dbPTM

HS90A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HS90A_MOUSE
UniProt AC	P07901
Protein Name	Heat shock protein HSP 90-alpha
Gene Name	Hsp90aa1
Organism	Mus musculus (Mouse).
Sequence Length	733
Subcellular Localization	Nucleus . Cytoplasm . Melanosome . Cell membrane .
Protein Description	Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself. Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle. Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels. In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues. Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment. Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression. Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation..
Protein Sequence	MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPSKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKEEKEEEKEKEEKESDDKPEIEDVGSDEEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEEHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHIYFITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTVDDTSAAVTEEMPPLEGDDDTSRMEEVD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MPEETQTQDQPM ---CCCCCCCCCCCC	34.94	2507541
7	Phosphorylation	-MPEETQTQDQPMEE -CCCCCCCCCCCCCH	41.34	2507541
38	Phosphorylation	SLIINTFYSNKEIFL HHHHHHHCCCHHHHH	14.86	-
41	Acetylation	INTFYSNKEIFLREL HHHHCCCHHHHHHHH	46.37	22826441
41	Succinylation	INTFYSNKEIFLREL HHHHCCCHHHHHHHH	46.37	23954790
52	Phosphorylation	LRELISNSSDALDKI HHHHHHCCCHHHHHH	23.86	22817900
53	Phosphorylation	RELISNSSDALDKIR HHHHHCCCHHHHHHC	31.02	19854140
58	Acetylation	NSSDALDKIRYESLT CCCHHHHHHCHHHCC	29.90	23806337
58	Ubiquitination	NSSDALDKIRYESLT CCCHHHHHHCHHHCC	29.90	22790023
61	Phosphorylation	DALDKIRYESLTDPS HHHHHHCHHHCCCHH	17.22	22817900
63	Phosphorylation	LDKIRYESLTDPSKL HHHHCHHHCCCHHHC	27.86	24899341
65	Phosphorylation	KIRYESLTDPSKLDS HHCHHHCCCHHHCCC	55.96	21183079
68	Phosphorylation	YESLTDPSKLDSGKE HHHCCCHHHCCCCCE	48.97	21183079
69	Acetylation	ESLTDPSKLDSGKEL HHCCCHHHCCCCCEE	62.80	23806337
69	Ubiquitination	ESLTDPSKLDSGKEL HHCCCHHHCCCCCEE	62.80	22790023
72	Phosphorylation	TDPSKLDSGKELHIN CCHHHCCCCCEEEEE	63.30	26370283
74	Ubiquitination	PSKLDSGKELHINLI HHHCCCCCEEEEEEC	62.14	22790023
84	Acetylation	HINLIPSKQDRTLTI EEEECCCCCCCEEEE	51.36	23806337
84	Ubiquitination	HINLIPSKQDRTLTI EEEECCCCCCCEEEE	51.36	22790023
90	Phosphorylation	SKQDRTLTIVDTGIG CCCCCEEEEEECCCC	20.52	22006019
98	Sulfoxidation	IVDTGIGMTKADLIN EEECCCCCCHHHHHH	3.08	21406390
99	Phosphorylation	VDTGIGMTKADLINN EECCCCCCHHHHHHH	20.19	-
100	Ubiquitination	DTGIGMTKADLINNL ECCCCCCHHHHHHHH	30.89	-
109	Phosphorylation	DLINNLGTIAKSGTK HHHHHHHHHHHHHHH	22.41	29514104
112	Acetylation	NNLGTIAKSGTKAFM HHHHHHHHHHHHHHH	45.64	23806337
112	Succinylation	NNLGTIAKSGTKAFM HHHHHHHHHHHHHHH	45.64	23806337
112	Ubiquitination	NNLGTIAKSGTKAFM HHHHHHHHHHHHHHH	45.64	-
116	Ubiquitination	TIAKSGTKAFMEALQ HHHHHHHHHHHHHHH	43.05	-
160	Phosphorylation	KHNDDEQYAWESSAG CCCCCCCEEEECCCC	16.19	25168779
164	Phosphorylation	DEQYAWESSAGGSFT CCCEEEECCCCCEEE	18.13	26525534
165	Phosphorylation	EQYAWESSAGGSFTV CCEEEECCCCCEEEE	21.29	26525534
169	Phosphorylation	WESSAGGSFTVRTDT EECCCCCEEEEEECC	19.47	25168779
171	Phosphorylation	SSAGGSFTVRTDTGE CCCCCEEEEEECCCC	15.69	25168779
185	Ubiquitination	EPMGRGTKVILHLKE CCCCCCEEEEEEECC	30.06	-
191	Acetylation	TKVILHLKEDQTEYL EEEEEEECCCHHHHH	48.80	22826441
191	Ubiquitination	TKVILHLKEDQTEYL EEEEEEECCCHHHHH	48.80	-
195	Phosphorylation	LHLKEDQTEYLEERR EEECCCHHHHHHHHH	38.63	28066266
197	Phosphorylation	LKEDQTEYLEERRIK ECCCHHHHHHHHHHH	23.85	22817900
204	Acetylation	YLEERRIKEIVKKHS HHHHHHHHHHHHHHH	39.31	23576753
208	Acetylation	RRIKEIVKKHSQFIG HHHHHHHHHHHHHCC	50.89	23576753
209	Acetylation	RIKEIVKKHSQFIGY HHHHHHHHHHHHCCC	37.28	23576753
211	Phosphorylation	KEIVKKHSQFIGYPI HHHHHHHHHHCCCCE	35.35	27841257
224	Acetylation	PITLFVEKERDKEVS CEEEEEEHHHCCCCC	53.39	22826441
224	Ubiquitination	PITLFVEKERDKEVS CEEEEEEHHHCCCCC	53.39	22790023
231	Phosphorylation	KERDKEVSDDEAEEK HHHCCCCCHHHHHHH	40.20	27087446
252	Phosphorylation	KEKEEKESDDKPEIE HHHHHHHCCCCCCCC	63.28	25521595
263	Phosphorylation	PEIEDVGSDEEEEEK CCCCCCCCCHHHHHH	41.52	24925903
275	Acetylation	EEKKDGDKKKKKKIK HHHCCCCHHHHHHHH	72.52	7719459
275	Malonylation	EEKKDGDKKKKKKIK HHHCCCCHHHHHHHH	72.52	26320211
276	Acetylation	EKKDGDKKKKKKIKE HHCCCCHHHHHHHHH	74.66	7719473
282	Malonylation	KKKKKKIKEKYIDQE HHHHHHHHHHHCCHH	57.97	26320211
284	Acetylation	KKKKIKEKYIDQEEL HHHHHHHHHCCHHHH	42.37	69965
284	Malonylation	KKKKIKEKYIDQEEL HHHHHHHHHCCHHHH	42.37	26320211
284	Ubiquitination	KKKKIKEKYIDQEEL HHHHHHHHHCCHHHH	42.37	-
285	Phosphorylation	KKKIKEKYIDQEELN HHHHHHHHCCHHHHH	15.72	25159016
293	Acetylation	IDQEELNKTKPIWTR CCHHHHHCCCCCCCC	71.23	22826441
293	Malonylation	IDQEELNKTKPIWTR CCHHHHHCCCCCCCC	71.23	26320211
293	Succinylation	IDQEELNKTKPIWTR CCHHHHHCCCCCCCC	71.23	23806337
293	Ubiquitination	IDQEELNKTKPIWTR CCHHHHHCCCCCCCC	71.23	-
294	Phosphorylation	DQEELNKTKPIWTRN CHHHHHCCCCCCCCC	40.76	27600695
295	Acetylation	QEELNKTKPIWTRNP HHHHHCCCCCCCCCC	35.79	183491
295	Ubiquitination	QEELNKTKPIWTRNP HHHHHCCCCCCCCCC	35.79	22790023
314	Phosphorylation	NEEYGEFYKSLTNDW HHHHHHHHHHHCCCH	8.72	22817900
315	Acetylation	EEYGEFYKSLTNDWE HHHHHHHHHHCCCHH	44.29	23954790
315	Ubiquitination	EEYGEFYKSLTNDWE HHHHHHHHHHCCCHH	44.29	-
316	Phosphorylation	EYGEFYKSLTNDWEE HHHHHHHHHCCCHHH	29.10	26745281
318	Phosphorylation	GEFYKSLTNDWEEHL HHHHHHHCCCHHHHE	37.92	26745281
363	Ubiquitination	RKKKNNIKLYVRRVF CCCCCCCEEEEEEEE	35.57	-
375	Glutathionylation	RVFIMDNCEELIPEY EEECCCCHHHHHHHH	3.61	24333276
375	S-palmitoylation	RVFIMDNCEELIPEY EEECCCCHHHHHHHH	3.61	28526873
392	Phosphorylation	FIRGVVDSEDLPLNI HHHCCCCCCCCCCCC	22.77	26525534
400	Phosphorylation	EDLPLNISREMLQQS CCCCCCCCHHHHHHH	22.55	27742792
407	Phosphorylation	SREMLQQSKILKVIR CHHHHHHHHHHHHHH	14.54	26745281
408	Acetylation	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	22826441
408	Malonylation	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	26320211
408	Succinylation	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	23806337
408	Ubiquitination	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	-
411	Acetylation	LQQSKILKVIRKNLV HHHHHHHHHHHHHHH	38.80	22826441
411	Malonylation	LQQSKILKVIRKNLV HHHHHHHHHHHHHHH	38.80	25418362
420	Ubiquitination	IRKNLVKKCLELFTE HHHHHHHHHHHHHHH	36.25	22790023
432	Acetylation	FTELAEDKENYKKFY HHHHHHCHHHHHHHH	39.09	155729
432	Ubiquitination	FTELAEDKENYKKFY HHHHHHCHHHHHHHH	39.09	-
436	Acetylation	AEDKENYKKFYEQFS HHCHHHHHHHHHHHH	48.24	129217
437	Acetylation	EDKENYKKFYEQFSK HCHHHHHHHHHHHHH	42.70	23806337
437	Malonylation	EDKENYKKFYEQFSK HCHHHHHHHHHHHHH	42.70	26320211
437	Succinylation	EDKENYKKFYEQFSK HCHHHHHHHHHHHHH	42.70	-
437	Ubiquitination	EDKENYKKFYEQFSK HCHHHHHHHHHHHHH	42.70	-
443	Phosphorylation	KKFYEQFSKNIKLGI HHHHHHHHHHCCCCC	25.20	22006019
444	Acetylation	KFYEQFSKNIKLGIH HHHHHHHHHCCCCCC	65.07	23236377
444	Ubiquitination	KFYEQFSKNIKLGIH HHHHHHHHHCCCCCC	65.07	22790023
454	Phosphorylation	KLGIHEDSQNRKKLS CCCCCCCCHHHHHHH	26.77	26824392
459	Acetylation	EDSQNRKKLSELLRY CCCHHHHHHHHHHHH	54.75	22826441
461	O-linked_Glycosylation	SQNRKKLSELLRYYT CHHHHHHHHHHHHHH	34.77	21540332
461	Phosphorylation	SQNRKKLSELLRYYT CHHHHHHHHHHHHHH	34.77	-
466	Phosphorylation	KLSELLRYYTSASGD HHHHHHHHHHCCCCC	15.86	27149854
467	Phosphorylation	LSELLRYYTSASGDE HHHHHHHHHCCCCCC	6.44	27149854
468	Phosphorylation	SELLRYYTSASGDEM HHHHHHHHCCCCCCC	14.64	27149854
469	Phosphorylation	ELLRYYTSASGDEMV HHHHHHHCCCCCCCE	12.33	23984901
471	Phosphorylation	LRYYTSASGDEMVSL HHHHHCCCCCCCEEH	46.69	26239621
477	Phosphorylation	ASGDEMVSLKDYCTR CCCCCCEEHHHHHHH	28.52	27149854
479	Acetylation	GDEMVSLKDYCTRMK CCCCEEHHHHHHHHH	38.86	22826441
479	Ubiquitination	GDEMVSLKDYCTRMK CCCCEEHHHHHHHHH	38.86	22790023
482	S-palmitoylation	MVSLKDYCTRMKENQ CEEHHHHHHHHHHHC	2.52	28680068
483	Phosphorylation	VSLKDYCTRMKENQK EEHHHHHHHHHHHCC	27.80	21183079
486	Acetylation	KDYCTRMKENQKHIY HHHHHHHHHHCCEEE	50.66	22826441
490	Acetylation	TRMKENQKHIYFITG HHHHHHCCEEEEEEC	43.48	22826441
493	Phosphorylation	KENQKHIYFITGETK HHHCCEEEEEECCCH	6.66	18779572
496	Phosphorylation	QKHIYFITGETKDQV CCEEEEEECCCHHHH	21.04	18779572
499	Phosphorylation	IYFITGETKDQVANS EEEEECCCHHHHHHH	41.06	22345495
500	Acetylation	YFITGETKDQVANSA EEEECCCHHHHHHHH	41.69	22826441
506	Phosphorylation	TKDQVANSAFVERLR CHHHHHHHHHHHHHH	17.22	22006019
514	Acetylation	AFVERLRKHGLEVIY HHHHHHHHCCCEEEE	46.76	22826441
529	Phosphorylation	MIEPIDEYCVQQLKE EECCCCHHHHHHHHH	8.32	22817900
540	Acetylation	QLKEFEGKTLVSVTK HHHHCCCCEEEEEEH	31.33	23806337
540	Succinylation	QLKEFEGKTLVSVTK HHHHCCCCEEEEEEH	31.33	23954790
540	Ubiquitination	QLKEFEGKTLVSVTK HHHHCCCCEEEEEEH	31.33	-
547	Acetylation	KTLVSVTKEGLELPE CEEEEEEHHCCCCCC	47.86	22826441
547	Succinylation	KTLVSVTKEGLELPE CEEEEEEHHCCCCCC	47.86	23954790
547	Ubiquitination	KTLVSVTKEGLELPE CEEEEEEHHCCCCCC	47.86	-
559	Acetylation	LPEDEEEKKKQEEKK CCCCHHHHHHHHHHH	69.42	23236377
559	Ubiquitination	LPEDEEEKKKQEEKK CCCCHHHHHHHHHHH	69.42	-
561	Ubiquitination	EDEEEKKKQEEKKTK CCHHHHHHHHHHHHH	74.20	-
566	Acetylation	KKKQEEKKTKFENLC HHHHHHHHHHHHHHH	61.29	22826441
567	Phosphorylation	KKQEEKKTKFENLCK HHHHHHHHHHHHHHH	52.62	22817900
568	Acetylation	KQEEKKTKFENLCKI HHHHHHHHHHHHHHH	60.61	22826441
568	Ubiquitination	KQEEKKTKFENLCKI HHHHHHHHHHHHHHH	60.61	-
573	S-nitrosylation	KTKFENLCKIMKDIL HHHHHHHHHHHHHHH	4.18	24926564
577	Acetylation	ENLCKIMKDILEKKV HHHHHHHHHHHHHHC	45.12	23236377
582	Ubiquitination	IMKDILEKKVEKVVV HHHHHHHHHCCEEEE	59.69	-
583	Acetylation	MKDILEKKVEKVVVS HHHHHHHHCCEEEEC	46.37	22826441
586	Acetylation	ILEKKVEKVVVSNRL HHHHHCCEEEECCCC	43.23	22826441
586	Malonylation	ILEKKVEKVVVSNRL HHHHHCCEEEECCCC	43.23	26320211
586	Ubiquitination	ILEKKVEKVVVSNRL HHHHHCCEEEECCCC	43.23	-
595	Phosphorylation	VVSNRLVTSPCCIVT EECCCCCCCCEEEEE	31.38	26745281
596	Phosphorylation	VSNRLVTSPCCIVTS ECCCCCCCCEEEEEE	14.41	25266776
598	Glutathionylation	NRLVTSPCCIVTSTY CCCCCCCEEEEEECC	2.18	24333276
598	S-palmitoylation	NRLVTSPCCIVTSTY CCCCCCCEEEEEECC	2.18	28680068
599	S-nitrosocysteine	RLVTSPCCIVTSTYG CCCCCCEEEEEECCC	2.96	-
599	Glutathionylation	RLVTSPCCIVTSTYG CCCCCCEEEEEECCC	2.96	24333276
599	S-nitrosylation	RLVTSPCCIVTSTYG CCCCCCEEEEEECCC	2.96	-
602	Phosphorylation	TSPCCIVTSTYGWTA CCCEEEEEECCCCHH	8.74	23984901
603	Phosphorylation	SPCCIVTSTYGWTAN CCEEEEEECCCCHHC	14.56	23984901
604	Phosphorylation	PCCIVTSTYGWTANM CEEEEEECCCCHHCH	19.38	23984901
605	Phosphorylation	CCIVTSTYGWTANME EEEEEECCCCHHCHH	15.50	20116462
608	Phosphorylation	VTSTYGWTANMERIM EEECCCCHHCHHHHH	12.09	25777480
616	Acetylation	ANMERIMKAQALRDN HCHHHHHHHHHHHCC	34.67	23806337
616	Methylation	ANMERIMKAQALRDN HCHHHHHHHHHHHCC	34.67	-
616	Succinylation	ANMERIMKAQALRDN HCHHHHHHHHHHHCC	34.67	23806337
616	Ubiquitination	ANMERIMKAQALRDN HCHHHHHHHHHHHCC	34.67	-
624	Phosphorylation	AQALRDNSTMGYMAA HHHHHCCCHHHHHHH	24.86	27841257
625	Phosphorylation	QALRDNSTMGYMAAK HHHHCCCHHHHHHHH	22.37	22006019
628	Phosphorylation	RDNSTMGYMAAKKHL HCCCHHHHHHHHHHC	3.46	29899451
632	Acetylation	TMGYMAAKKHLEINP HHHHHHHHHHCCCCC	31.05	23806337
632	Malonylation	TMGYMAAKKHLEINP HHHHHHHHHHCCCCC	31.05	26320211
632	Succinylation	TMGYMAAKKHLEINP HHHHHHHHHHCCCCC	31.05	-
632	Ubiquitination	TMGYMAAKKHLEINP HHHHHHHHHHCCCCC	31.05	-
633	Acetylation	MGYMAAKKHLEINPD HHHHHHHHHCCCCCC	49.01	23806337
633	Ubiquitination	MGYMAAKKHLEINPD HHHHHHHHHCCCCCC	49.01	22790023
642	Phosphorylation	LEINPDHSIIETLRQ CCCCCCCHHHHHHHH	32.42	25521595
646	Phosphorylation	PDHSIIETLRQKAEA CCCHHHHHHHHHHHH	19.48	26745281
655	Acetylation	RQKAEADKNDKSVKD HHHHHHCCCCCCHHH	74.27	23864654
705	Phosphorylation	GIDEDDPTVDDTSAA CCCCCCCCCCCCCCC	43.49	25777480
709	Phosphorylation	DDPTVDDTSAAVTEE CCCCCCCCCCCCCCC	18.79	25777480
710	Phosphorylation	DPTVDDTSAAVTEEM CCCCCCCCCCCCCCC	22.64	25777480
714	Phosphorylation	DDTSAAVTEEMPPLE CCCCCCCCCCCCCCC	22.85	25777480
726	Phosphorylation	PLEGDDDTSRMEEVD CCCCCCCCCCCCCCC	25.81	21183079
727	Phosphorylation	LEGDDDTSRMEEVD- CCCCCCCCCCCCCC-	36.30	19060867

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
5	T	Phosphorylation	Kinase	PRKDC	P97313	Uniprot
7	T	Phosphorylation	Kinase	PRKDC	P97313	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of HS90A_MOUSE !!

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 HS90A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDC37_MOUSE	Cdc37	physical	17189825
CHRD1_MOUSE	Chordc1	physical	23184943
CDK4_MOUSE	Cdk4	physical	11867521
IMB1_MOUSE	Kpnb1	physical	19581287
NUP62_MOUSE	Nup62	physical	19581287

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of HS90A_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-263, ANDMASS SPECTROMETRY.	19367708 [Abstract]
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS."; Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.; Mol. Cell. Proteomics 6:669-676(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231, AND MASSSPECTROMETRY.	17208939 [Abstract]
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263, AND MASSSPECTROMETRY.	17203969 [Abstract]
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis."; Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.; J. Proteome Res. 7:3957-3967(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-231 AND SER-263, ANDMASS SPECTROMETRY.	18630941 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-314, AND MASSSPECTROMETRY.	18034455 [Abstract]
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling."; Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.; J. Immunol. 179:5864-5876(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-493, AND MASSSPECTROMETRY.	17947660 [Abstract]