dbPTM

RHG35_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RHG35_HUMAN
UniProt AC	Q9NRY4
Protein Name	Rho GTPase-activating protein 35 {ECO:0000312\|HGNC:HGNC:4591}
Gene Name	ARHGAP35 {ECO:0000312\|HGNC:HGNC:4591}
Organism	Homo sapiens (Human).
Sequence Length	1499
Subcellular Localization	Cytoplasm, cytoskeleton, cilium basal body . Cytoplasm . Nucleus . Cell membrane . In response to integrins and SDC4 and upon phosphorylation by PKC, relocalizes from the cytoplasm to regions of plasma membrane ruffling where it colocalizes with poly
Protein Description	Rho GTPase-activating protein (GAP). [PubMed: 19673492]
Protein Sequence	MMMARKQDVRIPTYNISVVGLSGTEKEKGQCGIGKSCLCNRFVRPSADEFHLDHTSVLSTSDFGGRVVNNDHFLYWGEVSRSLEDCVECKMHIVEQTEFIDDQTFQPHRSTALQPYIKRAAATKLASAEKLMYFCTDQLGLEQDFEQKQMPDGKLLVDGFLLGIDVSRGMNRNFDDQLKFVSNLYNQLAKTKKPIVVVLTKCDEGVERYIRDAHTFALSKKNLQVVETSARSNVNVDLAFSTLVQLIDKSRGKTKIIPYFEALKQQSQQIATAKDKYEWLVSRIVKNHNENWLSVSRKMQASPEYQDYVYLEGTQKAKKLFLQHIHRLKHEHIERRRKLYLAALPLAFEALIPNLDEIDHLSCIKAKKLLETKPEFLKWFVVLEETPWDATSHIDNMENERIPFDLMDTVPAEQLYEAHLEKLRNERKRVEMRRAFKENLETSPFITPGKPWEEARSFIMNEDFYQWLEESVYMDIYGKHQKQIIDKAKEEFQELLLEYSELFYELELDAKPSKEKMGVIQDVLGEEQRFKALQKLQAERDALILKHIHFVYHPTKETCPSCPACVDAKIEHLISSRFIRPSDRNQKNSLSDPNIDRINLVILGKDGLARELANEIRALCTNDDKYVIDGKMYELSLRPIEGNVRLPVNSFQTPTFQPHGCLCLYNSKESLSYVVESIEKSRESTLGRRDNHLVHLPLTLILVNKRGDTSGETLHSLIQQGQQIASKLQCVFLDPASAGIGYGRNINEKQISQVLKGLLDSKRNLNLVSSTASIKDLADVDLRIVMCLMCGDPFSADDILFPVLQSQTCKSSHCGSNNSVLLELPIGLHKKRIELSVLSYHSSFSIRKSRLVHGYIVFYSAKRKASLAMLRAFLCEVQDIIPIQLVALTDGAVDVLDNDLSREQLTEGEEIAQEIDGRFTSIPCSQPQHKLEIFHPFFKDVVEKKNIIEATHMYDNAAEACSTTEEVFNSPRAGSPLCNSNLQDSEEDIEPSYSLFREDTSLPSLSKDHSKLSMELEGNDGLSFIMSNFESKLNNKVPPPVKPKPPVHFEITKGDLSYLDQGHRDGQRKSVSSSPWLPQDGFDPSDYAEPMDAVVKPRNEEENIYSVPHDSTQGKIITIRNINKAQSNGSGNGSDSEMDTSSLERGRKVSIVSKPVLYRTRCTRLGRFASYRTSFSVGSDDELGPIRKKEEDQASQGYKGDNAVIPYETDEDPRRRNILRSLRRNTKKPKPKPRPSITKATWESNYFGVPLTTVVTPEKPIPIFIERCIEYIEATGLSTEGIYRVSGNKSEMESLQRQFDQDHNLDLAEKDFTVNTVAGAMKSFFSELPDPLVPYNMQIDLVEAHKINDREQKLHALKEVLKKFPKENHEVFKYVISHLNKVSHNNKVNLMTSENLSICFWPTLMRPDFSTMDALTATRTYQTIIELFIQQCPFFFYNRPITEPPGARPSSPSAVASTVPFLTSTPVTSQPSPPQSPPPTPQSPMQPLLPSQLQAEHTL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	QDVRIPTYNISVVGL CCCCCCCCEEEEEEC	12.73	22468782
46	Phosphorylation	CNRFVRPSADEFHLD CCCCCCCCCCCCCCC	37.48	-
118	Acetylation	TALQPYIKRAAATKL HHHHHHHHHHHHHHH	30.09	25953088
118	Malonylation	TALQPYIKRAAATKL HHHHHHHHHHHHHHH	30.09	26320211
124	Acetylation	IKRAAATKLASAEKL HHHHHHHHHCCHHHH	37.01	25953088
124	Malonylation	IKRAAATKLASAEKL HHHHHHHHHCCHHHH	37.01	26320211
133	Phosphorylation	ASAEKLMYFCTDQLG CCHHHHHHHHHHHCC	13.11	-
136	Phosphorylation	EKLMYFCTDQLGLEQ HHHHHHHHHHCCCCC	19.51	-
182	Phosphorylation	DDQLKFVSNLYNQLA HHHHHHHHHHHHHHH	25.01	20068231
185	Phosphorylation	LKFVSNLYNQLAKTK HHHHHHHHHHHHCCC	12.71	20068231
193	Acetylation	NQLAKTKKPIVVVLT HHHHCCCCCEEEEEE	45.25	88891
209	Phosphorylation	CDEGVERYIRDAHTF CCHHHHHHHHHHHHH	6.18	-
221	Malonylation	HTFALSKKNLQVVET HHHHCCCCCEEEEEC	60.56	26320211
277	Phosphorylation	IATAKDKYEWLVSRI HHHHHHHHHHHHHHH	23.59	26699800
294	Phosphorylation	NHNENWLSVSRKMQA CCCCCCCCHHHHHCC	15.06	24719451
296	Phosphorylation	NENWLSVSRKMQASP CCCCCCHHHHHCCCH	23.86	28509920
308	Phosphorylation	ASPEYQDYVYLEGTQ CCHHHCCCEEEECHH	3.88	19393245
368	Ubiquitination	LSCIKAKKLLETKPE HHHHHHHHHHHCCHH	64.26	30230243
442	Phosphorylation	AFKENLETSPFITPG HHHHHHCCCCCCCCC	44.88	22199227
443	Phosphorylation	FKENLETSPFITPGK HHHHHCCCCCCCCCC	14.40	22199227
447	Phosphorylation	LETSPFITPGKPWEE HCCCCCCCCCCCHHH	26.77	22199227
457	Phosphorylation	KPWEEARSFIMNEDF CCHHHHHHHHHCHHH	26.60	28674151
471	Phosphorylation	FYQWLEESVYMDIYG HHHHHHHHHCHHHHC	14.79	28674151
575	Phosphorylation	AKIEHLISSRFIRPS HHHHHHHHCCCCCCC	23.09	-
576	Phosphorylation	KIEHLISSRFIRPSD HHHHHHHCCCCCCCC	24.98	-
589	Phosphorylation	SDRNQKNSLSDPNID CCCCCCCCCCCCCCC	35.96	23927012
591	Phosphorylation	RNQKNSLSDPNIDRI CCCCCCCCCCCCCCE	51.33	23927012
625	Acetylation	ALCTNDDKYVIDGKM HHHCCCCCEEECCEE	44.26	26051181
636	Phosphorylation	DGKMYELSLRPIEGN CCEEEEEEECCCCCC	15.47	24719451
655	Phosphorylation	VNSFQTPTFQPHGCL CCCCCCCCCCCCCEE	37.99	28348404
667	Phosphorylation	GCLCLYNSKESLSYV CEEEEECCHHHHHHH	25.01	-
684	Phosphorylation	SIEKSRESTLGRRDN HHHHHHHHHCCCCCC	28.02	28258704
685	Phosphorylation	IEKSRESTLGRRDNH HHHHHHHHCCCCCCC	28.60	28258704
709	Phosphorylation	LVNKRGDTSGETLHS EECCCCCCCHHHHHH	41.26	28555341
761	Phosphorylation	VLKGLLDSKRNLNLV HHHHHHCCCCCCCCC	33.22	26074081
762	Ubiquitination	LKGLLDSKRNLNLVS HHHHHCCCCCCCCCC	45.00	29967540
769	Phosphorylation	KRNLNLVSSTASIKD CCCCCCCCCCCCHHH	25.74	25159151
770	Phosphorylation	RNLNLVSSTASIKDL CCCCCCCCCCCHHHH	22.10	23401153
771	Phosphorylation	NLNLVSSTASIKDLA CCCCCCCCCCHHHHH	19.54	25159151
773	Phosphorylation	NLVSSTASIKDLADV CCCCCCCCHHHHHCC	30.20	28355574
836	Phosphorylation	HKKRIELSVLSYHSS CCCCEEEEEEEECCC	14.28	29083192
839	Phosphorylation	RIELSVLSYHSSFSI CEEEEEEEECCCCCC	20.74	29083192
840	Phosphorylation	IELSVLSYHSSFSIR EEEEEEEECCCCCCC	11.10	29083192
842	Phosphorylation	LSVLSYHSSFSIRKS EEEEEECCCCCCCHH	25.50	29083192
843	Phosphorylation	SVLSYHSSFSIRKSR EEEEECCCCCCCHHH	15.08	24719451
845	Phosphorylation	LSYHSSFSIRKSRLV EEECCCCCCCHHHHH	24.35	24719451
849	Phosphorylation	SSFSIRKSRLVHGYI CCCCCCHHHHHCEEE	22.46	29083192
855	Phosphorylation	KSRLVHGYIVFYSAK HHHHHCEEEEEEECC	4.50	29083192
859	Phosphorylation	VHGYIVFYSAKRKAS HCEEEEEEECCHHHH	9.23	29083192
860	Phosphorylation	HGYIVFYSAKRKASL CEEEEEEECCHHHHH	18.82	29083192
906	Phosphorylation	DLSREQLTEGEEIAQ CCCHHHHCCHHHHHH	41.46	-
951	Phosphorylation	KKNIIEATHMYDNAA HCCHHHHHHCCCCHH	8.39	23403867
954	Phosphorylation	IIEATHMYDNAAEAC HHHHHHCCCCHHHHC	9.84	27080861
962	Phosphorylation	DNAAEACSTTEEVFN CCHHHHCCCHHHHHC	45.47	30266825
963	Phosphorylation	NAAEACSTTEEVFNS CHHHHCCCHHHHHCC	37.80	30266825
964	Phosphorylation	AAEACSTTEEVFNSP HHHHCCCHHHHHCCC	17.54	30266825
970	Phosphorylation	TTEEVFNSPRAGSPL CHHHHHCCCCCCCCC	12.33	29255136
975	Phosphorylation	FNSPRAGSPLCNSNL HCCCCCCCCCCCCCC	17.45	29255136
980	Phosphorylation	AGSPLCNSNLQDSEE CCCCCCCCCCCCCHH	37.61	29255136
985	Phosphorylation	CNSNLQDSEEDIEPS CCCCCCCCHHHCCCC	29.89	29255136
992	Phosphorylation	SEEDIEPSYSLFRED CHHHCCCCHHHHCCC	17.98	28796482
993	Phosphorylation	EEDIEPSYSLFREDT HHHCCCCHHHHCCCC	21.80	28796482
994	Phosphorylation	EDIEPSYSLFREDTS HHCCCCHHHHCCCCC	25.93	28796482
1000	Phosphorylation	YSLFREDTSLPSLSK HHHHCCCCCCCCCCC	27.66	26074081
1001	Phosphorylation	SLFREDTSLPSLSKD HHHCCCCCCCCCCCC	51.08	25159151
1004	Phosphorylation	REDTSLPSLSKDHSK CCCCCCCCCCCCCCC	51.04	21815630
1006	Phosphorylation	DTSLPSLSKDHSKLS CCCCCCCCCCCCCCC	40.13	21815630
1010	Phosphorylation	PSLSKDHSKLSMELE CCCCCCCCCCCEEEC	45.48	27251275
1013	Phosphorylation	SKDHSKLSMELEGND CCCCCCCCEEECCCC	17.59	28348404
1023	Phosphorylation	LEGNDGLSFIMSNFE ECCCCCHHHHHHHHH	20.46	27251275
1057	Phosphorylation	EITKGDLSYLDQGHR EECCCCHHHHCCCCC	28.52	25849741
1058	Phosphorylation	ITKGDLSYLDQGHRD ECCCCHHHHCCCCCC	22.92	27642862
1070	Phosphorylation	HRDGQRKSVSSSPWL CCCCCCCCCCCCCCC	29.44	21945579
1072	Phosphorylation	DGQRKSVSSSPWLPQ CCCCCCCCCCCCCCC	31.99	21945579
1073	Phosphorylation	GQRKSVSSSPWLPQD CCCCCCCCCCCCCCC	37.96	21945579
1074	Phosphorylation	QRKSVSSSPWLPQDG CCCCCCCCCCCCCCC	16.76	21945579
1085	Phosphorylation	PQDGFDPSDYAEPMD CCCCCCHHHCCCCCC	45.13	21945579
1087	Phosphorylation	DGFDPSDYAEPMDAV CCCCHHHCCCCCCEE	19.73	21945579
1096	Ubiquitination	EPMDAVVKPRNEEEN CCCCEEECCCCCCCC	31.49	22817900
1096 (in isoform 1)	Ubiquitination	-	31.49	21906983
1104	Phosphorylation	PRNEEENIYSVPHDS CCCCCCCCEECCCCC	2.83	17389395
1105	Dephosphorylation	RNEEENIYSVPHDST CCCCCCCEECCCCCC	18.39	16513268
1105	Phosphorylation	RNEEENIYSVPHDST CCCCCCCEECCCCCC	18.39	29255136
1106	Phosphorylation	NEEENIYSVPHDSTQ CCCCCCEECCCCCCC	25.94	21945579
1111	Phosphorylation	IYSVPHDSTQGKIIT CEECCCCCCCCEEEE	21.42	21945579
1112	Phosphorylation	YSVPHDSTQGKIITI EECCCCCCCCEEEEE	47.61	21945579
1115	Ubiquitination	PHDSTQGKIITIRNI CCCCCCCEEEEEEEC	22.55	29967540
1127	Phosphorylation	RNINKAQSNGSGNGS EECCHHHCCCCCCCC	48.28	30278072
1130	Phosphorylation	NKAQSNGSGNGSDSE CHHHCCCCCCCCCCC	33.08	23927012
1134	Phosphorylation	SNGSGNGSDSEMDTS CCCCCCCCCCCCCCC	41.80	23927012
1136	Phosphorylation	GSGNGSDSEMDTSSL CCCCCCCCCCCCCHH	36.20	25159151
1140	Phosphorylation	GSDSEMDTSSLERGR CCCCCCCCCHHCCCC	20.93	23927012
1141	Phosphorylation	SDSEMDTSSLERGRK CCCCCCCCHHCCCCC	28.76	23927012
1142	Phosphorylation	DSEMDTSSLERGRKV CCCCCCCHHCCCCCE	36.02	23927012
1150	Phosphorylation	LERGRKVSIVSKPVL HCCCCCEEECCCCCC	21.95	23927012
1153	Phosphorylation	GRKVSIVSKPVLYRT CCCEEECCCCCCCCC	29.58	23927012
1158	Phosphorylation	IVSKPVLYRTRCTRL ECCCCCCCCCCCCCC	15.35	23403867
1170	Phosphorylation	TRLGRFASYRTSFSV CCCCCCEECEEEECC	16.67	30576142
1171	Phosphorylation	RLGRFASYRTSFSVG CCCCCEECEEEECCC	17.93	22199227
1173	Phosphorylation	GRFASYRTSFSVGSD CCCEECEEEECCCCC	26.37	22167270
1174	Phosphorylation	RFASYRTSFSVGSDD CCEECEEEECCCCCC	13.41	22167270
1176	Phosphorylation	ASYRTSFSVGSDDEL EECEEEECCCCCCCC	25.90	22167270
1179	Phosphorylation	RTSFSVGSDDELGPI EEEECCCCCCCCCCC	39.47	19664994
1195	Phosphorylation	KKEEDQASQGYKGDN CCHHHHHCCCCCCCC	20.64	17525332
1198	Phosphorylation	EDQASQGYKGDNAVI HHHHCCCCCCCCCCC	12.26	26074081
1207	Phosphorylation	GDNAVIPYETDEDPR CCCCCCCCCCCCCHH	21.97	21609022
1209	Phosphorylation	NAVIPYETDEDPRRR CCCCCCCCCCCHHHH	38.55	-
1221	Phosphorylation	RRRNILRSLRRNTKK HHHHHHHHHHHCCCC	23.84	19673492
1226	Phosphorylation	LRSLRRNTKKPKPKP HHHHHHCCCCCCCCC	38.34	19103606
1236	Phosphorylation	PKPKPRPSITKATWE CCCCCCCCCCHHHEE	44.14	23401153
1238	Phosphorylation	PKPRPSITKATWESN CCCCCCCCHHHEECC	20.97	29514088
1289	Ubiquitination	IYRVSGNKSEMESLQ EEEECCCHHHHHHHH	51.85	22817900
1289 (in isoform 1)	Ubiquitination	-	51.85	21906983
1290	Phosphorylation	YRVSGNKSEMESLQR EEECCCHHHHHHHHH	46.29	21815630
1313	Phosphorylation	DLAEKDFTVNTVAGA CHHHCCCCHHHHHHH	23.99	28555341
1353	Ubiquitination	KINDREQKLHALKEV CCCHHHHHHHHHHHH	37.17	29967540
1358	Ubiquitination	EQKLHALKEVLKKFP HHHHHHHHHHHHHCC	46.70	29967540
1381	Ubiquitination	YVISHLNKVSHNNKV HHHHHHHCCCCCCCC	52.02	29967540
1450	Phosphorylation	EPPGARPSSPSAVAS CCCCCCCCCHHHHHH	49.69	20873877
1451	Phosphorylation	PPGARPSSPSAVAST CCCCCCCCHHHHHHC	26.09	20068231
1453	Phosphorylation	GARPSSPSAVASTVP CCCCCCHHHHHHCCC	37.01	20068231
1457	Phosphorylation	SSPSAVASTVPFLTS CCHHHHHHCCCCCCC	24.28	20068231
1458	Phosphorylation	SPSAVASTVPFLTST CHHHHHHCCCCCCCC	23.59	20068231
1463	Phosphorylation	ASTVPFLTSTPVTSQ HHCCCCCCCCCCCCC	30.82	28348404
1464	Phosphorylation	STVPFLTSTPVTSQP HCCCCCCCCCCCCCC	32.62	28348404
1465	Phosphorylation	TVPFLTSTPVTSQPS CCCCCCCCCCCCCCC	19.28	28348404
1468	Phosphorylation	FLTSTPVTSQPSPPQ CCCCCCCCCCCCCCC	23.89	20068231
1469	Phosphorylation	LTSTPVTSQPSPPQS CCCCCCCCCCCCCCC	40.09	20068231
1472	Phosphorylation	TPVTSQPSPPQSPPP CCCCCCCCCCCCCCC	41.39	20068231
1476	Phosphorylation	SQPSPPQSPPPTPQS CCCCCCCCCCCCCCC	45.18	20068231
1480	Phosphorylation	PPQSPPPTPQSPMQP CCCCCCCCCCCCCCC	39.47	20873877
1483	Phosphorylation	SPPPTPQSPMQPLLP CCCCCCCCCCCCCCH	24.44	27251275
1491	Phosphorylation	PMQPLLPSQLQAEHT CCCCCCHHHHHHHCC	39.81	20068231
1498	Phosphorylation	SQLQAEHTL------ HHHHHHCCC------	45.45	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
1105	Y	Phosphorylation	Kinase	ABL2	P42684	Uniprot
1105	Y	Phosphorylation	Kinase	PTK6	Q13882	Uniprot
1105	Y	Phosphorylation	Kinase	SRC	P12931	GPS
1105	Y	Phosphorylation	Kinase	SRC64	-	PhosphoELM
1150	S	Phosphorylation	Kinase	ROCK1	Q13464	PSP
1173	T	Phosphorylation	Kinase	ROCK1	Q13464	PSP
1174	S	Phosphorylation	Kinase	ROCK1	Q13464	PSP
1221	S	Phosphorylation	Kinase	PKCA	P17252	PSP
1226	T	Phosphorylation	Kinase	PKCA	P17252	PSP
1226	T	Phosphorylation	Kinase	ROCK1	Q13464	PSP
1236	S	Phosphorylation	Kinase	PKCA	P17252	PSP
1236	S	Phosphorylation	Kinase	ROCK1	Q13464	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	TRIM65	Q6PJ69	PMID:31332286

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
1221	S	Phosphorylation	19673492
Phosphorylated by PRKCA at Ser-1221 and Thr-1226, induces relocalization from the cytoplasm to regions of plasma membrane ruffling and prevents the binding and substrate specificity regulation by phospholipids.
1226	T	Phosphorylation	19673492
Phosphorylated by PRKCA at Ser-1221 and Thr-1226, induces relocalization from the cytoplasm to regions of plasma membrane ruffling and prevents the binding and substrate specificity regulation by phospholipids.
1451	S	Phosphorylation	19673492
During focal adhesion formation, phosphorylated by MAPK1 and MAPK3 at the C-terminal region, probably at Ser-1451, Ser-1476, Thr-1480 and Ser-1483.
1476	S	Phosphorylation	19673492
During focal adhesion formation, phosphorylated by MAPK1 and MAPK3 at the C-terminal region, probably at Ser-1451, Ser-1476, Thr-1480 and Ser-1483.
1476	S	Phosphorylation	19673492
Phosphorylation at Ser-1476 and Thr-1480 by GSK3B requires priming by MAPK and inhibits RhoGAP activity and modulates polarized cell migration (By similarity).
1480	T	Phosphorylation	19673492
During focal adhesion formation, phosphorylated by MAPK1 and MAPK3 at the C-terminal region, probably at Ser-1451, Ser-1476, Thr-1480 and Ser-1483.
1480	T	Phosphorylation	19673492
Phosphorylation at Ser-1476 and Thr-1480 by GSK3B requires priming by MAPK and inhibits RhoGAP activity and modulates polarized cell migration (By similarity).
1483	S	Phosphorylation	19673492
During focal adhesion formation, phosphorylated by MAPK1 and MAPK3 at the C-terminal region, probably at Ser-1451, Ser-1476, Thr-1480 and Ser-1483.

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 RHG35_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RASA1_HUMAN	RASA1	physical	9034330
K1H1_HUMAN	KRT31	physical	25416956
TCRG1_HUMAN	TCERG1	physical	26344197
RHOA_HUMAN	RHOA	physical	9535855
CDC42_HUMAN	CDC42	physical	9535855
RAC1_HUMAN	RAC1	physical	9535855

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 RHG35_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-589; SER-773; SER-975;SER-1072; TYR-1087; TYR-1105; SER-1134 AND SER-1179, AND MASSSPECTROMETRY.	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-1179, 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-1179, 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-589; THR-963; SER-970;SER-975; SER-980; SER-1150 AND SER-1179, 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-970 AND SER-1179, ANDMASS 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-1179, AND MASSSPECTROMETRY.	18088087 [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 SER-1195, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Global phosphoproteome of HT-29 human colon adenocarcinoma cells."; Kim J.-E., Tannenbaum S.R., White F.M.; J. Proteome Res. 4:1339-1346(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1150, AND MASSSPECTROMETRY.	16083285 [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-1179, ANDMASS SPECTROMETRY.	15302935 [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-685, AND MASSSPECTROMETRY.	17081983 [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-1087 AND TYR-1105, ANDMASS SPECTROMETRY.	19534553 [Abstract]
"Breast tumor kinase phosphorylates p190RhoGAP to regulate rho and rasand promote breast carcinoma growth, migration, and invasion."; Shen C.H., Chen H.Y., Lin M.S., Li F.Y., Chang C.C., Kuo M.L.,Settleman J., Chen R.H.; Cancer Res. 68:7779-7787(2008). Cited for: PHOSPHORYLATION AT TYR-1105.	18829532 [Abstract]
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"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1087 AND TYR-1105, ANDMASS SPECTROMETRY.	18083107 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1105, AND MASSSPECTROMETRY.	15592455 [Abstract]

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