dbPTM

SEPT9_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SEPT9_HUMAN
UniProt AC	Q9UHD8
Protein Name	Septin-9
Gene Name	9-Sep
Organism	Homo sapiens (Human).
Sequence Length	586
Subcellular Localization	Cytoplasm, cytoskeleton . In an epithelial cell line, concentrates at cell-cell contact areas. After TGF-beta1 treatment and induction of epithelial to mesenchymal transition, colocalizes partly with actin stress fibers. During bacterial infection, d
Protein Description	Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in the internalization of 2 intracellular microbial pathogens, Listeria monocytogenes and Shigella flexneri..
Protein Sequence	MKKSYSGGTRTSSGRLRRLGDSSGPALKRSFEVEEVETPNSTPPRRVQTPLLRATVASSTQKFQDLGVKNSEPSARHVDSLSQRSPKASLRRVELSGPKAAEPVSRRTELSIDISSKQVENAGAIGPSRFGLKRAEVLGHKTPEPAPRRTEITIVKPQESAHRRMEPPASKVPEVPTAPATDAAPKRVEIQMPKPAEAPTAPSPAQTLENSEPAPVSQLQSRLEPKPQPPVAEATPRSQEATEAAPSCVGDMADTPRDAGLKQAPASRNEKAPVDFGYVGIDSILEQMRRKAMKQGFEFNIMVVGQSGLGKSTLINTLFKSKISRKSVQPTSEERIPKTIEIKSITHDIEEKGVRMKLTVIDTPGFGDHINNENCWQPIMKFINDQYEKYLQEEVNINRKKRIPDTRVHCCLYFIPATGHSLRPLDIEFMKRLSKVVNIVPVIAKADTLTLEERVHFKQRITADLLSNGIDVYPQKEFDEDSEDRLVNEKFREMIPFAVVGSDHEYQVNGKRILGRKTKWGTIEVENTTHCEFAYLRDLLIRTHMQNIKDITSSIHFEAYRVKRLNEGSSAMANGMEEKEPEAPEM

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MKKSYSGG -------CCCCCCCC	12.76	22814378
1 (in isoform 3)	Acetylation	-	12.76	22814378
2	Methylation	------MKKSYSGGT ------CCCCCCCCC	50.88	115981497
2 (in isoform 5)	Phosphorylation	-	50.88	29507054
3	Methylation	-----MKKSYSGGTR -----CCCCCCCCCC	54.01	80499923
4	Phosphorylation	----MKKSYSGGTRT ----CCCCCCCCCCC	21.00	28102081
5	Phosphorylation	---MKKSYSGGTRTS ---CCCCCCCCCCCC	21.88	28102081
6	Phosphorylation	--MKKSYSGGTRTSS --CCCCCCCCCCCCC	37.53	22798277
6 (in isoform 7)	Phosphorylation	-	37.53	-
7 (in isoform 2)	Phosphorylation	-	33.00	28450419
9	Phosphorylation	KKSYSGGTRTSSGRL CCCCCCCCCCCCCCE	34.01	28509920
9 (in isoform 7)	Methylation	-	34.01	-
10	Methylation	KSYSGGTRTSSGRLR CCCCCCCCCCCCCEE	35.57	54559139
11	Phosphorylation	SYSGGTRTSSGRLRR CCCCCCCCCCCCEEE	27.38	26074081
12	Phosphorylation	YSGGTRTSSGRLRRL CCCCCCCCCCCEEEC	27.75	19664994
12 (in isoform 2)	Phosphorylation	-	27.75	19664994
13	Phosphorylation	SGGTRTSSGRLRRLG CCCCCCCCCCEEECC	27.59	30576142
20 (in isoform 2)	Phosphorylation	-	30.83	-
22	Phosphorylation	RLRRLGDSSGPALKR CEEECCCCCCCCHHE	35.08	30278072
23	Phosphorylation	LRRLGDSSGPALKRS EEECCCCCCCCHHEE	54.24	23927012
23 (in isoform 2)	Phosphorylation	-	54.24	-
23 (in isoform 5)	Phosphorylation	-	54.24	27107777
24 (in isoform 2)	Phosphorylation	-	18.56	-
28	2-Hydroxyisobutyrylation	DSSGPALKRSFEVEE CCCCCCHHEEEEEEE	48.37	-
28	Acetylation	DSSGPALKRSFEVEE CCCCCCHHEEEEEEE	48.37	26051181
28	Methylation	DSSGPALKRSFEVEE CCCCCCHHEEEEEEE	48.37	12431781
28	Ubiquitination	DSSGPALKRSFEVEE CCCCCCHHEEEEEEE	48.37	-
30	Phosphorylation	SGPALKRSFEVEEVE CCCCHHEEEEEEEEC	24.95	19664994
31 (in isoform 2)	Phosphorylation	-	16.50	-
38	Phosphorylation	FEVEEVETPNSTPPR EEEEEECCCCCCCCC	32.71	22167270
41	Phosphorylation	EEVETPNSTPPRRVQ EEECCCCCCCCCCCC	43.42	29255136
42	Phosphorylation	EVETPNSTPPRRVQT EECCCCCCCCCCCCC	43.91	29255136
49	Phosphorylation	TPPRRVQTPLLRATV CCCCCCCCHHHHHHH	17.04	30266825
50 (in isoform 8)	Phosphorylation	-	16.59	24719451
51 (in isoform 2)	Ubiquitination	-	6.00	-
55	Phosphorylation	QTPLLRATVASSTQK CCHHHHHHHCCCCHH	15.35	30624053
58	Phosphorylation	LLRATVASSTQKFQD HHHHHHCCCCHHHHH	29.58	24732914
59	Phosphorylation	LRATVASSTQKFQDL HHHHHCCCCHHHHHH	25.72	25849741
60	Phosphorylation	RATVASSTQKFQDLG HHHHCCCCHHHHHHC	33.03	24732914
62	Acetylation	TVASSTQKFQDLGVK HHCCCCHHHHHHCCC	45.11	23954790
62	Ubiquitination	TVASSTQKFQDLGVK HHCCCCHHHHHHCCC	45.11	-
62 (in isoform 2)	Phosphorylation	-	45.11	-
64 (in isoform 2)	Phosphorylation	-	52.64	-
67 (in isoform 2)	Phosphorylation	-	36.32	-
71	Phosphorylation	QDLGVKNSEPSARHV HHHCCCCCCCCHHHH	45.20	26074081
71 (in isoform 2)	Phosphorylation	-	45.20	-
74	Phosphorylation	GVKNSEPSARHVDSL CCCCCCCCHHHHHHH	33.61	29514088
78 (in isoform 2)	Phosphorylation	-	4.45	-
80	Phosphorylation	PSARHVDSLSQRSPK CCHHHHHHHHHCCCC	28.91	23927012
82	Phosphorylation	ARHVDSLSQRSPKAS HHHHHHHHHCCCCHH	27.74	22167270
85	Phosphorylation	VDSLSQRSPKASLRR HHHHHHCCCCHHHEE	24.10	22167270
89	Phosphorylation	SQRSPKASLRRVELS HHCCCCHHHEEEECC	28.65	23401153
96	Phosphorylation	SLRRVELSGPKAAEP HHEEEECCCCCCCCC	39.27	25159151
101	Acetylation	ELSGPKAAEPVSRRT ECCCCCCCCCCCCCC	27.96	19608861
101	Ubiquitination	ELSGPKAAEPVSRRT ECCCCCCCCCCCCCC	27.96	19608861
105	Phosphorylation	PKAAEPVSRRTELSI CCCCCCCCCCCEEEE	27.10	23532336
108	Phosphorylation	AEPVSRRTELSIDIS CCCCCCCCEEEEECC	39.92	24117733
111	Phosphorylation	VSRRTELSIDISSKQ CCCCCEEEEECCCHH	16.39	25159151
115	Phosphorylation	TELSIDISSKQVENA CEEEEECCCHHHHCC	27.95	24117733
116	Phosphorylation	ELSIDISSKQVENAG EEEEECCCHHHHCCC	27.69	24117733
124 (in isoform 2)	Phosphorylation	-	10.93	-
128	Acetylation	NAGAIGPSRFGLKRA CCCCCCCCHHCCCHH	34.72	19608861
128	Ubiquitination	NAGAIGPSRFGLKRA CCCCCCCCHHCCCHH	34.72	19608861
141	Acetylation	RAEVLGHKTPEPAPR HHHHHCCCCCCCCCC	65.07	25953088
141	Ubiquitination	RAEVLGHKTPEPAPR HHHHHCCCCCCCCCC	65.07	-
142	O-linked_Glycosylation	AEVLGHKTPEPAPRR HHHHCCCCCCCCCCC	27.49	30379171
142	Phosphorylation	AEVLGHKTPEPAPRR HHHHCCCCCCCCCCC	27.49	29255136
150	Phosphorylation	PEPAPRRTEITIVKP CCCCCCCCEEEEECC	32.78	20363803
153	Phosphorylation	APRRTEITIVKPQES CCCCCEEEEECCCHH	17.31	20363803
156	Acetylation	RTEITIVKPQESAHR CCEEEEECCCHHHHC	36.81	26051181
160	Phosphorylation	TIVKPQESAHRRMEP EEECCCHHHHCCCCC	24.91	30266825
168 (in isoform 2)	Ubiquitination	-	35.54	-
171	Acetylation	RMEPPASKVPEVPTA CCCCCHHHCCCCCCC	65.01	26051181
177	Phosphorylation	SKVPEVPTAPATDAA HHCCCCCCCCCCCCC	50.91	28555341
181	Phosphorylation	EVPTAPATDAAPKRV CCCCCCCCCCCCCCE	25.72	28555341
185 (in isoform 2)	Phosphorylation	-	27.06	-
186	Acetylation	PATDAAPKRVEIQMP CCCCCCCCCEEEECC	65.43	26051181
186	Ubiquitination	PATDAAPKRVEIQMP CCCCCCCCCEEEECC	65.43	21906983
188	Acetylation	TDAAPKRVEIQMPKP CCCCCCCEEEECCCC	10.70	19608861
188	Ubiquitination	TDAAPKRVEIQMPKP CCCCCCCEEEECCCC	10.70	19608861
194	Acetylation	RVEIQMPKPAEAPTA CEEEECCCCCCCCCC	52.06	26051181
200	Phosphorylation	PKPAEAPTAPSPAQT CCCCCCCCCCCHHHC	59.24	29255136
203	Phosphorylation	AEAPTAPSPAQTLEN CCCCCCCCHHHCCCC	30.33	29255136
207	Phosphorylation	TAPSPAQTLENSEPA CCCCHHHCCCCCCCC	37.84	29255136
211	Phosphorylation	PAQTLENSEPAPVSQ HHHCCCCCCCCCHHH	35.27	24732914
217	Phosphorylation	NSEPAPVSQLQSRLE CCCCCCHHHHHHHCC	24.90	-
217 (in isoform 2)	Phosphorylation	-	24.90	-
220 (in isoform 2)	Phosphorylation	-	20.90	-
226	Acetylation	LQSRLEPKPQPPVAE HHHHCCCCCCCCCCC	47.08	26051181
226	Malonylation	LQSRLEPKPQPPVAE HHHHCCCCCCCCCCC	47.08	26320211
235	Phosphorylation	QPPVAEATPRSQEAT CCCCCCCCCCCHHHH	15.67	20068231
238	Phosphorylation	VAEATPRSQEATEAA CCCCCCCCHHHHHHC	33.31	25159151
240	Acetylation	EATPRSQEATEAAPS CCCCCCHHHHHHCCC	59.82	19608861
240	Ubiquitination	EATPRSQEATEAAPS CCCCCCHHHHHHCCC	59.82	19608861
242	Phosphorylation	TPRSQEATEAAPSCV CCCCHHHHHHCCCCC	25.96	24732914
247	Phosphorylation	EATEAAPSCVGDMAD HHHHHCCCCCHHCCC	19.39	24732914
248	Glutathionylation	ATEAAPSCVGDMADT HHHHCCCCCHHCCCC	3.74	22555962
252	Sulfoxidation	APSCVGDMADTPRDA CCCCCHHCCCCCCCC	2.75	21406390
253 (in isoform 2)	Ubiquitination	-	23.43	-
255	Phosphorylation	CVGDMADTPRDAGLK CCHHCCCCCCCCCCC	15.64	25159151
259 (in isoform 7)	Phosphorylation	-	26.88	27642862
260 (in isoform 2)	Phosphorylation	-	37.38	-
262	Acetylation	TPRDAGLKQAPASRN CCCCCCCCCCCCCCC	43.42	25953088
262	Ubiquitination	TPRDAGLKQAPASRN CCCCCCCCCCCCCCC	43.42	21906983
267	Phosphorylation	GLKQAPASRNEKAPV CCCCCCCCCCCCCCC	34.28	21082442
271	Ubiquitination	APASRNEKAPVDFGY CCCCCCCCCCCCCCC	62.63	21906983
278	Phosphorylation	KAPVDFGYVGIDSIL CCCCCCCCCCHHHHH	8.76	27273156
283	Phosphorylation	FGYVGIDSILEQMRR CCCCCHHHHHHHHHH	27.44	26356563
288	Sulfoxidation	IDSILEQMRRKAMKQ HHHHHHHHHHHHHHC	3.06	28183972
291	Ubiquitination	ILEQMRRKAMKQGFE HHHHHHHHHHHCCCE	42.33	-
307	Phosphorylation	NIMVVGQSGLGKSTL EEEEECCCCCCHHHH	30.01	-
312	Phosphorylation	GQSGLGKSTLINTLF CCCCCCHHHHHHHHH	27.01	21406692
313	Phosphorylation	QSGLGKSTLINTLFK CCCCCHHHHHHHHHH	34.83	21406692
317	Phosphorylation	GKSTLINTLFKSKIS CHHHHHHHHHHHCCC	26.95	21406692
320	Acetylation	TLINTLFKSKISRKS HHHHHHHHHCCCCCC	54.69	25953088
320	Methylation	TLINTLFKSKISRKS HHHHHHHHHCCCCCC	54.69	54417081
320	Ubiquitination	TLINTLFKSKISRKS HHHHHHHHHCCCCCC	54.69	-
322	Methylation	INTLFKSKISRKSVQ HHHHHHHCCCCCCCC	45.34	115981521
322	Ubiquitination	INTLFKSKISRKSVQ HHHHHHHCCCCCCCC	45.34	-
324	Phosphorylation	TLFKSKISRKSVQPT HHHHHCCCCCCCCCC	37.07	23312004
326	Ubiquitination	FKSKISRKSVQPTSE HHHCCCCCCCCCCCC	48.46	-
327	Phosphorylation	KSKISRKSVQPTSEE HHCCCCCCCCCCCCC	25.52	30266825
331	Phosphorylation	SRKSVQPTSEERIPK CCCCCCCCCCCCCCC	31.51	30266825
332	Phosphorylation	RKSVQPTSEERIPKT CCCCCCCCCCCCCCE	44.11	25159151
333	Acetylation	KSVQPTSEERIPKTI CCCCCCCCCCCCCEE	54.49	19608861
333	Ubiquitination	KSVQPTSEERIPKTI CCCCCCCCCCCCCEE	54.49	19608861
334 (in isoform 2)	Acetylation	-	56.53	-
334 (in isoform 2)	Ubiquitination	-	56.53	-
338	Acetylation	TSEERIPKTIEIKSI CCCCCCCCEEEEEEE	60.82	27452117
338	Malonylation	TSEERIPKTIEIKSI CCCCCCCCEEEEEEE	60.82	26320211
338	Ubiquitination	TSEERIPKTIEIKSI CCCCCCCCEEEEEEE	60.82	-
343	Acetylation	IPKTIEIKSITHDIE CCCEEEEEEEECCHH	24.02	25953088
343	Malonylation	IPKTIEIKSITHDIE CCCEEEEEEEECCHH	24.02	26320211
343	Ubiquitination	IPKTIEIKSITHDIE CCCEEEEEEEECCHH	24.02	-
345	Acetylation	KTIEIKSITHDIEEK CEEEEEEEECCHHHH	3.17	19608861
345	Ubiquitination	KTIEIKSITHDIEEK CEEEEEEEECCHHHH	3.17	19608861
352	Acetylation	ITHDIEEKGVRMKLT EECCHHHHCCEEEEE	50.33	23954790
352	Malonylation	ITHDIEEKGVRMKLT EECCHHHHCCEEEEE	50.33	26320211
352	Ubiquitination	ITHDIEEKGVRMKLT EECCHHHHCCEEEEE	50.33	-
357	Ubiquitination	EEKGVRMKLTVIDTP HHHCCEEEEEEEECC	30.37	-
359	Phosphorylation	KGVRMKLTVIDTPGF HCCEEEEEEEECCCC	15.19	23401153
363	Phosphorylation	MKLTVIDTPGFGDHI EEEEEEECCCCCCCC	17.75	23401153
381	Acetylation	NCWQPIMKFINDQYE CCHHHHHHHHHHHHH	43.76	26051181
381	Ubiquitination	NCWQPIMKFINDQYE CCHHHHHHHHHHHHH	43.76	-
387	Phosphorylation	MKFINDQYEKYLQEE HHHHHHHHHHHHHHH	19.77	23401153
389	Acetylation	FINDQYEKYLQEEVN HHHHHHHHHHHHHHC	46.45	26051181
389	Ubiquitination	FINDQYEKYLQEEVN HHHHHHHHHHHHHHC	46.45	-
400	Ubiquitination	EEVNINRKKRIPDTR HHHCCCCCCCCCCCC	41.75	-
427 (in isoform 2)	Ubiquitination	-	6.07	-
431	Acetylation	PLDIEFMKRLSKVVN CCCHHHHHHHHHHHC	56.35	26051181
431	Ubiquitination	PLDIEFMKRLSKVVN CCCHHHHHHHHHHHC	56.35	-
435	Acetylation	EFMKRLSKVVNIVPV HHHHHHHHHHCHHHE	55.59	26051181
435	Malonylation	EFMKRLSKVVNIVPV HHHHHHHHHHCHHHE	55.59	26320211
435	Ubiquitination	EFMKRLSKVVNIVPV HHHHHHHHHHCHHHE	55.59	-
445	Ubiquitination	NIVPVIAKADTLTLE CHHHEEEECCCCCHH	35.35	21906983
448	Phosphorylation	PVIAKADTLTLEERV HEEEECCCCCHHHHH	26.88	30108239
450	Phosphorylation	IAKADTLTLEERVHF EEECCCCCHHHHHHH	33.93	24114839
458	Ubiquitination	LEERVHFKQRITADL HHHHHHHHHHHHHHH	24.64	-
458 (in isoform 2)	Ubiquitination	-	24.64	-
472 (in isoform 2)	Ubiquitination	-	7.69	-
476	Acetylation	GIDVYPQKEFDEDSE CCEECCCHHCCCCCC	56.71	26051181
476	Ubiquitination	GIDVYPQKEFDEDSE CCEECCCHHCCCCCC	56.71	21906983
482	Phosphorylation	QKEFDEDSEDRLVNE CHHCCCCCCHHHHCH	39.07	28450419
485	Methylation	FDEDSEDRLVNEKFR CCCCCCHHHHCHHHH	36.16	115916461
490	2-Hydroxyisobutyrylation	EDRLVNEKFREMIPF CHHHHCHHHHHHCCE	44.51	-
490	Acetylation	EDRLVNEKFREMIPF CHHHHCHHHHHHCCE	44.51	27452117
490	Ubiquitination	EDRLVNEKFREMIPF CHHHHCHHHHHHCCE	44.51	21906983
502	Phosphorylation	IPFAVVGSDHEYQVN CCEEEECCCCEEEEC	24.96	19835603
506	Phosphorylation	VVGSDHEYQVNGKRI EECCCCEEEECCEEE	17.84	19835603
511	Acetylation	HEYQVNGKRILGRKT CEEEECCEEECCCCC	30.94	25953088
511	Ubiquitination	HEYQVNGKRILGRKT CEEEECCEEECCCCC	30.94	-
517	Ubiquitination	GKRILGRKTKWGTIE CEEECCCCCCCEEEE	53.29	-
518	Phosphorylation	KRILGRKTKWGTIEV EEECCCCCCCEEEEE	30.57	27251275
519	Acetylation	RILGRKTKWGTIEVE EECCCCCCCEEEEEE	46.81	25953088
519	Ubiquitination	RILGRKTKWGTIEVE EECCCCCCCEEEEEE	46.81	-
522	Phosphorylation	GRKTKWGTIEVENTT CCCCCCEEEEEECCC	16.92	27251275
528	Phosphorylation	GTIEVENTTHCEFAY EEEEEECCCCEEHHH	12.38	27251275
529	Phosphorylation	TIEVENTTHCEFAYL EEEEECCCCEEHHHH	35.79	27251275
543	Phosphorylation	LRDLLIRTHMQNIKD HHHHHHHHHHHHHHH	18.08	-
549	2-Hydroxyisobutyrylation	RTHMQNIKDITSSIH HHHHHHHHHHHHHHH	51.10	-
549	Ubiquitination	RTHMQNIKDITSSIH HHHHHHHHHHHHHHH	51.10	-
553	Phosphorylation	QNIKDITSSIHFEAY HHHHHHHHHHHEEEE	27.85	27251275
554	Phosphorylation	NIKDITSSIHFEAYR HHHHHHHHHHEEEEE	16.07	27251275
569	Phosphorylation	VKRLNEGSSAMANGM EEECCCCCCHHHCCC	14.56	22210691
570	Phosphorylation	KRLNEGSSAMANGME EECCCCCCHHHCCCC	32.68	22210691

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
24	T	Phosphorylation	Kinase	CDK1	P06493	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SEPT9_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 SEPT9_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SEPT2_HUMAN	SEPT2	physical	12388755
SEPT6_HUMAN	SEPT6	physical	12388755
SEPT7_HUMAN	SEPT7	physical	12388755
HIF1A_HUMAN	HIF1A	physical	16424018
A4_HUMAN	APP	physical	21832049
TIM44_HUMAN	TIMM44	physical	22939629
VAMP2_HUMAN	VAMP2	physical	22939629
SUCB2_HUMAN	SUCLG2	physical	22939629
TOIP1_HUMAN	TOR1AIP1	physical	22939629
SUCA_HUMAN	SUCLG1	physical	22939629
UCRI_HUMAN	UQCRFS1	physical	22939629
VAPB_HUMAN	VAPB	physical	22939629
TMED9_HUMAN	TMED9	physical	22939629
SVIL_HUMAN	SVIL	physical	22939629
RIDA_HUMAN	HRSP12	physical	22939629
TPM3_HUMAN	TPM3	physical	22939629
VMA21_HUMAN	VMA21	physical	22939629
SEPT6_HUMAN	SEPT6	physical	25416956
SEPT6_HUMAN	SEPT6	physical	21516116

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
	Note=A chromosomal aberration involving SEPT9/MSF is found in therapy-related acute myeloid leukemia (t-AML). Translocation t(11
	17)(q23
0000269\|PubMed	q25) with KMT2A/MLL1. {ECO
162100
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of SEPT9_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-352 AND LYS-431, AND MASSSPECTROMETRY.	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-30; THR-38 AND TYR-278,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-42; SER-82 AND SER-85,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-30; THR-38; THR-42 ANDTHR-49, AND MASS 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-30 AND SER-80, AND MASSSPECTROMETRY.	18691976 [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-30, AND MASSSPECTROMETRY.	18220336 [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-82; SER-85; SER-89 ANDTHR-142, AND MASS SPECTROMETRY.	17287340 [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-30 AND THR-42, 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-85, AND MASSSPECTROMETRY.	17081983 [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-85, AND MASSSPECTROMETRY.	16083285 [Abstract]
"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-278, AND MASSSPECTROMETRY.	18083107 [Abstract]