HSP90AB1
Heat shock protein HSP 90-beta
Also known as: HS90B_HUMAN, HSPC2, HSPCB
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P08238
- Gene
- HSP90AB1
- Ensembl
- ENSG00000096384
- Chromosome
- 6
- Canonical length
- 724 aa
- Protein class
- Cancer-related genes, Plasma proteins, Predicted intracellular proteins, Transporters
- Subcellular location
- Plasma membrane,Cytosol
- Secretome location
- Intracellular and membrane
- Quaternary structure
- Homodimer
OverviewNCBI Gene
This gene encodes a member of the heat shock protein 90 family; these proteins are involved in signal transduction, protein folding and degradation and morphological evolution. This gene encodes the constitutive form of the cytosolic 90 kDa heat-shock protein and is thought to play a role in gastric apoptosis and inflammation. Alternative splicing results in multiple transcript variants. Pseudogenes have been identified on multiple chromosomes. [provided by RefSeq, Dec 2012]
Canonical amino-acid sequenceUniProt
724 residues, UniProt reviewed canonical sequence.
>P08238|HSP90AB1
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 EEVDLocalizationUniProt · AlphaFold · HPA
Whether an antibody against HSP90AB1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.31
- Highest tissue expression
- 1,322 nTPM
Expression across tissuesHPA
Tissue
- skeletal muscle: 1,322 nTPM
- ovary: 1,020 nTPM
- tongue: 933 nTPM
- heart muscle: 734 nTPM
- pancreas: 687 nTPM
- adrenal gland: 687 nTPM
Single-cell type
- pancreatic duct cells: 2,925 nCPM
- epididymal efferent duct absorptive cells: 2,290 nCPM
- pancreatic acinar cells: 2,161 nCPM
- endometrial secretory cells: 2,081 nCPM
- fallopian secretory cells: 2,039 nCPM
- epididymal basal cells: 1,674 nCPM
Immune cell
- total PBMC: 678 nTPM
- MAIT T-cell: 579 nTPM
- memory B-cell: 546 nTPM
- naive CD4 T-cell: 511 nTPM
- naive CD8 T-cell: 495 nTPM
- naive B-cell: 475 nTPM
Brain region
- hypothalamus: 1,005 nTPM
- white matter: 980 nTPM
- pons: 913 nTPM
- midbrain: 854 nTPM
- cerebral cortex: 842 nTPM
- medulla oblongata: 752 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about HSP90AB1.
Disease | ImmuneIEDB
Conditions an epitope on HSP90AB1 was assayed in.
- candidiasis B cell
- allergic bronchopulmonary aspergillosis B cell
- systemic lupus erythematosus B cell
- infective endocarditis B cell
- Plasmodium vivax malaria B cell
- multiple sclerosis B cell
- infertility B cell
- measles T cell
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 0.21
- gnomAD pLI
- 1
- gnomAD missense Z
- 2.05
- DepMap mean gene effect
- -0.28
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 8% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- cellular response to heat
- cellular response to interleukin-4
- chaperone-mediated protein complex assembly
- negative regulation of apoptotic process
- negative regulation of proteasomal protein catabolic process
- negative regulation of proteasomal ubiquitin-dependent protein catabolic process
- placenta development
- positive regulation of cell differentiation
- positive regulation of nitric oxide biosynthetic process
- positive regulation of protein localization to cell surface
- positive regulation of transforming growth factor beta receptor signaling pathway
- protein folding
- protein stabilization
- regulation of cell cycle
- regulation of protein localization
- regulation of protein ubiquitination
- response to unfolded protein
- supramolecular fiber organization
- telomerase holoenzyme complex assembly
- telomere maintenance via telomerase
- virion attachment to host cell
Molecular functions
- ATP binding
- ATP hydrolysis activity
- ATP-dependent protein binding
- ATP-dependent protein folding chaperone
- cadherin binding
- disordered domain specific binding
- DNA polymerase binding
- double-stranded RNA binding
- heat shock protein binding
- histone deacetylase binding
- histone methyltransferase binding
- identical protein binding
- kinase binding
- MHC class II protein complex binding
- nitric-oxide synthase regulator activity
- peptide binding
- protein dimerization activity
- protein folding chaperone
- protein homodimerization activity
- protein kinase binding
- protein kinase regulator activity
- protein phosphatase activator activity
- receptor ligand inhibitor activity
- RNA binding
- tau protein binding
- TPR domain binding
- ubiquitin protein ligase binding
- unfolded protein binding
Cellular components
- aryl hydrocarbon receptor complex
- axonal growth cone
- cell surface
- cytoplasm
- cytosol
- dendritic growth cone
- dynein axonemal particle
- extracellular exosome
- extracellular region
- ficolin-1-rich granule lumen
- HSP90-CDC37 chaperone complex
- melanosome
- membrane
- mitochondrion
- neuronal cell body
- nucleoplasm
- nucleus
- perinuclear region of cytoplasm
- plasma membrane
- protein folding chaperone complex
- protein-containing complex
- secretory granule lumen
Protein domainsUniProt · Pfam · InterPro
- Heat shock protein Hsp90 family
- Histidine kinase/HSP90-like ATPase domain
- Heat shock protein Hsp90, conserved site
- Ribosomal protein uS5 domain 2-type superfamily
- Heat shock protein Hsp90, N-terminal
- Histidine kinase/HSP90-like ATPase superfamily
- HSP90, C-terminal domain
- Hsp90 protein
- Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of HSP90AB1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads HSP90AB1 as an antibody target. Whether an autoantibody or antibody against HSP90AB1 could matter depends on whether native HSP90AB1 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
HSP90AB1 is annotated at the cell surface, where native HSP90AB1 is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label HSP90AB1 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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