dbPTM

HS90B_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HS90B_RAT
UniProt AC	P34058
Protein Name	Heat shock protein HSP 90-beta
Gene Name	Hsp90ab1
Organism	Rattus norvegicus (Rat).
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
36	Acetylation	INTFYSNKEIFLREL HHHHCCCHHHHHHHH	46.37	22902405
45	Phosphorylation	IFLRELISNASDALD HHHHHHHHCHHHHHH	38.68	23984901
48	Phosphorylation	RELISNASDALDKIR HHHHHCHHHHHHHHC	27.89	23984901
53	Acetylation	NASDALDKIRYESLT CHHHHHHHHCHHHCC	29.90	22902405
56	Phosphorylation	DALDKIRYESLTDPS HHHHHHCHHHCCCHH	17.22	23984901
58	Phosphorylation	LDKIRYESLTDPSKL HHHHCHHHCCCHHHC	27.86	23984901
60	Phosphorylation	KIRYESLTDPSKLDS HHCHHHCCCHHHCCC	55.96	23984901
69	Acetylation	PSKLDSGKELKIDII HHHCCCCCEEEEEEC	64.92	22902405
83	Phosphorylation	IPNPQERTLTLVDTG CCCHHCCEEEEEECC	24.28	23984901
85	Phosphorylation	NPQERTLTLVDTGIG CHHCCEEEEEECCCC	24.91	23984901
95	Acetylation	DTGIGMTKADLINNL ECCCCCCHHHHHHHH	30.89	22902405
104	Phosphorylation	DLINNLGTIAKSGTK HHHHHHHHHHHHHHH	22.41	23984901
107	Ubiquitination	NNLGTIAKSGTKAFM HHHHHHHHHHHHHHH	45.64	-
180	Ubiquitination	EPIGRGTKVILHLKE CCCCCCCEEEEEECC	30.06	-
186	Acetylation	TKVILHLKEDQTEYL CEEEEEECCCHHHHH	48.80	30596363
192	Phosphorylation	LKEDQTEYLEERRVK ECCCHHHHHHHHHHH	23.85	-
206	Phosphorylation	KEVVKKHSQFIGYPI HHHHHHHHHHCCCCE	35.35	23984901
219	Succinylation	PITLYLEKEREKEIS CEEEEEHHHHHHCCC	60.52	-
219	Succinylation	PITLYLEKEREKEIS CEEEEEHHHHHHCCC	60.52	-
226	Phosphorylation	KEREKEISDDEAEEE HHHHHCCCHHHHHHH	39.85	23991683
255	Phosphorylation	PKIEDVGSDEEDDSG CCCCCCCCCCCCCCC	41.52	23991683
261	Phosphorylation	GSDEEDDSGKDKKKK CCCCCCCCCCCCHHH	61.13	23991683
275	Acetylation	KTKKIKEKYIDQEEL HHHHHHHHHCCHHHH	42.37	174223
275	Ubiquitination	KTKKIKEKYIDQEEL HHHHHHHHHCCHHHH	42.37	-
284	Acetylation	IDQEELNKTKPIWTR CCHHHHHCCCCCCCC	71.23	22902405
285	Phosphorylation	DQEELNKTKPIWTRN CHHHHHCCCCCCCCC	40.76	28432305
286	Acetylation	QEELNKTKPIWTRNP HHHHHCCCCCCCCCC	35.79	22902405
290	Phosphorylation	NKTKPIWTRNPDDIT HCCCCCCCCCCCCCC	22.68	28432305
297	Phosphorylation	TRNPDDITQEEYGEF CCCCCCCCHHHHHHH	36.60	-
301	Phosphorylation	DDITQEEYGEFYKSL CCCCHHHHHHHHHHH	22.62	27097102
305	Phosphorylation	QEEYGEFYKSLTNDW HHHHHHHHHHHCCCH	8.72	27097102
307	Phosphorylation	EYGEFYKSLTNDWED HHHHHHHHHCCCHHH	29.10	23984901
309	Phosphorylation	GEFYKSLTNDWEDHL HHHHHHHCCCHHHCE	37.92	23984901
322	Phosphorylation	HLAVKHFSVEGQLEF CEEEEEEEEECEEEE	20.98	23984901
350	Acetylation	LFENKKKKNNIKLYV CCCCCCCCCCCEEEE	65.20	22902405
354	Acetylation	KKKKNNIKLYVRRVF CCCCCCCEEEEEEEE	35.57	22902405
365	Phosphorylation	RRVFIMDSCDELIPE EEEECCCCHHHHHHH	13.19	23800682
391	Phosphorylation	EDLPLNISREMLQQS CCCCCCCCHHHHHHH	22.55	27097102
398	Phosphorylation	SREMLQQSKILKVIR CHHHHHHHHHHHHHH	14.54	23984901
399	N6-malonyllysine	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	-
399	Acetylation	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	25786129
399	Malonylation	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	-
402	Acetylation	LQQSKILKVIRKNIV HHHHHHHHHHHHHHH	38.80	22902405
428	Acetylation	EDKENYKKFYEAFSK HCHHHHHHHHHHHHH	42.70	174219
434	O-linked_Glycosylation	KKFYEAFSKNLKLGI HHHHHHHHHHCCCCC	27.90	-
435	Acetylation	KFYEAFSKNLKLGIH HHHHHHHHHCCCCCC	60.90	22902405
438	Acetylation	EAFSKNLKLGIHEDS HHHHHHCCCCCCCCC	54.80	22902405
445	Phosphorylation	KLGIHEDSTNRRRLS CCCCCCCCCCHHHHH	25.29	27097102
446	Phosphorylation	LGIHEDSTNRRRLSE CCCCCCCCCHHHHHH	45.10	27097102
452	Phosphorylation	STNRRRLSELLRYHT CCCHHHHHHHHHHHH	25.12	27097102
452	O-linked_Glycosylation	STNRRRLSELLRYHT CCCHHHHHHHHHHHH	25.12	-
457	Phosphorylation	RLSELLRYHTSQSGD HHHHHHHHHHCCCCC	14.93	23984901
459	Phosphorylation	SELLRYHTSQSGDEM HHHHHHHHCCCCCCC	21.37	23984901
460	Phosphorylation	ELLRYHTSQSGDEMT HHHHHHHCCCCCCCC	14.72	23984901
462	Phosphorylation	LRYHTSQSGDEMTSL HHHHHCCCCCCCCHH	48.23	23984901
467	Phosphorylation	SQSGDEMTSLSEYVS CCCCCCCCHHHHHHH	25.19	23984901
468	Phosphorylation	QSGDEMTSLSEYVSR CCCCCCCHHHHHHHH	28.70	23984901
477	Acetylation	SEYVSRMKETQKSIY HHHHHHHHHHHCCEE	57.40	22902405
479	Phosphorylation	YVSRMKETQKSIYYI HHHHHHHHHCCEEEE	35.46	-
481	Acetylation	SRMKETQKSIYYITG HHHHHHHCCEEEECC	46.36	22902405
482	Phosphorylation	RMKETQKSIYYITGE HHHHHHCCEEEECCC	13.15	23984901
484	Phosphorylation	KETQKSIYYITGESK HHHHCCEEEECCCCH	8.91	-
491	Acetylation	YYITGESKEQVANSA EEECCCCHHHHHHHH	48.11	22902405
531	Succinylation	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	-
531	Succinylation	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	-
531	Acetylation	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	22902405
531	Methylation	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	-
532	Phosphorylation	LKEFDGKSLVSVTKE HHHCCCCCCEEEEHH	39.26	28432305
538	Acetylation	KSLVSVTKEGLELPE CCCEEEEHHCCCCCC	47.86	22902405
550	Succinylation	LPEDEEEKKKMEESK CCCCHHHHHHHHHHH	62.06	26843850
568	Acetylation	ENLCKLMKEILDKKV HHHHHHHHHHHHHCC	52.63	22902405
574	Methylation	MKEILDKKVEKVTIS HHHHHHHCCEEEEEC	56.12	-
574	Acetylation	MKEILDKKVEKVTIS HHHHHHHCCEEEEEC	56.12	22902405
577	Succinylation	ILDKKVEKVTISNRL HHHHCCEEEEECCCC	47.90	-
577	Succinylation	ILDKKVEKVTISNRL HHHHCCEEEEECCCC	47.90	-
590	S-nitrosylation	RLVSSPCCIVTSTYG CCCCCCEEEEEECCC	2.96	-
595	Phosphorylation	PCCIVTSTYGWTANM CEEEEEECCCCHHCH	19.38	22276854
596	Phosphorylation	CCIVTSTYGWTANME EEEEEECCCCHHCHH	15.50	22276854
615	Phosphorylation	AQALRDNSTMGYMMA HHHHHCCCHHHHHHH	24.86	28432305
616	Phosphorylation	QALRDNSTMGYMMAK HHHHCCCHHHHHHHH	22.37	28432305
619	Phosphorylation	RDNSTMGYMMAKKHL HCCCHHHHHHHHHHC	3.48	-
623	Acetylation	TMGYMMAKKHLEINP HHHHHHHHHHCCCCC	23.88	22902405
624	Acetylation	MGYMMAKKHLEINPD HHHHHHHHHCCCCCC	43.83	-
624	Ubiquitination	MGYMMAKKHLEINPD HHHHHHHHHCCCCCC	43.83	-
669	Phosphorylation	ALLSSGFSLEDPQTH HHHHCCCCCCCCCCH	34.08	-
718	Phosphorylation	LEGDEDASRMEEVD- CCCCCCHHHCCCCC-	44.47	-

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
452	S	Phosphorylation	Kinase	PRKACA	P00517	GPS
718	S	Phosphorylation	Kinase	PLK2	Q9R012	Uniprot
718	S	Phosphorylation	Kinase	PLK3	Q9R011	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
226	S	Phosphorylation	22673903
Phosphorylation at Ser-226 and Ser-255 inhibits AHR interaction.
255	S	Phosphorylation	22673903
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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of HS90B_RAT !!

Drug and Disease Associations

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

Regulatory Network of HS90B_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites."; Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.; Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-255, ANDMASS SPECTROMETRY.	16641100 [Abstract]
"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."; Moser K., White F.M.; J. Proteome Res. 5:98-104(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-255, AND MASSSPECTROMETRY.	16396499 [Abstract]

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