Hsp90ab1
entrez
301252
canonical
uniprot
P34058
canonical
ensembl
ENSRNOG00000019834
resolver
ensp
ENSRNOP00000026920
resolver
genesymbol
Hsp90ab1
resolver
genesymbol_syn
Hsp84
resolver
genesymbol_syn
Hspc3
resolver
genesymbol_syn
Hspcb
resolver
uniprot
Q1PSW2
resolver
uniprot
Q66H55
resolver
uniprot
Q68GV5
resolver
uniprot
Q9QWC6
resolver
uniprot_entry
HS90B_RAT
resolver
uniprot_sec
Q1PSW2
resolver
uniprot_sec
Q66H55
resolver
uniprot_sec
Q68GV5
resolver
uniprot_sec
Q9QWC6
resolver
activity_regulation
ACTIVITY REGULATION: 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. {ECO:0000250|UniProtKB:P08238}.
uniprot
proteins
amino_acid_sequence
MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEEDKEDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQSGDEMTSLSEYVSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKSLVSVTKEGLELPEDEEEKKKMEESKAKFENLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVKDLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVTAEEPSAAVPDEIPPLEGDEDASRMEEVD
uniprot
proteins
function
FUNCTION: 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 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. They first 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 involved in the phosphorylation/activation of the STAT1 by chaperoning both JAK2 and PRKCE under heat shock and in turn, activates its own transcription. Involved in the translocation into ERGIC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1; the translocation process is mediated by the cargo receptor TMED10. {ECO:0000250|UniProtKB:P08238}.
uniprot
proteins
mass_dalton
83281
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro). {ECO:0000250|UniProtKB:P08238}.; PTM: ISGylated. {ECO:0000250|UniProtKB:P08238}.; PTM: S-nitrosylated; negatively regulates the ATPase activity. {ECO:0000250|UniProtKB:P08238}.; PTM: Phosphorylation at Tyr-301 by SRC is induced by lipopolysaccharide. Phosphorylation at Ser-226 and Ser-255 inhibits AHR interaction. {ECO:0000250|UniProtKB:P08238}.; PTM: Methylated by SMYD2; facilitates dimerization and chaperone complex formation; promotes cancer cell proliferation. {ECO:0000250|UniProtKB:P08238}.; PTM: Cleaved following oxidative stress resulting in HSP90AB1 protein radicals formation; disrupts the chaperoning function and the degradation of its client proteins. {ECO:0000250|UniProtKB:P08238}.
uniprot
proteins
protein_family
Heat shock protein 90 family
uniprot
proteins
pubmed
11732320
uniprot
proteins
pubmed
1525042
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15808839
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
27496612
uniprot
proteins
pubmed
3189818
uniprot
proteins
pubmed
8663025
uniprot
proteins
sequence_length
724
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8663025}. Melanosome {ECO:0000250|UniProtKB:P08238}. Nucleus {ECO:0000250|UniProtKB:P08238}. Secreted {ECO:0000250|UniProtKB:P08238}. Cell membrane {ECO:0000250|UniProtKB:P08238}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q6AZV1}. Note=Translocates with BIRC2 from the nucleus to the cytoplasm during differentiation. Secreted when associated with TGFB1 processed form (LAP). {ECO:0000250|UniProtKB:P08238}.
uniprot
proteins