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HSPH1 (heat shock 105kDa/110kDa protein 1)

Identity

Other namesHSP105alpha
HSP105beta
HSP110
HSP105
KIAA0201
NY-CO-25
HGNC (Hugo) HSPH1
LocusID (NCBI) 10808
Location 13q12.3
Location_base_pair Starts at 31710763 and ends at 31736117 bp from pter ( according to hg19-Feb_2009)  [Mapping]

DNA/RNA

 
  Genomic organization of the mouse HSP105 gene. The linear map of the exon-intron structure is shown schematically. Exons are represented as numbered boxes. Two alternative splicing patterns gave rise to HSP105alpha and HSP105beta transcripts. ATG and TAG indicate the positions of initiation and termination codons, respectively. (DDBJ/EMBL/GenBank DNA databases with accession Nos. AB005267-AB005282).
Description 18 exons on 22 kb
Transcription Hsp105alpha is transcribed constitutively and also by a variety of stresses. 4 kb mRNA Hsp105beta is an alternative spliced isoform only produced during heat shock at 42 degree.

Protein

 
  Shematic structures of HSP105alpha and HSP105beta proteins. Shaded box represents the spliced out region of HSP105alpha which is lacking in HSP105beta.
Description Hsp105alpha: 858 amino acids, 105 kDa; contains an ATP binding domain (residues 1-383), b-sheet domain (residues 384-511), loop domain (residues 512-607) and alpha-helix domain (residues 608-858). Hsp105beta: 814 amino acids, 90 kDa; contains an ATP binding domain (residues 1-383), b-sheet domain (residues 384-511), loop domain (residues 512-563) and alpha-helix domain (residues 564-814).
Expression wide, highly expressed in brain
Localisation Hsp105alpha, cytoplasmic; Hsp105beta, nuclear
Function Hsp105alpha and Hsp105beta suppress the aggregation of denatured proteins; function as a substitute for Hsp70 family proteins to suppress the aggregation of denatured proteins in cells under severe stress; regulate substrate binding cycle of Hsp70/Hsc70 by inhibiting the ATPase activity of Hsp70/Hsc70.
Homology With mouse apg-1, mouse apg-2, sea urchin egg receptor, C. elegans 86.9-kDa protein, A. thaliana hsp91 and S. cerevisiae SSE1, human hsp70 and human hsc70.

Implicated in

Entity Lung cancers
Prognosis Poor
Oncogenesis Low expression of hsp105 was identified as predictors of survival in lung adenocarcinomas.
  
Entity Colorectal cancers
Prognosis Survival is not much more than 50% after 5 years.
Oncogenesis Overexpression of hsp105 is a late event in the colorectal adenoma-carcinoma sequence.
  

External links

Nomenclature
HGNC (Hugo)HSPH1   16969
Entrez_Gene (NCBI)HSPH1  10808  heat shock 105kDa/110kDa protein 1
Cards
AtlasHSPH1ID40891ch13q12
GeneCards (Weizmann)HSPH1
Ensembl (Hinxton)ENSG00000120694 [Gene_View]  chr13:31710763-31736117 [Contig_View]  HSPH1 [Vega]
AceView (NCBI)HSPH1
Genatlas (Paris)HSPH1
euGene (Indiana)10808
SOURCE (Stanford)NM_006644
Genomic and cartography
GoldenPath (UCSC)HSPH1  -  13q12.3   chr13:31710763-31736117 -  13q12.3   [Description]    (hg19-Feb_2009)
EnsemblHSPH1 - 13q12.3 [CytoView]
Mapping of homologs : NCBIHSPH1 [Mapview]
OMIM610703   
Gene and transcription
Genbank (Entrez)AB003333 AB003334 AF039695 AK293955 AK302294
RefSeq transcript (SRS)NM_006644
RefSeq transcript (Entrez)NM_006644
RefSeq genomic (SRS)AC_000145 NC_000013 NT_024524 NW_001838072
RefSeq genomic (Entrez)AC_000145 NC_000013 NT_024524 NW_001838072
Consensus coding sequences : CCDS (NCBI)HSPH1
Cluster EST : UnigeneHs.706314 [ SRS ] Hs.706314 [ NCBI ]
Alternative Splicing : Fast-db (Paris)2467
Alternative Splicing GalleryENSG00000120694
Gene ExpressionHSPH1 [ NCBI-GEO ]   HSPH1 [ EBI - ARRAY_EXPRESS ]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ92598 (SRS) Q92598 (Uniprot)
With graphics : InterProQ92598
Splice isoforms : SwissVarQ92598(Swissvar)
Domaine pattern : Prosite (SRS)HSP70_1 (PS00297)    HSP70_2 (PS00329)    HSP70_3 (PS01036)   
Domaine pattern : Prosite (Expaxy)HSP70_1 (PS00297)    HSP70_2 (PS00329)    HSP70_3 (PS01036)   
Domains : Interpro (SRS)Heat_shock_70_CS    Hsp70    Hsp_70   
Domains : Interpro (EBI)Heat_shock_70_CS    Hsp70    Hsp_70   
Related proteins : CluSTrQ92598
Domain families : Pfam (SRS)HSP70 (PF00012)   
Domain families : Pfam (Sanger)HSP70 (PF00012)   
Domain families : Pfam (NCBI)pfam00012   
Blocks (Seattle)Q92598
Human Protein AtlasENSG00000120694
HPRD09990
IPIIPI00939163   IPI00218993   IPI00513743   IPI00908988   IPI00514983   IPI00910755   IPI00910341   IPI00794417   
dbDEPCIPI00218993   
Protein Interaction databases
DIP (DOE-UCLA)Q92598
IntAct (EBI)Q92598
FunCoupENSG00000120694
REACTOMEHSPH1
BioGRIDHSPH1
InParanoidQ92598
Interologous Interaction database Q92598
Polymorphism : SNP, mutations, diseases
SNP Single Nucleotide Polymorphism (NCBI)HSPH1
SNP (GeneSNP Utah)HSPH1
SNP : HGBaseHSPH1
Genetic variants : HAPMAPHSPH1
Somatic Mutations in Cancer : COSMICHSPH1 
CONAN: Copy Number AnalysisHSPH1 
Mutations and Diseases : HGMDHSPH1
OMIM610703   
GENETests610703   
Disease Genetic AssociationHSPH1
Huge Navigator HSPH1 [HugePedia]  HSPH1 [HugeCancerGEM]
Genomic VariantsHSPH1
snp3D : Map Gene to Disease10808
General knowledge
Homologs : HomoloGeneHSPH1
Homology/Alignments : Family Browser (UCSC)HSPH1
Phylogenetic Trees/Animal Genes : TreeFamHSPH1
Chemical/Protein Interactions : CTD10808
Chemical/Pharm GKB GenePA134869917
Clinical trialHSPH1
Cancer Resource (Charite)ENSG00000120694
Ontology : AmiGOnucleotide binding  ATP binding  extracellular region  nucleus  nucleolus  cytoplasm  microtubule  response to stress  response to unfolded protein  alpha-tubulin binding  positive regulation of MHC class I biosynthetic process  chaperone mediated protein folding requiring cofactor  positive regulation of NK T cell activation  
Ontology : EGO-EBInucleotide binding  ATP binding  extracellular region  nucleus  nucleolus  cytoplasm  microtubule  response to stress  response to unfolded protein  alpha-tubulin binding  positive regulation of MHC class I biosynthetic process  chaperone mediated protein folding requiring cofactor  positive regulation of NK T cell activation  
Other databases
Probes
Probes : ImagenesHSPH1 Related clones (RZPD - Berlin)
Litterature
PubMed39 Pubmed reference(s) in Entrez
PubGeneHSPH1
iHOPHSPH1

Bibliography

Cloning and expression of murine high molecular mass heat shock proteins, HSP105.
Yasuda K, Nakai A, Hatayama T, Nagata K
The Journal of biological chemistry. 1995 ; 270 (50) : 29718-29723.
PMID 8530361
 
Molecular cloning, expression and localization of human 105 kDa heat shock protein, hsp105.
Ishihara K, Yasuda K, Hatayama T
Biochimica et biophysica acta. 1999 ; 1444 (1) : 138-142.
PMID 9931472
 
Genomic cloning and promoter analysis of the mouse 105-kDa heat shock protein (HSP105) gene.
Yasuda K, Ishihara K, Nakashima K, Hatayama T
Biochemical and biophysical research communications. 1999 ; 256 (1) : 75-80.
PMID 10066425
 
Gene cloning of immunogenic antigens overexpressed in pancreatic cancer.
Nakatsura T, Senju S, Yamada K, Jotsuka T, Ogawa M, Nishimura Y
Biochemical and biophysical research communications. 2001 ; 281 (4) : 936-944.
PMID 11237751
 
Gene cloning of immunogenic antigens overexpressed in pancreatic cancer.
Nakatsura T, Senju S, Yamada K, Jotsuka T, Ogawa M, Nishimura Y
Biochemical and biophysical research communications. 2001 ; 281 (4) : 936-944.
PMID 11237751
 
Heat shock protein 105 is overexpressed in a variety of human tumors.
Kai M, Nakatsura T, Egami H, Senju S, Nishimura Y, Ogawa M
Oncology reports. 2003 ; 10 (6) : 1777-1782.
PMID 14534695
 
Hsp105 but not Hsp70 family proteins suppress the aggregation of heat-denatured protein in the presence of ADP.
Yamagishi N, Ishihara K, Saito Y, Hatayama T
FEBS letters. 2003 ; 555 (2) : 390-396.
PMID 14644449
 
Hsp105 but not Hsp70 family proteins suppress the aggregation of heat-denatured protein in the presence of ADP.
Yamagishi N, Ishihara K, Saito Y, Hatayama T
FEBS letters. 2003 ; 555 (2) : 390-396.
PMID 14644449
 
DNA vaccination of HSP105 leads to tumor rejection of colorectal cancer and melanoma in mice through activation of both CD4 T cells and CD8 T cells.
Miyazaki M, Nakatsura T, Yokomine K, Senju S, Monji M, Hosaka S, Komori H, Yoshitake Y, Motomura Y, Minohara M, Kubo T, Ishihara K, Hatayama T, Ogawa M, Nishimura Y
Cancer science. 2005 ; 96 (10) : 695-705.
PMID 16232202
 
Hsp105 family proteins suppress staurosporine-induced apoptosis by inhibiting the translocation of Bax to mitochondria in HeLa cells.
Yamagishi N, Ishihara K, Saito Y, Hatayama T
Experimental cell research. 2006 ; 312 (17) : 3215-3223.
PMID 16857185
 
Synthetic small interfering RNA targeting heat shock protein 105 induces apoptosis of various cancer cells both in vitro and in vivo.
Hosaka S, Nakatsura T, Tsukamoto H, Hatayama T, Baba H, Nishimura Y
Cancer science. 2006 ; 97 (7) : 623-632.
PMID 16827803
 
Heat shock protein 105 is overexpressed in squamous cell carcinoma and extramammary Paget disease but not in basal cell carcinoma.
Muchemwa FC, Nakatsura T, Ihn H, Kageshita T
The British journal of dermatology. 2006 ; 155 (3) : 582-585.
PMID 16911285
 
alpha"%5BTI%5D%20OR%20"HSP105beta"%5BTI%5D%20OR%20"HSP110"%5BTI%5D%20OR%20"HSP105"%5BTI%5D%20OR%20"KIAA0201"%5BTI%5D%20OR%20"NY-CO-25"%5BTI%5D%20)%20AND%20REVIEW%5BPT%5D%20AND%20ENGLISH%5BLA%5D&field=titl&dispmax=50>REVIEW articlesautomatic search in PubMed
alpha"%5BTI%5D%20OR%20"HSP105beta"%5BTI%5D%20OR%20"HSP110"%5BTI%5D%20OR%20"HSP105"%5BTI%5D%20OR%20"KIAA0201"%5BTI%5D%20OR%20"NY-CO-25"%5BTI%5D%20)%20AND%20(2009%5BDP%5D%20OR%202010%5BDP%5D%20OR%202011%5BDP%5D)&field=titl&dispmax=50>Last year publicationsautomatic search in PubMed

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Contributor(s)

Written02-2007Takumi Hatayama, Nobuyuki Yamagishi

Citation

This paper should be referenced as such :
Hatayama T, Yamagishi N . HSPH1 (heat shock 105kDa/110kDa protein 1). Atlas Genet Cytogenet Oncol Haematol. February 2007 .
URL : http://AtlasGeneticsOncology.org/Genes/HSPH1ID40891ch13q12.html

This paper is referenced by INIST as such :
http://documents.irevues.inist.fr/bitstream/2042/38439/1/02-2007-HSPH1ID40891ch13q12.pdf   [ Bibliographic record ]

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indexed on : Sat Apr 28 15:11:09 CEST 2012

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