dbPTM

RGAP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RGAP1_HUMAN
UniProt AC	Q9H0H5
Protein Name	Rac GTPase-activating protein 1
Gene Name	RACGAP1 {ECO:0000312\|HGNC:HGNC:9804}
Organism	Homo sapiens (Human).
Sequence Length	632
Subcellular Localization	Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, spindle. Cytoplasmic vesicle, secretory vesicle, acrosome. Cleavage furrow. Midbody, Midbody ring . Cell membrane Peripheral membrane protein Cytoplasmic side. Colocalizes with RND2 in Golgi-derived proa
Protein Description	Component of the centralspindlin complex that serves as a microtubule-dependent and Rho-mediated signaling required for the myosin contractile ring formation during the cell cycle cytokinesis. Required for proper attachment of the midbody to the cell membrane during cytokinesis. Plays key roles in controlling cell growth and differentiation of hematopoietic cells through mechanisms other than regulating Rac GTPase activity. Also involved in the regulation of growth-related processes in adipocytes and myoblasts. May be involved in regulating spermatogenesis and in the RACGAP1 pathway in neuronal proliferation. Shows strong GAP (GTPase activation) activity towards CDC42 and RAC1 and less towards RHOA. Essential for the early stages of embryogenesis. May play a role in regulating cortical activity through RHOA during cytokinesis. May participate in the regulation of sulfate transport in male germ cells..
Protein Sequence	MDTMMLNVRNLFEQLVRRVEILSEGNEVQFIQLAKDFEDFRKKWQRTDHELGKYKDLLMKAETERSALDVKLKHARNQVDVEIKRRQRAEADCEKLERQIQLIREMLMCDTSGSIQLSEEQKSALAFLNRGQPSSSNAGNKRLSTIDESGSILSDISFDKTDESLDWDSSLVKTFKLKKREKRRSTSRQFVDGPPGPVKKTRSIGSAVDQGNESIVAKTTVTVPNDGGPIEAVSTIETVPYWTRSRRKTGTLQPWNSDSTLNSRQLEPRTETDSVGTPQSNGGMRLHDFVSKTVIKPESCVPCGKRIKFGKLSLKCRDCRVVSHPECRDRCPLPCIPTLIGTPVKIGEGMLADFVSQTSPMIPSIVVHCVNEIEQRGLTETGLYRISGCDRTVKELKEKFLRVKTVPLLSKVDDIHAICSLLKDFLRNLKEPLLTFRLNRAFMEAAEITDEDNSIAAMYQAVGELPQANRDTLAFLMIHLQRVAQSPHTKMDVANLAKVFGPTIVAHAVPNPDPVTMLQDIKRQPKVVERLLSLPLEYWSQFMMVEQENIDPLHVIENSNAFSTPQTPDIKVSLLGPVTTPEHQLLKTPSSSSLSQRVRSTLTKNTPRFGSKSKSATNLGRQGNFFASPMLK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDTMMLNV -------CCCHHHHH	9.75	22814378
3	Phosphorylation	-----MDTMMLNVRN -----CCCHHHHHHH	11.81	20068231
53	Acetylation	RTDHELGKYKDLLMK HCHHHHHHHHHHHHH	62.85	25953088
53	Ubiquitination	RTDHELGKYKDLLMK HCHHHHHHHHHHHHH	62.85	-
60	Sumoylation	KYKDLLMKAETERSA HHHHHHHHHHHHHHH	42.94	-
60	Sumoylation	KYKDLLMKAETERSA HHHHHHHHHHHHHHH	42.94	-
60	Ubiquitination	KYKDLLMKAETERSA HHHHHHHHHHHHHHH	42.94	-
63	Phosphorylation	DLLMKAETERSALDV HHHHHHHHHHHHHHH	41.37	29759185
66	Phosphorylation	MKAETERSALDVKLK HHHHHHHHHHHHHHH	27.27	29759185
71	Ubiquitination	ERSALDVKLKHARNQ HHHHHHHHHHHHHHH	52.03	-
84	Ubiquitination	NQVDVEIKRRQRAEA HHCHHHHHHHHHHHH	28.20	-
95	Acetylation	RAEADCEKLERQIQL HHHHHHHHHHHHHHH	63.08	26051181
95	Ubiquitination	RAEADCEKLERQIQL HHHHHHHHHHHHHHH	63.08	-
111	Phosphorylation	REMLMCDTSGSIQLS HHHHCCCCCCCEECC	30.02	27251275
112	Phosphorylation	EMLMCDTSGSIQLSE HHHCCCCCCCEECCH	19.79	29978859
114	Phosphorylation	LMCDTSGSIQLSEEQ HCCCCCCCEECCHHH	13.61	27050516
123	Phosphorylation	QLSEEQKSALAFLNR ECCHHHHHHHHHHHC	28.36	30266825
134	Phosphorylation	FLNRGQPSSSNAGNK HHHCCCCCCCCCCCC	38.21	29514088
135	Phosphorylation	LNRGQPSSSNAGNKR HHCCCCCCCCCCCCC	34.00	29514088
136	Phosphorylation	NRGQPSSSNAGNKRL HCCCCCCCCCCCCCC	34.73	29514088
141	Ubiquitination	SSSNAGNKRLSTIDE CCCCCCCCCCCCCCC	54.52	-
144	Phosphorylation	NAGNKRLSTIDESGS CCCCCCCCCCCCCCC	27.61	17081983
145	Phosphorylation	AGNKRLSTIDESGSI CCCCCCCCCCCCCCC	36.72	14744859
149	Phosphorylation	RLSTIDESGSILSDI CCCCCCCCCCCEEEC	33.81	22115753
151	Phosphorylation	STIDESGSILSDISF CCCCCCCCCEEECCC	29.63	22115753
154	Phosphorylation	DESGSILSDISFDKT CCCCCCEEECCCCCC	31.09	29255136
157	Phosphorylation	GSILSDISFDKTDES CCCEEECCCCCCCCC	32.17	29255136
161	Phosphorylation	SDISFDKTDESLDWD EECCCCCCCCCCCCC	47.01	16565220
164	Phosphorylation	SFDKTDESLDWDSSL CCCCCCCCCCCCHHH	34.14	25159151
169	Phosphorylation	DESLDWDSSLVKTFK CCCCCCCHHHHHHHC	22.71	25159151
170	Phosphorylation	ESLDWDSSLVKTFKL CCCCCCHHHHHHHCC	34.41	25159151
173	Ubiquitination	DWDSSLVKTFKLKKR CCCHHHHHHHCCCCH	54.24	21890473
185	Phosphorylation	KKREKRRSTSRQFVD CCHHHHHCCCCCCCC	34.46	14744859
186	Phosphorylation	KREKRRSTSRQFVDG CHHHHHCCCCCCCCC	26.56	14744859
187	Phosphorylation	REKRRSTSRQFVDGP HHHHHCCCCCCCCCC	25.90	14744859
199	Sumoylation	DGPPGPVKKTRSIGS CCCCCCCCCCCCCCC	52.11	-
199	Acetylation	DGPPGPVKKTRSIGS CCCCCCCCCCCCCCC	52.11	25953088
199	Sumoylation	DGPPGPVKKTRSIGS CCCCCCCCCCCCCCC	52.11	-
199	Ubiquitination	DGPPGPVKKTRSIGS CCCCCCCCCCCCCCC	52.11	21890473
200	Ubiquitination	GPPGPVKKTRSIGSA CCCCCCCCCCCCCCE	49.78	-
201	Phosphorylation	PPGPVKKTRSIGSAV CCCCCCCCCCCCCEE	24.75	25159151
203	Phosphorylation	GPVKKTRSIGSAVDQ CCCCCCCCCCCEECC	36.21	29255136
206	Phosphorylation	KKTRSIGSAVDQGNE CCCCCCCCEECCCCC	24.37	23927012
214	Phosphorylation	AVDQGNESIVAKTTV EECCCCCEEEEEEEE	26.77	30266825
219	Phosphorylation	NESIVAKTTVTVPND CCEEEEEEEEECCCC	19.43	20068231
220	Phosphorylation	ESIVAKTTVTVPNDG CEEEEEEEEECCCCC	17.30	20068231
222	Phosphorylation	IVAKTTVTVPNDGGP EEEEEEEECCCCCCC	28.31	20068231
234	O-linked_Glycosylation	GGPIEAVSTIETVPY CCCEEEEEEEEECCC	30.62	30379171
234	Phosphorylation	GGPIEAVSTIETVPY CCCEEEEEEEEECCC	30.62	20068231
235	Phosphorylation	GPIEAVSTIETVPYW CCEEEEEEEEECCCC	19.08	20068231
238	Phosphorylation	EAVSTIETVPYWTRS EEEEEEEECCCCCCC	23.95	20068231
241	Phosphorylation	STIETVPYWTRSRRK EEEEECCCCCCCCCC	18.31	25884760
243	Phosphorylation	IETVPYWTRSRRKTG EEECCCCCCCCCCCC	16.96	20068231
248	Sumoylation	YWTRSRRKTGTLQPW CCCCCCCCCCCCCCC	50.63	-
248	Sumoylation	YWTRSRRKTGTLQPW CCCCCCCCCCCCCCC	50.63	28112733
248	Ubiquitination	YWTRSRRKTGTLQPW CCCCCCCCCCCCCCC	50.63	21890473
249	Phosphorylation	WTRSRRKTGTLQPWN CCCCCCCCCCCCCCC	33.32	25159151
251	Phosphorylation	RSRRKTGTLQPWNSD CCCCCCCCCCCCCCC	27.70	25159151
257	Phosphorylation	GTLQPWNSDSTLNSR CCCCCCCCCCCCCCC	29.12	22167270
259	Phosphorylation	LQPWNSDSTLNSRQL CCCCCCCCCCCCCCC	34.32	22167270
260	Phosphorylation	QPWNSDSTLNSRQLE CCCCCCCCCCCCCCC	34.64	22167270
263	Phosphorylation	NSDSTLNSRQLEPRT CCCCCCCCCCCCCCC	25.23	30108239
270	Phosphorylation	SRQLEPRTETDSVGT CCCCCCCCCCCCCCC	54.69	28450419
272	Phosphorylation	QLEPRTETDSVGTPQ CCCCCCCCCCCCCCC	32.72	21815630
274	Phosphorylation	EPRTETDSVGTPQSN CCCCCCCCCCCCCCC	29.84	25159151
277	Phosphorylation	TETDSVGTPQSNGGM CCCCCCCCCCCCCCC	18.92	25159151
280	Phosphorylation	DSVGTPQSNGGMRLH CCCCCCCCCCCCCHH	38.35	25159151
291	Phosphorylation	MRLHDFVSKTVIKPE CCHHHEEECCCCCCH	23.70	26471730
292	Ubiquitination	RLHDFVSKTVIKPES CHHHEEECCCCCCHH	41.32	21890473
293	Phosphorylation	LHDFVSKTVIKPESC HHHEEECCCCCCHHH	21.69	29396449
296	Sumoylation	FVSKTVIKPESCVPC EEECCCCCCHHHCCC	38.09	-
296	Sumoylation	FVSKTVIKPESCVPC EEECCCCCCHHHCCC	38.09	-
296	Ubiquitination	FVSKTVIKPESCVPC EEECCCCCCHHHCCC	38.09	21906983
299	Phosphorylation	KTVIKPESCVPCGKR CCCCCCHHHCCCCCE	29.01	29396449
305	Acetylation	ESCVPCGKRIKFGKL HHHCCCCCEEEECCE	58.63	25953088
305	Ubiquitination	ESCVPCGKRIKFGKL HHHCCCCCEEEECCE	58.63	-
311	Sumoylation	GKRIKFGKLSLKCRD CCEEEECCEEEEECC	37.73	-
311	Acetylation	GKRIKFGKLSLKCRD CCEEEECCEEEEECC	37.73	25953088
311	Sumoylation	GKRIKFGKLSLKCRD CCEEEECCEEEEECC	37.73	-
313	Phosphorylation	RIKFGKLSLKCRDCR EEEECCEEEEECCCE	29.30	23312004
338	Phosphorylation	CPLPCIPTLIGTPVK CCCCCCCCCCCCCEE	15.88	30266825
342	Phosphorylation	CIPTLIGTPVKIGEG CCCCCCCCCEEECCC	20.22	29255136
356	Phosphorylation	GMLADFVSQTSPMIP CHHHHHHHCCCCCCC	27.95	25627689
358	Phosphorylation	LADFVSQTSPMIPSI HHHHHHCCCCCCCHH	27.56	24719451
359	Phosphorylation	ADFVSQTSPMIPSIV HHHHHCCCCCCCHHH	12.58	25159151
387	Phosphorylation	ETGLYRISGCDRTVK HHCCEECCCCCCHHH	25.11	22817900
404	Sumoylation	KEKFLRVKTVPLLSK HHHHCCCCCCCCCCC	37.05	28112733
404	Ubiquitination	KEKFLRVKTVPLLSK HHHHCCCCCCCCCCC	37.05	-
405	Phosphorylation	EKFLRVKTVPLLSKV HHHCCCCCCCCCCCH	25.21	20363803
410	Phosphorylation	VKTVPLLSKVDDIHA CCCCCCCCCHHHHHH	38.01	15108802
411	Ubiquitination	KTVPLLSKVDDIHAI CCCCCCCCHHHHHHH	50.05	-
420	Phosphorylation	DDIHAICSLLKDFLR HHHHHHHHHHHHHHH	30.53	24719451
423	Ubiquitination	HAICSLLKDFLRNLK HHHHHHHHHHHHHCC	52.29	-
430	2-Hydroxyisobutyrylation	KDFLRNLKEPLLTFR HHHHHHCCCCHHHHH	61.92	-
430	Acetylation	KDFLRNLKEPLLTFR HHHHHHCCCCHHHHH	61.92	26051181
430	Ubiquitination	KDFLRNLKEPLLTFR HHHHHHCCCCHHHHH	61.92	21890473
490	Ubiquitination	VAQSPHTKMDVANLA HHCCCCCCCCHHHHH	30.03	21890473
522	Ubiquitination	VTMLQDIKRQPKVVE CCHHHHHHHCHHHHH	53.95	-
533	Phosphorylation	KVVERLLSLPLEYWS HHHHHHHHCCHHHHH	32.31	20068231
538	Phosphorylation	LLSLPLEYWSQFMMV HHHCCHHHHHHHHCE	20.31	20068231
540	Phosphorylation	SLPLEYWSQFMMVEQ HCCHHHHHHHHCEEC	16.79	20068231
559	Phosphorylation	PLHVIENSNAFSTPQ CCEEEECCCCCCCCC	19.42	20068231
563	Phosphorylation	IENSNAFSTPQTPDI EECCCCCCCCCCCCC	36.45	20068231
564	Phosphorylation	ENSNAFSTPQTPDIK ECCCCCCCCCCCCCE	16.98	20068231
567	Phosphorylation	NAFSTPQTPDIKVSL CCCCCCCCCCCEEEE	24.92	20068231
571	Sumoylation	TPQTPDIKVSLLGPV CCCCCCCEEEEECCC	32.90	-
573	Phosphorylation	QTPDIKVSLLGPVTT CCCCCEEEEECCCCC	16.93	23927012
579	Phosphorylation	VSLLGPVTTPEHQLL EEEECCCCCCHHHCC	39.50	30266825
580	Phosphorylation	SLLGPVTTPEHQLLK EEECCCCCCHHHCCC	27.24	29255136
587	Methylation	TPEHQLLKTPSSSSL CCHHHCCCCCCCCCH	67.96	30985377
587	Ubiquitination	TPEHQLLKTPSSSSL CCHHHCCCCCCCCCH	67.96	21890473
588	Dephosphorylation	PEHQLLKTPSSSSLS CHHHCCCCCCCCCHH	28.51	18201571
588	Phosphorylation	PEHQLLKTPSSSSLS CHHHCCCCCCCCCHH	28.51	30266825
590	Phosphorylation	HQLLKTPSSSSLSQR HHCCCCCCCCCHHHH	48.35	30266825
591	O-linked_Glycosylation	QLLKTPSSSSLSQRV HCCCCCCCCCHHHHH	25.75	30379171
591	Phosphorylation	QLLKTPSSSSLSQRV HCCCCCCCCCHHHHH	25.75	30266825
592	Phosphorylation	LLKTPSSSSLSQRVR CCCCCCCCCHHHHHH	39.37	30266825
593	Phosphorylation	LKTPSSSSLSQRVRS CCCCCCCCHHHHHHH	33.71	30266825
595	Phosphorylation	TPSSSSLSQRVRSTL CCCCCCHHHHHHHHH	20.21	25159151
600	Phosphorylation	SLSQRVRSTLTKNTP CHHHHHHHHHCCCCC	25.55	25159151
601	Phosphorylation	LSQRVRSTLTKNTPR HHHHHHHHHCCCCCC	28.07	25159151
603	Phosphorylation	QRVRSTLTKNTPRFG HHHHHHHCCCCCCCC	23.49	25159151
604	Ubiquitination	RVRSTLTKNTPRFGS HHHHHHCCCCCCCCC	63.03	-
606	Phosphorylation	RSTLTKNTPRFGSKS HHHHCCCCCCCCCCC	19.87	25159151
611	Phosphorylation	KNTPRFGSKSKSATN CCCCCCCCCCCCCCC	30.92	22199227
613	Phosphorylation	TPRFGSKSKSATNLG CCCCCCCCCCCCCCC	33.27	24719451
614	Methylation	PRFGSKSKSATNLGR CCCCCCCCCCCCCCC	48.09	80499953
614	Ubiquitination	PRFGSKSKSATNLGR CCCCCCCCCCCCCCC	48.09	-
615	Phosphorylation	RFGSKSKSATNLGRQ CCCCCCCCCCCCCCC	47.63	30576142
617	Phosphorylation	GSKSKSATNLGRQGN CCCCCCCCCCCCCCC	37.76	29970186
628	Phosphorylation	RQGNFFASPMLK--- CCCCCCCCCCCC---	12.99	22167270
632	Acetylation	FFASPMLK------- CCCCCCCC-------	52.63	71323

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
149	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot
157	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot
164	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot
170	S	Phosphorylation	Kinase	PLK1	P53350	Uniprot
203	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
214	S	Phosphorylation	Kinase	PLK1	P53350	PSP
249	T	Phosphorylation	Kinase	AKT2	P31751	PSP
249	T	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
260	T	Phosphorylation	Kinase	PLK1	P53350	PSP
387	S	Phosphorylation	Kinase	AURB	Q96GD4	PSP
410	S	Phosphorylation	Kinase	AURKB	Q96GD4	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
157	S	Phosphorylation	19468302
Phosphorylation on Ser-157 does not appear to contribute to binding to ECT2.
164	S	Phosphorylation	17081983
Phosphorylation on Ser-164 plays a major role in mediating interaction with ECT2.
387	S	Phosphorylation	12689593
Phosphorylation by AURKB on Ser-387 at the midbody is, at least in part, responsible for exerting its latent GAP activity towards RhoA.

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 RGAP1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RND2_HUMAN	RND2	physical	12590651
S26A8_HUMAN	SLC26A8	physical	11278976
NEMO_HUMAN	IKBKG	physical	18511905
PTPA_HUMAN	PPP2R4	physical	18201571
ECT2_HUMAN	ECT2	physical	18201571
TANK_HUMAN	TANK	physical	21988832
TXD11_HUMAN	TXNDC11	physical	21988832
PSMD1_HUMAN	PSMD1	physical	26344197
AKT2_HUMAN	AKT2	physical	26496610
ENTP6_HUMAN	ENTPD6	physical	26496610
DLG3_HUMAN	DLG3	physical	26496610
HMGA1_HUMAN	HMGA1	physical	26496610
DHB4_HUMAN	HSD17B4	physical	26496610
IPP_HUMAN	IPP	physical	26496610
PCNT_HUMAN	PCNT	physical	26496610
TRI27_HUMAN	TRIM27	physical	26496610
1433G_HUMAN	YWHAG	physical	26496610
PKP4_HUMAN	PKP4	physical	26496610
BCL7B_HUMAN	BCL7B	physical	26496610
MED21_HUMAN	MED21	physical	26496610
KIF23_HUMAN	KIF23	physical	26496610
RPGF2_HUMAN	RAPGEF2	physical	26496610
C2CD5_HUMAN	C2CD5	physical	26496610
BAZ2A_HUMAN	BAZ2A	physical	26496610
RB6I2_HUMAN	ERC1	physical	26496610
DAPK2_HUMAN	DAPK2	physical	26496610
CD2AP_HUMAN	CD2AP	physical	26496610
TECT3_HUMAN	TCTN3	physical	26496610
ANR11_HUMAN	ANKRD11	physical	26496610
RM35_HUMAN	MRPL35	physical	26496610
RSRC1_HUMAN	RSRC1	physical	26496610
STX18_HUMAN	STX18	physical	26496610
RAIN_HUMAN	RASIP1	physical	26496610
SYBU_HUMAN	SYBU	physical	26496610
RABL6_HUMAN	RABL6	physical	26496610
MICA3_HUMAN	MICAL3	physical	26496610
TPC11_HUMAN	TRAPPC11	physical	26496610
SHCBP_HUMAN	SHCBP1	physical	26496610
ACTL8_HUMAN	ACTL8	physical	26496610
ARI5B_HUMAN	ARID5B	physical	26496610
CHD6_HUMAN	CHD6	physical	26496610
STON2_HUMAN	STON2	physical	26496610
PHLB2_HUMAN	PHLDB2	physical	26496610
EOGT_HUMAN	EOGT	physical	26496610
KIF23_HUMAN	KIF23	physical	28514442
SHCBP_HUMAN	SHCBP1	physical	28514442
KLHL8_HUMAN	KLHL8	physical	28514442
CD2AP_HUMAN	CD2AP	physical	28514442
CSTF1_HUMAN	CSTF1	physical	28514442
CHK1_HUMAN	CHEK1	physical	28514442
FA98A_HUMAN	FAM98A	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 RGAP1_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-154; SER-157; SER-203AND SER-206, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Polo-like kinase 1 directs assembly of the HsCyk-4 RhoGAP/Ect2 RhoGEFcomplex to initiate cleavage furrow formation."; Wolfe B.A., Takaki T., Petronczki M., Glotzer M.; PLoS Biol. 7:E1000110-E1000110(2009). Cited for: FUNCTION, INTERACTION WITH ECT2, PHOSPHORYLATION AT SER-149; SER-157;SER-164 AND SER-170, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-149;SER-157; SER-164 AND SER-170.	19468300 [Abstract]
"Plk1 self-organization and priming phosphorylation of HsCYK-4 at thespindle midzone regulate the onset of division in human cells."; Burkard M.E., Maciejowski J., Rodriguez-Bravo V., Repka M.,Lowery D.M., Clauser K.R., Zhang C., Shokat K.M., Carr S.A.,Yaffe M.B., Jallepalli P.V.; PLoS Biol. 7:E1000111-E1000111(2009). Cited for: FUNCTION, PHOSPHORYLATION AT SER-157; SER-164; SER-170; SER-214 ANDTHR-260, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-157; SER-164;SER-170 AND SER-214.	19468302 [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-203; SER-206; SER-257;THR-342; SER-573; THR-580; THR-588; SER-591; SER-600; THR-601; THR-606AND SER-628, AND MASS SPECTROMETRY.	18669648 [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-144; THR-145; SER-154;SER-157; SER-170; SER-203; SER-206; SER-214; SER-591; SER-592 ANDSER-593, AND MASS SPECTROMETRY.	19007248 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND SER-187, ANDMASS SPECTROMETRY.	17287340 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-606 AND SER-628, ANDMASS SPECTROMETRY.	17924679 [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 THR-161; SER-164; SER-170;SER-203; SER-214; THR-342; THR-580; THR-588; SER-590 AND SER-628, 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-203, 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 THR-161; SER-164; SER-203AND SER-206, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Phosphorylation by aurora B converts MgcRacGAP to a RhoGAP duringcytokinesis."; Minoshima Y., Kawashima T., Hirose K., Tonozuka Y., Kawajiri A.,Bao Y.C., Deng X., Tatsuka M., Narumiya S., May W.S. Jr., Nosaka T.,Semba K., Inoue T., Satoh T., Inagaki M., Kitamura T.; Dev. Cell 4:549-560(2003). Cited for: INTERACTION WITH AURKB, AND PHOSPHORYLATION AT SER-387.	12689593 [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 THR-580, AND MASSSPECTROMETRY.	18691976 [Abstract]

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