dbPTM

PAK2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PAK2_HUMAN
UniProt AC	Q13177
Protein Name	Serine/threonine-protein kinase PAK 2
Gene Name	PAK2
Organism	Homo sapiens (Human).
Sequence Length	524
Subcellular Localization	Serine/threonine-protein kinase PAK 2: Cytoplasm. MYO18A mediates the cellular distribution of the PAK2-ARHGEF7-GIT1 complex to the inner surface of the cell membrane. PAK-2p34: Nucleus. Cytoplasm, perinuclear region. Membrane Lipid-anchor. In
Protein Description	Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell motility, cell cycle progression, apoptosis or proliferation. Acts as downstream effector of the small GTPases CDC42 and RAC1. Activation by the binding of active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Full-length PAK2 stimulates cell survival and cell growth. Phosphorylates MAPK4 and MAPK6 and activates the downstream target MAPKAPK5, a regulator of F-actin polymerization and cell migration. Phosphorylates JUN and plays an important role in EGF-induced cell proliferation. Phosphorylates many other substrates including histone H4 to promote assembly of H3.3 and H4 into nucleosomes, BAD, ribosomal protein S6, or MBP. Additionally, associates with ARHGEF7 and GIT1 to perform kinase-independent functions such as spindle orientation control during mitosis. On the other hand, apoptotic stimuli such as DNA damage lead to caspase-mediated cleavage of PAK2, generating PAK-2p34, an active p34 fragment that translocates to the nucleus and promotes cellular apoptosis involving the JNK signaling pathway. Caspase-activated PAK2 phosphorylates MKNK1 and reduces cellular translation..
Protein Sequence	MSDNGELEDKPPAPPVRMSSTIFSTGGKDPLSANHSLKPLPSVPEEKKPRHKIISIFSGTEKGSKKKEKERPEISPPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKLEQKKNPQAVLDVLKFYDSNTVKQKYLSFTPPEKDGFPSGTPALNAKGTEAPAVVTEEEDDDEETAPPVIAPRPDHTKSIYTRSVIDPVPAPVGDSHVDGAAKSLDKQKKKTKMTDEEIMEKLRTIVSIGDPKKKYTRYEKIGQGASGTVFTATDVALGQEVAIKQINLQKQPKKELIINEILVMKELKNPNIVNFLDSYLVGDELFVVMEYLAGGSLTDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMEGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTPLIMAAKEAMKSNR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSDNGELED ------CCCCCCCCC	39.52	20068231
2	Phosphorylation	------MSDNGELED ------CCCCCCCCC	39.52	29255136
18	Sulfoxidation	PPAPPVRMSSTIFST CCCCCCEEECEEEEC	3.65	21406390
19	Phosphorylation	PAPPVRMSSTIFSTG CCCCCEEECEEEECC	17.48	22322096
20	Phosphorylation	APPVRMSSTIFSTGG CCCCEEECEEEECCC	19.04	27273156
21	Phosphorylation	PPVRMSSTIFSTGGK CCCEEECEEEECCCC	20.80	27273156
24	Phosphorylation	RMSSTIFSTGGKDPL EEECEEEECCCCCCC	23.45	29514088
25	Phosphorylation	MSSTIFSTGGKDPLS EECEEEECCCCCCCC	38.92	22322096
28	Acetylation	TIFSTGGKDPLSANH EEEECCCCCCCCCCC	58.48	23749302
28	Ubiquitination	TIFSTGGKDPLSANH EEEECCCCCCCCCCC	58.48	-
32	Phosphorylation	TGGKDPLSANHSLKP CCCCCCCCCCCCCCC	32.20	22322096
36	Phosphorylation	DPLSANHSLKPLPSV CCCCCCCCCCCCCCC	37.58	23401153
38	Acetylation	LSANHSLKPLPSVPE CCCCCCCCCCCCCCC	47.74	23954790
38	Malonylation	LSANHSLKPLPSVPE CCCCCCCCCCCCCCC	47.74	32601280
38	Ubiquitination	LSANHSLKPLPSVPE CCCCCCCCCCCCCCC	47.74	19608861
42	Phosphorylation	HSLKPLPSVPEEKKP CCCCCCCCCCCCCCC	58.97	22322096
52	Acetylation	EEKKPRHKIISIFSG CCCCCCCEEEECCCC	42.91	25953088
52	Malonylation	EEKKPRHKIISIFSG CCCCCCCEEEECCCC	42.91	26320211
52	Ubiquitination	EEKKPRHKIISIFSG CCCCCCCEEEECCCC	42.91	-
55	Phosphorylation	KPRHKIISIFSGTEK CCCCEEEECCCCCCC	22.51	30266825
58	Phosphorylation	HKIISIFSGTEKGSK CEEEECCCCCCCCCC	43.04	29255136
60	Phosphorylation	IISIFSGTEKGSKKK EEECCCCCCCCCCCC	33.07	29255136
62	Acetylation	SIFSGTEKGSKKKEK ECCCCCCCCCCCCCC	69.21	23954790
62	Malonylation	SIFSGTEKGSKKKEK ECCCCCCCCCCCCCC	69.21	32601280
62	Ubiquitination	SIFSGTEKGSKKKEK ECCCCCCCCCCCCCC	69.21	-
64	Phosphorylation	FSGTEKGSKKKEKER CCCCCCCCCCCCCCC	52.98	23401153
65	Ubiquitination	SGTEKGSKKKEKERP CCCCCCCCCCCCCCC	76.24	-
75	Phosphorylation	EKERPEISPPSDFEH CCCCCCCCCCCHHCC	29.15	28464451
78	Phosphorylation	RPEISPPSDFEHTIH CCCCCCCCHHCCEEE	59.31	28464451
83	Phosphorylation	PPSDFEHTIHVGFDA CCCHHCCEEEEEEEC	12.94	25159151
92	Phosphorylation	HVGFDAVTGEFTGMP EEEEECCCCCCCCCH	32.49	28464451
96	Phosphorylation	DAVTGEFTGMPEQWA ECCCCCCCCCHHHHH	28.41	28634298
108	Phosphorylation	QWARLLQTSNITKLE HHHHHHHHCCHHHHH	24.58	28857561
109	Phosphorylation	WARLLQTSNITKLEQ HHHHHHHCCHHHHHH	17.18	28857561
112	Phosphorylation	LLQTSNITKLEQKKN HHHHCCHHHHHHCCC	33.55	20068231
113	Ubiquitination	LQTSNITKLEQKKNP HHHCCHHHHHHCCCH	46.35	21890473
117	Malonylation	NITKLEQKKNPQAVL CHHHHHHCCCHHHHH	45.18	32601280
117	Ubiquitination	NITKLEQKKNPQAVL CHHHHHHCCCHHHHH	45.18	-
118	Ubiquitination	ITKLEQKKNPQAVLD HHHHHHCCCHHHHHH	73.82	-
128	Acetylation	QAVLDVLKFYDSNTV HHHHHHHHHCCCCCC	41.55	19608861
128	Ubiquitination	QAVLDVLKFYDSNTV HHHHHHHHHCCCCCC	41.55	19608861
130	Phosphorylation	VLDVLKFYDSNTVKQ HHHHHHHCCCCCCEE	19.51	25159151
132	Phosphorylation	DVLKFYDSNTVKQKY HHHHHCCCCCCEEEE	24.03	23401153
134	Phosphorylation	LKFYDSNTVKQKYLS HHHCCCCCCEEEEEC	32.79	30266825
136	Ubiquitination	FYDSNTVKQKYLSFT HCCCCCCEEEEECCC	38.75	-
138	Ubiquitination	DSNTVKQKYLSFTPP CCCCCEEEEECCCCC	42.30	-
139	Phosphorylation	SNTVKQKYLSFTPPE CCCCEEEEECCCCCC	12.70	22167270
141	Phosphorylation	TVKQKYLSFTPPEKD CCEEEEECCCCCCCC	24.80	19664994
143	Phosphorylation	KQKYLSFTPPEKDGF EEEEECCCCCCCCCC	34.26	22167270
147	Acetylation	LSFTPPEKDGFPSGT ECCCCCCCCCCCCCC	69.77	25953088
147	Ubiquitination	LSFTPPEKDGFPSGT ECCCCCCCCCCCCCC	69.77	-
152	Phosphorylation	PEKDGFPSGTPALNA CCCCCCCCCCCCCCC	53.70	19664994
154	Phosphorylation	KDGFPSGTPALNAKG CCCCCCCCCCCCCCC	15.10	30266825
162	Phosphorylation	PALNAKGTEAPAVVT CCCCCCCCCCCEEEE	28.41	30278072
169	O-linked_Glycosylation	TEAPAVVTEEEDDDE CCCCEEEECCCCCCC	30.95	28510447
169	Phosphorylation	TEAPAVVTEEEDDDE CCCCEEEECCCCCCC	30.95	29255136
178	O-linked_Glycosylation	EEDDDEETAPPVIAP CCCCCCCCCCCEECC	42.28	28510447
178	Phosphorylation	EEDDDEETAPPVIAP CCCCCCCCCCCEECC	42.28	30278072
190	Phosphorylation	IAPRPDHTKSIYTRS ECCCCCCCCCCEECC	33.59	23401153
191	Acetylation	APRPDHTKSIYTRSV CCCCCCCCCCEECCC	31.28	26051181
191	Ubiquitination	APRPDHTKSIYTRSV CCCCCCCCCCEECCC	31.28	-
192	Phosphorylation	PRPDHTKSIYTRSVI CCCCCCCCCEECCCC	23.22	25159151
194	Phosphorylation	PDHTKSIYTRSVIDP CCCCCCCEECCCCCC	11.82	23403867
195	Phosphorylation	DHTKSIYTRSVIDPV CCCCCCEECCCCCCC	18.13	25159151
197	Phosphorylation	TKSIYTRSVIDPVPA CCCCEECCCCCCCCC	18.67	29255136
209	Phosphorylation	VPAPVGDSHVDGAAK CCCCCCCCCHHHHHH	21.34	23403867
213	N-myristoyl glycine	VGDSHVDGAAKSLDK CCCCCHHHHHHHHHH	26.75	-
213	Myristoylation	VGDSHVDGAAKSLDK CCCCCHHHHHHHHHH	26.75	16617111
216	Acetylation	SHVDGAAKSLDKQKK CCHHHHHHHHHHHHH	51.52	25953088
216	Ubiquitination	SHVDGAAKSLDKQKK CCHHHHHHHHHHHHH	51.52	-
217	Phosphorylation	HVDGAAKSLDKQKKK CHHHHHHHHHHHHHH	36.75	28464451
226	Acetylation	DKQKKKTKMTDEEIM HHHHHHCCCCHHHHH	49.00	25953088
226	Ubiquitination	DKQKKKTKMTDEEIM HHHHHHCCCCHHHHH	49.00	-
228	Phosphorylation	QKKKTKMTDEEIMEK HHHHCCCCHHHHHHH	41.64	-
235	Acetylation	TDEEIMEKLRTIVSI CHHHHHHHHHHHHCC	26.37	26822725
235	Ubiquitination	TDEEIMEKLRTIVSI CHHHHHHHHHHHHCC	26.37	-
238	Phosphorylation	EIMEKLRTIVSIGDP HHHHHHHHHHCCCCC	35.85	29514088
241	Phosphorylation	EKLRTIVSIGDPKKK HHHHHHHCCCCCCCC	19.60	29514088
254	Ubiquitination	KKYTRYEKIGQGASG CCEECEEECCCCCCC	43.11	-
278	Ubiquitination	LGQEVAIKQINLQKQ CCHHEEEHHCCCCCC	35.07	-
284	Acetylation	IKQINLQKQPKKELI EHHCCCCCCCCHHHE	72.27	25953088
284	Ubiquitination	IKQINLQKQPKKELI EHHCCCCCCCCHHHE	72.27	-
299	Ubiquitination	INEILVMKELKNPNI EEEHHHHHHCCCCCH	53.03	-
302	Ubiquitination	ILVMKELKNPNIVNF HHHHHHCCCCCHHHH	72.02	-
370	Ubiquitination	QVIHRDIKSDNVLLG CCEECCCCCCCEEEC	56.92	21906983
371	Ubiquitination	VIHRDIKSDNVLLGM CEECCCCCCCEEECC	34.45	21890473
378	Sulfoxidation	SDNVLLGMEGSVKLT CCCEEECCCCEEEEE	5.49	21406390
381	Phosphorylation	VLLGMEGSVKLTDFG EEECCCCEEEEECCC	11.63	27067055
394	Phosphorylation	FGFCAQITPEQSKRS CCEEEECCHHHHCCC	14.53	25159151
398	Phosphorylation	AQITPEQSKRSTMVG EECCHHHHCCCCCCC	28.51	28787133
399	Acetylation	QITPEQSKRSTMVGT ECCHHHHCCCCCCCC	50.49	24179729
399	Ubiquitination	QITPEQSKRSTMVGT ECCHHHHCCCCCCCC	50.49	21906983
400	Ubiquitination	ITPEQSKRSTMVGTP CCHHHHCCCCCCCCC	42.48	21890473
401	Phosphorylation	TPEQSKRSTMVGTPY CHHHHCCCCCCCCCC	25.29	27461979
402	Phosphorylation	PEQSKRSTMVGTPYW HHHHCCCCCCCCCCC	21.65	22153498
406	Phosphorylation	KRSTMVGTPYWMAPE CCCCCCCCCCCCCCH	11.20	23401153
408	Phosphorylation	STMVGTPYWMAPEVV CCCCCCCCCCCCHHH	13.98	23401153
416	Phosphorylation	WMAPEVVTRKAYGPK CCCCHHHCCCCCCCC	31.46	23401153
443	Phosphorylation	MVEGEPPYLNENPLR ECCCCCCCCCCCHHH	32.64	-
453	Phosphorylation	ENPLRALYLIATNGT CCHHHHHHHHHCCCC	8.62	28152594
457	Phosphorylation	RALYLIATNGTPELQ HHHHHHHCCCCHHHC	27.47	28152594
460	Phosphorylation	YLIATNGTPELQNPE HHHHCCCCHHHCCHH	18.69	22817901
468	Acetylation	PELQNPEKLSPIFRD HHHCCHHHCCHHHHH	56.36	25953088
468	Ubiquitination	PELQNPEKLSPIFRD HHHCCHHHCCHHHHH	56.36	21906983
469	Ubiquitination	ELQNPEKLSPIFRDF HHCCHHHCCHHHHHH	7.59	21890473
487	Ubiquitination	CLEMDVEKRGSAKEL HHHCCHHHCCCHHHH	63.00	-
490	Phosphorylation	MDVEKRGSAKELLQH CCHHHCCCHHHHHCC	39.95	24719451
492	Acetylation	VEKRGSAKELLQHPF HHHCCCHHHHHCCHH	51.06	11921293
492	Ubiquitination	VEKRGSAKELLQHPF HHHCCCHHHHHCCHH	51.06	2190698
493	Ubiquitination	EKRGSAKELLQHPFL HHCCCHHHHHCCHHH	55.20	21890473
501	Acetylation	LLQHPFLKLAKPLSS HHCCHHHHHHHCHHH	46.94	19608861
501	Ubiquitination	LLQHPFLKLAKPLSS HHCCHHHHHHHCHHH	46.94	19608861
502	Ubiquitination	LQHPFLKLAKPLSSL HCCHHHHHHHCHHHH	8.89	21890473
504	Ubiquitination	HPFLKLAKPLSSLTP CHHHHHHHCHHHHHH	57.85	-
507	Phosphorylation	LKLAKPLSSLTPLIM HHHHHCHHHHHHHHH	31.65	20068231
508	Phosphorylation	KLAKPLSSLTPLIMA HHHHCHHHHHHHHHH	43.90	28102081
510	Phosphorylation	AKPLSSLTPLIMAAK HHCHHHHHHHHHHHH	20.28	20068231
517	Ubiquitination	TPLIMAAKEAMKSNR HHHHHHHHHHHHHCC	36.15	-
522	Phosphorylation	AAKEAMKSNR----- HHHHHHHHCC-----	25.42	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
20	S	Phosphorylation	Kinase	PRKAA2	P54646	GPS
130	Y	Phosphorylation	Kinase	SRC	P12931	GPS
130	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
134	T	Phosphorylation	Kinase	CDK12	Q9NYV4	PSP
141	S	Phosphorylation	Kinase	PAK2	Q13177	PSP
169	T	Phosphorylation	Kinase	CDK12	Q9NYV4	PSP
192	S	Phosphorylation	Kinase	PAK2	Q13177	PSP
197	S	Phosphorylation	Kinase	PAK2	Q13177	PSP
402	T	Phosphorylation	Kinase	PAK2	Q13177	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
402	T	Phosphorylation		9786869
Autophosphorylation of PAK-2p27 can occur in the absence of any effectors and is dependent on phosphorylation of Thr-402, because PAK-2p27 is acting as an exogenous substrate.

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 PAK2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GIT1_HUMAN	GIT1	physical	17353931
GIT2_HUMAN	GIT2	physical	17353931
MYH10_HUMAN	MYH10	physical	17353931
MCM3_HUMAN	MCM3	physical	17353931
CDC42_HUMAN	CDC42	physical	10320322
MLRV_HUMAN	MYL2	physical	10047984
DOCK2_HUMAN	DOCK2	physical	12176041
RAC2_HUMAN	RAC2	physical	12176041
ABL1_HUMAN	ABL1	physical	11121037
DYST_HUMAN	DST	physical	20936779
EP300_HUMAN	EP300	physical	20936779
RAC1_HUMAN	RAC1	physical	20696164
CDC42_HUMAN	CDC42	physical	20696164
HCK_HUMAN	HCK	physical	16374509
LCK_HUMAN	LCK	physical	16374509
SRC_HUMAN	SRC	physical	16374509
SH3R3_HUMAN	SH3RF3	physical	16374509
VINEX_HUMAN	SORBS3	physical	16374509
ARHG7_HUMAN	ARHGEF7	physical	16374509
A4_HUMAN	APP	physical	21832049
MYC_HUMAN	MYC	physical	14749374
PAK2_HUMAN	PAK2	physical	7673144
RIOK3_HUMAN	RIOK3	physical	21988832
G6PD_HUMAN	G6PD	physical	22863883
PSA_HUMAN	NPEPPS	physical	22863883
PUR4_HUMAN	PFAS	physical	22863883
1433S_HUMAN	SFN	physical	22863883
TGM2_HUMAN	TGM2	physical	22863883
UB2R2_HUMAN	UBE2R2	physical	22863883
UBFD1_HUMAN	UBFD1	physical	22863883
1433E_HUMAN	YWHAE	physical	22863883
1433G_HUMAN	YWHAG	physical	22863883
ANCHR_HUMAN	ZFYVE19	physical	22863883
VINEX_HUMAN	SORBS3	physical	25416956
RHOJ_HUMAN	RHOJ	physical	25416956
GDIA_HUMAN	GDI1	physical	26344197
MYO6_HUMAN	MYO6	physical	26344197
PDIA3_HUMAN	PDIA3	physical	26344197
STAT1_HUMAN	STAT1	physical	26344197
SKP1_HUMAN	SKP1	physical	26496610
ARHG7_HUMAN	ARHGEF7	physical	26496610
GIT2_HUMAN	GIT2	physical	26496610
FBX28_HUMAN	FBXO28	physical	26496610
GIT1_HUMAN	GIT1	physical	26496610

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 PAK2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-38 AND LYS-128, AND MASSSPECTROMETRY.	19608861 [Abstract]
Myristoylation
Reference	PubMed
"Posttranslational myristoylation of caspase-activated p21-activatedprotein kinase 2 (PAK2) potentiates late apoptotic events."; Vilas G.L., Corvi M.M., Plummer G.J., Seime A.M., Lambkin G.R.,Berthiaume L.G.; Proc. Natl. Acad. Sci. U.S.A. 103:6542-6547(2006). Cited for: FUNCTION (PAK-2P34), MYRISTOYLATION AT GLY-213 (PAK-2P34), ANDSUBCELLULAR LOCATION.	16617111 [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-55; SER-141; THR-143 ANDSER-197, AND MASS SPECTROMETRY.	19690332 [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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-141, 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-58; SER-141 AND THR-169,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-141, 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-2; SER-141 AND THR-143,AND MASS SPECTROMETRY.	17081983 [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 THR-60, AND MASSSPECTROMETRY.	18088087 [Abstract]

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