HS90B_RAT
ID HS90B_RAT Reviewed; 724 AA.
AC P34058; Q1PSW2; Q66H55; Q68GV5; Q9QWC6;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 207.
DE RecName: Full=Heat shock protein HSP 90-beta;
DE AltName: Full=Heat shock 84 kDa;
DE Short=HSP 84;
DE Short=HSP84;
GN Name=Hsp90ab1; Synonyms=Hsp84, Hspcb;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1525042; DOI=10.1016/0960-0760(92)90089-2;
RA McGuire J.A., Poellinger L., Wikstroem A.-C., Gustafsson J.-A.;
RT "Cloning and regulation by glucocorticoid receptor ligands of a rat
RT hsp90.";
RL J. Steroid Biochem. Mol. Biol. 42:813-822(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Brown Norway/NHsdMcwi, and SS/JrHsdMcwi; TISSUE=Heart;
RX PubMed=15808839; DOI=10.1016/j.yjmcc.2005.02.005;
RA Shi Y., Hutchins W., Ogawa H., Chang C.-C., Pritchard K.A. Jr., Zhang C.,
RA Khampang P., Lazar J., Jacob H.J., Rafiee P., Baker J.E.;
RT "Increased resistance to myocardial ischemia in the Brown Norway vs. Dahl S
RT rat: role of nitric oxide synthase and Hsp90.";
RL J. Mol. Cell. Cardiol. 38:625-635(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Chang Y.S., Chao C.C., Wang C.H., Lai Y.K.;
RT "Promoter analysis and gene regulation of rat 84 kDa heat shock protein.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-26.
RX PubMed=3189818; DOI=10.1016/0003-2697(88)90207-2;
RA Denis M.;
RT "Two-step purification and N-terminal amino acid sequence analysis of the
RT rat Mr 90,000 heat shock protein.";
RL Anal. Biochem. 173:405-411(1988).
RN [6]
RP PROTEIN SEQUENCE OF 2-16.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=11732320; DOI=10.1007/bf01288360;
RA Langer T., Fasold H.;
RT "Isolation and quantification of the heat shock protein 90 alpha and beta
RT isoforms from rat liver.";
RL Protoplasma 218:54-56(2001).
RN [7]
RP PROTEIN SEQUENCE OF 181-196 AND 320-330, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (NOV-2006) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 205-218; 306-330 AND 413-427, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH TP53.
RC TISSUE=Embryo;
RX PubMed=8663025; DOI=10.1074/jbc.271.25.15084;
RA Sepehrnia B., Paz I.B., Dasgupta G., Momand J.;
RT "Heat shock protein 84 forms a complex with mutant p53 protein
RT predominantly within a cytoplasmic compartment of the cell.";
RL J. Biol. Chem. 271:15084-15090(1996).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226; SER-255; SER-261 AND
RP SER-445, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [10]
RP INTERACTION WITH PDCL3.
RX PubMed=27496612; DOI=10.1002/jcb.25669;
RA Krzemien-Ojak L., Goral A., Joachimiak E., Filipek A., Fabczak H.;
RT "Interaction of a Novel Chaperone PhLP2A With the Heat Shock Protein
RT Hsp90.";
RL J. Cell. Biochem. 118:420-429(2017).
CC -!- FUNCTION: Molecular chaperone that promotes the maturation, structural
CC maintenance and proper regulation of specific target proteins involved
CC for instance in cell cycle control and signal transduction. Undergoes a
CC functional cycle linked to its ATPase activity. This cycle probably
CC induces conformational changes in the client proteins, thereby causing
CC their activation. Interacts dynamically with various co-chaperones that
CC modulate its substrate recognition, ATPase cycle and chaperone
CC function. Engages with a range of client protein classes via its
CC interaction with various co-chaperone proteins or complexes, that act
CC as adapters, simultaneously able to interact with the specific client
CC and the central chaperone itself. Recruitment of ATP and co-chaperone
CC followed by client protein forms a functional chaperone. After the
CC completion of the chaperoning process, properly folded client protein
CC and co-chaperone leave HSP90 in an ADP-bound partially open
CC conformation and finally, ADP is released from HSP90 which acquires an
CC open conformation for the next cycle. Apart from its chaperone
CC activity, it also plays a role in the regulation of the transcription
CC machinery. HSP90 and its co-chaperones modulate transcription at least
CC at three different levels. They first alter the steady-state levels of
CC certain transcription factors in response to various physiological
CC cues. Second, they modulate the activity of certain epigenetic
CC modifiers, such as histone deacetylases or DNA methyl transferases, and
CC thereby respond to the change in the environment. Third, they
CC participate in the eviction of histones from the promoter region of
CC certain genes and thereby turn on gene expression. Antagonizes STUB1-
CC mediated inhibition of TGF-beta signaling via inhibition of STUB1-
CC mediated SMAD3 ubiquitination and degradation. Promotes cell
CC differentiation by chaperoning BIRC2 and thereby protecting from auto-
CC ubiquitination and degradation by the proteasomal machinery. Main
CC chaperone involved in the phosphorylation/activation of the STAT1 by
CC chaperoning both JAK2 and PRKCE under heat shock and in turn, activates
CC its own transcription. Involved in the translocation into ERGIC
CC (endoplasmic reticulum-Golgi intermediate compartment) of leaderless
CC cargos (lacking the secretion signal sequence) such as the interleukin
CC 1/IL-1; the translocation process is mediated by the cargo receptor
CC TMED10. {ECO:0000250|UniProtKB:P08238}.
CC -!- ACTIVITY REGULATION: In the resting state, through the dimerization of
CC its C-terminal domain, HSP90 forms a homodimer which is defined as the
CC open conformation. Upon ATP-binding, the N-terminal domain undergoes
CC significant conformational changes and comes in contact to form an
CC active closed conformation. After HSP90 finishes its chaperoning tasks
CC of assisting the proper folding, stabilization and activation of client
CC proteins under the active state, ATP molecule is hydrolyzed to ADP
CC which then dissociates from HSP90 and directs the protein back to the
CC resting state. {ECO:0000250|UniProtKB:P08238}.
CC -!- SUBUNIT: Monomer. Homodimer (By similarity). Forms a complex with CDK6
CC and CDC37. Interacts with UNC45A; binding to UNC45A involves 2 UNC45A
CC monomers per HSP90AB1 dimer (By similarity). Interacts with CHORDC1 (By
CC similarity). Interacts with DNAJC7. Interacts with FKBP4. May interact
CC with NWD1. Interacts with SGTA. Interacts with HSF1 in an ATP-dependent
CC manner. Interacts with MET; the interaction suppresses MET kinase
CC activity. Interacts with ERBB2 in an ATP-dependent manner; the
CC interaction suppresses ERBB2 kinase activity. Interacts with HIF1A,
CC KEAP1 and RHOBTB2. Interacts with STUB1 and SMAD3. Interacts with XPO1
CC and AHSA1. Interacts with BIRC2. Interacts with KCNQ4; promotes cell
CC surface expression of KCNQ4. Interacts with BIRC2; prevents auto-
CC ubiquitination and degradation of its client protein BIRC2. Interacts
CC with NOS3. Interacts with AHR; interaction is inhibited by HSP90AB1
CC phosphorylation on Ser-226 and Ser-255. Interacts with STIP1 and CDC37;
CC upon SMYD2-dependent methylation. Interacts with JAK2 and PRKCE;
CC promotes functional activation in a heat shock-dependent manner.
CC Interacts with HSP90AA1; interaction is constitutive. HSP90AB1-CDC37
CC chaperone complex interacts with inactive MAPK7 (via N-terminal half)
CC in resting cells; the interaction is MAP2K5-independent and prevents
CC from ubiquitination and proteasomal degradation. Interacts with CDC25A;
CC prevents heat shock-mediated CDC25A degradation and contributes to cell
CC cycle progression (By similarity). Interacts with TP53 (via DNA binding
CC domain); suppresses TP53 aggregation and prevents from irreversible
CC thermal inactivation (PubMed:8663025). Interacts with TGFB1 processed
CC form (LAP); inhibits latent TGFB1 activation (By similarity). Interacts
CC with TRIM8; prevents nucleus translocation of phosphorylated STAT3 and
CC HSP90AB1 (By similarity). Interacts with NR3C1 (via domain NR LBD) and
CC NR1D1 (via domain NR LBD) (By similarity). Interacts with PDCL3
CC (PubMed:27496612).Interacts with TTC4 (via TPR repeats) (By
CC similarity). Interacts with IL1B; the interaction facilitates cargo
CC translocation into the ERGIC (By similarity).
CC {ECO:0000250|UniProtKB:P08238, ECO:0000250|UniProtKB:P11499,
CC ECO:0000269|PubMed:27496612, ECO:0000269|PubMed:8663025}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8663025}.
CC Melanosome {ECO:0000250|UniProtKB:P08238}. Nucleus
CC {ECO:0000250|UniProtKB:P08238}. Secreted
CC {ECO:0000250|UniProtKB:P08238}. Cell membrane
CC {ECO:0000250|UniProtKB:P08238}. Dynein axonemal particle
CC {ECO:0000250|UniProtKB:Q6AZV1}. Note=Translocates with BIRC2 from the
CC nucleus to the cytoplasm during differentiation. Secreted when
CC associated with TGFB1 processed form (LAP).
CC {ECO:0000250|UniProtKB:P08238}.
CC -!- DOMAIN: The TPR repeat-binding motif mediates interaction with TPR
CC repeat-containing proteins. {ECO:0000250|UniProtKB:P07900}.
CC -!- PTM: Ubiquitinated in the presence of STUB1-UBE2D1 complex (in vitro).
CC {ECO:0000250|UniProtKB:P08238}.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P08238}.
CC -!- PTM: S-nitrosylated; negatively regulates the ATPase activity.
CC {ECO:0000250|UniProtKB:P08238}.
CC -!- PTM: Phosphorylation at Tyr-301 by SRC is induced by
CC lipopolysaccharide. Phosphorylation at Ser-226 and Ser-255 inhibits AHR
CC interaction. {ECO:0000250|UniProtKB:P08238}.
CC -!- PTM: Methylated by SMYD2; facilitates dimerization and chaperone
CC complex formation; promotes cancer cell proliferation.
CC {ECO:0000250|UniProtKB:P08238}.
CC -!- PTM: Cleaved following oxidative stress resulting in HSP90AB1 protein
CC radicals formation; disrupts the chaperoning function and the
CC degradation of its client proteins. {ECO:0000250|UniProtKB:P08238}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family. {ECO:0000305}.
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DR EMBL; S45392; AAB23369.1; -; mRNA.
DR EMBL; AY695392; AAT99568.1; -; mRNA.
DR EMBL; AY695393; AAT99569.1; -; mRNA.
DR EMBL; DQ022068; ABE27999.1; -; Genomic_DNA.
DR EMBL; BC082009; AAH82009.1; -; mRNA.
DR PIR; S71306; S71306.
DR RefSeq; NP_001004082.3; NM_001004082.3.
DR AlphaFoldDB; P34058; -.
DR SMR; P34058; -.
DR BioGRID; 256892; 13.
DR CORUM; P34058; -.
DR IntAct; P34058; 8.
DR MINT; P34058; -.
DR STRING; 10116.ENSRNOP00000026920; -.
DR GlyGen; P34058; 2 sites.
DR iPTMnet; P34058; -.
DR PhosphoSitePlus; P34058; -.
DR World-2DPAGE; 0004:P34058; -.
DR jPOST; P34058; -.
DR PaxDb; P34058; -.
DR PRIDE; P34058; -.
DR ABCD; P34058; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000086986; ENSRNOP00000074112; ENSRNOG00000019834.
DR GeneID; 301252; -.
DR KEGG; rno:301252; -.
DR UCSC; RGD:1303075; rat.
DR CTD; 3326; -.
DR RGD; 1303075; Hsp90ab1.
DR eggNOG; KOG0019; Eukaryota.
DR GeneTree; ENSGT01020000230401; -.
DR HOGENOM; CLU_006684_1_3_1; -.
DR InParanoid; P34058; -.
DR OMA; TRMKAEQ; -.
DR OrthoDB; 924636at2759; -.
DR PhylomeDB; P34058; -.
DR TreeFam; TF300686; -.
DR Reactome; R-RNO-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR Reactome; R-RNO-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-RNO-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-RNO-3371511; HSF1 activation.
DR Reactome; R-RNO-3371568; Attenuation phase.
DR Reactome; R-RNO-3371571; HSF1-dependent transactivation.
DR Reactome; R-RNO-399954; Sema3A PAK dependent Axon repulsion.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-844456; The NLRP3 inflammasome.
DR Reactome; R-RNO-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-RNO-8937144; Aryl hydrocarbon receptor signalling.
DR Reactome; R-RNO-8939211; ESR-mediated signaling.
DR Reactome; R-RNO-9013418; RHOBTB2 GTPase cycle.
DR Reactome; R-RNO-9018519; Estrogen-dependent gene expression.
DR PRO; PR:P34058; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000019834; Expressed in Ammon's horn and 20 other tissues.
DR ExpressionAtlas; P34058; baseline and differential.
DR Genevisible; P34058; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; ISS:UniProtKB.
DR GO; GO:0044295; C:axonal growth cone; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0008180; C:COP9 signalosome; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0044294; C:dendritic growth cone; ISO:RGD.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:1990565; C:HSP90-CDC37 chaperone complex; ISO:RGD.
DR GO; GO:0016234; C:inclusion body; IDA:RGD.
DR GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
DR GO; GO:0005765; C:lysosomal membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:1990917; C:ooplasm; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:1990913; C:sperm head plasma membrane; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:RGD.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0043008; F:ATP-dependent protein binding; ISO:RGD.
DR GO; GO:0002135; F:CTP binding; IDA:RGD.
DR GO; GO:0032564; F:dATP binding; IDA:RGD.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
DR GO; GO:0070182; F:DNA polymerase binding; ISO:RGD.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
DR GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
DR GO; GO:1901363; F:heterocyclic compound binding; IPI:RGD.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
DR GO; GO:1990226; F:histone methyltransferase binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0042277; F:peptide binding; ISO:RGD.
DR GO; GO:0140597; F:protein carrier chaperone; NAS:ParkinsonsUK-UCL.
DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB.
DR GO; GO:0044183; F:protein folding chaperone; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0019887; F:protein kinase regulator activity; IEA:Ensembl.
DR GO; GO:0017098; F:sulfonylurea receptor binding; IPI:RGD.
DR GO; GO:0048156; F:tau protein binding; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0002134; F:UTP binding; IDA:RGD.
DR GO; GO:0048675; P:axon extension; ISO:RGD.
DR GO; GO:0034605; P:cellular response to heat; ISO:RGD.
DR GO; GO:0071353; P:cellular response to interleukin-4; ISO:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0021955; P:central nervous system neuron axonogenesis; ISO:RGD.
DR GO; GO:0061684; P:chaperone-mediated autophagy; NAS:ParkinsonsUK-UCL.
DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; ISO:RGD.
DR GO; GO:0030010; P:establishment of cell polarity; ISO:RGD.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
DR GO; GO:1903660; P:negative regulation of complement-dependent cytotoxicity; IMP:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
DR GO; GO:1901799; P:negative regulation of proteasomal protein catabolic process; IMP:ARUK-UCL.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0051248; P:negative regulation of protein metabolic process; IMP:ARUK-UCL.
DR GO; GO:1901389; P:negative regulation of transforming growth factor beta activation; ISS:UniProtKB.
DR GO; GO:0001890; P:placenta development; ISO:RGD.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISO:RGD.
DR GO; GO:0045793; P:positive regulation of cell size; IMP:RGD.
DR GO; GO:1904031; P:positive regulation of cyclin-dependent protein kinase activity; IMP:ARUK-UCL.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:RGD.
DR GO; GO:0032092; P:positive regulation of protein binding; IMP:RGD.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:RGD.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
DR GO; GO:2000010; P:positive regulation of protein localization to cell surface; ISO:RGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:RGD.
DR GO; GO:0051973; P:positive regulation of telomerase activity; ISO:RGD.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006457; P:protein folding; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
DR GO; GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; ISO:RGD.
DR GO; GO:0061635; P:regulation of protein complex stability; NAS:ParkinsonsUK-UCL.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:0031396; P:regulation of protein ubiquitination; ISO:RGD.
DR GO; GO:0060338; P:regulation of type I interferon-mediated signaling pathway; ISO:RGD.
DR GO; GO:0042220; P:response to cocaine; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; ISO:RGD.
DR GO; GO:0009651; P:response to salt stress; IEP:RGD.
DR GO; GO:0006986; P:response to unfolded protein; TAS:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0097435; P:supramolecular fiber organization; ISO:RGD.
DR GO; GO:1905323; P:telomerase holoenzyme complex assembly; ISO:RGD.
DR GO; GO:0007004; P:telomere maintenance via telomerase; ISO:RGD.
DR GO; GO:0019062; P:virion attachment to host cell; ISO:RGD.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell membrane; Chaperone; Cytoplasm;
KW Direct protein sequencing; Glycoprotein; Membrane; Methylation;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW S-nitrosylation; Secreted; Stress response; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11732320,
FT ECO:0000269|PubMed:3189818"
FT CHAIN 2..724
FT /note="Heat shock protein HSP 90-beta"
FT /id="PRO_0000062920"
FT REGION 2..527
FT /note="Interaction with TP53"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT REGION 2..214
FT /note="Interaction with BIRC2"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT REGION 9..231
FT /note="Interaction with NR3C1"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT REGION 215..552
FT /note="Interaction with AHSA1"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT REGION 222..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..608
FT /note="Interaction with NR3C1"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT REGION 620..723
FT /note="Interaction with NR1D1"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT REGION 694..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 720..724
FT /note="TPR repeat-binding"
FT COMPBIAS 241..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 392
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT SITE 126..127
FT /note="Cleaved under oxidative stress"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 219
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 297
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 301
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 305
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 399
FT /note="N6-malonyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 435
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 479
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 481
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 484
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT MOD_RES 531
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 531
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT MOD_RES 574
FT /note="N6-methylated lysine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 577
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT MOD_RES 590
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 624
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P11499"
FT MOD_RES 669
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT MOD_RES 718
FT /note="Phosphoserine; by PLK2 and PLK3"
FT /evidence="ECO:0000250|UniProtKB:P08238"
FT CARBOHYD 434
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 452
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CONFLICT 6..7
FT /note="HH -> QK (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 11
FT /note="E -> P (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="F -> T (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 20
FT /note="E -> F (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="S -> F (in Ref. 4; AAH82009)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="R -> A (in Ref. 1; AAB23369)"
FT /evidence="ECO:0000305"
FT CONFLICT 368
FT /note="E -> D (in Ref. 1; AAB23369)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="N -> D (in Ref. 3; ABE27999)"
FT /evidence="ECO:0000305"
FT CONFLICT 559
FT /note="K -> R (in Ref. 1; AAB23369)"
FT /evidence="ECO:0000305"
FT CONFLICT 664..674
FT /note="LSSGFSLEDPQ -> SSLASHFRRPK (in Ref. 1; AAB23369)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 724 AA; 83281 MW; CE323E81CE173ECB CRC64;
MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT
DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN NLGTIAKSGT KAFMEALQAG
ADISMIGQFG VGFYSAYLVA EKVVVITKHN DDEQYAWESS AGGSFTVRAD HGEPIGRGTK
VILHLKEDQT EYLEERRVKE VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE
DKEDEEKPKI EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE
YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK NNIKLYVRRV
FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI LKVIRKNIVK KCLELFSELA
EDKENYKKFY EAFSKNLKLG IHEDSTNRRR LSELLRYHTS QSGDEMTSLS EYVSRMKETQ
KSIYYITGES KEQVANSAFV ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG
LELPEDEEEK KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA
NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA VKDLVVLLFE
TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVTAEEP SAAVPDEIPP LEGDEDASRM
EEVD
