HSPA1A
Heat shock 70 kDa protein 1A
Also known as: HS71A_HUMAN, HSP70-1, HSPA1
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P0DMV8
- Gene
- HSPA1A
- Ensembl
- ENSG00000204389
- Chromosome
- 6
- Canonical length
- 641 aa
- Protein class
- Disease related genes, Predicted intracellular proteins
- Subcellular location
- Vesicles,Perinuclear theca,Calyx,Flagellar centriole,Annulus
- Secretome location
- Intracellular and membrane
OverviewNCBI Gene
This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. In conjuction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins. [provided by RefSeq, Jul 2008]
Canonical amino-acid sequenceUniProt
641 residues, UniProt reviewed canonical sequence.
>P0DMV8|HSPA1A
1 MAKAAAIGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
61 LNPQNTVFDA KRLIGRKFGD PVVQSDMKHW PFQVINDGDK PKVQVSYKGE TKAFYPEEIS
121 SMVLTKMKEI AEAYLGYPVT NAVITVPAYF NDSQRQATKD AGVIAGLNVL RIINEPTAAA
181 IAYGLDRTGK GERNVLIFDL GGGTFDVSIL TIDDGIFEVK ATAGDTHLGG EDFDNRLVNH
241 FVEEFKRKHK KDISQNKRAV RRLRTACERA KRTLSSSTQA SLEIDSLFEG IDFYTSITRA
301 RFEELCSDLF RSTLEPVEKA LRDAKLDKAQ IHDLVLVGGS TRIPKVQKLL QDFFNGRDLN
361 KSINPDEAVA YGAAVQAAIL MGDKSENVQD LLLLDVAPLS LGLETAGGVM TALIKRNSTI
421 PTKQTQIFTT YSDNQPGVLI QVYEGERAMT KDNNLLGRFE LSGIPPAPRG VPQIEVTFDI
481 DANGILNVTA TDKSTGKANK ITITNDKGRL SKEEIERMVQ EAEKYKAEDE VQRERVSAKN
541 ALESYAFNMK SAVEDEGLKG KISEADKKKV LDKCQEVISW LDANTLAEKD EFEHKRKELE
601 QVCNPIISGL YQGAGGPGPG GFGAQGPKGG SGSGPTIEEV DLocalizationUniProt · AlphaFold · HPA
Whether an antibody against HSPA1A 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
- Secreted
- Secreted
- Yes
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.26
- Highest tissue expression
- 1,155 nTPM
Expression across tissuesHPA
Tissue
- liver: 1,155 nTPM
- lung: 1,054 nTPM
- cerebellum: 1,051 nTPM
- heart muscle: 935 nTPM
- spinal cord: 799 nTPM
- kidney: 742 nTPM
Single-cell type
- microglia: 1,396 nCPM
- astrocytes: 396 nCPM
- ependymal cells: 350 nCPM
- oligodendrocytes: 190 nCPM
- bergmann glia: 177 nCPM
- podocytes: 69 nCPM
Immune cell
- neutrophil: 6.9 nTPM
- intermediate monocyte: 3.6 nTPM
- eosinophil: 3.2 nTPM
- T-reg: 3.1 nTPM
- basophil: 2.3 nTPM
- classical monocyte: 2.3 nTPM
Brain region
- medulla oblongata: 5.8 nTPM
- cerebellum: 5.7 nTPM
- white matter: 5.7 nTPM
- midbrain: 3.8 nTPM
- cerebral cortex: 2.5 nTPM
- hippocampal formation: 2.5 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about HSPA1A.
Disease | ImmuneIEDB
Conditions an epitope on HSPA1A was assayed in.
- rheumatoid arthritis B cell
- multiple sclerosis B cell
- esophagus squamous cell carcinoma T cell
- hepatocellular carcinoma T cell
- colorectal cancer T cell
- Timothy grass allergy T cell
- allergic disease T cell
- renal cell carcinoma T cell
- pancreatic ductal adenocarcinoma T cell
- stomach cancer T cell
- brain glioma T cell
- type 1 diabetes mellitus 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)
- 1.29
- gnomAD pLI
- 0.03
- gnomAD missense Z
- 1.43
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- ATP metabolic process
- cellular heat acclimation
- cellular response to heat
- cellular response to oxidative stress
- cellular response to steroid hormone stimulus
- cellular response to unfolded protein
- chaperone-mediated protein complex assembly
- endoplasmic reticulum unfolded protein response
- lysosomal transport
- mRNA catabolic process
- negative regulation of apoptotic process
- negative regulation of cell growth
- negative regulation of cell population proliferation
- negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway
- negative regulation of extrinsic apoptotic signaling pathway in absence of ligand
- negative regulation of inclusion body assembly
- negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway
- negative regulation of protein ubiquitination
- negative regulation of transcription by RNA polymerase II
- negative regulation of transforming growth factor beta receptor signaling pathway
- positive regulation of erythrocyte differentiation
- positive regulation of gene expression
- positive regulation of interleukin-8 production
- positive regulation of microtubule nucleation
- positive regulation of NF-kappaB transcription factor activity
- positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process
- positive regulation of RNA splicing
- positive regulation of tumor necrosis factor-mediated signaling pathway
- protein refolding
- protein stabilization
- regulation of mitotic spindle assembly
- regulation of protein ubiquitination
- response to unfolded protein
Molecular functions
- ATP binding
- ATP hydrolysis activity
- ATP-dependent protein disaggregase activity
- ATP-dependent protein folding chaperone
- C3HC4-type RING finger domain binding
- cadherin binding
- denatured protein binding
- disordered domain specific binding
- enzyme binding
- G protein-coupled receptor binding
- heat shock protein binding
- histone deacetylase binding
- misfolded protein binding
- protein folding chaperone
- receptor ligand activity
- RNA binding
- signaling receptor binding
- transcription corepressor activity
- transcription regulator inhibitor activity
- ubiquitin protein ligase binding
- unfolded protein binding
- virus receptor activity
Cellular components
- aggresome
- blood microparticle
- centriole
- centrosome
- cytoplasm
- cytosol
- endoplasmic reticulum
- extracellular exosome
- extracellular region
- extracellular space
- ficolin-1-rich granule lumen
- focal adhesion
- inclusion body
- mitochondrion
- nuclear speck
- nucleoplasm
- nucleus
- perinuclear region of cytoplasm
- plasma membrane
- protein-containing complex
- ribonucleoprotein complex
- vesicle
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of HSPA1A 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 HSPA1A as an antibody target. Whether an autoantibody or antibody against HSPA1A could matter depends on whether native HSPA1A is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
HSPA1A is annotated as secreted, so native HSPA1A circulates and is directly accessible to antibodies. Secreted and cell-surface proteins are the autoantibody targets most likely to act like drugs, blocking or depleting the native protein.
Annotation status
The present source text does not explicitly label HSPA1A as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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