHHCCCHHHHHCH	32.16	-
132	Acetylation	KKKLTGIKHELQANC HHHHHCCCHHHHHCH	32.16	16916647
132	Malonylation	KKKLTGIKHELQANC HHHHHCCCHHHHHCH	32.16	26320211
132	Sumoylation	KKKLTGIKHELQANC HHHHHCCCHHHHHCH	32.16	28112733
132	Ubiquitination	KKKLTGIKHELQANC HHHHHCCCHHHHHCH	32.16	-
139	S-nitrosocysteine	KHELQANCYEEVKDR CHHHHHCHHHHHHHH	5.19	-
139	Glutathionylation	KHELQANCYEEVKDR CHHHHHCHHHHHHHH	5.19	22555962
139	S-nitrosylation	KHELQANCYEEVKDR CHHHHHCHHHHHHHH	5.19	24105792
140	Nitration	HELQANCYEEVKDRC HHHHHCHHHHHHHHC	18.22	-
140	Phosphorylation	HELQANCYEEVKDRC HHHHHCHHHHHHHHC	18.22	25159151
144	2-Hydroxyisobutyrylation	ANCYEEVKDRCTLAE HCHHHHHHHHCHHHH	42.61	-
144	Acetylation	ANCYEEVKDRCTLAE HCHHHHHHHHCHHHH	42.61	19608861
144	Malonylation	ANCYEEVKDRCTLAE HCHHHHHHHHCHHHH	42.61	26320211
144	Ubiquitination	ANCYEEVKDRCTLAE HCHHHHHHHHCHHHH	42.61	19608861
147	S-nitrosocysteine	YEEVKDRCTLAEKLG HHHHHHHCHHHHHHC	5.40	-
147	S-nitrosylation	YEEVKDRCTLAEKLG HHHHHHHCHHHHHHC	5.40	19483679
148	Phosphorylation	EEVKDRCTLAEKLGG HHHHHHCHHHHHHCC	29.87	20068231
152	Acetylation	DRCTLAEKLGGSAVI HHCHHHHHHCCCEEE	46.99	25953088
152	Ubiquitination	DRCTLAEKLGGSAVI HHCHHHHHHCCCEEE	46.99	-
156	Phosphorylation	LAEKLGGSAVISLEG HHHHHCCCEEEEECC	19.98	29255136
160	Phosphorylation	LGGSAVISLEGKPL- HCCCEEEEECCEEC-	17.48	30266825
164	Sumoylation	AVISLEGKPL----- EEEEECCEEC-----	33.50	-
164	Acetylation	AVISLEGKPL----- EEEEECCEEC-----	33.50	25953088
164	Sumoylation	AVISLEGKPL----- EEEEECCEEC-----	33.50	-
164	Ubiquitination	AVISLEGKPL----- EEEEECCEEC-----	33.50	21906983

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
3	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
3	S	Phosphorylation	Kinase	LIMK1	P53667	PSP
3	S	Phosphorylation	Kinase	LIMK1	P53669	PSP
3	S	Phosphorylation	Kinase	LIMK2	P53671	PSP
3	S	Phosphorylation	Kinase	NRK	Q7Z2Y5	Uniprot
3	S	Phosphorylation	Kinase	ROCK2	P70336	PSP
3	S	Phosphorylation	Kinase	TESK1	Q15569	PSP
3	S	Phosphorylation	Kinase	TESK1	Q63572	PSP
3	S	Phosphorylation	Kinase	TESK2	Q96S53	PhosphoELM
23	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
24	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
68	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
3	S	Phosphorylation	12837278
Inactivated by phosphorylation on Ser-3.
3	S	Phosphorylation	12837278
Phosphorylated on Ser-3 in resting cells (By similarity).
24	S	Phosphorylation	23633677
The phosphorylation of Ser-24 may prevent recognition of the nuclear localization signal (By similarity).

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 COF1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TAGL_HUMAN	TAGLN	physical	17353931
CAP1_HUMAN	CAP1	physical	11950878
ACTS_HUMAN	ACTA1	physical	11950878
ROCK1_HUMAN	ROCK1	physical	10436159
LIMK2_HUMAN	LIMK2	physical	10436159
TPIS_HUMAN	TPI1	physical	12359716
RPAC1_HUMAN	POLR1C	physical	22939629
RL40_HUMAN	UBA52	physical	22939629
ARRB1_HUMAN	ARRB1	physical	17500066
ARRB2_HUMAN	ARRB2	physical	17500066
MTAP_HUMAN	MTAP	physical	22863883
SGT1_HUMAN	SUGT1	physical	22863883
COF2_HUMAN	CFL2	physical	25416956
CAP1_HUMAN	CAP1	physical	26186194
CAP2_HUMAN	CAP2	physical	26186194
GABT_HUMAN	ABAT	physical	26344197
THIM_HUMAN	ACAA2	physical	26344197
AK1A1_HUMAN	AKR1A1	physical	26344197
AL4A1_HUMAN	ALDH4A1	physical	26344197
ALDOA_HUMAN	ALDOA	physical	26344197
ARF4_HUMAN	ARF4	physical	26344197
CATA_HUMAN	CAT	physical	26344197
COX17_HUMAN	COX17	physical	26344197
CSRP1_HUMAN	CSRP1	physical	26344197
DBNL_HUMAN	DBNL	physical	26344197
DUT_HUMAN	DUT	physical	26344197
ENOA_HUMAN	ENO1	physical	26344197
FAHD1_HUMAN	FAHD1	physical	26344197
G3P_HUMAN	GAPDH	physical	26344197
HDHD1_HUMAN	HDHD1	physical	26344197
JUPI1_HUMAN	HN1	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
LDHA_HUMAN	LDHA	physical	26344197
LDH6A_HUMAN	LDHAL6A	physical	26344197
LDHB_HUMAN	LDHB	physical	26344197
LYPA2_HUMAN	LYPLA2	physical	26344197
MDHM_HUMAN	MDH2	physical	26344197
NDKA_HUMAN	NME1	physical	26344197
NDKB_HUMAN	NME2	physical	26344197
PEBP1_HUMAN	PEBP1	physical	26344197
PIN1_HUMAN	PIN1	physical	26344197
KPYM_HUMAN	PKM	physical	26344197
PPIA_HUMAN	PPIA	physical	26344197
PRDX1_HUMAN	PRDX1	physical	26344197
PRDX5_HUMAN	PRDX5	physical	26344197
RTN4_HUMAN	RTN4	physical	26344197
TAGL2_HUMAN	TAGLN2	physical	26344197
TNG2_HUMAN	TANGO2	physical	26344197
TKT_HUMAN	TKT	physical	26344197
TRAP1_HUMAN	TRAP1	physical	26344197
UFD1_HUMAN	UFD1L	physical	26344197
UFM1_HUMAN	UFM1	physical	26344197
COF2_HUMAN	CFL2	physical	21516116
CAP2_HUMAN	CAP2	physical	28514442
CAP1_HUMAN	CAP1	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442

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 COF1_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-3, 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-13; LYS-19; LYS-73 ANDLYS-144, AND MASS SPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-132, AND MASS SPECTROMETRY.	16916647 [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-3; TYR-68 AND SER-156,AND MASS SPECTROMETRY.	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 SER-3, 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-3, AND MASS SPECTROMETRY.	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-3; SER-41 AND SER-156,AND MASS SPECTROMETRY.	18669648 [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-156, 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-3 AND THR-25, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Cofilin phosphorylation and actin polymerization by NRK/NESK, amember of the germinal center kinase family."; Nakano K., Kanai-Azuma M., Kanai Y., Moriyama K., Yazaki K.,Hayashi Y., Kitamura N.; Exp. Cell Res. 287:219-227(2003). Cited for: PHOSPHORYLATION AT SER-3 BY NRK.	12837278 [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-89 AND TYR-140, AND MASSSPECTROMETRY.	19534553 [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-140, 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-140, AND MASSSPECTROMETRY.	18083107 [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-140, AND MASSSPECTROMETRY.	15592455 [Abstract]

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