dbPTM

HS90B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HS90B_HUMAN
UniProt AC	P08238
Protein Name	Heat shock protein HSP 90-beta
Gene Name	HSP90AB1
Organism	Homo sapiens (Human).
Sequence Length	724
Subcellular Localization	Cytoplasm . Melanosome . Nucleus . Secreted . Cell membrane . Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). Translocates with BIRC2 from the nucleus to the cytoplasm during differentiation (PubMed
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. 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. [PubMed: 16478993]
Protein Sequence	MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEEDKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQSGDEMTSLSEYVSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKSLVSVTKEGLELPEDEEEKKKMEESKAKFENLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVKDLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVAAEEPNAAVPDEIPPLEGDEDASRMEEVD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
25	Sulfoxidation	QAEIAQLMSLIINTF HHHHHHHHHHHHHHH	1.72	28183972
31	Phosphorylation	LMSLIINTFYSNKEI HHHHHHHHHCCCHHH	17.34	21945579
33	Nitration	SLIINTFYSNKEIFL HHHHHHHCCCHHHHH	14.86	-
33	Phosphorylation	SLIINTFYSNKEIFL HHHHHHHCCCHHHHH	14.86	21945579
34	Phosphorylation	LIINTFYSNKEIFLR HHHHHHCCCHHHHHH	36.92	21945579
36	Acetylation	INTFYSNKEIFLREL HHHHCCCHHHHHHHH	46.37	72623285
36	Ubiquitination	INTFYSNKEIFLREL HHHHCCCHHHHHHHH	46.37	21906983
45	Phosphorylation	IFLRELISNASDALD HHHHHHHHCHHHHHH	38.68	20164059
48	Phosphorylation	RELISNASDALDKIR HHHHHCHHHHHHHHC	27.89	28152594
53	Acetylation	NASDALDKIRYESLT CHHHHHHHHCHHHCC	29.90	25953088
53	Ubiquitination	NASDALDKIRYESLT CHHHHHHHHCHHHCC	29.90	21890473
56	Nitration	DALDKIRYESLTDPS HHHHHHCHHHCCCHH	17.22	-
56	Phosphorylation	DALDKIRYESLTDPS HHHHHHCHHHCCCHH	17.22	27273156
58	Phosphorylation	LDKIRYESLTDPSKL HHHHCHHHCCCHHHC	27.86	25159151
60	Phosphorylation	KIRYESLTDPSKLDS HHCHHHCCCHHHCCC	55.96	25159151
63	Phosphorylation	YESLTDPSKLDSGKE HHHCCCHHHCCCCCE	48.97	21815630
64	Acetylation	ESLTDPSKLDSGKEL HHCCCHHHCCCCCEE	62.80	22640955
64	Ubiquitination	ESLTDPSKLDSGKEL HHCCCHHHCCCCCEE	62.80	21890473
67	Phosphorylation	TDPSKLDSGKELKID CCHHHCCCCCEEEEE	63.30	30108239
69	Acetylation	PSKLDSGKELKIDII HHHCCCCCEEEEEEC	64.92	23749302
69	Ubiquitination	PSKLDSGKELKIDII HHHCCCCCEEEEEEC	64.92	21890473
72	Acetylation	LDSGKELKIDIIPNP CCCCCEEEEEECCCH	39.15	27452117
72	Succinylation	LDSGKELKIDIIPNP CCCCCEEEEEECCCH	39.15	23954790
72	Sumoylation	LDSGKELKIDIIPNP CCCCCEEEEEECCCH	39.15	-
72	Ubiquitination	LDSGKELKIDIIPNP CCCCCEEEEEECCCH	39.15	-
83	Phosphorylation	IPNPQERTLTLVDTG CCCHHCCEEEEEECC	24.28	20873877
85	Phosphorylation	NPQERTLTLVDTGIG CHHCCEEEEEECCCC	24.91	20873877
89	Phosphorylation	RTLTLVDTGIGMTKA CEEEEEECCCCCCHH	24.18	29514088
93	Sulfoxidation	LVDTGIGMTKADLIN EEECCCCCCHHHHHH	3.08	28183972
94	Phosphorylation	VDTGIGMTKADLINN EECCCCCCHHHHHHH	20.19	21712546
95	Ubiquitination	DTGIGMTKADLINNL ECCCCCCHHHHHHHH	30.89	21890473
104	Phosphorylation	DLINNLGTIAKSGTK HHHHHHHHHHHHHHH	22.41	25159151
107	Malonylation	NNLGTIAKSGTKAFM HHHHHHHHHHHHHHH	45.64	26320211
107	Ubiquitination	NNLGTIAKSGTKAFM HHHHHHHHHHHHHHH	45.64	21890473
108	Phosphorylation	NLGTIAKSGTKAFME HHHHHHHHHHHHHHH	42.55	30624053
110	Phosphorylation	GTIAKSGTKAFMEAL HHHHHHHHHHHHHHH	26.70	28464451
111	Ubiquitination	TIAKSGTKAFMEALQ HHHHHHHHHHHHHHH	43.05	-
114	Sulfoxidation	KSGTKAFMEALQAGA HHHHHHHHHHHHCCC	3.35	28183972
124	Phosphorylation	LQAGADISMIGQFGV HHCCCCEEEEECCCC	12.61	-
125	Sulfoxidation	QAGADISMIGQFGVG HCCCCEEEEECCCCH	4.00	28183972
148	Ubiquitination	EKVVVITKHNDDEQY EEEEEEECCCCCCCE	29.32	21906983
155	Phosphorylation	KHNDDEQYAWESSAG CCCCCCCEEEECCCC	16.19	28152594
159	Phosphorylation	DEQYAWESSAGGSFT CCCEEEECCCCCEEE	18.13	21964256
160	Phosphorylation	EQYAWESSAGGSFTV CCEEEECCCCCEEEE	21.29	25693802
164	Phosphorylation	WESSAGGSFTVRADH EECCCCCEEEEEECC	19.47	21964256
166	Phosphorylation	SSAGGSFTVRADHGE CCCCCEEEEEECCCC	15.69	24719451
177	Methylation	DHGEPIGRGTKVILH CCCCCCCCCCEEEEE	50.78	115479847
179	Phosphorylation	GEPIGRGTKVILHLK CCCCCCCCEEEEEEC	22.30	21964256
180	Sumoylation	EPIGRGTKVILHLKE CCCCCCCEEEEEECC	30.06	-
180	Ubiquitination	EPIGRGTKVILHLKE CCCCCCCEEEEEECC	30.06	21906983
186	Acetylation	TKVILHLKEDQTEYL CEEEEEECCCHHHHH	48.80	30583301
186	Methylation	TKVILHLKEDQTEYL CEEEEEECCCHHHHH	48.80	30583301
186	Ubiquitination	TKVILHLKEDQTEYL CEEEEEECCCHHHHH	48.80	21906983
190	Phosphorylation	LHLKEDQTEYLEERR EEECCCHHHHHHHHH	38.63	28152594
192	Phosphorylation	LKEDQTEYLEERRVK ECCCHHHHHHHHHHH	23.85	27273156
196	Methylation	QTEYLEERRVKEVVK HHHHHHHHHHHHHHH	39.04	-
204	Acetylation	RVKEVVKKHSQFIGY HHHHHHHHHHHHCCC	36.56	26051181
204	Ubiquitination	RVKEVVKKHSQFIGY HHHHHHHHHHHHCCC	36.56	21890473
206	Phosphorylation	KEVVKKHSQFIGYPI HHHHHHHHHHCCCCE	35.35	28152594
211	Phosphorylation	KHSQFIGYPITLYLE HHHHHCCCCEEEEEH	6.14	28152594
214	Phosphorylation	QFIGYPITLYLEKER HHCCCCEEEEEHHHH	12.59	28152594
216	Phosphorylation	IGYPITLYLEKEREK CCCCEEEEEHHHHHH	12.26	28152594
219	Acetylation	PITLYLEKEREKEIS CEEEEEHHHHHHCCC	60.52	23236377
219	Succinylation	PITLYLEKEREKEIS CEEEEEHHHHHHCCC	60.52	-
219	Succinylation	PITLYLEKEREKEIS CEEEEEHHHHHHCCC	60.52	23954790
219	Ubiquitination	PITLYLEKEREKEIS CEEEEEHHHHHHCCC	60.52	21890473
226	Phosphorylation	KEREKEISDDEAEEE HHHHHCCCHHHHHHH	39.85	19664994
237	Acetylation	AEEEKGEKEEEDKDD HHHHHCCCCCCCCCC	78.19	21339330
237	Ubiquitination	AEEEKGEKEEEDKDD HHHHHCCCCCCCCCC	78.19	21906983
255	Phosphorylation	PKIEDVGSDEEDDSG CCHHCCCCCCCCCCC	41.52	19664994
261	Phosphorylation	GSDEEDDSGKDKKKK CCCCCCCCCCCCHHH	61.13	29255136
263	Acetylation	DEEDDSGKDKKKKTK CCCCCCCCCCHHHHH	71.03	23236377
263	Ubiquitination	DEEDDSGKDKKKKTK CCCCCCCCCCHHHHH	71.03	-
269	Phosphorylation	GKDKKKKTKKIKEKY CCCCHHHHHHHHHHH	46.58	26074081
273	Ubiquitination	KKKTKKIKEKYIDQE HHHHHHHHHHHCCHH	57.97	-
275	Acetylation	KTKKIKEKYIDQEEL HHHHHHHHHCCHHHH	42.37	26051181
275	Methylation	KTKKIKEKYIDQEEL HHHHHHHHHCCHHHH	42.37	129319
275	Ubiquitination	KTKKIKEKYIDQEEL HHHHHHHHHCCHHHH	42.37	21906983
276	Nitration	TKKIKEKYIDQEELN HHHHHHHHCCHHHHH	15.72	-
276	Phosphorylation	TKKIKEKYIDQEELN HHHHHHHHCCHHHHH	15.72	25159151
284	Acetylation	IDQEELNKTKPIWTR CCHHHHHCCCCCCCC	71.23	22640947
284	Malonylation	IDQEELNKTKPIWTR CCHHHHHCCCCCCCC	71.23	26320211
284	Ubiquitination	IDQEELNKTKPIWTR CCHHHHHCCCCCCCC	71.23	21906983
285	Phosphorylation	DQEELNKTKPIWTRN CHHHHHCCCCCCCCC	40.76	23401153
286	Acetylation	QEELNKTKPIWTRNP HHHHHCCCCCCCCCC	35.79	-
286	Methylation	QEELNKTKPIWTRNP HHHHHCCCCCCCCCC	35.79	42353157
286	Ubiquitination	QEELNKTKPIWTRNP HHHHHCCCCCCCCCC	35.79	21906983
290	Phosphorylation	NKTKPIWTRNPDDIT HCCCCCCCCCCCCCC	22.68	29978859
291	Methylation	KTKPIWTRNPDDITQ CCCCCCCCCCCCCCH	37.37	115479887
297	Phosphorylation	TRNPDDITQEEYGEF CCCCCCCCHHHHHHH	36.60	17525332
301	Phosphorylation	DDITQEEYGEFYKSL CCCCHHHHHHHHHHH	22.62	21712546
305	Phosphorylation	QEEYGEFYKSLTNDW HHHHHHHHHHHCCCH	8.72	28796482
306	Acetylation	EEYGEFYKSLTNDWE HHHHHHHHHHCCCHH	44.29	26822725
306	Sumoylation	EEYGEFYKSLTNDWE HHHHHHHHHHCCCHH	44.29	-
306	Ubiquitination	EEYGEFYKSLTNDWE HHHHHHHHHHCCCHH	44.29	21906983
307	Phosphorylation	EYGEFYKSLTNDWED HHHHHHHHHCCCHHH	29.10	30266825
309	Phosphorylation	GEFYKSLTNDWEDHL HHHHHHHCCCHHHCE	37.92	30266825
319	Acetylation	WEDHLAVKHFSVEGQ HHHCEEEEEEEEECE	33.07	156797
319	Ubiquitination	WEDHLAVKHFSVEGQ HHHCEEEEEEEEECE	33.07	21906983
322	Phosphorylation	HLAVKHFSVEGQLEF CEEEEEEEEECEEEE	20.98	27251275
347	Acetylation	PFDLFENKKKKNNIK CCCCCCCCCCCCCCE	59.79	25953088
347	Malonylation	PFDLFENKKKKNNIK CCCCCCCCCCCCCCE	59.79	26320211
347	Methylation	PFDLFENKKKKNNIK CCCCCCCCCCCCCCE	59.79	-
347	Ubiquitination	PFDLFENKKKKNNIK CCCCCCCCCCCCCCE	59.79	-
348	Acetylation	FDLFENKKKKNNIKL CCCCCCCCCCCCCEE	79.25	30583295
348	Ubiquitination	FDLFENKKKKNNIKL CCCCCCCCCCCCCEE	79.25	-
350	Ubiquitination	LFENKKKKNNIKLYV CCCCCCCCCCCEEEE	65.20	-
354	Acetylation	KKKKNNIKLYVRRVF CCCCCCCEEEEEEEE	35.57	12421637
354	Malonylation	KKKKNNIKLYVRRVF CCCCCCCEEEEEEEE	35.57	26320211
354	Ubiquitination	KKKKNNIKLYVRRVF CCCCCCCEEEEEEEE	35.57	21906983
363	Sulfoxidation	YVRRVFIMDSCDELI EEEEEECCCCHHHHH	1.79	28465586
365	O-linked_Glycosylation	RRVFIMDSCDELIPE EEEECCCCHHHHHHH	13.19	23301498
365	Phosphorylation	RRVFIMDSCDELIPE EEEECCCCHHHHHHH	13.19	21406692
366	Glutathionylation	RVFIMDSCDELIPEY EEECCCCHHHHHHHH	4.03	22555962
373	Phosphorylation	CDELIPEYLNFIRGV HHHHHHHHHHHHHCC	11.11	27251275
383	Phosphorylation	FIRGVVDSEDLPLNI HHHCCCCCCCCCCCC	22.77	20873877
387	Acetylation	VVDSEDLPLNISREM CCCCCCCCCCCCHHH	35.37	19608861
387	Ubiquitination	VVDSEDLPLNISREM CCCCCCCCCCCCHHH	35.37	19608861
391	Phosphorylation	EDLPLNISREMLQQS CCCCCCCCHHHHHHH	22.55	30266825
398	Phosphorylation	SREMLQQSKILKVIR CHHHHHHHHHHHHHH	14.54	29116813
399	N6-malonyllysine	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	-
399	Acetylation	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	22640939
399	Malonylation	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	26320211
399	Sumoylation	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	-
399	Ubiquitination	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	-
402	Acetylation	LQQSKILKVIRKNIV HHHHHHHHHHHHHHH	38.80	26051181
411	Acetylation	IRKNIVKKCLELFSE HHHHHHHHHHHHHHH	32.91	26051181
411	Malonylation	IRKNIVKKCLELFSE HHHHHHHHHHHHHHH	32.91	26320211
411	Ubiquitination	IRKNIVKKCLELFSE HHHHHHHHHHHHHHH	32.91	21890473
412	S-nitrosocysteine	RKNIVKKCLELFSEL HHHHHHHHHHHHHHH	2.71	-
412	Glutathionylation	RKNIVKKCLELFSEL HHHHHHHHHHHHHHH	2.71	22555962
412	S-nitrosylation	RKNIVKKCLELFSEL HHHHHHHHHHHHHHH	2.71	20140087
417	Phosphorylation	KKCLELFSELAEDKE HHHHHHHHHHHHCHH	44.30	21406692
423	Acetylation	FSELAEDKENYKKFY HHHHHHCHHHHHHHH	39.09	26822725
423	Ubiquitination	FSELAEDKENYKKFY HHHHHHCHHHHHHHH	39.09	-
426	Phosphorylation	LAEDKENYKKFYEAF HHHCHHHHHHHHHHH	19.35	21406692
427	Acetylation	AEDKENYKKFYEAFS HHCHHHHHHHHHHHH	48.24	25953088
427	Ubiquitination	AEDKENYKKFYEAFS HHCHHHHHHHHHHHH	48.24	-
428	Acetylation	EDKENYKKFYEAFSK HCHHHHHHHHHHHHH	42.70	27178108
428	Succinylation	EDKENYKKFYEAFSK HCHHHHHHHHHHHHH	42.70	23954790
428	Ubiquitination	EDKENYKKFYEAFSK HCHHHHHHHHHHHHH	42.70	21890473
430	Phosphorylation	KENYKKFYEAFSKNL HHHHHHHHHHHHHHC	18.41	28152594
433	Acetylation	YKKFYEAFSKNLKLG HHHHHHHHHHHCCCC	7.74	19608861
433	Ubiquitination	YKKFYEAFSKNLKLG HHHHHHHHHHHCCCC	7.74	19608861
434	O-linked_Glycosylation	KKFYEAFSKNLKLGI HHHHHHHHHHCCCCC	27.90	UniProtKB CARBOHYD
434	Phosphorylation	KKFYEAFSKNLKLGI HHHHHHHHHHCCCCC	27.90	30266825
435	Acetylation	KFYEAFSKNLKLGIH HHHHHHHHHCCCCCC	60.90	19608861
435	Malonylation	KFYEAFSKNLKLGIH HHHHHHHHHCCCCCC	60.90	26320211
435	Methylation	KFYEAFSKNLKLGIH HHHHHHHHHCCCCCC	60.90	19608861
435	Ubiquitination	KFYEAFSKNLKLGIH HHHHHHHHHCCCCCC	60.90	21890473
438	Acetylation	EAFSKNLKLGIHEDS HHHHHHCCCCCCCCC	54.80	25953088
438	Ubiquitination	EAFSKNLKLGIHEDS HHHHHHCCCCCCCCC	54.80	21890473
445	Phosphorylation	KLGIHEDSTNRRRLS CCCCCCCCCCHHHHH	25.29	23401153
446	Phosphorylation	LGIHEDSTNRRRLSE CCCCCCCCCHHHHHH	45.10	30266825
452	O-linked_Glycosylation	STNRRRLSELLRYHT CCCHHHHHHHHHHHH	25.12	UniProtKB CARBOHYD
452	Phosphorylation	STNRRRLSELLRYHT CCCHHHHHHHHHHHH	25.12	28355574
457	Phosphorylation	RLSELLRYHTSQSGD HHHHHHHHHHCCCCC	14.93	28152594
459	Phosphorylation	SELLRYHTSQSGDEM HHHHHHHHCCCCCCC	21.37	28152594
460	Phosphorylation	ELLRYHTSQSGDEMT HHHHHHHCCCCCCCC	14.72	28152594
462	Phosphorylation	LRYHTSQSGDEMTSL HHHHHCCCCCCCCHH	48.23	28152594
466	Sulfoxidation	TSQSGDEMTSLSEYV HCCCCCCCCHHHHHH	3.52	21406390
467	Phosphorylation	SQSGDEMTSLSEYVS CCCCCCCCHHHHHHH	25.19	28152594
468	Phosphorylation	QSGDEMTSLSEYVSR CCCCCCCHHHHHHHH	28.70	27422710
470	Phosphorylation	GDEMTSLSEYVSRMK CCCCCHHHHHHHHHH	27.01	28152594
472	Phosphorylation	EMTSLSEYVSRMKET CCCHHHHHHHHHHHH	10.59	28152594
474	Phosphorylation	TSLSEYVSRMKETQK CHHHHHHHHHHHHHC	26.25	28152594
475	Methylation	SLSEYVSRMKETQKS HHHHHHHHHHHHHCC	30.10	115479895
477	Acetylation	SEYVSRMKETQKSIY HHHHHHHHHHHCCEE	57.40	23749302
477	Ubiquitination	SEYVSRMKETQKSIY HHHHHHHHHHHCCEE	57.40	19913553
479	Phosphorylation	YVSRMKETQKSIYYI HHHHHHHHHCCEEEE	35.46	23312004
481	Acetylation	SRMKETQKSIYYITG HHHHHHHCCEEEECC	46.36	19608861
481	Malonylation	SRMKETQKSIYYITG HHHHHHHCCEEEECC	46.36	26320211
481	Ubiquitination	SRMKETQKSIYYITG HHHHHHHCCEEEECC	46.36	21890473
482	Phosphorylation	RMKETQKSIYYITGE HHHHHHCCEEEECCC	13.15	25159151
484	Nitration	KETQKSIYYITGESK HHHHCCEEEECCCCH	8.91	-
484	Phosphorylation	KETQKSIYYITGESK HHHHCCEEEECCCCH	8.91	27273156
485	Phosphorylation	ETQKSIYYITGESKE HHHCCEEEECCCCHH	7.13	27794612
487	Phosphorylation	QKSIYYITGESKEQV HCCEEEECCCCHHHH	20.83	25348954
490	Phosphorylation	IYYITGESKEQVANS EEEECCCCHHHHHHH	42.72	28152594
491	Acetylation	YYITGESKEQVANSA EEECCCCHHHHHHHH	48.11	23954790
491	Ubiquitination	YYITGESKEQVANSA EEECCCCHHHHHHHH	48.11	21906983
497	Phosphorylation	SKEQVANSAFVERVR CHHHHHHHHHHHHHH	17.22	28985074
505	Acetylation	AFVERVRKRGFEVVY HHHHHHHHCCCEEEE	54.75	26051181
505	Ubiquitination	AFVERVRKRGFEVVY HHHHHHHHCCCEEEE	54.75	-
506	Methylation	FVERVRKRGFEVVYM HHHHHHHCCCEEEEE	44.46	115479879
512	Phosphorylation	KRGFEVVYMTEPIDE HCCCEEEEECCCCCH	11.96	20068231
513	Sulfoxidation	RGFEVVYMTEPIDEY CCCEEEEECCCCCHH	2.01	30846556
514	Phosphorylation	GFEVVYMTEPIDEYC CCEEEEECCCCCHHH	22.41	20068231
520	Acetylation	MTEPIDEYCVQQLKE ECCCCCHHHHHHHHH	8.32	19608861
520	Phosphorylation	MTEPIDEYCVQQLKE ECCCCCHHHHHHHHH	8.32	25884760
520	Ubiquitination	MTEPIDEYCVQQLKE ECCCCCHHHHHHHHH	8.32	19608861
521	Glutathionylation	TEPIDEYCVQQLKEF CCCCCHHHHHHHHHC	1.78	22555962
521	S-palmitoylation	TEPIDEYCVQQLKEF CCCCCHHHHHHHHHC	1.78	26865113
526	Acetylation	EYCVQQLKEFDGKSL HHHHHHHHHCCCCCC	52.58	25953088
526	Ubiquitination	EYCVQQLKEFDGKSL HHHHHHHHHCCCCCC	52.58	-
531	Acetylation	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	23954790
531	Methylation	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	24880080
531	Succinylation	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	-
531	Succinylation	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	21906983
531	Sumoylation	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	-
531	Ubiquitination	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	21890473
532	Phosphorylation	LKEFDGKSLVSVTKE HHHCCCCCCEEEEHH	39.26	30266825
535	Phosphorylation	FDGKSLVSVTKEGLE CCCCCCEEEEHHCCC	29.39	30266825
537	Phosphorylation	GKSLVSVTKEGLELP CCCCEEEEHHCCCCC	18.83	30266825
538	Acetylation	KSLVSVTKEGLELPE CCCEEEEHHCCCCCC	47.86	23236377
538	Ubiquitination	KSLVSVTKEGLELPE CCCEEEEHHCCCCCC	47.86	21890473
550	Acetylation	LPEDEEEKKKMEESK CCCCHHHHHHHHHHH	62.06	26051181
550	Ubiquitination	LPEDEEEKKKMEESK CCCCHHHHHHHHHHH	62.06	21906983
551	Acetylation	PEDEEEKKKMEESKA CCCHHHHHHHHHHHH	61.71	26051181
551	Ubiquitination	PEDEEEKKKMEESKA CCCHHHHHHHHHHHH	61.71	-
552	Ubiquitination	EDEEEKKKMEESKAK CCHHHHHHHHHHHHH	63.71	-
553	Sulfoxidation	DEEEKKKMEESKAKF CHHHHHHHHHHHHHH	10.69	30846556
556	Phosphorylation	EKKKMEESKAKFENL HHHHHHHHHHHHHHH	25.30	28258704
559	Acetylation	KMEESKAKFENLCKL HHHHHHHHHHHHHHH	57.88	23749302
559	Methylation	KMEESKAKFENLCKL HHHHHHHHHHHHHHH	57.88	70059
559	Ubiquitination	KMEESKAKFENLCKL HHHHHHHHHHHHHHH	57.88	21890473
564	S-nitrosylation	KAKFENLCKLMKEIL HHHHHHHHHHHHHHH	4.85	2212679
565	Acetylation	AKFENLCKLMKEILD HHHHHHHHHHHHHHH	55.57	23749302
565	Malonylation	AKFENLCKLMKEILD HHHHHHHHHHHHHHH	55.57	26320211
565	Methylation	AKFENLCKLMKEILD HHHHHHHHHHHHHHH	55.57	42353145
565	Ubiquitination	AKFENLCKLMKEILD HHHHHHHHHHHHHHH	55.57	21906983
568	Acetylation	ENLCKLMKEILDKKV HHHHHHHHHHHHHCC	52.63	23749302
568	Malonylation	ENLCKLMKEILDKKV HHHHHHHHHHHHHCC	52.63	26320211
568	Ubiquitination	ENLCKLMKEILDKKV HHHHHHHHHHHHHCC	52.63	21890473
573	Ubiquitination	LMKEILDKKVEKVTI HHHHHHHHCCEEEEE	56.10	-
574	Acetylation	MKEILDKKVEKVTIS HHHHHHHCCEEEEEC	56.12	23749302
574	Methylation	MKEILDKKVEKVTIS HHHHHHHCCEEEEEC	56.12	24880080
574	Succinylation	MKEILDKKVEKVTIS HHHHHHHCCEEEEEC	56.12	23954790
574	Ubiquitination	MKEILDKKVEKVTIS HHHHHHHCCEEEEEC	56.12	-
577	Acetylation	ILDKKVEKVTISNRL HHHHCCEEEEECCCC	47.90	25953088
577	Succinylation	ILDKKVEKVTISNRL HHHHCCEEEEECCCC	47.90	-
577	Succinylation	ILDKKVEKVTISNRL HHHHCCEEEEECCCC	47.90	27452117
577	Ubiquitination	ILDKKVEKVTISNRL HHHHCCEEEEECCCC	47.90	-
579	Phosphorylation	DKKVEKVTISNRLVS HHCCEEEEECCCCCC	29.74	23312004
581	Phosphorylation	KVEKVTISNRLVSSP CCEEEEECCCCCCCC	13.41	23312004
586	Phosphorylation	TISNRLVSSPCCIVT EECCCCCCCCEEEEE	32.90	21945579
587	Phosphorylation	ISNRLVSSPCCIVTS ECCCCCCCCEEEEEE	17.93	21945579
590	S-nitrosocysteine	RLVSSPCCIVTSTYG CCCCCCEEEEEECCC	2.96	-
590	Glutathionylation	RLVSSPCCIVTSTYG CCCCCCEEEEEECCC	2.96	22555962
590	S-nitrosylation	RLVSSPCCIVTSTYG CCCCCCEEEEEECCC	2.96	19696785
593	Phosphorylation	SSPCCIVTSTYGWTA CCCEEEEEECCCCHH	8.74	21945579
594	Phosphorylation	SPCCIVTSTYGWTAN CCEEEEEECCCCHHC	14.56	21945579
595	Phosphorylation	PCCIVTSTYGWTANM CEEEEEECCCCHHCH	19.38	21945579
596	Nitration	CCIVTSTYGWTANME EEEEEECCCCHHCHH	15.50	-
596	Phosphorylation	CCIVTSTYGWTANME EEEEEECCCCHHCHH	15.50	21945579
599	Phosphorylation	VTSTYGWTANMERIM EEECCCCHHCHHHHH	12.09	21945579
602	Sulfoxidation	TYGWTANMERIMKAQ CCCCHHCHHHHHHHH	3.21	30846556
607	Acetylation	ANMERIMKAQALRDN HCHHHHHHHHHHHCC	34.67	7289923
607	Methylation	ANMERIMKAQALRDN HCHHHHHHHHHHHCC	34.67	-
607	Ubiquitination	ANMERIMKAQALRDN HCHHHHHHHHHHHCC	34.67	21906983
612	Methylation	IMKAQALRDNSTMGY HHHHHHHHCCCHHHH	44.04	-
615	Phosphorylation	AQALRDNSTMGYMMA HHHHHCCCHHHHHHH	24.86	21945579
616	Phosphorylation	QALRDNSTMGYMMAK HHHHCCCHHHHHHHH	22.37	21945579
617	Sulfoxidation	ALRDNSTMGYMMAKK HHHCCCHHHHHHHHH	3.48	30846556
619	Phosphorylation	RDNSTMGYMMAKKHL HCCCHHHHHHHHHHC	3.48	21945579
620	Sulfoxidation	DNSTMGYMMAKKHLE CCCHHHHHHHHHHCC	1.42	28465586
621	Sulfoxidation	NSTMGYMMAKKHLEI CCHHHHHHHHHHCCC	3.58	28465586
623	Acetylation	TMGYMMAKKHLEINP HHHHHHHHHHCCCCC	23.88	23954790
623	Malonylation	TMGYMMAKKHLEINP HHHHHHHHHHCCCCC	23.88	26320211
623	Methylation	TMGYMMAKKHLEINP HHHHHHHHHHCCCCC	23.88	23748837
623	Ubiquitination	TMGYMMAKKHLEINP HHHHHHHHHHCCCCC	23.88	21890473
624	Acetylation	MGYMMAKKHLEINPD HHHHHHHHHCCCCCC	43.83	16916647
624	Ubiquitination	MGYMMAKKHLEINPD HHHHHHHHHCCCCCC	43.83	21890473
637	Phosphorylation	PDHPIVETLRQKAEA CCCHHHHHHHHHHHH	19.15	28985074
639	Methylation	HPIVETLRQKAEADK CHHHHHHHHHHHHCC	43.29	115479871
641	Ubiquitination	IVETLRQKAEADKND HHHHHHHHHHHCCCC	41.58	-
649	Ubiquitination	AEADKNDKAVKDLVV HHHCCCCHHHHHHHH	65.55	21906983
669	Phosphorylation	ALLSSGFSLEDPQTH HHHHCCCCCCCCCCH	34.08	20068231
685	Ubiquitination	NRIYRMIKLGLGIDE HHHHHHHHHCCCCCH	27.45	21906983
718	Phosphorylation	LEGDEDASRMEEVD- CCCCCCHHHCCCCC-	44.47	29255136
720	Sulfoxidation	GDEDASRMEEVD--- CCCCHHHCCCCC---	4.82	30846556

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
89	T	Phosphorylation	Kinase	PNCK	Q6P2M8	GPS
89	T	Phosphorylation	Kinase	PKACA	P17612	PSP
226	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
226	S	Phosphorylation	Kinase	CSK21	P68400	PhosphoELM
226	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
226	S	Phosphorylation	Kinase	CSNK2A1	P33674	GPS
255	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
255	S	Phosphorylation	Kinase	CK2_GROUP	-	PhosphoELM
255	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
255	S	Phosphorylation	Kinase	CSNK2A1	P33674	GPS
255	S	Phosphorylation	Kinase	CSK21	P68400	PhosphoELM
301	Y	Phosphorylation	Kinase	SRC	P12931	Uniprot
452	S	Phosphorylation	Kinase	AURKB	Q96GD4	GPS
718	S	Phosphorylation	Kinase	CK1A	P48729	PSP
718	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
718	S	Phosphorylation	Kinase	PLK2	Q9NYY3	Uniprot
718	S	Phosphorylation	Kinase	PLK3	Q9H4B4	Uniprot
718	S	Phosphorylation	Kinase	CK2A1	P68400	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
226	S	Phosphorylation	15581363
Phosphorylation at Ser-226 and Ser-255 inhibits AHR interaction.
255	S	Phosphorylation
Phosphorylation at Ser-226 and Ser-255 inhibits AHR interaction.

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 HS90B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HS90A_HUMAN	HSP90AA1	physical	20353823
KPCE_HUMAN	PRKCE	physical	20353823
FGFR3_HUMAN	FGFR3	physical	21487019
RS6_HUMAN	RPS6	physical	22939629
RL6_HUMAN	RPL6	physical	22939629
MYH9_HUMAN	MYH9	physical	22939629
RL17_HUMAN	RPL17	physical	22939629
RL14_HUMAN	RPL14	physical	22939629
RL7A_HUMAN	RPL7A	physical	22939629
RS2_HUMAN	RPS2	physical	22939629
RS26_HUMAN	RPS26	physical	22939629
RS23_HUMAN	RPS23	physical	22939629
RL32_HUMAN	RPL32	physical	22939629
RL10A_HUMAN	RPL10A	physical	22939629
RS16_HUMAN	RPS16	physical	22939629
RL3_HUMAN	RPL3	physical	22939629
STIP1_HUMAN	STIP1	physical	22939629
MYL6_HUMAN	MYL6	physical	22939629
IF4A1_HUMAN	EIF4A1	physical	22939629
STML2_HUMAN	STOML2	physical	22939629
MCM5_HUMAN	MCM5	physical	22939629
VATB2_HUMAN	ATP6V1B2	physical	22939629
SMD1_HUMAN	SNRPD1	physical	22939629
WASL_HUMAN	WASL	physical	15791211
TCPA_HUMAN	TCP1	physical	16263121
HS105_HUMAN	HSPH1	physical	16263121
PRKDC_HUMAN	PRKDC	physical	16263121
GNAI2_HUMAN	GNAI2	physical	16263121
XPO1_HUMAN	XPO1	physical	16263121
KPYM_HUMAN	PKM	physical	16263121
G3P_HUMAN	GAPDH	physical	16263121
PGK1_HUMAN	PGK1	physical	16263121
LDHA_HUMAN	LDHA	physical	16263121
ALDOA_HUMAN	ALDOA	physical	16263121
MDHC_HUMAN	MDH1	physical	16263121
C1TC_HUMAN	MTHFD1	physical	16263121
SERC_HUMAN	PSAT1	physical	16263121
FAS_HUMAN	FASN	physical	16263121
SIAS_HUMAN	NANS	physical	16263121
ACTG_HUMAN	ACTG1	physical	16263121
TPM3_HUMAN	TPM3	physical	16263121
FLNA_HUMAN	FLNA	physical	16263121
MYH9_HUMAN	MYH9	physical	16263121
SPTN1_HUMAN	SPTAN1	physical	16263121
NUMA1_HUMAN	NUMA1	physical	16263121
ACTN1_HUMAN	ACTN1	physical	16263121
UBA1_HUMAN	UBA1	physical	16263121
PSMD1_HUMAN	PSMD1	physical	16263121
PSB5_HUMAN	PSMB5	physical	16263121
SYAC_HUMAN	AARS	physical	16263121
EF2_HUMAN	EEF2	physical	16263121
EIF3H_HUMAN	EIF3H	physical	16263121
RLA0_HUMAN	RPLP0	physical	16263121
RS6_HUMAN	RPS6	physical	16263121
RS4X_HUMAN	RPS4X	physical	16263121
RL7_HUMAN	RPL7	physical	16263121
RS3A_HUMAN	RPS3A	physical	16263121
RL5_HUMAN	RPL5	physical	16263121
SYIM_HUMAN	IARS2	physical	16263121
RSSA_HUMAN	RPSA	physical	16263121
AHSA1_HUMAN	AHSA1	physical	20226818
MK07_HUMAN	MAPK7	physical	23428871
CDC37_HUMAN	CDC37	physical	23428871
CHRD1_MOUSE	Chordc1	physical	15642353
SGTA_HUMAN	SGTA	physical	21988832
TEBP_HUMAN	PTGES3	physical	21988832
CSN4_HUMAN	COPS4	physical	22863883
MCM2_HUMAN	MCM2	physical	22863883
MVP_HUMAN	MVP	physical	22863883
HS90A_HUMAN	HSP90AA1	physical	25036637
CC117_HUMAN	CCDC117	physical	25036637
PPP5_HUMAN	PPP5C	physical	25036637
TTC4_HUMAN	TTC4	physical	25036637
CHIP_HUMAN	STUB1	physical	25036637
TOM34_HUMAN	TOMM34	physical	25036637
FKBP5_HUMAN	FKBP5	physical	25036637
CDC37_HUMAN	CDC37	physical	25036637
FKBP4_HUMAN	FKBP4	physical	25036637
AHSA1_HUMAN	AHSA1	physical	25036637
HGH1_HUMAN	HGH1	physical	25036637
TBA1A_HUMAN	TUBA1A	physical	25036637
TEBP_HUMAN	PTGES3	physical	25036637
STIP1_HUMAN	STIP1	physical	25036637
TMOD4_HUMAN	TMOD4	physical	25036637
CYBP_HUMAN	CACYBP	physical	25036637
AIP_HUMAN	AIP	physical	25036637
HS90B_HUMAN	HSP90AB1	physical	10543959
CD37L_HUMAN	CDC37L1	physical	25416956
AHSA1_HUMAN	AHSA1	physical	26344197
ATPA_HUMAN	ATP5A1	physical	26344197
CALR_HUMAN	CALR	physical	26344197
OST48_HUMAN	DDOST	physical	26344197
DNJA2_HUMAN	DNAJA2	physical	26344197
G3P_HUMAN	GAPDH	physical	26344197
HSP74_HUMAN	HSPA4	physical	26344197
HSP7C_HUMAN	HSPA8	physical	26344197
CH60_HUMAN	HSPD1	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
IPO7_HUMAN	IPO7	physical	26344197
NPM3_HUMAN	NPM3	physical	26344197
PDIA1_HUMAN	P4HB	physical	26344197
SSRD_HUMAN	SSR4	physical	26344197
STIP1_HUMAN	STIP1	physical	26344197
TBB5_HUMAN	TUBB	physical	26344197
RL40_HUMAN	UBA52	physical	26344197
QCR2_HUMAN	UQCRC2	physical	26344197
TRAF2_HUMAN	TRAF2	physical	25241761
IKKB_HUMAN	IKBKB	physical	25241761
GNAI2_HUMAN	GNAI2	physical	25241761
FLNA_HUMAN	FLNA	physical	25241761
NFKB1_HUMAN	NFKB1	physical	25241761
HSF1_HUMAN	HSF1	physical	26517842
HIF1A_HUMAN	HIF1A	physical	26517842
ERR2_HUMAN	ESRRB	physical	26517842
MET_HUMAN	MET	physical	26517842
KEAP1_HUMAN	KEAP1	physical	26517842
RHBT2_HUMAN	RHOBTB2	physical	26517842
EGLN1_HUMAN	EGLN1	physical	23413029
TEBP_HUMAN	PTGES3	physical	21183720
EGLN1_HUMAN	EGLN1	physical	24711448
SRC_HUMAN	SRC	physical	28215707
FANCA_HUMAN	FANCA	physical	28215707
CDC37_HUMAN	CDC37	physical	28215707
SODC_HUMAN	SOD1	physical	28215707
AHSA1_HUMAN	AHSA1	physical	25486457
CDC37_HUMAN	CDC37	physical	25486457

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 HS90B_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-275; LYS-284; LYS-354;LYS-399; LYS-402; LYS-435; LYS-481 AND LYS-568, AND MASS SPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-624, AND MASS SPECTROMETRY.	16916647 [Abstract]
Malonylation
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-399.	21908771 [Abstract]
N6-malonyllysine
Reference	PubMed
"The first identification of lysine malonylation substrates and itsregulatory enzyme."; Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,Dai J., Verdin E., Ye Y., Zhao Y.; Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). Cited for: MALONYLATION AT LYS-399.	21908771 [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-255, 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-255, AND MASSSPECTROMETRY.	19369195 [Abstract]
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography."; Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.; Proteomics 8:1346-1361(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, ANDMASS SPECTROMETRY.	18318008 [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-226; SER-255; SER-261;SER-307; SER-452; SER-532 AND SER-718, 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-226; SER-255 ANDSER-261, AND MASS SPECTROMETRY.	18691976 [Abstract]
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment."; Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; J. Proteome Res. 7:5167-5176(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND MASSSPECTROMETRY.	19367720 [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-226 AND SER-255, ANDMASS SPECTROMETRY.	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-226 AND SER-255, ANDMASS 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-226 AND SER-255, ANDMASS SPECTROMETRY.	17287340 [Abstract]
"Toward a global characterization of the phosphoproteome in prostatecancer cells: identification of phosphoproteins in the LNCaP cellline."; Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; Electrophoresis 28:2027-2034(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASSSPECTROMETRY.	17487921 [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-255, AND MASSSPECTROMETRY.	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-226; SER-255 ANDSER-261, AND MASS SPECTROMETRY.	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-226 AND SER-255, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASSSPECTROMETRY.	16094384 [Abstract]
"Phosphoproteomic analysis of synaptosomes from human cerebralcortex."; DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P.,Pant H.C., Dosemeci A.; J. Proteome Res. 4:306-315(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASSSPECTROMETRY.	15822905 [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-255 AND SER-261, ANDMASS SPECTROMETRY.	15302935 [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 THR-297, AND MASSSPECTROMETRY.	17525332 [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-484, AND MASSSPECTROMETRY.	19534553 [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-484, AND MASSSPECTROMETRY.	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-484, AND MASSSPECTROMETRY.	15592455 [Abstract]

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