TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


8.A.163.1.1
HSP90AB1 (HSP90B, HSPC2, HSPCB) of 724 aas, which forms a complex with the cochaparone protein, CDC37 (378 aas) and AHA1 (338 aas), in the cytoplasm.  HSP90 is an ATP-driven chaparone. It promotes the maturation, structural maintenance and proper regulation of specific target proteins including integral membrane proteins and transporters involved, for instance, in cell cycle control, signal transduction and transport. It undergoes a functional cycle linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. It also interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function (Chadli et al. 2006, Retzlaff et al. 2009). In the resting state, through the dimerization of its C-terminal domain, HSP90 forms a homodimer which is defined as the open conformation. Upon ATP-binding, the N-terminal domain undergoes significant conformational changes and comes in contact to form an active closed conformation. After HSP90 finishes its chaperoning tasks of assisting the proper folding, stabilization and activation of client proteins under the active state, ATP molecule is hydrolyzed to ADP which then dissociates from HSP90 and directs the protein back to the resting state (Richter et al. 2008). The chaparone complex interacts with cereblon (CDBN; TC# 8.A.162.1.1) which determines HSP90 activity toward transmembrane proteins (Heider et al. 2021).  

Accession Number:P08238
Protein Name:Heat shock protein HSP 90-beta
Length:724
Molecular Weight:83264.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:1
Location1 / Topology2 / Orientation3: Cytoplasm1
Substrate protein

Cross database links:

External Searches:

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence
1:	MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT 
61:	DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN NLGTIAKSGT KAFMEALQAG 
121:	ADISMIGQFG VGFYSAYLVA EKVVVITKHN DDEQYAWESS AGGSFTVRAD HGEPIGRGTK 
181:	VILHLKEDQT EYLEERRVKE VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE 
241:	DKDDEEKPKI EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE 
301:	YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK NNIKLYVRRV 
361:	FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI LKVIRKNIVK KCLELFSELA 
421:	EDKENYKKFY EAFSKNLKLG IHEDSTNRRR LSELLRYHTS QSGDEMTSLS EYVSRMKETQ 
481:	KSIYYITGES KEQVANSAFV ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG 
541:	LELPEDEEEK KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA 
601:	NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA VKDLVVLLFE 
661:	TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVAAEEP NAAVPDEIPP LEGDEDASRM 
721:	EEVD