HS90A_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HS90A_RAT
• UniProt AC: P82995
• Protein Name: Heat shock protein HSP 90-alpha
• Gene Name: Hsp90aa1
• Organism: Rattus norvegicus (Rat).
• 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: MPEETQTQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKEEKEEEKEKEEKESDDKPEIEDVGSDEEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEEHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHIYFITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTVDDTSAAVTEEMPPLEGDDDTSRMEEVD

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MPEETQTQDQPM ---CCCCCCCCCCCC	34.94	-
7	Phosphorylation	-MPEETQTQDQPMEE -CCCCCCCCCCCCCH	41.34	-
50	Phosphorylation	IFLRELISNSSDALD HHHHHHHHCCCHHHH	43.19	23984901
52	Phosphorylation	LRELISNSSDALDKI HHHHHHCCCHHHHHH	23.86	23984901
53	Phosphorylation	RELISNSSDALDKIR HHHHHCCCHHHHHHC	31.02	23984901
58	Acetylation	NSSDALDKIRYESLT CCCHHHHHHCHHHCC	29.90	22902405
61	Nitration	DALDKIRYESLTDPS HHHHHHCHHHCCCHH	17.22	-
61	Phosphorylation	DALDKIRYESLTDPS HHHHHHCHHHCCCHH	17.22	23984901
63	Phosphorylation	LDKIRYESLTDPSKL HHHHCHHHCCCHHHC	27.86	23984901
65	Phosphorylation	KIRYESLTDPSKLDS HHCHHHCCCHHHCCC	55.96	23984901
84	Acetylation	HINLIPNKQDRTLTI EEEECCCCCCCCEEE	48.50	22902405
100	Acetylation	DTGIGMTKADLINNL ECCCCCCHHHHHHHH	30.89	-
109	Phosphorylation	DLINNLGTIAKSGTK HHHHHHHHHHHHHHH	22.41	23984901
197	Phosphorylation	LKEDQTEYLEERRIK ECCCHHHHHHHHHHH	23.85	-
197	Nitration	LKEDQTEYLEERRIK ECCCHHHHHHHHHHH	23.85	-
211	Phosphorylation	KEIVKKHSQFIGYPI HHHHHHHHHHCCCCE	35.35	17564427
219	Phosphorylation	QFIGYPITLFVEKER HHCCCCEEEEEEHHH	15.05	21373199
231	Phosphorylation	KERDKEVSDDEAEEK HHHCCCCCHHHHHHH	40.20	23712012
252	Phosphorylation	KEKEEKESDDKPEIE HHHHHHHCCCCCCCC	63.28	23712012
263	Phosphorylation	PEIEDVGSDEEEEEK CCCCCCCCCHHHHHH	41.52	23712012
294	Phosphorylation	DQEELNKTKPIWTRN CHHHHHCCCCCCCCC	40.76	28432305
299	Phosphorylation	NKTKPIWTRNPDDIT HCCCCCCCCCCCCCC	22.68	28432305
314	Phosphorylation	NEEYGEFYKSLTNDW HHHHHHHHHHHCCCH	8.72	-
316	Phosphorylation	EYGEFYKSLTNDWEE HHHHHHHHHCCCHHH	29.10	23984901
318	Phosphorylation	GEFYKSLTNDWEEHL HHHHHHHCCCHHHHE	37.92	23984901
331	Phosphorylation	HLAVKHFSVEGQLEF HEEECEEEEECEEEE	20.98	23984901
400	Phosphorylation	EDLPLNISREMLQQS CCCCCCCCHHHHHHH	22.55	27097102
407	Phosphorylation	SREMLQQSKILKVIR CHHHHHHHHHHHHHH	14.54	23984901
437	Acetylation	EDKENYKKFYEQFSK HCHHHHHHHHHHHHH	42.70	22902405
444	Acetylation	KFYEQFSKNIKLGIH HHHHHHHHHCCCCCC	65.07	22902405
447	Acetylation	EQFSKNIKLGIHEDS HHHHHHCCCCCCCCC	50.48	22902405
454	Phosphorylation	KLGIHEDSQNRKKLS CCCCCCCCHHHHHHH	26.77	29779826
458	Acetylation	HEDSQNRKKLSELLR CCCCHHHHHHHHHHH	66.66	22902405
459	Acetylation	EDSQNRKKLSELLRY CCCHHHHHHHHHHHH	54.75	22902405
466	Nitration	KLSELLRYYTSASGD HHHHHHHHHHCCCCC	15.86	-
467	Nitration	LSELLRYYTSASGDE HHHHHHHHHCCCCCC	6.44	-
477	Phosphorylation	ASGDEMVSLKDYCTR CCCCCCEEHHHHHHH	28.52	30181290
479	Acetylation	GDEMVSLKDYCTRMK CCCCEEHHHHHHHHH	38.86	22902405
486	Acetylation	KDYCTRMKENQKHIY HHHHHHHHHHCCEEE	50.66	22902405
490	Acetylation	TRMKENQKHIYFITG HHHHHHCCEEEEEEC	43.48	22902405
493	Nitration	KENQKHIYFITGETK HHHCCEEEEEECCCH	6.66	-
493	Phosphorylation	KENQKHIYFITGETK HHHCCEEEEEECCCH	6.66	-
500	Acetylation	YFITGETKDQVANSA EEEECCCHHHHHHHH	41.69	22902405
540	Acetylation	QLKEFEGKTLVSVTK HHHHCCCCEEEEEEH	31.33	22902405
547	Acetylation	KTLVSVTKEGLELPE CEEEEEEHHCCCCCC	47.86	22902405
577	Acetylation	ENLCKIMKDILEKKV HHHHHHHHHHHHHHC	45.12	22902405
586	Acetylation	ILEKKVEKVVVSNRL HHHHHCCEEEECCCC	43.23	22902405
599	S-nitrosocysteine	RLVTSPCCIVTSTYG CCCCCCEEEEEECCC	2.96	-
599	S-nitrosylation	RLVTSPCCIVTSTYG CCCCCCEEEEEECCC	2.96	-
605	Phosphorylation	CCIVTSTYGWTANME EEEEEECCCCHHCHH	15.50	22276854
628	Nitration	RDNSTMGYMAAKKHL HCCCHHHHHHHHHHC	3.46	-
628	Phosphorylation	RDNSTMGYMAAKKHL HCCCHHHHHHHHHHC	3.46	-
632	Acetylation	TMGYMAAKKHLEINP HHHHHHHHHHCCCCC	31.05	22902405
642	Phosphorylation	LEINPDHSIIETLRQ CCCCCCCHHHHHHHH	32.42	-
726	Phosphorylation	PLEGDDDTSRMEEVD CCCCCCCCCCCCCCC	25.81	22673903
727	Phosphorylation	LEGDDDTSRMEEVD- CCCCCCCCCCCCCC-	36.30	22673903

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	-	Uniprot
7	T	Phosphorylation	Kinase	PRKDC	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HS90A_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of HS90A_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FCERB_RAT	Ms4a2	physical	19356729
AKT1_RAT	Akt1	physical	19356729
LYN_RAT	Lyn	physical	19356729
KPCD_RAT	Prkcd	physical	19356729

Drug and Disease Associations

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