Type |
Details |
Score |
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2009 |
Journal: |
Database Download |
Title: |
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform |
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•
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•
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•
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Publication |
First Author: |
Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI) |
Year: |
2010 |
Journal: |
Database Download |
Title: |
Consensus CDS project |
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•
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•
•
•
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Publication |
First Author: |
Mouse Genome Informatics Group |
Year: |
2003 |
Journal: |
Database Procedure |
Title: |
Automatic Encodes (AutoE) Reference |
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•
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•
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Publication |
First Author: |
Bairoch A |
Year: |
1999 |
Journal: |
Database Release |
Title: |
SWISS-PROT Annotated protein sequence database |
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Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2005 |
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Title: |
Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations |
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•
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Publication |
First Author: |
Mouse Genome Informatics |
Year: |
2010 |
Journal: |
Database Release |
Title: |
Protein Ontology Association Load. |
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•
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Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and loading genome assembly coordinates from NCBI annotations |
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•
•
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•
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Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2009 |
Journal: |
Database Download |
Title: |
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform |
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•
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•
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Publication |
First Author: |
Yang Y |
Year: |
2022 |
Journal: |
Biochim Biophys Acta Mol Basis Dis |
Title: |
SIRT1 attenuates neuroinflammation by deacetylating HSPA4 in a mouse model of Parkinson's disease. |
Volume: |
1868 |
Issue: |
5 |
Pages: |
166365 |
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•
•
•
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•
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HT Experiment |
Series Id: |
GSE32885 |
Experiment Type: |
transcription profiling by array |
Study Type: |
WT vs. Mutant |
Source: |
ArrayExpress |
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•
•
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•
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Publication |
First Author: |
Kang CM |
Year: |
2002 |
Journal: |
Radiat Res |
Title: |
Hspa4 (HSP70) is involved in the radioadaptive response: results from mouse splenocytes. |
Volume: |
157 |
Issue: |
6 |
Pages: |
650-5 |
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•
•
•
•
•
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Publication |
First Author: |
Wu CY |
Year: |
2011 |
Journal: |
J Biomed Sci |
Title: |
Induction of HSPA4 and HSPA14 by NBS1 overexpression contributes to NBS1-induced in vitro metastatic and transformation activity. |
Volume: |
18 |
|
Pages: |
1 |
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•
•
•
•
•
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Publication |
First Author: |
Ferlin A |
Year: |
2010 |
Journal: |
J Urol |
Title: |
Heat shock protein and heat shock factor expression in sperm: relation to oligozoospermia and varicocele. |
Volume: |
183 |
Issue: |
3 |
Pages: |
1248-52 |
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•
•
•
•
•
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Protein Domain |
Type: |
Domain |
Description: |
Human HSPA4 (also known as 70kDa heat shock protein 4, APG-2, HS24/P52, hsp70 RY, and HSPH2) responds to acidic pH stress, is involved in the radioadaptive response, is required for normal spermatogenesis and is overexpressed in hepatocellular carcinoma [, , ]. It participates in a pathway along with NBS1 (Nijmegen breakage syndrome 1, also known as p85 or nibrin), heat shock transcription factor 4b (HDF4b), and HSPA14 (belonging to a different HSP70 subfamily) that induces tumor migration, invasion, and transformation []. HSPA4 expression in sperm was increased in men with oligozoospermia, especially in those with varicocele []. HSPA4 belongs to the 105/110kDa heat shock protein (HSP105/110) subfamily of the HSP70-like family []. HSP105/110s are believed to function generally as co-chaperones of HSP70 chaperones, acting as nucleotide exchange factors (NEFs), to remove ADP from their HSP70 chaperone partners during the ATP hydrolysis cycle. HSP70 chaperones assist in protein folding and assembly, and can direct incompetent 'client' proteins towards degradation. Like HSP70 chaperones, HSP105/110s have an N-terminal nucleotide-binding domain (NBD) and a C-terminal substrate-binding domain (SBD) [].This entry represents the N-terminal nucleotide-binding domain of HSPA4. |
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Publication |
First Author: |
Gu Y |
Year: |
2019 |
Journal: |
Nat Med |
Title: |
Tumor-educated B cells selectively promote breast cancer lymph node metastasis by HSPA4-targeting IgG. |
Volume: |
25 |
Issue: |
2 |
Pages: |
312-322 |
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•
•
•
•
|
Publication |
First Author: |
Otto H |
Year: |
2005 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
The chaperones MPP11 and Hsp70L1 form the mammalian ribosome-associated complex. |
Volume: |
102 |
Issue: |
29 |
Pages: |
10064-9 |
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•
•
•
•
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Publication |
First Author: |
Wan T |
Year: |
2004 |
Journal: |
Blood |
Title: |
Novel heat shock protein Hsp70L1 activates dendritic cells and acts as a Th1 polarizing adjuvant. |
Volume: |
103 |
Issue: |
5 |
Pages: |
1747-54 |
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•
•
•
•
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Publication |
First Author: |
Fang H |
Year: |
2011 |
Journal: |
J Biol Chem |
Title: |
Toll-like receptor 4 (TLR4) is essential for Hsp70-like protein 1 (HSP70L1) to activate dendritic cells and induce Th1 response. |
Volume: |
286 |
Issue: |
35 |
Pages: |
30393-400 |
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•
•
•
•
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Protein Domain |
Type: |
Domain |
Description: |
Human HSPA14 (also known as 70kDa heat shock protein 14 or HSP70L1), is ribosome-associated and belongs to the heat shock protein 70 (HSP70) family of chaperones that assist in protein folding and assembly, and can direct incompetent 'client' proteins towards degradation. Typically, HSP70s have a nucleotide-binding domain (NBD) and a substrate-binding domain (SBD). The nucleotide sits in a deep cleft formed between the two lobes of the NBD. The two subdomains of each lobe change conformation between ATP-bound, ADP-bound, and nucleotide-free states. ATP binding opens up the substrate-binding site; substrate-binding increases the rate of ATP hydrolysis. HSP70 chaperone activity is regulated by various co-chaperones: J-domain proteins and nucleotide exchange factors (NEFs). HSPA14 interacts with the J-protein MPP11 to form the mammalian ribosome-associated complex (mRAC) []. HSPA14 participates in a pathway along with Nijmegen breakage syndrome 1 (NBS1, also known as p85 or nibrin), heat shock transcription factor 4b (HSF4b), and HSPA4 (belonging to a different subfamily), that induces tumor migration, invasion, and transformation []. HSPA14 is a potent T helper cell (Th1) polarizing adjuvant that contributes to antitumor immune responses [, ]. |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
841
 |
Fragment?: |
false |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
841
 |
Fragment?: |
false |
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•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
930
 |
Fragment?: |
true |
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•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
842
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Mayer MP |
Year: |
2005 |
Journal: |
Cell Mol Life Sci |
Title: |
Hsp70 chaperones: cellular functions and molecular mechanism. |
Volume: |
62 |
Issue: |
6 |
Pages: |
670-84 |
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•
•
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
509
 |
Fragment?: |
false |
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•
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