HS90B_CHICK - dbPTM
HS90B_CHICK - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HS90B_CHICK
UniProt AC Q04619
Protein Name Heat shock cognate protein HSP 90-beta
Gene Name HSP90AB1
Organism Gallus gallus (Chicken).
Sequence Length 725
Subcellular Localization Cytoplasm . Melanosome .
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..
Protein Sequence MPEQVQHGEDEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDTGKDLKIDIVPNPRDPTLTLLDTGIGMTKADLVNNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRTDHGEPIGRGTKVILYLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYVEKEREKEVSDDEAEEEKVEKEEEESKDEEKPKIEDVGSDEEEEEGEKSKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFTELAEDKENYKKFYEAFSKNLKLGIHEDSTNRKRLSELLRYHTSQSGDEMTSLSEYVSRMKESQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKTLVSVTKEGLELPEDEEEKKNMEESKAKFETLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKADANKNDKAVKDLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVIAEESSIAPPDEIPPLEGDEDTSRMEEVD
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 Orthologous
Protein Cluster
226PhosphorylationKEREKEVSDDEAEEE
HHHHCCCCCCHHHHH
40.20-
255PhosphorylationPKIEDVGSDEEEEEG
CCCCCCCCHHHHHHH
41.5221736374

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

Oops, there are no upstream regulatory protein records of HS90B_CHICK !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HS90B_CHICK !!

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_CHICK !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KCMA1_CHICKKCNMA1physical
22174833
CH60_CHICKHSPD1physical
8423808
HSP70_CHICKHSPA2physical
8423808
HSP70_CHICKHSPA2physical
8603045

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HS90B_CHICK

loading...

Related Literatures of Post-Translational Modification

TOP