GENERAL INFORMATIONi
Gene namei HSPA1A
Synonyms HSP70-1, HSPA1
Gene descriptioni Heat shock protein family A (Hsp70) member 1A
Protein classi Disease related genes
Predicted locationi Intracellular
Protein evidence Evidence at protein level (all genes)
GENE INFORMATIONi
Chromosome 6
Cytoband p21.33
Chromosome location (bp) 31815543 - 31817946
Number of transcriptsi 2
Ensembl ENSG00000204389 (version 109)
Entrez gene 3303
HGNC HGNC:5232
UniProt P0DMV8 (UniProt - Evidence at protein level)
neXtProt NX_P0DMV8
GeneCards HSPA1A
Antibodypedia HSPA1A antibodies


PROTEIN FUNCTION
Protein function (UniProt)i Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release. The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 1, 2, 3. Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation 4. Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle 5. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling 6. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation 7. Required as a co-chaperone for optimal STUB1/CHIP ubiquitination of NFATC3 (By similarity). Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response 8. Involved in the clearance of misfolded PRDM1/Blimp-1 proteins. Sequesters them in the cytoplasm and promotes their association with SYNV1/HRD1, leading to proteasomal degradation 9. show less
Molecular function (UniProt)i Chaperone, Host cell receptor for virus entry, Receptor
Biological process (UniProt)i Host-virus interaction, Stress response
Ligand (UniProt)i ATP-binding, Nucleotide-binding
Gene summary (Entrez)i 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] show less
PROTEIN INFORMATIONi
Splice variant SwissProt TrEMBL Protein class Gene ontology Length & mass Signal peptide
(predicted)		 Transmembrane regions
(predicted)
HSPA1A-201
ENSP00000364802
ENST00000375651
P0DMV8
[Direct mapping] Heat shock 70 kDa protein 1A
Show all
A8K5I0
[Target identity:100%; Query identity:100%] Epididymis secretory protein Li 103; Epididymis secretory sperm binding protein; HSPA1A; HSPA1B; Heat shock 70kDa protein 1A; Heat shock 70kDa protein 1B; cDNA FLJ75127, highly similar to Homo sapiens heat shock 70kDa protein 1A, mRNA
Show all
Predicted intracellular proteins
   Intracellular proteins predicted by MDM and MDSEC
Disease related genes
Mapped to neXtProt
   neXtProt - Evidence at protein level
Show all
GO:0000122 [negative regulation of transcription by RNA polymerase II]
GO:0000166 [nucleotide binding]
GO:0001618 [virus receptor activity]
GO:0001664 [G protein-coupled receptor binding]
GO:0003714 [transcription corepressor activity]
GO:0003723 [RNA binding]
GO:0005102 [signaling receptor binding]
GO:0005515 [protein binding]
GO:0005524 [ATP binding]
GO:0005576 [extracellular region]
GO:0005634 [nucleus]
GO:0005654 [nucleoplasm]
GO:0005737 [cytoplasm]
GO:0005739 [mitochondrion]
GO:0005783 [endoplasmic reticulum]
GO:0005813 [centrosome]
GO:0005814 [centriole]
GO:0005815 [microtubule organizing center]
GO:0005829 [cytosol]
GO:0005856 [cytoskeleton]
GO:0005886 [plasma membrane]
GO:0005925 [focal adhesion]
GO:0006402 [mRNA catabolic process]
GO:0006457 [protein folding]
GO:0006986 [response to unfolded protein]
GO:0007041 [lysosomal transport]
GO:0008180 [COP9 signalosome]
GO:0008285 [negative regulation of cell population proliferation]
GO:0010628 [positive regulation of gene expression]
GO:0016192 [vesicle-mediated transport]
GO:0016234 [inclusion body]
GO:0016235 [aggresome]
GO:0016607 [nuclear speck]
GO:0016887 [ATP hydrolysis activity]
GO:0019899 [enzyme binding]
GO:0030308 [negative regulation of cell growth]
GO:0030512 [negative regulation of transforming growth factor beta receptor signaling pathway]
GO:0031072 [heat shock protein binding]
GO:0031249 [denatured protein binding]
GO:0031396 [regulation of protein ubiquitination]
GO:0031397 [negative regulation of protein ubiquitination]
GO:0031625 [ubiquitin protein ligase binding]
GO:0031982 [vesicle]
GO:0032436 [positive regulation of proteasomal ubiquitin-dependent protein catabolic process]
GO:0032757 [positive regulation of interleukin-8 production]
GO:0032991 [protein-containing complex]
GO:0033120 [positive regulation of RNA splicing]
GO:0034599 [cellular response to oxidative stress]
GO:0034605 [cellular response to heat]
GO:0034620 [cellular response to unfolded protein]
GO:0042026 [protein refolding]
GO:0042826 [histone deacetylase binding]
GO:0043066 [negative regulation of apoptotic process]
GO:0044183 [protein folding chaperone]
GO:0045296 [cadherin binding]
GO:0045648 [positive regulation of erythrocyte differentiation]
GO:0046034 [ATP metabolic process]
GO:0046718 [viral entry into host cell]
GO:0047485 [protein N-terminus binding]
GO:0048471 [perinuclear region of cytoplasm]
GO:0050821 [protein stabilization]
GO:0051082 [unfolded protein binding]
GO:0051085 [chaperone cofactor-dependent protein refolding]
GO:0051092 [positive regulation of NF-kappaB transcription factor activity]
GO:0051131 [chaperone-mediated protein complex assembly]
GO:0051787 [misfolded protein binding]
GO:0055131 [C3HC4-type RING finger domain binding]
GO:0060548 [negative regulation of cell death]
GO:0070062 [extracellular exosome]
GO:0070370 [cellular heat acclimation]
GO:0070434 [positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway]
GO:0071383 [cellular response to steroid hormone stimulus]
GO:0072562 [blood microparticle]
GO:0090063 [positive regulation of microtubule nucleation]
GO:0090084 [negative regulation of inclusion body assembly]
GO:0097718 [disordered domain specific binding]
GO:0140416 [transcription regulator inhibitor activity]
GO:0140545 [ATP-dependent protein disaggregase activity]
GO:0140662 [ATP-dependent protein folding chaperone]
GO:1901029 [negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway]
GO:1901673 [regulation of mitotic spindle assembly]
GO:1902236 [negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway]
GO:1902380 [positive regulation of endoribonuclease activity]
GO:1903265 [positive regulation of tumor necrosis factor-mediated signaling pathway]
GO:1904813 [ficolin-1-rich granule lumen]
GO:1990904 [ribonucleoprotein complex]
GO:2001240 [negative regulation of extrinsic apoptotic signaling pathway in absence of ligand]
Show all
 641 aa
70.1 kDa 		No 0
HSPA1A-202
ENSP00000477378
ENST00000608703
V9GZ37
[Direct mapping] Heat shock 70 kDa protein 1A
Show all
Predicted intracellular proteins
   Intracellular proteins predicted by MDM and MDSEC
Show all
GO:0000166 [nucleotide binding]
GO:0005524 [ATP binding]
GO:0006457 [protein folding]
GO:0140662 [ATP-dependent protein folding chaperone]
Show all
 476 aa
51.9 kDa 		No 0

Contact

The Project

The Human Protein Atlas

The Human Protein Atlas project is funded
by the Knut & Alice Wallenberg Foundation.


contact@proteinatlas.org