dbPTM

HS90B_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HS90B_MOUSE
UniProt AC	P11499
Protein Name	Heat shock protein HSP 90-beta
Gene Name	Hsp90ab1
Organism	Mus musculus (Mouse).
Sequence Length	724
Subcellular Localization	Cytoplasm . Melanosome . Nucleus . Secreted . Cell membrane . Translocates with BIRC2 from the nucleus to the cytoplasm during differentiation. Secreted when associated with TGFB1 processed form (LAP).
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. 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. Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation. Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery. Main chaperone that is involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription..
Protein Sequence	MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEEDKEDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQSGDEMTSLSEYVSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKSLVSVTKEGLELPEDEEEKKKMEESKAKFENLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVKDLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVTAEEPSAAVPDEIPPLEGDEDASRMEEVD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
33	Phosphorylation	SLIINTFYSNKEIFL HHHHHHHCCCHHHHH	14.86	-
45	Phosphorylation	IFLRELISNASDALD HHHHHHHHCHHHHHH	38.68	18779572
48	Phosphorylation	RELISNASDALDKIR HHHHHCHHHHHHHHC	27.89	18779572
53	Acetylation	NASDALDKIRYESLT CHHHHHHHHCHHHCC	29.90	23806337
53	Succinylation	NASDALDKIRYESLT CHHHHHHHHCHHHCC	29.90	23806337
53	Ubiquitination	NASDALDKIRYESLT CHHHHHHHHCHHHCC	29.90	-
56	Phosphorylation	DALDKIRYESLTDPS HHHHHHCHHHCCCHH	17.22	21183079
58	Phosphorylation	LDKIRYESLTDPSKL HHHHCHHHCCCHHHC	27.86	24899341
60	Phosphorylation	KIRYESLTDPSKLDS HHCHHHCCCHHHCCC	55.96	21183079
63	Phosphorylation	YESLTDPSKLDSGKE HHHCCCHHHCCCCCE	48.97	21183079
64	Ubiquitination	ESLTDPSKLDSGKEL HHCCCHHHCCCCCEE	62.80	22790023
67	Phosphorylation	TDPSKLDSGKELKID CCHHHCCCCCEEEEE	63.30	29514104
69	Malonylation	PSKLDSGKELKIDII HHHCCCCCEEEEEEC	64.92	26320211
69	Ubiquitination	PSKLDSGKELKIDII HHHCCCCCEEEEEEC	64.92	-
72	Acetylation	LDSGKELKIDIIPNP CCCCCEEEEEECCCH	39.15	23806337
72	Succinylation	LDSGKELKIDIIPNP CCCCCEEEEEECCCH	39.15	23806337
72	Ubiquitination	LDSGKELKIDIIPNP CCCCCEEEEEECCCH	39.15	-
94	Phosphorylation	VDTGIGMTKADLINN EECCCCCCHHHHHHH	20.19	20139300
95	Ubiquitination	DTGIGMTKADLINNL ECCCCCCHHHHHHHH	30.89	22790023
104	Phosphorylation	DLINNLGTIAKSGTK HHHHHHHHHHHHHHH	22.41	29514104
107	Ubiquitination	NNLGTIAKSGTKAFM HHHHHHHHHHHHHHH	45.64	22790023
111	Ubiquitination	TIAKSGTKAFMEALQ HHHHHHHHHHHHHHH	43.05	-
155	Phosphorylation	KHNDDEQYAWESSAG CCCCCCCEEEECCCC	16.19	25168779
159	Phosphorylation	DEQYAWESSAGGSFT CCCEEEECCCCCEEE	18.13	26525534
160	Phosphorylation	EQYAWESSAGGSFTV CCEEEECCCCCEEEE	21.29	26525534
164	Phosphorylation	WESSAGGSFTVRADH EECCCCCEEEEEECC	19.47	25168779
166	Phosphorylation	SSAGGSFTVRADHGE CCCCCEEEEEECCCC	15.69	25168779
180	Ubiquitination	EPIGRGTKVILHLKE CCCCCCCEEEEEECC	30.06	22790023
186	Ubiquitination	TKVILHLKEDQTEYL CEEEEEECCCHHHHH	48.80	22790023
190	Phosphorylation	LHLKEDQTEYLEERR EEECCCHHHHHHHHH	38.63	28066266
192	Phosphorylation	LKEDQTEYLEERRVK ECCCHHHHHHHHHHH	23.85	17242355
204	Acetylation	RVKEVVKKHSQFIGY HHHHHHHHHHHHCCC	36.56	23806337
204	Succinylation	RVKEVVKKHSQFIGY HHHHHHHHHHHHCCC	36.56	23806337
204	Ubiquitination	RVKEVVKKHSQFIGY HHHHHHHHHHHHCCC	36.56	-
211	Phosphorylation	KHSQFIGYPITLYLE HHHHHCCCCEEEEEH	6.14	29899451
214	Phosphorylation	QFIGYPITLYLEKER HHCCCCEEEEEHHHH	12.59	26745281
216	Phosphorylation	IGYPITLYLEKEREK CCCCEEEEEHHHHHH	12.26	26745281
219	Acetylation	PITLYLEKEREKEIS CEEEEEHHHHHHCCC	60.52	23806337
219	Succinylation	PITLYLEKEREKEIS CEEEEEHHHHHHCCC	60.52	-
219	Succinylation	PITLYLEKEREKEIS CEEEEEHHHHHHCCC	60.52	23806337
219	Ubiquitination	PITLYLEKEREKEIS CEEEEEHHHHHHCCC	60.52	-
226	Phosphorylation	KEREKEISDDEAEEE HHHHHCCCHHHHHHH	39.85	27087446
237	Ubiquitination	AEEEKGEKEEEDKED HHHHHCCCCCCCCCC	78.19	22790023
255	Phosphorylation	PKIEDVGSDEEDDSG CCCCCCCCCCCCCCC	41.52	27087446
261	Phosphorylation	GSDEEDDSGKDKKKK CCCCCCCCCCCCHHH	61.13	24925903
273	Acetylation	KKKTKKIKEKYIDQE HHHHHHHHHHHCCHH	57.97	22826441
273	Malonylation	KKKTKKIKEKYIDQE HHHHHHHHHHHCCHH	57.97	26320211
275	Acetylation	KTKKIKEKYIDQEEL HHHHHHHHHCCHHHH	42.37	22826441
275	Malonylation	KTKKIKEKYIDQEEL HHHHHHHHHCCHHHH	42.37	26320211
275	Ubiquitination	KTKKIKEKYIDQEEL HHHHHHHHHCCHHHH	42.37	22790023
276	Phosphorylation	TKKIKEKYIDQEELN HHHHHHHHCCHHHHH	15.72	25159016
284	Acetylation	IDQEELNKTKPIWTR CCHHHHHCCCCCCCC	71.23	22640951
284	Malonylation	IDQEELNKTKPIWTR CCHHHHHCCCCCCCC	71.23	26320211
284	Ubiquitination	IDQEELNKTKPIWTR CCHHHHHCCCCCCCC	71.23	22790023
285	Phosphorylation	DQEELNKTKPIWTRN CHHHHHCCCCCCCCC	40.76	27600695
286	Ubiquitination	QEELNKTKPIWTRNP HHHHHCCCCCCCCCC	35.79	22790023
297	Phosphorylation	TRNPDDITQEEYGEF CCCCCCCCHHHHHHH	36.60	-
301	Phosphorylation	DDITQEEYGEFYKSL CCCCHHHHHHHHHHH	22.62	-
305	Phosphorylation	QEEYGEFYKSLTNDW HHHHHHHHHHHCCCH	8.72	25177544
306	Acetylation	EEYGEFYKSLTNDWE HHHHHHHHHHCCCHH	44.29	87981
306	Ubiquitination	EEYGEFYKSLTNDWE HHHHHHHHHHCCCHH	44.29	22790023
307	Phosphorylation	EYGEFYKSLTNDWED HHHHHHHHHCCCHHH	29.10	25521595
309	Phosphorylation	GEFYKSLTNDWEDHL HHHHHHHCCCHHHCE	37.92	26745281
347	Acetylation	PFDLFENKKKKNNIK CCCCCCCCCCCCCCE	59.79	30583291
347	Malonylation	PFDLFENKKKKNNIK CCCCCCCCCCCCCCE	59.79	26320211
347	Ubiquitination	PFDLFENKKKKNNIK CCCCCCCCCCCCCCE	59.79	-
348	Ubiquitination	FDLFENKKKKNNIKL CCCCCCCCCCCCCEE	79.25	-
354	Acetylation	KKKKNNIKLYVRRVF CCCCCCCEEEEEEEE	35.57	23806337
354	Succinylation	KKKKNNIKLYVRRVF CCCCCCCEEEEEEEE	35.57	23806337
354	Ubiquitination	KKKKNNIKLYVRRVF CCCCCCCEEEEEEEE	35.57	-
365	Phosphorylation	RRVFIMDSCDELIPE EEEECCCCHHHHHHH	13.19	23984901
366	S-nitrosocysteine	RVFIMDSCDELIPEY EEECCCCHHHHHHHH	4.03	-
366	Glutathionylation	RVFIMDSCDELIPEY EEECCCCHHHHHHHH	4.03	24333276
366	S-nitrosylation	RVFIMDSCDELIPEY EEECCCCHHHHHHHH	4.03	21278135
383	Phosphorylation	FIRGVVDSEDLPLNI HHHCCCCCCCCCCCC	22.77	26525534
391	Phosphorylation	EDLPLNISREMLQQS CCCCCCCCHHHHHHH	22.55	27742792
398	Phosphorylation	SREMLQQSKILKVIR CHHHHHHHHHHHHHH	14.54	26745281
399	N6-malonyllysine	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	-
399	Acetylation	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	22640943
399	Malonylation	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	26073543
399	Ubiquitination	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	-
402	Malonylation	LQQSKILKVIRKNIV HHHHHHHHHHHHHHH	38.80	26073543
411	Ubiquitination	IRKNIVKKCLELFSE HHHHHHHHHHHHHHH	32.91	22790023
412	Glutathionylation	RKNIVKKCLELFSEL HHHHHHHHHHHHHHH	2.71	24333276
412	S-palmitoylation	RKNIVKKCLELFSEL HHHHHHHHHHHHHHH	2.71	26165157
417	Phosphorylation	KKCLELFSELAEDKE HHHHHHHHHHHHCHH	44.30	23608596
423	Acetylation	FSELAEDKENYKKFY HHHHHHCHHHHHHHH	39.09	7976649
427	Acetylation	AEDKENYKKFYEAFS HHCHHHHHHHHHHHH	48.24	70053
428	Acetylation	EDKENYKKFYEAFSK HCHHHHHHHHHHHHH	42.70	23806337
428	Succinylation	EDKENYKKFYEAFSK HCHHHHHHHHHHHHH	42.70	23806337
428	Ubiquitination	EDKENYKKFYEAFSK HCHHHHHHHHHHHHH	42.70	-
434	O-linked_Glycosylation	KKFYEAFSKNLKLGI HHHHHHHHHHCCCCC	27.90	22645316
434	Phosphorylation	KKFYEAFSKNLKLGI HHHHHHHHHHCCCCC	27.90	22006019
435	Acetylation	KFYEAFSKNLKLGIH HHHHHHHHHCCCCCC	60.90	22826441
435	Malonylation	KFYEAFSKNLKLGIH HHHHHHHHHCCCCCC	60.90	26320211
435	Ubiquitination	KFYEAFSKNLKLGIH HHHHHHHHHCCCCCC	60.90	-
438	Acetylation	EAFSKNLKLGIHEDS HHHHHHCCCCCCCCC	54.80	22826441
438	Ubiquitination	EAFSKNLKLGIHEDS HHHHHHCCCCCCCCC	54.80	22790023
445	Phosphorylation	KLGIHEDSTNRRRLS CCCCCCCCCCHHHHH	25.29	25521595
446	Phosphorylation	LGIHEDSTNRRRLSE CCCCCCCCCHHHHHH	45.10	21082442
452	O-linked_Glycosylation	STNRRRLSELLRYHT CCCHHHHHHHHHHHH	25.12	22645316
452	Phosphorylation	STNRRRLSELLRYHT CCCHHHHHHHHHHHH	25.12	26824392
457	Phosphorylation	RLSELLRYHTSQSGD HHHHHHHHHHCCCCC	14.93	27087446
459	Phosphorylation	SELLRYHTSQSGDEM HHHHHHHHCCCCCCC	21.37	26239621
460	Phosphorylation	ELLRYHTSQSGDEMT HHHHHHHCCCCCCCC	14.72	26239621
462	O-linked_Glycosylation	LRYHTSQSGDEMTSL HHHHHCCCCCCCCHH	48.23	22645316
462	Phosphorylation	LRYHTSQSGDEMTSL HHHHHCCCCCCCCHH	48.23	27087446
467	Phosphorylation	SQSGDEMTSLSEYVS CCCCCCCCHHHHHHH	25.19	26525534
468	Phosphorylation	QSGDEMTSLSEYVSR CCCCCCCHHHHHHHH	28.70	23984901
477	Acetylation	SEYVSRMKETQKSIY HHHHHHHHHHHCCEE	57.40	22826441
479	Phosphorylation	YVSRMKETQKSIYYI HHHHHHHHHCCEEEE	35.46	-
481	Acetylation	SRMKETQKSIYYITG HHHHHHHCCEEEECC	46.36	22826441
481	Succinylation	SRMKETQKSIYYITG HHHHHHHCCEEEECC	46.36	23806337
481	Ubiquitination	SRMKETQKSIYYITG HHHHHHHCCEEEECC	46.36	-
482	Phosphorylation	RMKETQKSIYYITGE HHHHHHCCEEEECCC	13.15	25521595
484	Phosphorylation	KETQKSIYYITGESK HHHHCCEEEECCCCH	8.91	19605366
485	Phosphorylation	ETQKSIYYITGESKE HHHCCEEEECCCCHH	7.13	25521595
490	Phosphorylation	IYYITGESKEQVANS EEEECCCCHHHHHHH	42.72	29514104
491	Acetylation	YYITGESKEQVANSA EEECCCCHHHHHHHH	48.11	23236377
491	Ubiquitination	YYITGESKEQVANSA EEECCCCHHHHHHHH	48.11	22790023
514	Phosphorylation	GFEVVYMTEPIDEYC CCEEEEECCCCCHHH	22.41	18779572
520	Phosphorylation	MTEPIDEYCVQQLKE ECCCCCHHHHHHHHH	8.32	18779572
521	S-nitrosocysteine	TEPIDEYCVQQLKEF CCCCCHHHHHHHHHC	1.78	-
521	Glutathionylation	TEPIDEYCVQQLKEF CCCCCHHHHHHHHHC	1.78	24333276
521	S-nitrosylation	TEPIDEYCVQQLKEF CCCCCHHHHHHHHHC	1.78	21278135
531	Acetylation	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	23806337
531	Methylation	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	-
531	Succinylation	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	-
531	Succinylation	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	23806337
531	Ubiquitination	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	-
532	Phosphorylation	LKEFDGKSLVSVTKE HHHCCCCCCEEEEHH	39.26	26824392
535	Phosphorylation	FDGKSLVSVTKEGLE CCCCCCEEEEHHCCC	29.39	25777480
538	Acetylation	KSLVSVTKEGLELPE CCCEEEEHHCCCCCC	47.86	23236377
538	Succinylation	KSLVSVTKEGLELPE CCCEEEEHHCCCCCC	47.86	23954790
538	Ubiquitination	KSLVSVTKEGLELPE CCCEEEEHHCCCCCC	47.86	-
550	Acetylation	LPEDEEEKKKMEESK CCCCHHHHHHHHHHH	62.06	23201123
551	Acetylation	PEDEEEKKKMEESKA CCCHHHHHHHHHHHH	61.71	23201123
559	Acetylation	KMEESKAKFENLCKL HHHHHHHHHHHHHHH	57.88	23806337
559	Succinylation	KMEESKAKFENLCKL HHHHHHHHHHHHHHH	57.88	23806337
559	Ubiquitination	KMEESKAKFENLCKL HHHHHHHHHHHHHHH	57.88	-
564	S-nitrosocysteine	KAKFENLCKLMKEIL HHHHHHHHHHHHHHH	4.85	-
564	S-nitrosylation	KAKFENLCKLMKEIL HHHHHHHHHHHHHHH	4.85	24926564
564	S-palmitoylation	KAKFENLCKLMKEIL HHHHHHHHHHHHHHH	4.85	26165157
565	Acetylation	AKFENLCKLMKEILD HHHHHHHHHHHHHHH	55.57	22826441
565	Ubiquitination	AKFENLCKLMKEILD HHHHHHHHHHHHHHH	55.57	22790023
568	Acetylation	ENLCKLMKEILDKKV HHHHHHHHHHHHHCC	52.63	22826441
568	Malonylation	ENLCKLMKEILDKKV HHHHHHHHHHHHHCC	52.63	26320211
568	Succinylation	ENLCKLMKEILDKKV HHHHHHHHHHHHHCC	52.63	23806337
574	Methylation	MKEILDKKVEKVTIS HHHHHHHCCEEEEEC	56.12	-
574	Ubiquitination	MKEILDKKVEKVTIS HHHHHHHCCEEEEEC	56.12	22790023
577	Acetylation	ILDKKVEKVTISNRL HHHHCCEEEEECCCC	47.90	23806337
577	Malonylation	ILDKKVEKVTISNRL HHHHCCEEEEECCCC	47.90	26320211
577	Succinylation	ILDKKVEKVTISNRL HHHHCCEEEEECCCC	47.90	-
577	Succinylation	ILDKKVEKVTISNRL HHHHCCEEEEECCCC	47.90	23806337
579	Phosphorylation	DKKVEKVTISNRLVS HHCCEEEEECCCCCC	29.74	25521595
586	Phosphorylation	TISNRLVSSPCCIVT EECCCCCCCCEEEEE	32.90	26745281
587	Phosphorylation	ISNRLVSSPCCIVTS ECCCCCCCCEEEEEE	17.93	26745281
589	Glutathionylation	NRLVSSPCCIVTSTY CCCCCCCEEEEEECC	2.39	24333276
590	Glutathionylation	RLVSSPCCIVTSTYG CCCCCCEEEEEECCC	2.96	24333276
590	S-nitrosylation	RLVSSPCCIVTSTYG CCCCCCEEEEEECCC	2.96	-
593	Phosphorylation	SSPCCIVTSTYGWTA CCCEEEEEECCCCHH	8.74	26643407
594	Phosphorylation	SPCCIVTSTYGWTAN CCEEEEEECCCCHHC	14.56	26643407
595	Phosphorylation	PCCIVTSTYGWTANM CEEEEEECCCCHHCH	19.38	25367039
596	Phosphorylation	CCIVTSTYGWTANME EEEEEECCCCHHCHH	15.50	20116462
607	Methylation	ANMERIMKAQALRDN HCHHHHHHHHHHHCC	34.67	-
607	Ubiquitination	ANMERIMKAQALRDN HCHHHHHHHHHHHCC	34.67	22790023
615	Phosphorylation	AQALRDNSTMGYMMA HHHHHCCCHHHHHHH	24.86	25521595
616	Phosphorylation	QALRDNSTMGYMMAK HHHHCCCHHHHHHHH	22.37	27600695
617	Sulfoxidation	ALRDNSTMGYMMAKK HHHCCCHHHHHHHHH	3.48	21406390
619	Phosphorylation	RDNSTMGYMMAKKHL HCCCHHHHHHHHHHC	3.48	25367039
620	Sulfoxidation	DNSTMGYMMAKKHLE CCCHHHHHHHHHHCC	1.42	21406390
621	Sulfoxidation	NSTMGYMMAKKHLEI CCHHHHHHHHHHCCC	3.58	21406390
623	Acetylation	TMGYMMAKKHLEINP HHHHHHHHHHCCCCC	23.88	22826441
623	Succinylation	TMGYMMAKKHLEINP HHHHHHHHHHCCCCC	23.88	23954790
623	Ubiquitination	TMGYMMAKKHLEINP HHHHHHHHHHCCCCC	23.88	-
624	Acetylation	MGYMMAKKHLEINPD HHHHHHHHHCCCCCC	43.83	23806337
624	Ubiquitination	MGYMMAKKHLEINPD HHHHHHHHHCCCCCC	43.83	22790023
646	Acetylation	RQKAEADKNDKAVKD HHHHHHCCCCHHHHH	74.27	23201123
649	Acetylation	AEADKNDKAVKDLVV HHHCCCCHHHHHHHH	65.55	23201123
669	Phosphorylation	ALLSSGFSLEDPQTH HHHHCCCCCCCCCCH	34.08	-
696	Phosphorylation	GIDEDEVTAEEPSAA CCCCCCCCCCCCCCC	26.72	25338131
701	Phosphorylation	EVTAEEPSAAVPDEI CCCCCCCCCCCCCCC	31.94	23649490
718	Phosphorylation	LEGDEDASRMEEVD- CCCCCCHHHCCCCC-	44.47	22006019

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
718	S	Phosphorylation	Kinase	PLK2	P53351	Uniprot
718	S	Phosphorylation	Kinase	PLK3	Q60806	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
226	S	Phosphorylation	17242355
Phosphorylation at Ser-226 and Ser-255 inhibits AHR interaction.
255	S	Phosphorylation	15345747
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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GLR_MOUSE	Gcgr	physical	22457490
CDN2A_MOUSE	Cdkn2a	physical	16582619
ARF_MOUSE	Cdkn2a	physical	16582619
IRF3_MOUSE	Irf3	physical	16394098
TEBP_MOUSE	Ptges3	physical	22123826
HSF1_MOUSE	Hsf1	physical	17785525
HDAC6_MOUSE	Hdac6	physical	17785525
TERA_MOUSE	Vcp	physical	17785525
ITBP2_MOUSE	Itgb1bp2	physical	18474241
HDAC6_MOUSE	Hdac6	physical	22367781
HS90B_MOUSE	Hsp90ab1	physical	22367781
HSF1_MOUSE	Hsf1	physical	22367781

Drug and Disease Associations

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

Regulatory Network of HS90B_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASSSPECTROMETRY.	19131326 [Abstract]
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASSSPECTROMETRY.	19144319 [Abstract]
"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-226 AND SER-255, ANDMASS SPECTROMETRY.	19367708 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASSSPECTROMETRY.	17242355 [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-255, AND MASSSPECTROMETRY.	17208939 [Abstract]
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASSSPECTROMETRY.	17114649 [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-226 AND SER-255, ANDMASS SPECTROMETRY.	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-226 AND SER-255, ANDMASS SPECTROMETRY.	18630941 [Abstract]
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells."; Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.; J. Proteome Res. 6:3174-3186(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255 AND SER-261, ANDMASS SPECTROMETRY.	17622165 [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-305, 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-484, AND MASSSPECTROMETRY.	17947660 [Abstract]

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