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GeneQ18027343· pop 5· linked from 108 articles

Also known as HSP70-1L, HSP70-HOM, HSP70T, hum70t, heat shock protein family A (Hsp70) member 1 like

Heat shock 70 kDa protein 1L is a protein that in humans is encoded by the HSPA1L gene on chromosome 6. As a member of the heat shock protein 70 (Hsp70) family and a chaperone protein, it facilitates the proper folding of newly translated and misfolded proteins, as well as stabilize or degrade mutant proteins. Its functions contribute to biological processes including signal transduction, apoptosis, protein homeostasis, and cell growth and differentiation. It has been associated with an extensive number of cancers, neurodegenerative diseases, cell senescence and aging, and Graft-versus-host di

Gene data

HSPA1L
Name
heat shock protein family A (Hsp70) member 1 like
Type
protein-coding
Position
31,809,619–31,815,788 (−)
Aliases
HSP70-1L, HSP70-HOM, HSP70T, hum70t
RefSeq RNA
NM_005527.4
RefSeq protein
NP_005518.3

This gene encodes a 70kDa heat shock protein. In conjunction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which also encode isoforms of the 70kDa heat shock protein. [provided by RefSeq, Jul 2008].

via MyGene.info

Gene · Ensembl

heat shock protein family A (Hsp70) member 1 like

Symbol
HSPA1L
Biotype
Protein coding
Organism
Homo sapiens
Location
Chr HSCHR6_MHC_DBB_CTG1:3,057,398-3,062,844
Strand
Reverse (−)
Assembly
GRCh38
View on Ensembl →

via Ensembl · EMBL-EBI

~7 min read

Encyclopedic overview

7 sections
Contents
  • Structure
  • Function
  • Clinical significance
  • Interactions
  • References
  • Further reading
  • External links

Heat shock 70 kDa protein 1L is a protein that in humans is encoded by the HSPA1L gene on chromosome 6. As a member of the heat shock protein 70 (Hsp70) family and a chaperone protein, it facilitates the proper folding of newly translated and misfolded proteins, as well as stabilize or degrade mutant proteins. Its functions contribute to biological processes including signal transduction, apoptosis, protein homeostasis, and cell growth and differentiation. It has been associated with an extensive number of cancers, neurodegenerative diseases, cell senescence and aging, and Graft-versus-host disease.

== Structure ==

Excerpted from Wikipedia’s “HSPA1L” article, available under the CC BY-SA 4.0 licence.

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