Protein:HSPA1A |
Protein Summary |
 Gene summary |
| Gene name: HSPA1A | ASpdb.0 ID: 3303 | Gene | Gene symbol | HSPA1A | Gene ID | 3303 |
| Gene name | heat shock protein family A (Hsp70) member 1A |
| Synonyms | HEL-S-103|HSP70|HSP70-1|HSP70-1A|HSP70-2|HSP70.1|HSP70.2|HSP70I|HSP72|HSPA1 |
| Cytomap | 6p21.33 |
| Type of gene | protein-coding |
| Description | heat shock 70 kDa protein 1AHSP70-1/HSP70-2HSP70.1/HSP70.2Heat shock 70 kDa protein 1BHeat shock 70 kDa protein 2dnaK-type molecular chaperone HSP70-1epididymis secretory protein Li 103epididymis secretory sperm binding proteinheat shock 70 kDa pr |
| Modification date | 20240411 |
| UniProtAcc | P0DMV8 |
| Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | HSPA1A | GO:0000122 | negative regulation of transcription by RNA polymerase II | 9499401 |
| Gene | HSPA1A | GO:0001664 | G protein-coupled receptor binding | 12150907 |
| Gene | HSPA1A | GO:0003714 | transcription corepressor activity | 9499401 |
| Gene | HSPA1A | GO:0005524 | ATP binding | 23921388 |
| Gene | HSPA1A | GO:0005615 | extracellular space | 17568691|26183779 |
| Gene | HSPA1A | GO:0005634 | nucleus | 10205060|17167422 |
| Gene | HSPA1A | GO:0005737 | cytoplasm | 9553041|11785981|24061851|24790089 |
| Gene | HSPA1A | GO:0005813 | centrosome | 27137183 |
| Gene | HSPA1A | GO:0005814 | centriole | 24061851 |
| Gene | HSPA1A | GO:0005829 | cytosol | 21231916 |
| Gene | HSPA1A | GO:0006402 | mRNA catabolic process | 10205060 |
| Gene | HSPA1A | GO:0006986 | response to unfolded protein | - |
| Gene | HSPA1A | GO:0008180 | COP9 signalosome | 18850735 |
| Gene | HSPA1A | GO:0016234 | inclusion body | 15603737 |
| Gene | HSPA1A | GO:0016235 | aggresome | 15885686 |
| Gene | HSPA1A | GO:0016607 | nuclear speck | 9553041 |
| Gene | HSPA1A | GO:0016887 | ATP hydrolysis activity | 21231916 |
| Gene | HSPA1A | GO:0031396 | regulation of protein ubiquitination | 16809764 |
| Gene | HSPA1A | GO:0031397 | negative regulation of protein ubiquitination | 12150907 |
| Gene | HSPA1A | GO:0032436 | positive regulation of proteasomal ubiquitin-dependent protein catabolic process | 24613385 |
| Gene | HSPA1A | GO:0032991 | protein-containing complex | 23349634 |
| Gene | HSPA1A | GO:0033120 | positive regulation of RNA splicing | 20625543 |
| Gene | HSPA1A | GO:0034605 | cellular response to heat | 9499401|24061851 |
| Gene | HSPA1A | GO:0038177 | death receptor agonist activity | 26183779 |
| Gene | HSPA1A | GO:0042026 | protein refolding | 15603737|21231916 |
| Gene | HSPA1A | GO:0044183 | protein folding chaperone | 15603737 |
| Gene | HSPA1A | GO:0046034 | ATP metabolic process | 23921388 |
| Gene | HSPA1A | GO:0048018 | receptor ligand activity | 17568691 |
| Gene | HSPA1A | GO:0048471 | perinuclear region of cytoplasm | 10205060|15603737 |
| Gene | HSPA1A | GO:0050821 | protein stabilization | 21909508 |
| Gene | HSPA1A | GO:0051082 | unfolded protein binding | 21231916 |
| Gene | HSPA1A | GO:0051131 | chaperone-mediated protein complex assembly | 10811660 |
| Gene | HSPA1A | GO:0051787 | misfolded protein binding | 28842558 |
| Gene | HSPA1A | GO:0090084 | negative regulation of inclusion body assembly | 15603737|21231916 |
| Gene | HSPA1A | GO:0140416 | transcription regulator inhibitor activity | 9499401 |
| Gene | HSPA1A | GO:0140545 | ATP-dependent protein disaggregase activity | 23921388 |
| Gene | HSPA1A | GO:1901029 | negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway | 20625543 |
| Gene | HSPA1A | GO:1902236 | negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway | 12150907|20625543 |
| Gene | HSPA1A | GO:1902380 | positive regulation of endoribonuclease activity | 20625543 |
| Gene | HSPA1A | GO:1990904 | ribonucleoprotein complex | 17289661 |
AS Summary |
| Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| P0DMV8-1 | P0DMV8-1_3a8y_A.pdb | 3A8Y | X-ray | 2.3 | A | 1 | 383 |
| ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| P0DMV8 | HSPA1A | P0DMV8-1 | P0DMV8-2 | 641 | 586 | 96 | 150 | Deletion | none | none | 95 | 95 |
| Multiple sequence alignment of our canonical and alternatively spliced HSPA1A |
| Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of HSPA1A |
| UniProt-id | ENSG | ENST | ENSP |
| P0DMV8-1 | ENSG00000204389.10 | ENST00000375651.7 | ENSP00000364802.5 |
| P0DMV8-1 | ENSG00000235941.5 | ENST00000430065.1 | ENSP00000404524.1 |
| P0DMV8-1 | ENSG00000234475.5 | ENST00000433487.1 | ENSP00000408907.1 |
| P0DMV8-1 | ENSG00000237724.5 | ENST00000441618.1 | ENSP00000406359.1 |
| UniProt-id | NM ID | NP ID |
| P0DMV8-1 | NM_005345.5 | NP_005336.3 |
| P0DMV8-1 | NM_005346.4 | NP_005337.2 |
| Amino acid sequences of our canonical and alternatively spliced HSPA1A |
| accession_id | Protein sequence |
| P0DMV8-1 | MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHW PFQVINDGDKPKVQVSYKGETKAFYPEEISSMVLTKMKEIAEAYLGYPVTNAVITVPAYFNDSQRQATKDAGVIAGLNVLRIINEPTAAA IAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDNRLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERA KRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLN KSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIKRNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMT KDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITNDKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKN ALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHKRKELEQVCNPIISGLYQGAGGPGPGGFGAQGPKGG |
| P0DMV8-2 | MAKAAAIGIDLGTTYSCVGVFQHGKVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVALNPQNTVFDAKRLIGRKFGDPVVQSDMKHW PFQVINDSQRQATKDAGVIAGLNVLRIINEPTAAAIAYGLDRTGKGERNVLIFDLGGGTFDVSILTIDDGIFEVKATAGDTHLGGEDFDN RLVNHFVEEFKRKHKKDISQNKRAVRRLRTACERAKRTLSSSTQASLEIDSLFEGIDFYTSITRARFEELCSDLFRSTLEPVEKALRDAK LDKAQIHDLVLVGGSTRIPKVQKLLQDFFNGRDLNKSINPDEAVAYGAAVQAAILMGDKSENVQDLLLLDVAPLSLGLETAGGVMTALIK RNSTIPTKQTQIFTTYSDNQPGVLIQVYEGERAMTKDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILNVTATDKSTGKANKITITN DKGRLSKEEIERMVQEAEKYKAEDEVQRERVSAKNALESYAFNMKSAVEDEGLKGKISEADKKKVLDKCQEVISWLDANTLAEKDEFEHK |
Protein Functional Features |
| Main function of this protein. (from UniProt) |
| HSPA1A (go to UniProt):P0DMV8 |
| Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| P0DMV8 | Region | 2 | 386 | Note=Nucleotide-binding domain (NBD);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P11142 | Type=Deletion;Start=96;End=150 |
Gene Isoform Structures and Expression Levels for HSPA1A |
| Gene structures of our canonical and alternative spliced genes of HSPA1A * Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
| Expression levels of gene isoforms across GTEx. |
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| Expression levels of gene isoforms across TCGA. |
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Protein Structures |
| PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of P0DMV8-1 |
| 3D view using mol* of P0DMV8-2 |
pLDDT Score Distribution |
| pLDDT score distribution of the predicted protein structures from AlphaFold2 * AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
| pLDDT distribution across the protein length of P0DMV8-1 |
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| pLDDT distribution across the protein length of P0DMV8-2 |
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Ramachandran Plot of Protein Structures |
| Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of P0DMV8-1 |
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| Ramachandran plot of P0DMV8-2 |
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Potential Active Site Information |
| The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| P0DMV8-1 | 1.107 | 220 | 0.894 | 302.869 | 0.343 | 0.858 | 1.145 | 0.307 | 1.721 | 0.178 | 0.611 | 10,12,13,14,15,17,37,41,56,71,147,175,199,201,202, 203,204,205,206,230,231,234,261,264,268,271,272,27 5,302,337,338,339,340,342,343,344,365,366,367,369, 370 |
| P0DMV8-2 | 1.106 | 219 | 0.927 | 317.961 | 0.275 | 0.857 | 1.142 | 0.324 | 1.616 | 0.201 | 0.589 | 10,12,13,14,15,16,17,37,41,56,68,69,71,120,144,146 ,147,148,149,151,175,176,179,213,216,217,220,282,2 83,284,285,287,288,310,311,312,313,314,315 |
Protein Structure and Feature Comparision |
| Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of P0DMV8-1_P0DMV8-1_3a8y_A.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P0DMV8-1_3a8y_A_P0DMV8-2.pdb |
| Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of P0DMV8-1_P0DMV8-2.pdb |
| Protein Feature Comparison of the protein sequendary structures among the protiens. |
| ./stats/secondary_structure/figure/P0DMV8-1_vs_P0DMV8-2.png |
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| Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
| ./stats/relative_asa/P0DMV8-1_vs_P0DMV8-2.png |
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Protein-Protein Interaction |
| Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to HSPA1A |
| Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
Related Diseases to HSPA1A |
| Previous studies relating to the alternative splicing of HSPA1A and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
Clinically important variants in HSPA1A |
| (ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
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