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Search results 1 to 58 out of 58 for Hspa14

0.021s
Type Details Score
Gene
Type: gene
Organism: Homo sapiens
Gene
Type: gene
Organism: Rattus norvegicus
Gene
Type: gene
Organism: Danio rerio
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus musculus
Publication    
First Author: Yang C
Year: 1994
Journal: GenBank Submission
Title: Mus musculus Hsp70-related NST-1 (hsr.1) mRNA, complete cds
Pages: U08215
Publication
First Author: Hudson JW
Year: 2000
Journal: Gene
Title: Sak kinase gene structure and transcriptional regulation.
Volume: 241
Issue: 1
Pages: 65-73
Publication        
First Author: Mouse Genome Informatics Scientfic Curators
Year: 2013
Title: Curated associations of genes in MGI and UniProt sequence records
Publication        
First Author: Mouse Genome Database and National Center for Biotechnology Information Editorial Staff Collaboration
Year: 2001
Title: LocusLink Collaboration
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Mouse Synonym Curation
Publication      
First Author: Helmholtz Zentrum Muenchen GmbH
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Helmholtz Zentrum Muenchen GmbH (Hmgu)
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Chromosome assignment of mouse genes using the Mouse Genome Sequencing Consortium (MGSC) assembly and the ENSEMBL Database
Publication
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
Publication
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
Publication          
First Author: MGD Nomenclature Committee
Year: 1995
Publication      
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
Publication
First Author: Gaudet P
Year: 2011
Journal: Brief Bioinform
Title: Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium.
Volume: 12
Issue: 5
Pages: 449-62
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
Publication
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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
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
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
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
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
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
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 [, ].
Publication
First Author: Huang P
Year: 2005
Journal: Nat Struct Mol Biol
Title: The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1.
Volume: 12
Issue: 6
Pages: 497-504
Publication
First Author: Lee K
Year: 2016
Journal: Nat Struct Mol Biol
Title: Dual interaction of the Hsp70 J-protein cochaperone Zuotin with the 40S and 60S ribosomal subunits.
Volume: 23
Issue: 11
Pages: 1003-1010
Publication
First Author: Conz C
Year: 2007
Journal: J Biol Chem
Title: Functional characterization of the atypical Hsp70 subunit of yeast ribosome-associated complex.
Volume: 282
Issue: 47
Pages: 33977-84
Protein Domain
Type: Family
Description: Ribosome-associated J protein-Hsp70 chaperones promote nascent-polypeptide folding and normal translational fidelity. This entry includes J protein DnaJC2 from humans, Zuo1 from budding yeasts, and their homologues from other animals, fungi and plants []. DnaJC2 stimulates the ATPase activity of Hsp70 (Ssb1/2 in yeast) []. Zuo1 forms a stable heterodimeric complex termed ribosome-associated complex (RAC) with Ssz1 (an atypical Hsp70 family member, known as HspA14 in humans), this complex is then anchored to the ribosome via its Zuo1 subunit []. These three proteins (Ssb, Zuo1 and Ssz1) referred to as a chaperone triad lay a role together in folding of nascent polypeptides []. Moreover, Zuo1 has been shown to interact with the 40S and 60S ribosomal subunits in budding yeasts [].
Protein
Organism: Mus musculus
Length: 509  
Fragment?: false
Publication
First Author: Kaneko Y
Year: 1997
Journal: Gene
Title: Cloning of apg-2 encoding a novel member of heat shock protein 110 family.
Volume: 189
Issue: 1
Pages: 19-24
Publication
First Author: Held T
Year: 2011
Journal: Reproduction
Title: Heat-shock protein HSPA4 is required for progression of spermatogenesis.
Volume: 142
Issue: 1
Pages: 133-44
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
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
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.
Protein
Organism: Mus musculus
Length: 841  
Fragment?: false
Protein
Organism: Mus musculus
Length: 206  
Fragment?: true
Protein
Organism: Mus musculus
Length: 841  
Fragment?: false
Protein
Organism: Mus musculus
Length: 930  
Fragment?: true
Protein
Organism: Mus musculus
Length: 284  
Fragment?: true
Protein
Organism: Mus musculus
Length: 324  
Fragment?: true
Protein
Organism: Mus musculus
Length: 256  
Fragment?: true
Protein
Organism: Mus musculus
Length: 191  
Fragment?: false
Protein
Organism: Mus musculus
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
Protein
Organism: Mus musculus
Length: 621  
Fragment?: false
Protein
Organism: Mus musculus
Length: 619  
Fragment?: false
Protein
Organism: Mus musculus
Length: 547  
Fragment?: false