HS90A_BOVIN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HS90A_BOVIN
• UniProt AC: Q76LV2
• Protein Name: Heat shock protein HSP 90-alpha
• Gene Name: HSP90AA1
• Organism: Bos taurus (Bovine).
• 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. Interacts with HECTD1 (via N-terminus) (By similarity)..
• Protein Sequence: MPEETQAQDQPMEEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNSSDALDKIRYESLTDPSKLDSGKELHINLIPNKQDRTLTIVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVTVITKHNDDEQYAWESSAGGSFTVRTDTGEPMGRGTKVILHLKEDQTEYLEERRIKEIVKKHSQFIGYPITLFVEKERDKEVSDDEAEEKEDKEEEKEKEEKESDDKPEIEDVGSDEEEEEKKDGDKKKKKKIKEKYIDQEELNKTKPIWTRNPDDITNEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFVPRRAPFDLFENRKKKNNIKLYVRRVFIMDNCEELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNLVKKCLELFTELAEDKENYKKFYEQFSKNIKLGIHEDSQNRKKLSELLRYYTSASGDEMVSLKDYCTRMKENQKHIYYITGETKDQVANSAFVERLRKHGLEVIYMIEPIDEYCVQQLKEFEGKTLVSVTKEGLELPEDEEEKKKQEEKKTKFENLCKIMKDILEKKVEKVVVSNRLVTSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMAAKKHLEINPDHSIIETLRQKAEADKNDKSVKDLVILLYETALLSSGFSLEDPQTHANRIYRMIKLGLGIDEDDPTADDSSAAVTEEMPPLEGDDDTSRMEEVD

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	---MPEETQAQDQPM ---CCHHHCCCCCCC	27.78	-
58	Acetylation	NSSDALDKIRYESLT CCCHHHHHHCHHHCC	29.90	-
84	Acetylation	HINLIPNKQDRTLTI EEEECCCCCCCCEEE	48.50	-
231	Phosphorylation	KERDKEVSDDEAEEK HHHCCCCCHHHHHHH	40.20	29541418
252	Phosphorylation	KEKEEKESDDKPEIE HHHHHHHCCCCCCCC	63.28	-
263	Phosphorylation	PEIEDVGSDEEEEEK CCCCCCCCCHHHHHH	41.52	28710545
314	Phosphorylation	NEEYGEFYKSLTNDW HHHHHHHHHHHCCCH	8.72	-
400	Phosphorylation	EDLPLNISREMLQQS CCCCCCCCHHHHHHH	22.55	-
444	Acetylation	KFYEQFSKNIKLGIH HHHHHHHHHCCCCCC	65.07	-
454	Phosphorylation	KLGIHEDSQNRKKLS CCCCCCCCHHHHHHH	26.77	-
459	Acetylation	EDSQNRKKLSELLRY CCCHHHHHHHHHHHH	54.75	-
477	Phosphorylation	ASGDEMVSLKDYCTR CCCCCCEEHHHHHHH	28.52	-
490	Acetylation	TRMKENQKHIYYITG HHHHHHCCEEEEEEC	43.48	-
493	Phosphorylation	KENQKHIYYITGETK HHHCCEEEEEECCCH	6.63	-
586	Acetylation	ILEKKVEKVVVSNRL HHHHHCCEEEECCCC	43.23	-
599	S-nitrosocysteine	RLVTSPCCIVTSTYG CCCCCCEEEEEECCC	2.96	-
599	S-nitrosylation	RLVTSPCCIVTSTYG CCCCCCEEEEEECCC	2.96	-
642	Phosphorylation	LEINPDHSIIETLRQ CCCCCCCHHHHHHHH	32.42	-

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HS90A_BOVIN !!

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_BOVIN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
P53_HUMAN	TP53	physical	15358769

Drug and Disease Associations

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