dbPTM

ROCK2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ROCK2_HUMAN
UniProt AC	O75116
Protein Name	Rho-associated protein kinase 2
Gene Name	ROCK2
Organism	Homo sapiens (Human).
Sequence Length	1388
Subcellular Localization	Cytoplasm. Cell membrane Peripheral membrane protein. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasmic, and associated with actin microfilaments and the plasma membrane..
Protein Description	Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2, EP300, MSN, MYL9/MLC2, NPM1, RDX, PPP1R12A and VIM. Phosphorylates SORL1 and IRF4. Acts as a negative regulator of VEGF-induced angiogenic endothelial cell activation. Positively regulates the activation of p42/MAPK1-p44/MAPK3 and of p90RSK/RPS6KA1 during myogenic differentiation. Plays an important role in the timely initiation of centrosome duplication. Inhibits keratinocyte terminal differentiation. May regulate closure of the eyelids and ventral body wall through organization of actomyosin bundles. Plays a critical role in the regulation of spine and synaptic properties in the hippocampus. Plays an important role in generating the circadian rhythm of the aortic myofilament Ca(2+) sensitivity and vascular contractility by modulating the myosin light chain phosphorylation..
Protein Sequence	MSRPPPTGKMPGAPETAPGDGAGASRQRKLEALIRDPRSPINVESLLDGLNSLVLDLDFPALRKNKNIDNFLNRYEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKHGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGFYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMDHKNSLCFPEDAEISKHAKNLICAFLTDREVRLGRNGVEEIRQHPFFKNDQWHWDNIRETAAPVVPELSSDIDSSNFDDIEDDKGDVETFPIPKAFVGNQLPFIGFTYYRENLLLSDSPSCRETDSIQSRKNEESQEIQKKLYTLEEHLSNEMQAKEELEQKCKSVNTRLEKTAKELEEEITLRKSVESALRQLEREKALLQHKNAEYQRKADHEADKKRNLENDVNSLKDQLEDLKKRNQNSQISTEKVNQLQRQLDETNALLRTESDTAARLRKTQAESSKQIQQLESNNRDLQDKNCLLETAKLKLEKEFINLQSALESERRDRTHGSEIINDLQGRICGLEEDLKNGKILLAKVELEKRQLQERFTDLEKEKSNMEIDMTYQLKVIQQSLEQEEAEHKATKARLADKNKIYESIEEAKSEAMKEMEKKLLEERTLKQKVENLLLEAEKRCSLLDCDLKQSQQKINELLKQKDVLNEDVRNLTLKIEQETQKRCLTQNDLKMQTQQVNTLKMSEKQLKQENNHLMEMKMNLEKQNAELRKERQDADGQMKELQDQLEAEQYFSTLYKTQVRELKEECEEKTKLGKELQQKKQELQDERDSLAAQLEITLTKADSEQLARSIAEEQYSDLEKEKIMKELEIKEMMARHKQELTEKDATIASLEETNRTLTSDVANLANEKEELNNKLKDVQEQLSRLKDEEISAAAIKAQFEKQLLTERTLKTQAVNKLAEIMNRKEPVKRGNDTDVRRKEKENRKLHMELKSEREKLTQQMIKYQKELNEMQAQIAEESQIRIELQMTLDSKDSDIEQLRSQLQALHIGLDSSSIGSGPGDAEADDGFPESRLEGWLSLPVRNNTKKFGWVKKYVIVSSKKILFYDSEQDKEQSNPYMVLDIDKLFHVRPVTQTDVYRADAKEIPRIFQILYANEGESKKEQEFPVEPVGEKSNYICHKGHEFIPTLYHFPTNCEACMKPLWHMFKPPPALECRRCHIKCHKDHMDKKEEIIAPCKVYYDISTAKNLLLLANSTEEQQKWVSRLVKKIPKKPPAPDPFARSSPRTSMKIQQNQSIRRPSRQLAPNKPS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSRPPPTGK ------CCCCCCCCC	65.87	20860994
7	Phosphorylation	-MSRPPPTGKMPGAP -CCCCCCCCCCCCCC	56.03	30387612
9	Acetylation	SRPPPTGKMPGAPET CCCCCCCCCCCCCCC	44.38	25953088
10	Sulfoxidation	RPPPTGKMPGAPETA CCCCCCCCCCCCCCC	3.81	28465586
16	Phosphorylation	KMPGAPETAPGDGAG CCCCCCCCCCCCCCC	36.77	23403867
25	Phosphorylation	PGDGAGASRQRKLEA CCCCCCHHHHHHHHH	28.20	23403867
29	Ubiquitination	AGASRQRKLEALIRD CCHHHHHHHHHHHCC	42.20	-
92	Phosphorylation	LQMKAEDYDVVKVIG CCCCCCCCCEEEEEC	11.35	-
96	Ubiquitination	AEDYDVVKVIGRGAF CCCCCEEEEECCCCC	28.16	-
121	Ubiquitination	SQKVYAMKLLSKFEM HHHHHHHHHHHHHHH	37.80	21906983
124	Phosphorylation	VYAMKLLSKFEMIKR HHHHHHHHHHHHHHC	45.81	29083192
125	Ubiquitination	YAMKLLSKFEMIKRS HHHHHHHHHHHHHCC	45.36	-
171	Phosphorylation	YLYMVMEYMPGGDLV EEEEEEECCCCCCHH	7.18	24275569
216	Ubiquitination	GLIHRDVKPDNMLLD CCCCCCCCCCCCEEC	51.44	21906983
224	Acetylation	PDNMLLDKHGHLKLA CCCCEECCCCCCCCC	52.00	23236377
237	Sulfoxidation	LADFGTCMKMDETGM CCCCCCCEECCCCCC	3.96	21406390
242	Phosphorylation	TCMKMDETGMVHCDT CCEECCCCCCEECCC	26.72	28060719
249	Phosphorylation	TGMVHCDTAVGTPDY CCCEECCCCCCCCCC	28.74	28060719
253	Phosphorylation	HCDTAVGTPDYISPE ECCCCCCCCCCCCHH	13.34	28060719
256	Phosphorylation	TAVGTPDYISPEVLK CCCCCCCCCCHHHHH	12.42	28060719
298	Phosphorylation	DTPFYADSLVGTYSK CCCCCCCHHHHHHHH	19.45	-
323	Acetylation	PEDAEISKHAKNLIC CCHHHHHHHHHHHHH	53.92	25953088
323	Malonylation	PEDAEISKHAKNLIC CCHHHHHHHHHHHHH	53.92	26320211
323	Ubiquitination	PEDAEISKHAKNLIC CCHHHHHHHHHHHHH	53.92	-
355	Ubiquitination	IRQHPFFKNDQWHWD HHCCCCCCCCCCCHH	61.05	-
391	Ubiquitination	FDDIEDDKGDVETFP CCCCCCCCCCCCCCC	70.14	-
396	Phosphorylation	DDKGDVETFPIPKAF CCCCCCCCCCCCHHH	34.26	-
414	Phosphorylation	QLPFIGFTYYRENLL CCCCCCEEEEECCCC	17.90	-
423	Phosphorylation	YRENLLLSDSPSCRE EECCCCCCCCCCCCC	35.69	30266825
425	Phosphorylation	ENLLLSDSPSCRETD CCCCCCCCCCCCCCC	18.48	30266825
427	Phosphorylation	LLLSDSPSCRETDSI CCCCCCCCCCCCCCH	29.74	23663014
442	Phosphorylation	QSRKNEESQEIQKKL HCCCCHHHHHHHHHH	27.25	29978859
448	Ubiquitination	ESQEIQKKLYTLEEH HHHHHHHHHHHHHHH	30.28	-
457	Phosphorylation	YTLEEHLSNEMQAKE HHHHHHHHHHHHHHH	32.43	20068231
482	Ubiquitination	TRLEKTAKELEEEIT HHHHHHHHHHHHHHH	68.98	-
492	Ubiquitination	EEEITLRKSVESALR HHHHHHHHHHHHHHH	63.06	-
505	Ubiquitination	LRQLEREKALLQHKN HHHHHHHHHHHHHHC	51.02	-
511	Ubiquitination	EKALLQHKNAEYQRK HHHHHHHHCHHHHHH	44.91	-
537	Ubiquitination	ENDVNSLKDQLEDLK HHHHHHHHHHHHHHH	43.16	-
556	Ubiquitination	NSQISTEKVNQLQRQ CCCCCHHHHHHHHHH	46.72	-
567	Phosphorylation	LQRQLDETNALLRTE HHHHHHHHCHHHHCH	26.00	20068231
573	Phosphorylation	ETNALLRTESDTAAR HHCHHHHCHHHHHHH	39.55	-
575	Phosphorylation	NALLRTESDTAARLR CHHHHCHHHHHHHHH	39.38	-
577	Phosphorylation	LLRTESDTAARLRKT HHHCHHHHHHHHHHH	31.34	24719451
590	Ubiquitination	KTQAESSKQIQQLES HHHHHHHHHHHHHHH	61.78	-
605	2-Hydroxyisobutyrylation	NNRDLQDKNCLLETA CCCHHHCCCCHHHHH	36.28	-
605	Acetylation	NNRDLQDKNCLLETA CCCHHHCCCCHHHHH	36.28	26051181
605	Ubiquitination	NNRDLQDKNCLLETA CCCHHHCCCCHHHHH	36.28	-
618	Ubiquitination	TAKLKLEKEFINLQS HHHHHHHHHHHCHHH	69.25	-
625	Phosphorylation	KEFINLQSALESERR HHHHCHHHHHHHHHC	37.68	23663014
629	Phosphorylation	NLQSALESERRDRTH CHHHHHHHHHCCCCC	36.93	23663014
669	Ubiquitination	LAKVELEKRQLQERF EEEHHHHHHHHHHHH	59.05	-
684	Phosphorylation	TDLEKEKSNMEIDMT CHHHHHHHCCCCCHH	42.36	26074081
691	Phosphorylation	SNMEIDMTYQLKVIQ HCCCCCHHHHHHHHH	12.36	26074081
692	Phosphorylation	NMEIDMTYQLKVIQQ CCCCCHHHHHHHHHH	12.76	26074081
700	Phosphorylation	QLKVIQQSLEQEEAE HHHHHHHHHHHHHHH	19.94	26074081
709	Ubiquitination	EQEEAEHKATKARLA HHHHHHHHHHHHHHH	49.62	-
720	2-Hydroxyisobutyrylation	ARLADKNKIYESIEE HHHHHHHHHHHHHHH	53.02	-
720	Ubiquitination	ARLADKNKIYESIEE HHHHHHHHHHHHHHH	53.02	-
722	Phosphorylation	LADKNKIYESIEEAK HHHHHHHHHHHHHHH	12.77	21945579
724	Phosphorylation	DKNKIYESIEEAKSE HHHHHHHHHHHHHHH	20.52	21945579
729	Ubiquitination	YESIEEAKSEAMKEM HHHHHHHHHHHHHHH	52.70	-
730	Phosphorylation	ESIEEAKSEAMKEME HHHHHHHHHHHHHHH	37.32	26074081
745	Phosphorylation	KKLLEERTLKQKVEN HHHHHHHHHHHHHHH	41.40	26074081
749	Ubiquitination	EERTLKQKVENLLLE HHHHHHHHHHHHHHH	50.34	-
759	Ubiquitination	NLLLEAEKRCSLLDC HHHHHHHHHHCHHHC	66.79	-
762	Phosphorylation	LEAEKRCSLLDCDLK HHHHHHHCHHHCCHH	35.68	28450419
769	Acetylation	SLLDCDLKQSQQKIN CHHHCCHHHHHHHHH	34.35	26051181
795	Ubiquitination	DVRNLTLKIEQETQK HHHHCHHHHHHHHHH	38.67	-
812	Sulfoxidation	LTQNDLKMQTQQVNT CCHHHHHHHHHHHHH	7.29	21406390
814	Phosphorylation	QNDLKMQTQQVNTLK HHHHHHHHHHHHHHH	19.92	21406692
819	Phosphorylation	MQTQQVNTLKMSEKQ HHHHHHHHHHHCHHH	28.97	21406692
835	Sulfoxidation	KQENNHLMEMKMNLE HHHHHHHHHHHHHHH	3.53	30846556
837	Sulfoxidation	ENNHLMEMKMNLEKQ HHHHHHHHHHHHHHH	2.88	30846556
860	Ubiquitination	QDADGQMKELQDQLE HCCHHHHHHHHHHHH	47.59	-
877	Ubiquitination	QYFSTLYKTQVRELK HHHHHHHHHHHHHHH	35.28	-
884	Acetylation	KTQVRELKEECEEKT HHHHHHHHHHHHHHH	46.87	26051181
890	Acetylation	LKEECEEKTKLGKEL HHHHHHHHHHHHHHH	28.77	25953088
892	Acetylation	EECEEKTKLGKELQQ HHHHHHHHHHHHHHH	67.33	25953088
895	Acetylation	EEKTKLGKELQQKKQ HHHHHHHHHHHHHHH	66.73	25953088
930	Phosphorylation	DSEQLARSIAEEQYS CHHHHHHHHHHHHHC	22.12	22199227
936	Phosphorylation	RSIAEEQYSDLEKEK HHHHHHHHCHHHHHH	13.87	29523821
937	Phosphorylation	SIAEEQYSDLEKEKI HHHHHHHCHHHHHHH	35.10	29523821
941	2-Hydroxyisobutyrylation	EQYSDLEKEKIMKEL HHHCHHHHHHHHHHH	72.16	-
946	Acetylation	LEKEKIMKELEIKEM HHHHHHHHHHHHHHH	63.72	23749302
951	Ubiquitination	IMKELEIKEMMARHK HHHHHHHHHHHHHHH	30.13	21890473
964	Ubiquitination	HKQELTEKDATIASL HHHHHCHHHHHHHHH	47.64	-
989	Acetylation	VANLANEKEELNNKL HHHHHHHHHHHHHHH	57.19	26051181
989	Ubiquitination	VANLANEKEELNNKL HHHHHHHHHHHHHHH	57.19	21906983
995	Ubiquitination	EKEELNNKLKDVQEQ HHHHHHHHHHHHHHH	56.70	21906983
997	Ubiquitination	EELNNKLKDVQEQLS HHHHHHHHHHHHHHH	58.42	-
1004	Phosphorylation	KDVQEQLSRLKDEEI HHHHHHHHHCCHHHH	34.95	29978859
1007	Ubiquitination	QEQLSRLKDEEISAA HHHHHHCCHHHHHHH	63.08	-
1017	Ubiquitination	EISAAAIKAQFEKQL HHHHHHHHHHHHHHH	31.26	-
1022	Malonylation	AIKAQFEKQLLTERT HHHHHHHHHHCCHHH	47.75	26320211
1022	Ubiquitination	AIKAQFEKQLLTERT HHHHHHHHHHCCHHH	47.75	-
1031	2-Hydroxyisobutyrylation	LLTERTLKTQAVNKL HCCHHHHHHHHHHHH	37.67	-
1037	Acetylation	LKTQAVNKLAEIMNR HHHHHHHHHHHHHHC	42.34	25953088
1068	Sulfoxidation	KENRKLHMELKSERE HHHHHHHHHHHHHHH	10.52	30846556
1071	Ubiquitination	RKLHMELKSEREKLT HHHHHHHHHHHHHHH	36.64	-
1072	Phosphorylation	KLHMELKSEREKLTQ HHHHHHHHHHHHHHH	55.28	26074081
1078	Phosphorylation	KSEREKLTQQMIKYQ HHHHHHHHHHHHHHH	28.02	17525332
1083	Ubiquitination	KLTQQMIKYQKELNE HHHHHHHHHHHHHHH	35.96	-
1084	Phosphorylation	LTQQMIKYQKELNEM HHHHHHHHHHHHHHH	17.56	26074081
1086	Ubiquitination	QQMIKYQKELNEMQA HHHHHHHHHHHHHHH	62.16	-
1091	Sulfoxidation	YQKELNEMQAQIAEE HHHHHHHHHHHHHHH	3.78	30846556
1108	Phosphorylation	IRIELQMTLDSKDSD HHHEEEEECCCCCCH	17.91	20860994
1111	Phosphorylation	ELQMTLDSKDSDIEQ EEEEECCCCCCHHHH	41.28	26270265
1114	Phosphorylation	MTLDSKDSDIEQLRS EECCCCCCHHHHHHH	44.20	-
1121	Phosphorylation	SDIEQLRSQLQALHI CHHHHHHHHHHHHHH	43.78	28176443
1132	Phosphorylation	ALHIGLDSSSIGSGP HHHHCCCHHHCCCCC	30.90	29209046
1133	Phosphorylation	LHIGLDSSSIGSGPG HHHCCCHHHCCCCCC	26.16	29209046
1134	Phosphorylation	HIGLDSSSIGSGPGD HHCCCHHHCCCCCCC	34.61	29209046
1137	Phosphorylation	LDSSSIGSGPGDAEA CCHHHCCCCCCCCCC	39.89	25159151
1151	Phosphorylation	ADDGFPESRLEGWLS CCCCCCHHHHCEEEE	42.26	28450419
1165	Phosphorylation	SLPVRNNTKKFGWVK ECCCCCCCCCCCCEE	38.88	27251275
1178	Phosphorylation	VKKYVIVSSKKILFY EEEEEEEECCEEEEE	25.89	20068231
1180	2-Hydroxyisobutyrylation	KYVIVSSKKILFYDS EEEEEECCEEEEEEC	36.01	-
1181	Ubiquitination	YVIVSSKKILFYDSE EEEEECCEEEEEECC	46.73	-
1187	Phosphorylation	KKILFYDSEQDKEQS CEEEEEECCCCHHHC	26.27	-
1194	Phosphorylation	SEQDKEQSNPYMVLD CCCCHHHCCCEEEEE	40.64	28188228
1197	Phosphorylation	DKEQSNPYMVLDIDK CHHHCCCEEEEEHHH	12.24	25072903
1212	Phosphorylation	LFHVRPVTQTDVYRA HCCCEECCCCCEECC	28.56	26657352
1214	Phosphorylation	HVRPVTQTDVYRADA CCEECCCCCEECCCH	20.33	26699800
1217	Phosphorylation	PVTQTDVYRADAKEI ECCCCCEECCCHHHC	11.68	28060719
1222	Ubiquitination	DVYRADAKEIPRIFQ CEECCCHHHCHHHHH	57.64	-
1232	Phosphorylation	PRIFQILYANEGESK HHHHHHHHCCCCCCC	14.71	-
1238	Phosphorylation	LYANEGESKKEQEFP HHCCCCCCCCCCCCC	60.94	-
1252	Ubiquitination	PVEPVGEKSNYICHK CCCCCCCCCCEECCC	37.76	-
1316	Ubiquitination	EEIIAPCKVYYDIST HHEEECCEEEEEHHH	32.01	-
1318	Phosphorylation	IIAPCKVYYDISTAK EEECCEEEEEHHHHH	4.86	21945579
1319	Phosphorylation	IAPCKVYYDISTAKN EECCEEEEEHHHHHH	15.13	21945579
1322	Phosphorylation	CKVYYDISTAKNLLL CEEEEEHHHHHHHHH	21.29	21945579
1323	Phosphorylation	KVYYDISTAKNLLLL EEEEEHHHHHHHHHH	41.82	21945579
1334	Phosphorylation	LLLLANSTEEQQKWV HHHHCCCHHHHHHHH	43.26	21712546
1339	Ubiquitination	NSTEEQQKWVSRLVK CCHHHHHHHHHHHHH	49.62	-
1350	Acetylation	RLVKKIPKKPPAPDP HHHHHCCCCCCCCCC	79.83	7380627
1351	Acetylation	LVKKIPKKPPAPDPF HHHHCCCCCCCCCCC	51.37	7380641
1351	Ubiquitination	LVKKIPKKPPAPDPF HHHHCCCCCCCCCCC	51.37	-
1361	Phosphorylation	APDPFARSSPRTSMK CCCCCCCCCCCCCHH	41.06	23401153
1362	Phosphorylation	PDPFARSSPRTSMKI CCCCCCCCCCCCHHH	16.91	25159151
1365	Phosphorylation	FARSSPRTSMKIQQN CCCCCCCCCHHHHHC	36.24	30576142
1366	Phosphorylation	ARSSPRTSMKIQQNQ CCCCCCCCHHHHHCC	21.25	26074081
1368	Acetylation	SSPRTSMKIQQNQSI CCCCCCHHHHHCCCC	36.81	25953088
1368	Methylation	SSPRTSMKIQQNQSI CCCCCCHHHHHCCCC	36.81	24129315
1368	Ubiquitination	SSPRTSMKIQQNQSI CCCCCCHHHHHCCCC	36.81	-
1374	Phosphorylation	MKIQQNQSIRRPSRQ HHHHHCCCCCCCCCC	26.13	29255136
1379	Phosphorylation	NQSIRRPSRQLAPNK CCCCCCCCCCCCCCC	30.74	27273156
1388	Phosphorylation	QLAPNKPS------- CCCCCCCC-------	55.23	24719451

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
414	T	Phosphorylation	Kinase	ROCK2	O75116	Uniprot
722	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
1366	S	Phosphorylation	Kinase	ROCK2	O75116	PSP
1374	S	Phosphorylation	Kinase	ROCK2	O75116	PSP
1379	S	Phosphorylation	Kinase	ROCK2	O75116	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ROCK2_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 ROCK2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
STK16_HUMAN	STK16	physical	17353931
WASC5_HUMAN	KIAA0196	physical	22863883
RABX5_HUMAN	RABGEF1	physical	22863883
RGAP1_HUMAN	RACGAP1	physical	26344197
RPAC1_HUMAN	POLR1C	physical	28514442
ROCK1_HUMAN	ROCK1	physical	28514442
DJB11_HUMAN	DNAJB11	physical	28514442
FBX42_HUMAN	FBXO42	physical	28514442
MLRV_HUMAN	MYL2	physical	25412762
LZTL1_HUMAN	LZTFL1	physical	27173435

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
D01840	Fasudil hydrochloride (JAN)
D03115	Fasudil hydrochloride hydrate (JAN); Eril-S (TN)
D07941	Fasudil (INN)
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ROCK2_HUMAN

Related Literatures of Post-Translational Modification

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-1137, AND MASSSPECTROMETRY.	19690332 [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-1133 AND SER-1137, ANDMASS SPECTROMETRY.	18669648 [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-425, AND MASSSPECTROMETRY.	18691976 [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-1374, 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-1362, AND MASSSPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1134 AND SER-1137, ANDMASS SPECTROMETRY.	15302935 [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 THR-1078, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Src-dependent phosphorylation of ROCK participates in regulation offocal adhesion dynamics."; Lee H.H., Tien S.C., Jou T.S., Chang Y.C., Jhong J.G., Chang Z.F.; J. Cell Sci. 123:3368-3377(2010). Cited for: PHOSPHORYLATION AT TYR-722.	20826462 [Abstract]
"Regulation of RhoA-dependent ROCKII activation by Shp2."; Lee H.H., Chang Z.F.; J. Cell Biol. 181:999-1012(2008). Cited for: PHOSPHORYLATION AT TYR-722, AND DEPHOSPHORYLATION.	18559669 [Abstract]