HSP90AB1
entrez
3326
canonical
uniprot
P08238
canonical
ensembl
ENSG00000096384
resolver
ensp
ENSP00000325875
resolver
ensp
ENSP00000360609
resolver
ensp
ENSP00000360709
resolver
ensp
ENSP00000481908
resolver
ensp
ENSP00000545019
resolver
ensp
ENSP00000545020
resolver
ensp
ENSP00000545021
resolver
ensp
ENSP00000545022
resolver
ensp
ENSP00000545023
resolver
ensp
ENSP00000545025
resolver
ensp
ENSP00000545026
resolver
ensp
ENSP00000545027
resolver
ensp
ENSP00000594618
resolver
ensp
ENSP00000594622
resolver
ensp
ENSP00000594624
resolver
ensp
ENSP00000594627
resolver
ensp
ENSP00000594633
resolver
ensp
ENSP00000594637
resolver
ensp
ENSP00000594638
resolver
ensp
ENSP00000615786
resolver
ensp
ENSP00000615788
resolver
ensp
ENSP00000615789
resolver
ensp
ENSP00000615790
resolver
ensp
ENSP00000615793
resolver
ensp
ENSP00000615794
resolver
enst
ENST00000353801
resolver
enst
ENST00000371554
resolver
enst
ENST00000371646
resolver
enst
ENST00000620073
resolver
enst
ENST00000874960
resolver
enst
ENST00000874961
resolver
enst
ENST00000874962
resolver
enst
ENST00000874963
resolver
enst
ENST00000874964
resolver
enst
ENST00000874966
resolver
enst
ENST00000874967
resolver
enst
ENST00000874968
resolver
enst
ENST00000924559
resolver
enst
ENST00000924563
resolver
enst
ENST00000924568
resolver
enst
ENST00000924574
resolver
enst
ENST00000924578
resolver
enst
ENST00000924579
resolver
enst
ENST00000945727
resolver
enst
ENST00000945729
resolver
enst
ENST00000945730
resolver
enst
ENST00000945731
resolver
enst
ENST00000945734
resolver
enst
ENST00000945735
resolver
genesymbol
HSP90AB1
resolver
genesymbol_syn
HSP90B
resolver
genesymbol_syn
HSPC2
resolver
genesymbol_syn
HSPC3
resolver
genesymbol_syn
HSPCB
resolver
hgnc
HGNC:5258
resolver
uniprot
B2R5P0
resolver
uniprot
B4DGL0
resolver
uniprot
Q5T9W7
resolver
uniprot
Q6PK50
resolver
uniprot
Q9NQW0
resolver
uniprot
Q9NTK6
resolver
uniprot_entry
B4DGL0_HUMAN
resolver
uniprot_entry
HS90B_HUMAN
resolver
uniprot_entry
Q6PK50_HUMAN
resolver
uniprot_sec
B2R5P0
resolver
uniprot_sec
Q5T9W7
resolver
uniprot_sec
Q9NQW0
resolver
uniprot_sec
Q9NTK6
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:0000269|PubMed:18400751}.
uniprot
proteins
amino_acid_sequence
MPEEVHHGEEEVETFAFQAEIAQLMSLIINTFYSNKEIFLRELISNASDALDKIRYESLTDPSKLDSGKELKIDIIPNPQERTLTLVDTGIGMTKADLINNLGTIAKSGTKAFMEALQAGADISMIGQFGVGFYSAYLVAEKVVVITKHNDDEQYAWESSAGGSFTVRADHGEPIGRGTKVILHLKEDQTEYLEERRVKEVVKKHSQFIGYPITLYLEKEREKEISDDEAEEEKGEKEEEDKDDEEKPKIEDVGSDEEDDSGKDKKKKTKKIKEKYIDQEELNKTKPIWTRNPDDITQEEYGEFYKSLTNDWEDHLAVKHFSVEGQLEFRALLFIPRRAPFDLFENKKKKNNIKLYVRRVFIMDSCDELIPEYLNFIRGVVDSEDLPLNISREMLQQSKILKVIRKNIVKKCLELFSELAEDKENYKKFYEAFSKNLKLGIHEDSTNRRRLSELLRYHTSQSGDEMTSLSEYVSRMKETQKSIYYITGESKEQVANSAFVERVRKRGFEVVYMTEPIDEYCVQQLKEFDGKSLVSVTKEGLELPEDEEEKKKMEESKAKFENLCKLMKEILDKKVEKVTISNRLVSSPCCIVTSTYGWTANMERIMKAQALRDNSTMGYMMAKKHLEINPDHPIVETLRQKAEADKNDKAVKDLVVLLFETALLSSGFSLEDPQTHSNRIYRMIKLGLGIDEDEVAAEEPNAAVPDEIPPLEGDEDASRMEEVD
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 (PubMed:16478993, PubMed:19696785). 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 (PubMed:26991466, PubMed:27295069). 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 (PubMed:25973397). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385). Promotes cell differentiation by chaperoning BIRC2 and thereby protecting from auto-ubiquitination and degradation by the proteasomal machinery (PubMed:18239673). 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 (PubMed:20353823). 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 (PubMed:32272059). {ECO:0000269|PubMed:16478993, ECO:0000269|PubMed:18239673, ECO:0000269|PubMed:19696785, ECO:0000269|PubMed:20353823, ECO:0000269|PubMed:24613385, ECO:0000269|PubMed:32272059, ECO:0000303|PubMed:25973397, ECO:0000303|PubMed:26991466, ECO:0000303|PubMed:27295069}.; FUNCTION: (Microbial infection) Binding to N.meningitidis NadA stimulates monocytes (PubMed:21949862). Seems to interfere with N.meningitidis NadA-mediated invasion of human cells (Probable). {ECO:0000269|PubMed:21949862, ECO:0000305|PubMed:22066472}.
uniprot
proteins
mass_dalton
83264
uniprot
proteins
mutagenesis
MUTAGEN 42; /note="E->A: Strong ATP-binding. Strong interaction with HSF1, HIF1A, ERBB2, MET, KEAP1 and RHOBTB2."; /evidence="ECO:0000269|PubMed:26517842"; MUTAGEN 88; /note="D->A: Impaired ATP-binding. Strong interaction with HIF1A, MET, KEAP1 and RHOBTB2. Loss of interaction with HSF1 and ERBB2."; /evidence="ECO:0000269|PubMed:26517842"; MUTAGEN 226; /note="S->A: Increases the binding affinity for AHR; when associated with A-255. Increases AHR transcription activity; when associated with A-255."; /evidence="ECO:0000269|PubMed:15581363"; MUTAGEN 226; /note="S->E: No effect on the interaction with AHR; when associated with E-255."; /evidence="ECO:0000269|PubMed:15581363"; MUTAGEN 255; /note="S->A: Increases the binding affinity for AHR; when associated with A-226. Increases AHR transcription activity; when associated with A-226."; /evidence="ECO:0000269|PubMed:15581363"; MUTAGEN 255; /note="S->E: No effect on the interaction with AHR; when associated with E-226."; /evidence="ECO:0000269|PubMed:15581363"; MUTAGEN 301; /note="Y->F: Decreases interaction with NOS3 and SRC. impairs resists LPS-induced tyrosine phosphorylation. Does not block LPS-induced pp60src phosphorylation."; /evidence="ECO:0000269|PubMed:23585225"; MUTAGEN 531; /note="K->A: Highly decreases the signal of SMYD2-dependent HSP90AB1 methylation; when associated with A-574. Diminishes dimerized form; when associated with A-574. Reduces interaction with STIP1 or CDC37; when associated with A-574."; /evidence="ECO:0000269|PubMed:24880080"; MUTAGEN 574; /note="K->A: Decreases the signal of SMYD2-dependent HSP90AB1 methylation. Highly decreases the signal of SMYD2-dependent HSP90AB1 methylation; when associated with A-531. Diminishes dimerized form; when associated with A-531. Reduces interaction with STIP1 or CDC37; when associated with A-531."; /evidence="ECO:0000269|PubMed:24880080"; MUTAGEN 590; /note="C->A,N,D: Reduced ATPase activity and client protein activation."; /evidence="ECO:0000269|PubMed:19696785
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro). {ECO:0000269|PubMed:18042044}.; PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; PTM: S-nitrosylated; negatively regulates the ATPase activity. {ECO:0000305|PubMed:19696785}.; PTM: Phosphorylation at Tyr-301 by SRC is induced by lipopolysaccharide (PubMed:23585225). Phosphorylation at Ser-226 and Ser-255 inhibits AHR interaction (PubMed:15581363). {ECO:0000269|PubMed:15581363, ECO:0000269|PubMed:23585225}.; PTM: Methylated by SMYD2; facilitates dimerization and chaperone complex formation; promotes cancer cell proliferation. {ECO:0000269|PubMed:24880080}.; PTM: Cleaved following oxidative stress resulting in HSP90AB1 protein radicals formation; disrupts the chaperoning function and the degradation of its client proteins. {ECO:0000269|PubMed:22848402}.
uniprot
proteins
protein_family
Heat shock protein 90 family
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15159550
uniprot
proteins
pubmed
15217611
uniprot
proteins
pubmed
15358771
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15581363
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
16139798
uniprot
proteins
pubmed
16478993
uniprot
proteins
pubmed
16580629
uniprot
proteins
pubmed
17081065
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
18042044
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18239673
uniprot
proteins
pubmed
18318008
uniprot
proteins
pubmed
18320024
uniprot
proteins
pubmed
18400751
uniprot
proteins
pubmed
18620420
uniprot
proteins
pubmed
18663603
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19696785
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20353823
uniprot
proteins
pubmed
20599762
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21908771
uniprot
proteins
pubmed
21949862
uniprot
proteins
pubmed
22022502
uniprot
proteins
pubmed
22066472
uniprot
proteins
pubmed
22828320
uniprot
proteins
pubmed
22843495
uniprot
proteins
pubmed
22848402
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23428871
uniprot
proteins
pubmed
23431407
uniprot
proteins
pubmed
23585225
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24613385
uniprot
proteins
pubmed
24681825
uniprot
proteins
pubmed
2469626
uniprot
proteins
pubmed
24880080
uniprot
proteins
pubmed
2492519
uniprot
proteins
pubmed
25486457
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
25973397
uniprot
proteins
pubmed
26517842
uniprot
proteins
pubmed
26991466
uniprot
proteins
pubmed
27295069
uniprot
proteins
pubmed
2768249
uniprot
proteins
pubmed
32272059
uniprot
proteins
pubmed
3301534
uniprot
proteins
pubmed
7588731
uniprot
proteins
pubmed
8180474
uniprot
proteins
pubmed
9150948
uniprot
proteins
pubmed
9482106
uniprot
proteins
sequence_length
724
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16580629, ECO:0000269|PubMed:18239673, ECO:0000269|PubMed:24880080, ECO:0000269|PubMed:9482106}. Melanosome {ECO:0000269|PubMed:17081065}. Nucleus {ECO:0000269|PubMed:18239673}. Secreted {ECO:0000269|PubMed:20599762}. Cell membrane {ECO:0000269|PubMed:20599762}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q6AZV1}. Cell surface {ECO:0000269|PubMed:21949862}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). Translocates with BIRC2 from the nucleus to the cytoplasm during differentiation (PubMed:18239673). Secreted when associated with TGFB1 processed form (LAP) (PubMed:20599762). {ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:18239673, ECO:0000269|PubMed:20599762}.
uniprot
proteins