dbPTM

PAK1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PAK1_HUMAN
UniProt AC	Q13153
Protein Name	Serine/threonine-protein kinase PAK 1 {ECO:0000303\|PubMed:8805275}
Gene Name	PAK1 {ECO:0000312\|HGNC:HGNC:8590}
Organism	Homo sapiens (Human).
Sequence Length	545
Subcellular Localization	Cytoplasm . Cell junction, focal adhesion . Cell membrane . Cell projection, ruffle membrane . Cell projection, invadopodium . Colocalizes with RUFY3, F-actin and other core migration components in invadopodia at the cell periphery (PubMed:25766321).
Protein Description	Protein kinase involved in intracellular signaling pathways downstream of integrins and receptor-type kinases that plays an important role in cytoskeleton dynamics, in cell adhesion, migration, proliferation, apoptosis, mitosis, and in vesicle-mediated transport processes. Can directly phosphorylate BAD and protects cells against apoptosis. Activated by interaction with CDC42 and RAC1. Functions as GTPase effector that links the Rho-related GTPases CDC42 and RAC1 to the JNK MAP kinase pathway. Phosphorylates and activates MAP2K1, and thereby mediates activation of downstream MAP kinases. Involved in the reorganization of the actin cytoskeleton, actin stress fibers and of focal adhesion complexes. Phosphorylates the tubulin chaperone TBCB and thereby plays a role in the regulation of microtubule biogenesis and organization of the tubulin cytoskeleton. Plays a role in the regulation of insulin secretion in response to elevated glucose levels. Part of a ternary complex that contains PAK1, DVL1 and MUSK that is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ). Activity is inhibited in cells undergoing apoptosis, potentially due to binding of CDC2L1 and CDC2L2. Phosphorylates MYL9/MLC2. Phosphorylates RAF1 at 'Ser-338' and 'Ser-339' resulting in: activation of RAF1, stimulation of RAF1 translocation to mitochondria, phosphorylation of BAD by RAF1, and RAF1 binding to BCL2. Phosphorylates SNAI1 at 'Ser-246' promoting its transcriptional repressor activity by increasing its accumulation in the nucleus. In podocytes, promotes NR3C2 nuclear localization. Required for atypical chemokine receptor ACKR2-induced phosphorylation of LIMK1 and cofilin (CFL1) and for the up-regulation of ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. In synapses, seems to mediate the regulation of F-actin cluster formation performed by SHANK3, maybe through CFL1 phosphorylation and inactivation. Plays a role in RUFY3-mediated facilitating gastric cancer cells migration and invasion. [PubMed: 25766321]
Protein Sequence	MSNNGLDIQDKPPAPPMRNTSTMIGAGSKDAGTLNHGSKPLPPNPEEKKKKDRFYRSILPGDKTNKKKEKERPEISLPSDFEHTIHVGFDAVTGEFTGMPEQWARLLQTSNITKSEQKKNPQAVLDVLEFYNSKKTSNSQKYMSFTDKSAEDYNSSNALNVKAVSETPAVPPVSEDEDDDDDDATPPPVIAPRPEHTKSVYTRSVIEPLPVTPTRDVATSPISPTENNTTPPDALTRNTEKQKKKPKMSDEEILEKLRSIVSVGDPKKKYTRFEKIGQGASGTVYTAMDVATGQEVAIKQMNLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTPLIAAAKEATKNNH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSNNGLDIQ ------CCCCCCCCC	38.72	22814378
2	Phosphorylation	------MSNNGLDIQ ------CCCCCCCCC	38.72	27050516
2 (in isoform 2)	Phosphorylation	-	38.72	24719451
11	Ubiquitination	NGLDIQDKPPAPPMR CCCCCCCCCCCCCCC	36.20	-
20	Phosphorylation	PAPPMRNTSTMIGAG CCCCCCCCCCCCCCC	18.40	21406692
20 (in isoform 2)	Phosphorylation	-	18.40	27251275
21	Phosphorylation	APPMRNTSTMIGAGS CCCCCCCCCCCCCCC	21.37	21406692
22	Phosphorylation	PPMRNTSTMIGAGSK CCCCCCCCCCCCCCC	15.69	21406692
28	Phosphorylation	STMIGAGSKDAGTLN CCCCCCCCCCCCCCC	27.16	21406692
28 (in isoform 2)	Phosphorylation	-	27.16	27251275
29	Acetylation	TMIGAGSKDAGTLNH CCCCCCCCCCCCCCC	51.16	23954790
29	Ubiquitination	TMIGAGSKDAGTLNH CCCCCCCCCCCCCCC	51.16	-
38	Phosphorylation	AGTLNHGSKPLPPNP CCCCCCCCCCCCCCH	24.45	24719451
39	Ubiquitination	GTLNHGSKPLPPNPE CCCCCCCCCCCCCHH	55.98	-
57	Phosphorylation	KKDRFYRSILPGDKT HHHHHHHHHCCCCCC	19.66	9032240
63	Acetylation	RSILPGDKTNKKKEK HHHCCCCCCCCCCCC	60.97	23749302
76	Phosphorylation	EKERPEISLPSDFEH CCCCCCCCCCCCCCC	32.34	27732954
79	Phosphorylation	RPEISLPSDFEHTIH CCCCCCCCCCCCEEE	61.29	27732954
84	Phosphorylation	LPSDFEHTIHVGFDA CCCCCCCEEEEEEEC	12.94	14707132
109	Phosphorylation	QWARLLQTSNITKSE HHHHHHHHCCCCHHH	24.58	30266825
110	Phosphorylation	WARLLQTSNITKSEQ HHHHHHHCCCCHHHH	17.18	30266825
113	Phosphorylation	LLQTSNITKSEQKKN HHHHCCCCHHHHHCC	32.54	30266825
115	Phosphorylation	QTSNITKSEQKKNPQ HHCCCCHHHHHCCHH	36.29	30266825
115 (in isoform 2)	Phosphorylation	-	36.29	24719451
131	Phosphorylation	VLDVLEFYNSKKTSN HHHHHHHHHCCCCCC	14.78	29978859
131 (in isoform 2)	Phosphorylation	-	14.78	27642862
133	Phosphorylation	DVLEFYNSKKTSNSQ HHHHHHHCCCCCCCC	24.93	29978859
136	Phosphorylation	EFYNSKKTSNSQKYM HHHHCCCCCCCCCCC	36.56	30108239
136 (in isoform 2)	Phosphorylation	-	36.56	27642862
137	Phosphorylation	FYNSKKTSNSQKYMS HHHCCCCCCCCCCCC	43.28	30108239
139	Phosphorylation	NSKKTSNSQKYMSFT HCCCCCCCCCCCCCC	28.02	30108239
139 (in isoform 2)	Phosphorylation	-	28.02	24719451
142	Phosphorylation	KTSNSQKYMSFTDKS CCCCCCCCCCCCCCC	7.14	29255136
142 (in isoform 2)	Phosphorylation	-	7.14	27642862
144	Phosphorylation	SNSQKYMSFTDKSAE CCCCCCCCCCCCCHH	23.16	19664994
144 (in isoform 2)	Phosphorylation	-	23.16	24719451
146	Phosphorylation	SQKYMSFTDKSAEDY CCCCCCCCCCCHHHH	34.90	30266825
148	Ubiquitination	KYMSFTDKSAEDYNS CCCCCCCCCHHHHCC	48.81	-
149	Phosphorylation	YMSFTDKSAEDYNSS CCCCCCCCHHHHCCC	39.43	21945579
149 (in isoform 2)	Phosphorylation	-	39.43	27251275
153	Phosphorylation	TDKSAEDYNSSNALN CCCCHHHHCCCCCCC	14.40	21945579
153 (in isoform 2)	Phosphorylation	-	14.40	27642862
155	Phosphorylation	KSAEDYNSSNALNVK CCHHHHCCCCCCCCE	20.81	21945579
155 (in isoform 2)	Phosphorylation	-	20.81	27251275
156	Phosphorylation	SAEDYNSSNALNVKA CHHHHCCCCCCCCEE	23.60	21945579
156 (in isoform 2)	Phosphorylation	-	23.60	24719451
165	Phosphorylation	ALNVKAVSETPAVPP CCCCEEEECCCCCCC	40.38	29255136
167	Phosphorylation	NVKAVSETPAVPPVS CCEEEECCCCCCCCC	14.72	29255136
174	Phosphorylation	TPAVPPVSEDEDDDD CCCCCCCCCCCCCCC	45.14	29255136
174 (in isoform 2)	Phosphorylation	-	45.14	27251275
185	Phosphorylation	DDDDDDATPPPVIAP CCCCCCCCCCCEECC	43.24	29255136
185 (in isoform 2)	Phosphorylation	-	43.24	27251275
197	Phosphorylation	IAPRPEHTKSVYTRS ECCCCCCCCCCCCCC	24.29	30278072
199	Phosphorylation	PRPEHTKSVYTRSVI CCCCCCCCCCCCCEE	22.85	21278788
201	Phosphorylation	PEHTKSVYTRSVIEP CCCCCCCCCCCEEEC	11.97	17726028
202	Phosphorylation	EHTKSVYTRSVIEPL CCCCCCCCCCEEECC	17.82	28634298
204	Phosphorylation	TKSVYTRSVIEPLPV CCCCCCCCEEECCCC	21.46	19664994
204 (in isoform 2)	Phosphorylation	-	21.46	24719451
212	Phosphorylation	VIEPLPVTPTRDVAT EEECCCCCCCCCCCC	19.59	19664994
212 (in isoform 2)	Phosphorylation	-	19.59	24719451
214	Phosphorylation	EPLPVTPTRDVATSP ECCCCCCCCCCCCCC	30.09	29255136
214 (in isoform 2)	Phosphorylation	-	30.09	24719451
219	Phosphorylation	TPTRDVATSPISPTE CCCCCCCCCCCCCCC	34.58	30266825
219 (in isoform 2)	Phosphorylation	-	34.58	27251275
220	Phosphorylation	PTRDVATSPISPTEN CCCCCCCCCCCCCCC	15.53	30266825
220 (in isoform 2)	Phosphorylation	-	15.53	24719451
223	Phosphorylation	DVATSPISPTENNTT CCCCCCCCCCCCCCC	29.20	29255136
223 (in isoform 2)	Phosphorylation	-	29.20	24719451
225	Phosphorylation	ATSPISPTENNTTPP CCCCCCCCCCCCCCC	44.55	29255136
225 (in isoform 2)	Phosphorylation	-	44.55	24719451
229	Phosphorylation	ISPTENNTTPPDALT CCCCCCCCCCCCHHC	52.87	29255136
230	Phosphorylation	SPTENNTTPPDALTR CCCCCCCCCCCHHCC	34.64	29255136
230 (in isoform 2)	Phosphorylation	-	34.64	24719451
236	Phosphorylation	TTPPDALTRNTEKQK CCCCCHHCCCCHHHH	24.48	30266825
239	Phosphorylation	PDALTRNTEKQKKKP CCHHCCCCHHHHCCC	41.07	26074081
245	Acetylation	NTEKQKKKPKMSDEE CCHHHHCCCCCCHHH	57.83	19413330
248	Sulfoxidation	KQKKKPKMSDEEILE HHHCCCCCCHHHHHH	9.17	21406390
249	Phosphorylation	QKKKPKMSDEEILEK HHCCCCCCHHHHHHH	48.25	26074081
256	Sumoylation	SDEEILEKLRSIVSV CHHHHHHHHHHHHCC	45.84	-
256	Acetylation	SDEEILEKLRSIVSV CHHHHHHHHHHHHCC	45.84	19608861
256	Sumoylation	SDEEILEKLRSIVSV CHHHHHHHHHHHHCC	45.84	-
256	Ubiquitination	SDEEILEKLRSIVSV CHHHHHHHHHHHHCC	45.84	-
259	Phosphorylation	EILEKLRSIVSVGDP HHHHHHHHHHCCCCC	37.47	28348404
262	Phosphorylation	EKLRSIVSVGDPKKK HHHHHHHCCCCCCCC	20.79	-
271	Phosphorylation	GDPKKKYTRFEKIGQ CCCCCCEECCEECCC	37.45	29496963
281	Phosphorylation	EKIGQGASGTVYTAM EECCCCCCCCEEEEE	41.65	22210691
285	Phosphorylation	QGASGTVYTAMDVAT CCCCCCEEEEEECCC	6.66	17726028
299	Ubiquitination	TGQEVAIKQMNLQQQ CCCCHHHHHCCCCCC	33.48	-
309	Ubiquitination	NLQQQPKKELIINEI CCCCCCCHHHEEEEH	65.52	-
391	Ubiquitination	QVIHRDIKSDNILLG CCEECCCCCCCEEEC	56.92	-
415	Phosphorylation	FGFCAQITPEQSKRS CCEEEECCHHHHCCC	14.53	25159151
419	Phosphorylation	AQITPEQSKRSTMVG EECCHHHHCCCCCCC	28.51	28787133
420	Acetylation	QITPEQSKRSTMVGT ECCHHHHCCCCCCCC	50.49	24179719
420	Ubiquitination	QITPEQSKRSTMVGT ECCHHHHCCCCCCCC	50.49	2190698
420 (in isoform 1)	Ubiquitination	-	50.49	21906983
420 (in isoform 2)	Ubiquitination	-	50.49	21906983
422	Phosphorylation	TPEQSKRSTMVGTPY CHHHHCCCCCCCCCC	25.29	27461979
423	Phosphorylation	PEQSKRSTMVGTPYW HHHHCCCCCCCCCCC	21.65	22153498
427	Phosphorylation	KRSTMVGTPYWMAPE CCCCCCCCCCCCCCH	11.20	23401153
429	Phosphorylation	STMVGTPYWMAPEVV CCCCCCCCCCCCHHH	13.98	23401153
437	Phosphorylation	WMAPEVVTRKAYGPK CCCCHHHCCCCCCCC	31.46	23401153
474	Phosphorylation	ENPLRALYLIATNGT CCHHHHHHHHHCCCC	8.62	28152594
478	Phosphorylation	RALYLIATNGTPELQ HHHHHHHCCCCHHHC	27.47	28152594
481	Phosphorylation	YLIATNGTPELQNPE HHHHCCCCHHHCCHH	18.69	22817901
491	Phosphorylation	LQNPEKLSAIFRDFL HCCHHHHHHHHHHHH	30.31	-
508	Ubiquitination	CLEMDVEKRGSAKEL HHHCCHHHCCCHHHH	63.00	-
511	Phosphorylation	MDVEKRGSAKELLQH CCHHHCCCHHHHHHH	39.95	24719451
513	Acetylation	VEKRGSAKELLQHQF HHHCCCHHHHHHHHH	51.06	11921281
528	Phosphorylation	LKIAKPLSSLTPLIA HHHHHCHHHHHHHHH	31.65	-
529	Phosphorylation	KIAKPLSSLTPLIAA HHHHCHHHHHHHHHH	43.90	-
531	Phosphorylation	AKPLSSLTPLIAAAK HHCHHHHHHHHHHHH	20.28	-

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
21	S	Phosphorylation	Kinase	PKB	P31749	Uniprot
21	S	Phosphorylation	Kinase	AKT-FAMILY	-	GPS
21	S	Phosphorylation	Kinase	PRKG1	Q13976-2	GPS
57	S	Phosphorylation	Kinase	PAK1	Q13153	GPS
84	T	Phosphorylation	Kinase	OXSR1	O95747	Uniprot
109	T	Phosphorylation	Kinase	LKB1	Q9WTK7	PSP
109	T	Phosphorylation	Kinase	STK11	Q15831	GPS
133	S	Phosphorylation	Kinase	MLK3	Q16584	PSP
144	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
153	Y	Phosphorylation	Kinase	BMX	P51813	GPS
153	Y	Phosphorylation	Kinase	JAK2	O60674	Uniprot
174	S	Phosphorylation	Kinase	CDK19	Q9BWU1	PSP
199	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
201	Y	Phosphorylation	Kinase	JAK2	O60674	Uniprot
204	S	Phosphorylation	Kinase	MLK3	Q16584	PSP
204	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
212	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
212	T	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
212	T	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
223	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
285	Y	Phosphorylation	Kinase	JAK2	O60674	Uniprot
423	T	Phosphorylation	Kinase	PAK1	Q13153	PSP
423	T	Phosphorylation	Kinase	PDK1	Q15118	GPS
423	T	Phosphorylation	Kinase	PDK1	O15530	PSP
423	T	Phosphorylation	Kinase	BRSK2	Q8IWQ3	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
21	S	Phosphorylation	14585966
Phosphorylated at Ser-21 by PKB/AKT; this reduces interaction with NCK1 and association with focal adhesion sites.
212	T	Phosphorylation	16964243
Upon DNA damage, phosphorylated at Thr-212 and translocates to the nucleoplasm.
423	T	Phosphorylation	10551809
Activated by autophosphorylation at Thr-423 in response to a conformation change, triggered by interaction with GTP-bound CDC42 or RAC1.
423	T	Phosphorylation	10551809
Activated by phosphorylation at Thr-423 by BRSK2 and by PDPK1.

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 PAK1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ARHG2_HUMAN	ARHGEF2	physical	14970201
ARC1B_HUMAN	ARPC1B	physical	14749719
RAC1_HUMAN	RAC1	physical	12879077
RAC1_HUMAN	RAC1	physical	12650940
CDC42_HUMAN	CDC42	physical	12650940
CD11A_HUMAN	CDK11A	physical	12624090
ERBB2_HUMAN	ERBB2	physical	9774445
DYL1_HUMAN	DYNLL1	physical	15193260
PK1IP_HUMAN	PAK1IP1	physical	11371639
LIMK1_HUMAN	LIMK1	physical	10559936
RAF1_HUMAN	RAF1	physical	11733498
HGS_HUMAN	HGS	physical	11397816
ARHG7_HUMAN	ARHGEF7	physical	11157752
MYLK_HUMAN	MYLK	physical	10092231
NCK1_HUMAN	NCK1	physical	8824201
BMX_HUMAN	BMX	physical	11382770
PAK1_HUMAN	PAK1	physical	11804587
PAK1_HUMAN	PAK1	physical	10975528
SH3K1_HUMAN	SH3KBP1	physical	16407834
HS90A_HUMAN	HSP90AA1	physical	20936779
1433G_HUMAN	YWHAG	physical	20936779
1433Z_HUMAN	YWHAZ	physical	20936779
ARHG7_HUMAN	ARHGEF7	physical	20936779
DYR1B_HUMAN	DYRK1B	physical	20936779
ZBT18_HUMAN	ZBTB18	physical	20936779
Z3H7A_HUMAN	ZC3H7A	physical	20936779
ZN823_HUMAN	ZNF823	physical	20936779
ZNF83_HUMAN	ZNF83	physical	20936779
MYNN_HUMAN	MYNN	physical	20936779
CE042_HUMAN	C5orf42	physical	20936779
ZN418_HUMAN	ZNF418	physical	20936779
RAC1_HUMAN	RAC1	physical	21474670
RAC1_HUMAN	RAC1	physical	15673687
RAC1_HUMAN	RAC1	physical	19327867
RAC1_HUMAN	RAC1	physical	16002993
NCK1_HUMAN	NCK1	physical	10372803
RAC1_HUMAN	RAC1	physical	16551621
ELF3_HUMAN	ELF3	physical	17491012
GBB1_HUMAN	GNB1	physical	12887923
M3K1_HUMAN	MAP3K1	physical	12228228
CDC42_HUMAN	CDC42	physical	16678097
RAC1_HUMAN	RAC1	physical	16678097
RAC1_HUMAN	RAC1	physical	15075243
MYO6_HUMAN	MYO6	physical	9852149
NCK2_HUMAN	NCK2	physical	11557983
NCK1_HUMAN	NCK1	physical	11557983
TGFR1_HUMAN	TGFBR1	physical	15761153
TGFR2_HUMAN	TGFBR2	physical	15761153
A4_HUMAN	APP	physical	21832049
CRPAK_HUMAN	CRIPAK	physical	16278681
PAK1_HUMAN	PAK1	physical	16278681
CHRD1_HUMAN	CHORDC1	physical	19910486
ESR1_HUMAN	ESR1	physical	16452229
BAD_HUMAN	BAD	physical	15849194
CDC42_YEAST	CDC42	physical	20171953
H31_HUMAN	HIST1H3A	physical	12151336
ESR1_HUMAN	ESR1	physical	12374744
BAD_HUMAN	BAD	physical	19667065
NCK2_HUMAN	NCK2	physical	23455922
CDC42_HUMAN	CDC42	physical	23455922
PAK2_HUMAN	PAK2	physical	23455922
ARHG7_HUMAN	ARHGEF7	physical	23455922
ARHG6_HUMAN	ARHGEF6	physical	23455922
FBX28_HUMAN	FBXO28	physical	23455922
GIT1_HUMAN	GIT1	physical	23455922
VINEX_HUMAN	SORBS3	physical	15784622
BAD_HUMAN	BAD	physical	15784622
NCK2_HUMAN	NCK2	physical	25416956
AKT1_HUMAN	AKT1	physical	24886428
BRSK1_HUMAN	BRSK1	physical	22669945
RAC1_HUMAN	RAC1	physical	19961560
GIT1_HUMAN	GIT1	physical	25852190
GIT2_HUMAN	GIT2	physical	25852190
H2AX_HUMAN	H2AFX	physical	25852190
CDC42_HUMAN	CDC42	physical	18057010
RAC1_HUMAN	RAC1	physical	11130076
TF65_HUMAN	RELA	physical	26036343
RHOU_HUMAN	RHOU	physical	26598620
RAC1_HUMAN	RAC1	physical	19277120
RAC1_HUMAN	RAC1	physical	25468898
PAK1_HUMAN	PAK1	physical	18586681
RAC1_HUMAN	RAC1	physical	15548653
CDC42_HUMAN	CDC42	physical	15548653
RAC1_HUMAN	RAC1	physical	15212766
RAC1_CAEEL	ced-10	physical	15700267
RAC1_HUMAN	RAC1	physical	25819133
BAD_HUMAN	BAD	physical	10611223
BAD_MOUSE	Bad	physical	10611223
RAC1_HUMAN	RAC1	physical	15143066

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 PAK1_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-256, AND MASS SPECTROMETRY.	19608861 [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-144; SER-204; THR-212;THR-219; SER-220 AND THR-230, 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 THR-212; THR-225; THR-229AND THR-230, 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 THR-230, AND MASSSPECTROMETRY.	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 THR-212, AND MASSSPECTROMETRY.	16964243 [Abstract]
"p21-activated kinase (PAK1) is phosphorylated and activated by 3-phosphoinositide-dependent kinase-1 (PDK1)."; King C.C., Gardiner E.M., Zenke F.T., Bohl B.P., Newton A.C.,Hemmings B.A., Bokoch G.M.; J. Biol. Chem. 275:41201-41209(2000). Cited for: PHOSPHORYLATION AT THR-423 BY PDPK1, INTERACTION WITH PDPK1, ANDENZYME REGULATION.	10995762 [Abstract]
"Identification of a central phosphorylation site in p21-activatedkinase regulating autoinhibition and kinase activity."; Zenke F.T., King C.C., Bohl B.P., Bokoch G.M.; J. Biol. Chem. 274:32565-32573(1999). Cited for: PHOSPHORYLATION AT THR-423, AND MUTAGENESIS OF THR-423.	10551809 [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-474, AND MASSSPECTROMETRY.	19534553 [Abstract]

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