HS90B_BOVIN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HS90B_BOVIN
• UniProt AC: Q76LV1
• Protein Name: Heat shock protein HSP 90-beta
• Gene Name: HSP90AB1
• Organism: Bos taurus (Bovine).
• 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: MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEEDKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQSGDEMTSLSEYVSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKSLVSVTKEGLELPEDEEEKKKMEESKAKFENLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVKDLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVTAEEPSAAVPDEIPPLEGDEDASRMEEVD

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
219	Succinylation	PITLYLEKEREKEIS CEEEEEHHHHHHCCC	60.52	-
219	Succinylation	PITLYLEKEREKEIS CEEEEEHHHHHHCCC	60.52	-
226	Phosphorylation	KEREKEISDDEAEEE HHHHHCCCHHHHHHH	39.85	-
255	Phosphorylation	PKIEDVGSDEEDDSG CCHHCCCCCCCCCCC	41.52	29541418
261	Phosphorylation	GSDEEDDSGKDKKKK CCCCCCCCCCCCHHH	61.13	-
297	Phosphorylation	TRNPDDITQEEYGEF CCCCCCCCHHHHHHH	36.60	-
301	Phosphorylation	DDITQEEYGEFYKSL CCCCHHHHHHHHHHH	22.62	-
305	Phosphorylation	QEEYGEFYKSLTNDW HHHHHHHHHHHCCCH	8.72	-
307	Phosphorylation	EYGEFYKSLTNDWED HHHHHHHHHCCCHHH	29.10	-
399	Malonylation	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	-
399	N6-malonyllysine	REMLQQSKILKVIRK HHHHHHHHHHHHHHH	47.95	-
434	O-linked_Glycosylation	KKFYEAFSKNLKLGI HHHHHHHHHHCCCCC	27.90	-
435	Acetylation	KFYEAFSKNLKLGIH HHHHHHHHHCCCCCC	60.90	-
445	Phosphorylation	KLGIHEDSTNRRRLS CCCCCCCCCCHHHHH	25.29	-
452	O-linked_Glycosylation	STNRRRLSELLRYHT CCCHHHHHHHHHHHH	25.12	-
452	Phosphorylation	STNRRRLSELLRYHT CCCHHHHHHHHHHHH	25.12	-
479	Phosphorylation	YVSRMKETQKSIYYI HHHHHHHHHCCEEEE	35.46	-
481	Acetylation	SRMKETQKSIYYITG HHHHHHHCCEEEECC	46.36	-
484	Phosphorylation	KETQKSIYYITGESK HHHHCCEEEECCCCH	8.91	-
531	Succinylation	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	-
531	Methylation	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	-
531	Succinylation	QLKEFDGKSLVSVTK HHHHCCCCCCEEEEH	42.32	-
532	Phosphorylation	LKEFDGKSLVSVTKE HHHCCCCCCEEEEHH	39.26	-
574	Methylation	MKEILDKKVEKVTIS HHHHHHHCCEEEEEC	56.12	-
577	Succinylation	ILDKKVEKVTISNRL HHHHCCEEEEECCCC	47.90	-
577	Succinylation	ILDKKVEKVTISNRL HHHHCCEEEEECCCC	47.90	-
590	S-nitrosylation	RLVSSPCCIVTSTYG CCCCCCEEEEEECCC	2.96	-
624	Acetylation	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
718	S	Phosphorylation	Kinase	PLK2	-	Uniprot
718	S	Phosphorylation	Kinase	PLK3	-	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of HS90B_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 HS90B_BOVIN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AKT1_BOVIN	AKT1	physical	15782121

Drug and Disease Associations

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