	FusionGeneSummary
	FusionProtFeature
	FusionGeneSequence
	FusionGenePPI
	RelatedDrugs
	RelatedDiseases

Fusion gene ID: 16871

FusionGeneSummary for HSPA8_HSPA8

Fusion gene summary

Fusion gene information	Fusion gene name: HSPA8_HSPA8
	Fusion gene ID: 16871
		Hgene	Tgene
	Gene symbol	HSPA8	HSPA8
	Gene ID	3312	3312
	Gene name	heat shock protein family A (Hsp70) member 8	heat shock protein family A (Hsp70) member 8
	Synonyms	HEL-33\|HEL-S-72p\|HSC54\|HSC70\|HSC71\|HSP71\|HSP73\|HSPA10\|LAP-1\|LAP1\|NIP71	HEL-33\|HEL-S-72p\|HSC54\|HSC70\|HSC71\|HSP71\|HSP73\|HSPA10\|LAP-1\|LAP1\|NIP71
	Cytomap	11q24.1	11q24.1
	Type of gene	protein-coding	protein-coding
	Description	heat shock cognate 71 kDa proteinLPS-associated protein 1N-myristoyltransferase inhibitor protein 71constitutive heat shock protein 70epididymis luminal protein 33epididymis secretory sperm binding protein Li 72pheat shock 70kDa protein 8heat shock	heat shock cognate 71 kDa proteinLPS-associated protein 1N-myristoyltransferase inhibitor protein 71constitutive heat shock protein 70epididymis luminal protein 33epididymis secretory sperm binding protein Li 72pheat shock 70kDa protein 8heat shock
	Modification date	20180527	20180527
	UniProtAcc	P11142	P11142
	Ensembl transtripts involved in fusion gene	ENST00000532636, ENST00000533540, ENST00000453788, ENST00000534624, ENST00000227378, ENST00000534319, ENST00000526110, ENST00000526862,	ENST00000532636, ENST00000533540, ENST00000453788, ENST00000534624, ENST00000227378, ENST00000534319, ENST00000526110, ENST00000526862,
Fusion gene scores	* DoF score	6 X 6 X 2=72	13 X 14 X 4=728
	# samples	9	16
	** MAII score	log2(9/72*10)=0.321928094887362 effective Gene in Pan-Cancer Fusion Genes (eGinPCFGs). DoF>8 and MAII>0	log2(16/728*10)=-2.18586654531133 possibly effective Gene in Pan-Cancer Fusion Genes (peGinPCFGs). DoF>8 and MAII<0
Context	PubMed: HSPA8 [Title/Abstract] AND HSPA8 [Title/Abstract] AND fusion [Title/Abstract]
Functional or gene categories assigned by FusionGDB annotation

* DoF score (Degree of Frequency) = # partners X # break points X # cancer types
** MAII score (Major Active Isofusion Index) = log2(# samples/DoF score*10)

Gene ontology of each fusion partner gene with evidence of Inferred from Direct Assay (IDA) from Entrez

Partner	Gene	GO ID	GO term	PubMed ID
Hgene	HSPA8	GO:0042026	protein refolding	21231916\|25719862
Hgene	HSPA8	GO:0045892	negative regulation of transcription, DNA-templated	10722728
Hgene	HSPA8	GO:0046034	ATP metabolic process	23921388
Hgene	HSPA8	GO:1902904	negative regulation of supramolecular fiber organization	23921388
Tgene	HSPA8	GO:0042026	protein refolding	21231916\|25719862
Tgene	HSPA8	GO:0045892	negative regulation of transcription, DNA-templated	10722728
Tgene	HSPA8	GO:0046034	ATP metabolic process	23921388
Tgene	HSPA8	GO:1902904	negative regulation of supramolecular fiber organization	23921388

Fusion gene information from three resources
(ChiTars (NAR, 2018), tumorfusions (NAR, 2018), Gao et al. (Cell, 2018))
* All genome coordinats were lifted-over on hg19.
* Click on the break point to see the gene structure around the break point region using the UCSC Genome Browser.

Data type	Source	Cancer type	Sample	Hgene	Hchr	Hbp	Hstrand	Tgene	Tchr	Tbp	Tstrand
ChiTaRS3.1			BE812526	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
ChiTaRS3.1			BF885577	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
ChiTaRS3.1			BF082086	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
ChiTaRS3.1			BF082156	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+

* LD: Li Ding group's fusion gene list
RV: Roel Verhaak group's fusion gene list
ChiTaRs fusion database

Open reading frame (ORF) analsis of fusion genes based on Ensembl gene isoform structure.
* Click on the break point to see the gene structure around the break point region using the UCSC Genome Browser.

ORF	Henst	Tenst	Hgene	Hchr	Hbp	Hstrand	Tgene	Tchr	Tbp	Tstrand
intron-3CDS	ENST00000532636	ENST00000532636	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-3CDS	ENST00000532636	ENST00000533540	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000532636	ENST00000453788	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000532636	ENST00000534624	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000532636	ENST00000227378	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000532636	ENST00000534319	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000532636	ENST00000526110	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000532636	ENST00000526862	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-3CDS	ENST00000533540	ENST00000532636	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-3CDS	ENST00000533540	ENST00000533540	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000533540	ENST00000453788	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000533540	ENST00000534624	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000533540	ENST00000227378	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000533540	ENST00000534319	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000533540	ENST00000526110	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000533540	ENST00000526862	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-3CDS	ENST00000453788	ENST00000532636	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-3CDS	ENST00000453788	ENST00000533540	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000453788	ENST00000453788	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000453788	ENST00000534624	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000453788	ENST00000227378	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000453788	ENST00000534319	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000453788	ENST00000526110	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000453788	ENST00000526862	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-3CDS	ENST00000534624	ENST00000532636	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-3CDS	ENST00000534624	ENST00000533540	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000534624	ENST00000453788	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000534624	ENST00000534624	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000534624	ENST00000227378	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000534624	ENST00000534319	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000534624	ENST00000526110	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000534624	ENST00000526862	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-3CDS	ENST00000227378	ENST00000532636	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-3CDS	ENST00000227378	ENST00000533540	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000227378	ENST00000453788	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000227378	ENST00000534624	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000227378	ENST00000227378	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000227378	ENST00000534319	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000227378	ENST00000526110	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000227378	ENST00000526862	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-3CDS	ENST00000534319	ENST00000532636	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-3CDS	ENST00000534319	ENST00000533540	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000534319	ENST00000453788	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000534319	ENST00000534624	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000534319	ENST00000227378	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000534319	ENST00000534319	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000534319	ENST00000526110	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000534319	ENST00000526862	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-3CDS	ENST00000526110	ENST00000532636	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-3CDS	ENST00000526110	ENST00000533540	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000526110	ENST00000453788	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000526110	ENST00000534624	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000526110	ENST00000227378	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000526110	ENST00000534319	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000526110	ENST00000526110	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000526110	ENST00000526862	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-3CDS	ENST00000526862	ENST00000532636	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-3CDS	ENST00000526862	ENST00000533540	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000526862	ENST00000453788	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000526862	ENST00000534624	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000526862	ENST00000227378	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000526862	ENST00000534319	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000526862	ENST00000526110	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-intron	ENST00000526862	ENST00000526862	HSPA8	chr11	122929465	+	HSPA8	chr11	122928553	+
intron-3CDS	ENST00000532636	ENST00000532636	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000532636	ENST00000533540	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000532636	ENST00000453788	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000532636	ENST00000534624	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000532636	ENST00000227378	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000532636	ENST00000534319	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000532636	ENST00000526110	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000532636	ENST00000526862	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-3CDS	ENST00000533540	ENST00000532636	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000533540	ENST00000533540	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000533540	ENST00000453788	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000533540	ENST00000534624	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000533540	ENST00000227378	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000533540	ENST00000534319	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000533540	ENST00000526110	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000533540	ENST00000526862	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-3CDS	ENST00000453788	ENST00000532636	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000453788	ENST00000533540	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000453788	ENST00000453788	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000453788	ENST00000534624	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000453788	ENST00000227378	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000453788	ENST00000534319	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000453788	ENST00000526110	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000453788	ENST00000526862	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-3CDS	ENST00000534624	ENST00000532636	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000534624	ENST00000533540	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000534624	ENST00000453788	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000534624	ENST00000534624	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000534624	ENST00000227378	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000534624	ENST00000534319	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000534624	ENST00000526110	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000534624	ENST00000526862	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-3CDS	ENST00000227378	ENST00000532636	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000227378	ENST00000533540	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000227378	ENST00000453788	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000227378	ENST00000534624	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000227378	ENST00000227378	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000227378	ENST00000534319	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000227378	ENST00000526110	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000227378	ENST00000526862	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-3CDS	ENST00000534319	ENST00000532636	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000534319	ENST00000533540	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000534319	ENST00000453788	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000534319	ENST00000534624	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000534319	ENST00000227378	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000534319	ENST00000534319	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000534319	ENST00000526110	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000534319	ENST00000526862	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-3CDS	ENST00000526110	ENST00000532636	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000526110	ENST00000533540	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000526110	ENST00000453788	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000526110	ENST00000534624	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000526110	ENST00000227378	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000526110	ENST00000534319	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000526110	ENST00000526110	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000526110	ENST00000526862	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-3CDS	ENST00000526862	ENST00000532636	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000526862	ENST00000533540	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000526862	ENST00000453788	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000526862	ENST00000534624	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000526862	ENST00000227378	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000526862	ENST00000534319	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000526862	ENST00000526110	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-
intron-intron	ENST00000526862	ENST00000526862	HSPA8	chr11	122929149	+	HSPA8	chr11	122930588	-

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FusionProtFeatures for HSPA8_HSPA8

Main function of each fusion partner protein. (from UniProt)

Hgene	Tgene
HSPA8 P11142	HSPA8 P11142
Molecular chaperone implicated in a wide variety ofcellular processes, including protection of the proteome fromstress, folding and transport of newly synthesized polypeptides,activation of proteolysis of misfolded proteins and the formationand dissociation of protein complexes. Plays a pivotal role in theprotein quality control system, ensuring the correct folding ofproteins, the re-folding of misfolded proteins and controlling thetargeting of proteins for subsequent degradation (PubMed:21150129,PubMed:21148293, PubMed:24732912, PubMed:27916661,PubMed:23018488). This is achieved through cycles of ATP binding,ATP hydrolysis and ADP release, mediated by co-chaperones(PubMed:21150129, PubMed:21148293, PubMed:24732912,PubMed:27916661, PubMed:23018488). The co-chaperones have beenshown to not only regulate different steps of the ATPase cycle ofHSP70, but they also have an individual specificity such that oneco-chaperone may promote folding of a substrate while another maypromote degradation (PubMed:21150129, PubMed:21148293,PubMed:24732912, PubMed:27916661, PubMed:23018488). The affinityof HSP70 for polypeptides is regulated by its nucleotide boundstate. In the ATP-bound form, it has a low affinity for substrateproteins. However, upon hydrolysis of the ATP to ADP, it undergoesa conformational change that increases its affinity for substrateproteins. HSP70 goes through repeated cycles of ATP hydrolysis andnucleotide exchange, which permits cycles of substrate binding andrelease. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis byHSP70), 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 TPRdomain chaperones such as HOPX and STUB1 (PubMed:24318877,PubMed:27474739, PubMed:24121476, PubMed:26865365). Acts as arepressor of transcriptional activation. Inhibits thetranscriptional coactivator activity of CITED1 on Smad-mediatedtranscription. Component of the PRP19-CDC5L complex that forms anintegral part of the spliceosome and is required for activatingpre-mRNA splicing. May have a scaffolding role in the spliceosomeassembly as it contacts all other components of the core complex.Binds bacterial lipopolysaccharide (LPS) and mediates LPS-inducedinflammatory response, including TNF secretion by monocytes(PubMed:10722728, PubMed:11276205). Participates in the ER-associated degradation (ERAD) quality control pathway inconjunction with J domain-containing co-chaperones and the E3ligase STUB1 (PubMed:23990462). {ECO:0000269\|PubMed:10722728,ECO:0000269\|PubMed:11276205, ECO:0000269\|PubMed:21148293,ECO:0000269\|PubMed:21150129, ECO:0000269\|PubMed:23018488,ECO:0000269\|PubMed:23990462, ECO:0000269\|PubMed:24318877,ECO:0000269\|PubMed:24732912, ECO:0000269\|PubMed:27474739,ECO:0000269\|PubMed:27916661, ECO:0000303\|PubMed:24121476,ECO:0000303\|PubMed:26865365}.	Molecular chaperone implicated in a wide variety ofcellular processes, including protection of the proteome fromstress, folding and transport of newly synthesized polypeptides,activation of proteolysis of misfolded proteins and the formationand dissociation of protein complexes. Plays a pivotal role in theprotein quality control system, ensuring the correct folding ofproteins, the re-folding of misfolded proteins and controlling thetargeting of proteins for subsequent degradation (PubMed:21150129,PubMed:21148293, PubMed:24732912, PubMed:27916661,PubMed:23018488). This is achieved through cycles of ATP binding,ATP hydrolysis and ADP release, mediated by co-chaperones(PubMed:21150129, PubMed:21148293, PubMed:24732912,PubMed:27916661, PubMed:23018488). The co-chaperones have beenshown to not only regulate different steps of the ATPase cycle ofHSP70, but they also have an individual specificity such that oneco-chaperone may promote folding of a substrate while another maypromote degradation (PubMed:21150129, PubMed:21148293,PubMed:24732912, PubMed:27916661, PubMed:23018488). The affinityof HSP70 for polypeptides is regulated by its nucleotide boundstate. In the ATP-bound form, it has a low affinity for substrateproteins. However, upon hydrolysis of the ATP to ADP, it undergoesa conformational change that increases its affinity for substrateproteins. HSP70 goes through repeated cycles of ATP hydrolysis andnucleotide exchange, which permits cycles of substrate binding andrelease. The HSP70-associated co-chaperones are of three types: J-domain co-chaperones HSP40s (stimulate ATPase hydrolysis byHSP70), 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 TPRdomain chaperones such as HOPX and STUB1 (PubMed:24318877,PubMed:27474739, PubMed:24121476, PubMed:26865365). Acts as arepressor of transcriptional activation. Inhibits thetranscriptional coactivator activity of CITED1 on Smad-mediatedtranscription. Component of the PRP19-CDC5L complex that forms anintegral part of the spliceosome and is required for activatingpre-mRNA splicing. May have a scaffolding role in the spliceosomeassembly as it contacts all other components of the core complex.Binds bacterial lipopolysaccharide (LPS) and mediates LPS-inducedinflammatory response, including TNF secretion by monocytes(PubMed:10722728, PubMed:11276205). Participates in the ER-associated degradation (ERAD) quality control pathway inconjunction with J domain-containing co-chaperones and the E3ligase STUB1 (PubMed:23990462). {ECO:0000269\|PubMed:10722728,ECO:0000269\|PubMed:11276205, ECO:0000269\|PubMed:21148293,ECO:0000269\|PubMed:21150129, ECO:0000269\|PubMed:23018488,ECO:0000269\|PubMed:23990462, ECO:0000269\|PubMed:24318877,ECO:0000269\|PubMed:24732912, ECO:0000269\|PubMed:27474739,ECO:0000269\|PubMed:27916661, ECO:0000303\|PubMed:24121476,ECO:0000303\|PubMed:26865365}.

Retention analysis result of each fusion partner 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
download page
.

* Minus value of BPloci means that the break pointn is located before the CDS.

- In-frame and retained protein feature among the 13 regional features.

Partner

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Protein feature

Protein feature note

- In-frame and not-retained protein feature among the 13 regional features.

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Protein feature note

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FusionGeneSequence for HSPA8_HSPA8

For in-frame fusion transcripts, we provide the fusion transcript sequences and fusion amino acid sequences.
(nt: nucleotides, aa: amino acids)

* Fusion amino acid sequences.

* Fusion transcript sequences (only coding sequence (CDS) region).

* Fusion transcript sequences (Full-length transcript).

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FusionGenePPI for HSPA8_HSPA8

Go to ChiPPI (Chimeric Protein-Protein interactions) to see the chimeric PPI interaction in
ChiPPI page
.

Protein-protein interactors with each fusion partner protein in wild-type (BIOGRID-3.4.160)

Hgene

Hgene's interactors

Tgene

Tgene's interactors

- Retained PPIs in in-frame fusion.

Partner

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Still interaction with

- Lost PPIs in in-frame fusion.

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Interaction lost with

- Retained PPIs, but lost function due to frame-shift fusion.

Partner

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TotalLen

Interaction lost with

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RelatedDrugs for HSPA8_HSPA8

Drugs targeting genes involved in this fusion gene.
(DrugBank Version 5.1.0 2018-04-02)

Partner	Gene	UniProtAcc	DrugBank ID	Drug name	Drug activity	Drug type	Drug status
Hgene	HSPA8	P11142	DB01254	Dasatinib	Heat shock cognate 71 kDa protein	small molecule	approved\|investigational
Hgene	HSPA8	P11142	DB11638	Artenimol	Heat shock cognate 71 kDa protein	small molecule	approved\|investigational
Tgene	HSPA8	P11142	DB01254	Dasatinib	Heat shock cognate 71 kDa protein	small molecule	approved\|investigational
Tgene	HSPA8	P11142	DB11638	Artenimol	Heat shock cognate 71 kDa protein	small molecule	approved\|investigational

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RelatedDiseases for HSPA8_HSPA8

Diseases associated with fusion partners.
(DisGeNet 4.0)

Partner	Gene	Disease ID	Disease name	# pubmeds	Source
Hgene	HSPA8	C0001418	Adenocarcinoma	1	CTD_human
Hgene	HSPA8	C0007137	Squamous cell carcinoma	1	CTD_human
Hgene	HSPA8	C0026640	Mouth Neoplasms	1	CTD_human
Hgene	HSPA8	C0035126	Reperfusion Injury	1	CTD_human
Hgene	HSPA8	C0038356	Stomach Neoplasms	1	CTD_human
Hgene	HSPA8	C0948089	Acute Coronary Syndrome	1	CTD_human
Hgene	HSPA8	C1846707	SPINOCEREBELLAR ATAXIA 17	1	CTD_human
Tgene	HSPA8	C0001418	Adenocarcinoma	1	CTD_human
Tgene	HSPA8	C0007137	Squamous cell carcinoma	1	CTD_human
Tgene	HSPA8	C0026640	Mouth Neoplasms	1	CTD_human
Tgene	HSPA8	C0035126	Reperfusion Injury	1	CTD_human
Tgene	HSPA8	C0038356	Stomach Neoplasms	1	CTD_human
Tgene	HSPA8	C0948089	Acute Coronary Syndrome	1	CTD_human
Tgene	HSPA8	C1846707	SPINOCEREBELLAR ATAXIA 17	1	CTD_human

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Fusion gene ID: 16871

FusionGeneSummary for HSPA8_HSPA8

FusionProtFeatures for HSPA8_HSPA8

FusionGeneSequence for HSPA8_HSPA8

FusionGenePPI for HSPA8_HSPA8

RelatedDrugs for HSPA8_HSPA8

RelatedDiseases for HSPA8_HSPA8