dbPTM

ARHG2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ARHG2_HUMAN
UniProt AC	Q92974
Protein Name	Rho guanine nucleotide exchange factor 2
Gene Name	ARHGEF2
Organism	Homo sapiens (Human).
Sequence Length	986
Subcellular Localization	Cytoplasm, cytoskeleton . Cytoplasm . Cell junction, tight junction . Golgi apparatus . Cytoplasm, cytoskeleton, spindle . Cell projection, ruffle membrane . Cytoplasmic vesicle . Localizes to the tips of cortical microtubules of the mitotic spindle
Protein Description	Activates Rho-GTPases by promoting the exchange of GDP for GTP. May be involved in epithelial barrier permeability, cell motility and polarization, dendritic spine morphology, antigen presentation, leukemic cell differentiation, cell cycle regulation, innate immune response, and cancer. Binds Rac-GTPases, but does not seem to promote nucleotide exchange activity toward Rac-GTPases, which was uniquely reported in PubMed:9857026. May stimulate instead the cortical activity of Rac. Inactive toward CDC42, TC10, or Ras-GTPases. Forms an intracellular sensing system along with NOD1 for the detection of microbial effectors during cell invasion by pathogens. Required for RHOA and RIP2 dependent NF-kappaB signaling pathways activation upon S.flexneri cell invasion. Involved not only in sensing peptidoglycan (PGN)-derived muropeptides through NOD1 that is independent of its GEF activity, but also in the activation of NF-kappaB by Shigella effector proteins (IpgB2 and OspB) which requires its GEF activity and the activation of RhoA. Involved in innate immune signaling transduction pathway promoting cytokine IL6/interleukin-6 and TNF-alpha secretion in macrophage upon stimulation by bacterial peptidoglycans; acts as a signaling intermediate between NOD2 receptor and RIPK2 kinase. Contributes to the tyrosine phosphorylation of RIPK2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Overexpression activates Rho-, but not Rac-GTPases, and increases paracellular permeability (By similarity). Involved in neuronal progenitor cell division and differentiation. [PubMed: 28453519 Involved in the migration of precerebellar neurons (By similarity]
Protein Sequence	MSRIESLTRARIDRSRELASKTREKEKMKEAKDARYTNGHLFTTISVSGMTMCYACNKSITAKEALICPTCNVTIHNRCKDTLANCTKVKQKQQKAALLKNNTALQSVSLRSKTTIRERPSSAIYPSDSFRQSLLGSRRGRSSLSLAKSVSTTNIAGHFNDESPLGLRRILSQSTDSLNMRNRTLSVESLIDEAEVIYSELMSDFEMDEKDFAADSWSLAVDSSFLQQHKKEVMKQQDVIYELIQTELHHVRTLKIMTRLFRTGMLEELHLEPGVVQGLFPCVDELSDIHTRFLSQLLERRRQALCPGSTRNFVIHRLGDLLISQFSGPSAEQMCKTYSEFCSRHSKALKLYKELYARDKRFQQFIRKVTRPAVLKRHGVQECILLVTQRITKYPLLISRILQHSHGIEEERQDLTTALGLVKELLSNVDEGIYQLEKGARLQEIYNRMDPRAQTPVPGKGPFGREELLRRKLIHDGCLLWKTATGRFKDVLVLLMTDVLVFLQEKDQKYIFPTLDKPSVVSLQNLIVRDIANQEKGMFLISAAPPEMYEVHTASRDDRSTWIRVIQQSVRTCPSREDFPLIETEDEAYLRRIKMELQQKDRALVELLREKVGLFAEMTHFQAEEDGGSGMALPTLPRGLFRSESLESPRGERLLQDAIREVEGLKDLLVGPGVELLLTPREPALPLEPDSGGNTSPGVTANGEARTFNGSIELCRADSDSSQRDRNGNQLRSPQEEALQRLVNLYGLLHGLQAAVAQQDTLMEARFPEGPERREKLCRANSRDGEAGRAGAAPVAPEKQATELALLQRQHALLQEELRRCRRLGEERATEAGSLEARLRESEQARALLEREAEEARRQLAALGQTEPLPAEAPWARRPVDPRRRSLPAGDALYLSFNPPQPSRGTDRLDLPVTTRSVHRNFEDRERQELGSPEERLQDSSDPDTGSEEEGSSRLSPPHSPRDFTRMQDIPEETESRDGEAVASES

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSRIESLTR ------CCHHHHHHH	41.80	20873877
6	Phosphorylation	--MSRIESLTRARID --CCHHHHHHHHHHH	32.44	20873877
8	Phosphorylation	MSRIESLTRARIDRS CCHHHHHHHHHHHHH	31.40	20873877
46	Phosphorylation	GHLFTTISVSGMTMC CCCEEEEEECCCCEE	14.24	30576142
51	Phosphorylation	TISVSGMTMCYACNK EEEECCCCEEHHCCC	13.96	30576142
63	Ubiquitination	CNKSITAKEALICPT CCCCCCCCCCEECCC	34.56	-
70	Phosphorylation	KEALICPTCNVTIHN CCCEECCCCCEEECC	16.58	27080861
74	Phosphorylation	ICPTCNVTIHNRCKD ECCCCCEEECCHHHH	11.52	27080861
80	Ubiquitination	VTIHNRCKDTLANCT EEECCHHHHHHHCCH	50.97	-
88	Ubiquitination	DTLANCTKVKQKQQK HHHHCCHHHHHHHHH	50.03	-
95	Ubiquitination	KVKQKQQKAALLKNN HHHHHHHHHHHHHCC	32.88	-
100	Methylation	QQKAALLKNNTALQS HHHHHHHHCCHHHHH	49.34	-
100	Ubiquitination	QQKAALLKNNTALQS HHHHHHHHCCHHHHH	49.34	-
100 (in isoform 2)	Ubiquitination	-	49.34	-
103	Phosphorylation	AALLKNNTALQSVSL HHHHHCCHHHHHHCC	37.83	26074081
107	Phosphorylation	KNNTALQSVSLRSKT HCCHHHHHHCCCCCC	17.96	29255136
109	Phosphorylation	NTALQSVSLRSKTTI CHHHHHHCCCCCCCC	24.26	23401153
112	Phosphorylation	LQSVSLRSKTTIRER HHHHCCCCCCCCCCC	39.38	29514088
115	Phosphorylation	VSLRSKTTIRERPSS HCCCCCCCCCCCCCC	23.05	-
121	Phosphorylation	TTIRERPSSAIYPSD CCCCCCCCCCCCCCH	38.33	23401153
122	Phosphorylation	TIRERPSSAIYPSDS CCCCCCCCCCCCCHH	22.74	29255136
125	Phosphorylation	ERPSSAIYPSDSFRQ CCCCCCCCCCHHHHH	9.08	23927012
127	Phosphorylation	PSSAIYPSDSFRQSL CCCCCCCCHHHHHHH	28.99	23927012
129	Phosphorylation	SAIYPSDSFRQSLLG CCCCCCHHHHHHHHC	27.02	23401153
133	Phosphorylation	PSDSFRQSLLGSRRG CCHHHHHHHHCCCCC	22.70	23401153
137	Phosphorylation	FRQSLLGSRRGRSSL HHHHHHCCCCCCHHH	20.83	21712546
142	Phosphorylation	LGSRRGRSSLSLAKS HCCCCCCHHHHHHHH	38.15	22617229
143	Phosphorylation	GSRRGRSSLSLAKSV CCCCCCHHHHHHHHC	22.18	21712546
145	Phosphorylation	RRGRSSLSLAKSVST CCCCHHHHHHHHCCC	28.38	23403867
148	Ubiquitination	RSSLSLAKSVSTTNI CHHHHHHHHCCCCCC	57.60	-
149	Phosphorylation	SSLSLAKSVSTTNIA HHHHHHHHCCCCCCC	18.72	22167270
151	Phosphorylation	LSLAKSVSTTNIAGH HHHHHHCCCCCCCCC	36.28	29255136
152	Phosphorylation	SLAKSVSTTNIAGHF HHHHHCCCCCCCCCC	23.00	29255136
153	Phosphorylation	LAKSVSTTNIAGHFN HHHHCCCCCCCCCCC	19.68	26846344
157 (in isoform 3)	Phosphorylation	-	23.32	28634298
159 (in isoform 3)	Phosphorylation	-	13.92	28634298
162 (in isoform 3)	Phosphorylation	-	56.19	27732954
163	Phosphorylation	AGHFNDESPLGLRRI CCCCCCCCHHHHHHH	28.43	23927012
170 (in isoform 3)	Phosphorylation	-	3.33	28634298
172	Phosphorylation	LGLRRILSQSTDSLN HHHHHHHHHCCCCCC	21.51	29255136
174	Phosphorylation	LRRILSQSTDSLNMR HHHHHHHCCCCCCCC	30.70	19664994
175	Phosphorylation	RRILSQSTDSLNMRN HHHHHHCCCCCCCCC	23.21	29255136
177	Phosphorylation	ILSQSTDSLNMRNRT HHHHCCCCCCCCCCC	23.02	29255136
180	Sulfoxidation	QSTDSLNMRNRTLSV HCCCCCCCCCCCCCH	4.95	21406390
184	Phosphorylation	SLNMRNRTLSVESLI CCCCCCCCCCHHHHH	27.25	26074081
184 (in isoform 2)	Phosphorylation	-	27.25	28634298
186	Phosphorylation	NMRNRTLSVESLIDE CCCCCCCCHHHHHCH	24.19	26074081
186 (in isoform 2)	Phosphorylation	-	24.19	28634298
189	Phosphorylation	NRTLSVESLIDEAEV CCCCCHHHHHCHHHH	28.59	26074081
189 (in isoform 2)	Phosphorylation	-	28.59	27732954
197 (in isoform 2)	Phosphorylation	-	2.05	28634298
198	Phosphorylation	IDEAEVIYSELMSDF HCHHHHHHHHHHCCC	10.98	27732954
199	Phosphorylation	DEAEVIYSELMSDFE CHHHHHHHHHHCCCC	17.09	27732954
230	Ubiquitination	SSFLQQHKKEVMKQQ HHHHHHHHHHHHHHH	46.41	-
235	Ubiquitination	QHKKEVMKQQDVIYE HHHHHHHHHHHHHHH	50.40	-
255	Acetylation	LHHVRTLKIMTRLFR HHHHHHHHHHHHHHH	29.80	27452117
255	Ubiquitination	LHHVRTLKIMTRLFR HHHHHHHHHHHHHHH	29.80	-
258	Phosphorylation	VRTLKIMTRLFRTGM HHHHHHHHHHHHHCC	27.91	29759185
295	Phosphorylation	DIHTRFLSQLLERRR HHHHHHHHHHHHHHH	18.97	21406692
309	Phosphorylation	RQALCPGSTRNFVIH HHHCCCCCCHHHHHH	14.88	21406692
310	Phosphorylation	QALCPGSTRNFVIHR HHCCCCCCHHHHHHH	35.23	21406692
325	Acetylation	LGDLLISQFSGPSAE HHHHHHHHCCCCCHH	29.54	19608861
335	Glutathionylation	GPSAEQMCKTYSEFC CCCHHHHHHHHHHHH	2.73	22555962
335 (in isoform 2)	Ubiquitination	-	2.73	21906983
336	Ubiquitination	PSAEQMCKTYSEFCS CCHHHHHHHHHHHHH	45.19	21906983
336 (in isoform 1)	Ubiquitination	-	45.19	21906983
347	Ubiquitination	EFCSRHSKALKLYKE HHHHHHHHHHHHHHH	52.17	-
352	Acetylation	HSKALKLYKELYARD HHHHHHHHHHHHHHH	10.79	19608861
353	Acetylation	SKALKLYKELYARDK HHHHHHHHHHHHHHH	52.24	19608861
353	Ubiquitination	SKALKLYKELYARDK HHHHHHHHHHHHHHH	52.24	19608861
356	Phosphorylation	LKLYKELYARDKRFQ HHHHHHHHHHHHHHH	10.73	27259358
376	Methylation	VTRPAVLKRHGVQEC HHHHHHHHHHCHHHH	35.43	-
388	Phosphorylation	QECILLVTQRITKYP HHHHHHHHHHHHHHH	16.46	-
392	Phosphorylation	LLVTQRITKYPLLIS HHHHHHHHHHHHHHH	27.07	-
393	Acetylation	LVTQRITKYPLLISR HHHHHHHHHHHHHHH	42.36	25953088
393	Ubiquitination	LVTQRITKYPLLISR HHHHHHHHHHHHHHH	42.36	-
394	Phosphorylation	VTQRITKYPLLISRI HHHHHHHHHHHHHHH	7.17	-
427	Phosphorylation	GLVKELLSNVDEGIY HHHHHHHCCCCHHHH	47.64	-
430 (in isoform 3)	Ubiquitination	-	53.29	21906983
434	Phosphorylation	SNVDEGIYQLEKGAR CCCCHHHHHHHHHHH	20.22	23071622
438	Ubiquitination	EGIYQLEKGARLQEI HHHHHHHHHHHHHHH	67.47	-
455	Phosphorylation	RMDPRAQTPVPGKGP HCCCCCCCCCCCCCC	25.85	-
460	Ubiquitination	AQTPVPGKGPFGREE CCCCCCCCCCCCHHH	58.29	-
472	Ubiquitination	REELLRRKLIHDGCL HHHHHHHHCHHCCCE	45.41	-
482	Acetylation	HDGCLLWKTATGRFK HCCCEEHHHCCCCHH	28.40	23749302
482	Ubiquitination	HDGCLLWKTATGRFK HCCCEEHHHCCCCHH	28.40	-
509	Ubiquitination	FLQEKDQKYIFPTLD HHHHCCCCCCCCCCC	50.91	-
510	Phosphorylation	LQEKDQKYIFPTLDK HHHCCCCCCCCCCCC	11.36	-
517	Ubiquitination	YIFPTLDKPSVVSLQ CCCCCCCCCCCEEEE	42.16	-
519	Phosphorylation	FPTLDKPSVVSLQNL CCCCCCCCCEEEEHH	40.67	-
522	Phosphorylation	LDKPSVVSLQNLIVR CCCCCCEEEEHHHHH	23.29	-
593 (in isoform 2)	Ubiquitination	-	3.94	21906983
594	Ubiquitination	EAYLRRIKMELQQKD HHHHHHHHHHHHHHH	25.22	21906983
594 (in isoform 1)	Ubiquitination	-	25.22	21906983
600	Ubiquitination	IKMELQQKDRALVEL HHHHHHHHHHHHHHH	35.90	-
629	Phosphorylation	QAEEDGGSGMALPTL ECCCCCCCCCCCCCC	30.81	25332170
643	Phosphorylation	LPRGLFRSESLESPR CCCCCCCCCCCCCHH	24.97	22167270
644	Phosphorylation	PRGLFRSESLESPRG CCCCCCCCCCCCHHH	55.90	18669648
645	Phosphorylation	RGLFRSESLESPRGE CCCCCCCCCCCHHHH	38.39	29255136
647	Phosphorylation	LFRSESLESPRGERL CCCCCCCCCHHHHHH	68.89	18669648
648	Phosphorylation	FRSESLESPRGERLL CCCCCCCCHHHHHHH	25.78	23401153
665 (in isoform 2)	Ubiquitination	-	2.17	21906983
666	Ubiquitination	IREVEGLKDLLVGPG HHHHCCCHHHHCCCC	58.13	2190698
666 (in isoform 1)	Ubiquitination	-	58.13	21906983
679	Phosphorylation	PGVELLLTPREPALP CCCEEEECCCCCCCC	21.92	29255136
688 (in isoform 3)	Ubiquitination	-	45.16	21906983
691	Phosphorylation	ALPLEPDSGGNTSPG CCCCCCCCCCCCCCC	60.35	23401153
694	Phosphorylation	LEPDSGGNTSPGVTA CCCCCCCCCCCCEEC	40.69	18669648
695	Phosphorylation	EPDSGGNTSPGVTAN CCCCCCCCCCCEECC	39.30	29255136
696	Phosphorylation	PDSGGNTSPGVTANG CCCCCCCCCCEECCC	24.53	29255136
700	Phosphorylation	GNTSPGVTANGEART CCCCCCEECCCCEEE	21.96	22167270
707	Phosphorylation	TANGEARTFNGSIEL ECCCCEEEECCEEEE	28.62	26074081
711	Phosphorylation	EARTFNGSIELCRAD CEEEECCEEEEEECC	17.62	22617229
719	Phosphorylation	IELCRADSDSSQRDR EEEEECCCCCCCCCC	38.11	26552605
721	Phosphorylation	LCRADSDSSQRDRNG EEECCCCCCCCCCCC	32.11	26552605
722	Phosphorylation	CRADSDSSQRDRNGN EECCCCCCCCCCCCC	33.94	26552605
733	Phosphorylation	RNGNQLRSPQEEALQ CCCCCCCCHHHHHHH	39.26	29255136
760 (in isoform 3)	Ubiquitination	-	29.72	21906983
782	Phosphorylation	EKLCRANSRDGEAGR HHHHHHCCCCCCCCC	30.66	26846344
799	Acetylation	AAPVAPEKQATELAL CCCCCCHHHHHHHHH	44.14	25953088
799	Ubiquitination	AAPVAPEKQATELAL CCCCCCHHHHHHHHH	44.14	-
802	Phosphorylation	VAPEKQATELALLQR CCCHHHHHHHHHHHH	29.10	23312004
830	Phosphorylation	RLGEERATEAGSLEA HHHHHHHHHHCCHHH	32.37	21406692
834	Phosphorylation	ERATEAGSLEARLRE HHHHHHCCHHHHHHH	30.04	21406692
885	Phosphorylation	RPVDPRRRSLPAGDA CCCCCCCCCCCCCCE	43.77	14970201
886	Phosphorylation	PVDPRRRSLPAGDAL CCCCCCCCCCCCCEE	36.57	29255136
894	Phosphorylation	LPAGDALYLSFNPPQ CCCCCEEEEECCCCC	11.30	21945579
896	Phosphorylation	AGDALYLSFNPPQPS CCCEEEEECCCCCCC	14.93	21945579
903	Phosphorylation	SFNPPQPSRGTDRLD ECCCCCCCCCCCCCC	37.79	21945579
904	Methylation	FNPPQPSRGTDRLDL CCCCCCCCCCCCCCC	59.73	-
914	O-linked_Glycosylation	DRLDLPVTTRSVHRN CCCCCCCCCHHHHHC	17.98	23301498
915	Phosphorylation	RLDLPVTTRSVHRNF CCCCCCCCHHHHHCH	22.60	24247654
932	Phosphorylation	RERQELGSPEERLQD HHHHHHCCHHHHHCC	41.59	29255136
940	Phosphorylation	PEERLQDSSDPDTGS HHHHHCCCCCCCCCC	24.55	29255136
941	Phosphorylation	EERLQDSSDPDTGSE HHHHCCCCCCCCCCC	62.54	23927012
945	Phosphorylation	QDSSDPDTGSEEEGS CCCCCCCCCCCCCCC	48.25	29255136
947	Phosphorylation	SSDPDTGSEEEGSSR CCCCCCCCCCCCCCC	43.88	29255136
952	Phosphorylation	TGSEEEGSSRLSPPH CCCCCCCCCCCCCCC	18.63	29255136
953	Phosphorylation	GSEEEGSSRLSPPHS CCCCCCCCCCCCCCC	48.36	29255136
956	Phosphorylation	EEGSSRLSPPHSPRD CCCCCCCCCCCCCCC	34.96	29255136
960	Phosphorylation	SRLSPPHSPRDFTRM CCCCCCCCCCCCCCC	27.66	29255136
965	Phosphorylation	PHSPRDFTRMQDIPE CCCCCCCCCCCCCCC	29.53	21082442
967	Sulfoxidation	SPRDFTRMQDIPEET CCCCCCCCCCCCCHH	3.69	21406390
974	Phosphorylation	MQDIPEETESRDGEA CCCCCCHHCCCCCCC	37.28	28348404
976	Phosphorylation	DIPEETESRDGEAVA CCCCHHCCCCCCCCC	42.99	28348404
984	Phosphorylation	RDGEAVASES----- CCCCCCCCCC-----	100.00	25262027
986	Phosphorylation	GEAVASES------- CCCCCCCC-------	100.00	23090842

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
143	S	Phosphorylation	Kinase	PAK4	O96013	Uniprot
143	S	Phosphorylation	Kinase	MARK2	Q7KZI7	PSP
151	S	Phosphorylation	Kinase	MARK3	P27448	PSP
172	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
172	S	Phosphorylation	Kinase	MARK2	Q7KZI7	PSP
186	S	Phosphorylation	Kinase	MARK2	Q7KZI7	PSP
678	T	Phosphorylation	Kinase	MAPK3	P27361	GPS
679	T	Phosphorylation	Kinase	ERK1	P27361	PSP
679	T	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
679	T	Phosphorylation	Kinase	ERK2	P28482	PSP
885	S	Phosphorylation	Kinase	PAK1	Q13153	PSP
885	S	Phosphorylation	Kinase	PAK1	Q13153	PhosphoELM
885	S	Phosphorylation	Kinase	MARK2	Q7KZI7	PSP
885	S	Phosphorylation	Kinase	PAK4	O96013	PSP
886	S	Phosphorylation	Kinase	AURA	O14965	PSP
886	S	Phosphorylation	Kinase	PAK1	Q13153	Uniprot
896	S	Phosphorylation	Kinase	PAK4	O96013	Uniprot
959	S	Phosphorylation	Kinase	MARK2	Q7KZI7	PSP
959	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
960	S	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
886	S	Phosphorylation		14970201
Phosphorylation of Ser-886 by PAK1 induces binding to protein YWHAZ, promoting its relocation to microtubules and the inhibition of its activity.

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 ARHG2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
1433T_HUMAN	YWHAQ	physical	14970201
RAC1_HUMAN	RAC1	physical	11595749
RHOA_HUMAN	RHOA	physical	9857026
PLCG1_HUMAN	PLCG1	physical	19805522
MARK2_HUMAN	MARK2	physical	22072711
1433Z_HUMAN	YWHAZ	physical	22072711
RP25L_HUMAN	RPP25L	physical	25416956
KLC2_HUMAN	KLC2	physical	26344197
PRDX1_HUMAN	PRDX1	physical	26344197
PSME3_HUMAN	PSME3	physical	26344197
MARK2_HUMAN	MARK2	physical	21513698

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 ARHG2_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-353, 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-151; SER-163; SER-172;SER-174; THR-679; SER-691; SER-696; SER-886; SER-941; THR-945;SER-947; SER-953; SER-956 AND SER-960, 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-932, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-177 ANDSER-696, 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-163; SER-645; SER-648;SER-696; SER-886; TYR-894; SER-932; SER-940; SER-941; SER-956 ANDSER-960, AND MASS SPECTROMETRY.	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-149; THR-152; THR-153AND SER-163, AND MASS SPECTROMETRY.	18220336 [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 SER-645, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645, AND MASSSPECTROMETRY.	19007248 [Abstract]
"GEF-H1 modulates localized RhoA activation during cytokinesis underthe control of mitotic kinases."; Birkenfeld J., Nalbant P., Bohl B.P., Pertz O., Hahn K.M.,Bokoch G.M.; Dev. Cell 12:699-712(2007). Cited for: PHOSPHORYLATION AT SER-886 AND SER-960, INTERACTION WITH AURKA, ANDSUBCELLULAR LOCATION.	17488622 [Abstract]
"Phosphoproteome analysis of the human mitotic spindle."; Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-696, ANDMASS SPECTROMETRY.	16565220 [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-696, AND MASSSPECTROMETRY.	16964243 [Abstract]
"PAK4 mediates morphological changes through the regulation of GEF-H1."; Callow M.G., Zozulya S., Gishizky M.L., Jallal B., Smeal T.; J. Cell Sci. 118:1861-1872(2005). Cited for: PHOSPHORYLATION AT SER-143 AND SER-896, MUTAGENESIS OF SER-143 ANDSER-896, SUBCELLULAR LOCATION, AND INTERACTION WITH PAK4.	15827085 [Abstract]
"p21-activated kinase 1 phosphorylates and regulates 14-3-3 binding toGEF-H1, a microtubule-localized Rho exchange factor."; Zenke F.T., Krendel M., DerMardirossian C., King C.C., Bohl B.P.,Bokoch G.M.; J. Biol. Chem. 279:18392-18400(2004). Cited for: PHOSPHORYLATION AT SER-886, AND INTERACTION WITH 14-3-3 ZETA.	14970201 [Abstract]
"ERK1/2 phosphorylate GEF-H1 to enhance its guanine nucleotideexchange activity toward RhoA."; Fujishiro S.H., Tanimura S., Mure S., Kashimoto Y., Watanabe K.,Kohno M.; Biochem. Biophys. Res. Commun. 368:162-167(2008). Cited for: PHOSPHORYLATION AT THR-679, INTERACTION WITH MAPK1, AND MUTAGENESIS OFTHR-679.	18211802 [Abstract]

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