HSPA1L information

HSPA1L
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3GDQ
Identifiers
Aliases	HSPA1L, HSP70-1L, HSP70-HOM, HSP70T, hum70t, heat shock protein family A (Hsp70) member 1 like
External IDs	OMIM: 140559 MGI: 96231 HomoloGene: 135835 GeneCards: HSPA1L
Gene location (Human)
Chr.	Chromosome 6 (human)
End	31,815,283 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	35,198,261 bp
RNA expression pattern
	Top expressed in
	skeletal muscle tissue; ; blood; ; gastrocnemius muscle; ; ganglionic eminence; ; right uterine tube; ; stromal cell of endometrium; ; monocyte; ; superior frontal gyrus; ; putamen; ; islet of Langerhans;
	Top expressed in
	seminiferous tubule; ; spermatid; ; soleus muscle; ; spermatocyte; ; tibialis anterior muscle; ; intercostal muscle; ; plantaris muscle; ; temporal muscle; ; sternocleidomastoid muscle; ; gastrocnemius muscle;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	unfolded protein binding; nucleotide binding; protein binding; ATP binding; heat shock protein binding; ubiquitin protein ligase binding; ATPase activity; protein folding chaperone activity; misfolded protein binding;
Cellular component	COP9 signalosome; cytosol; mitochondrial matrix; blood microparticle; mitochondrion; nucleoplasm; zona pellucida receptor complex; cell body; cytoplasm;
Biological process	regulation of cellular response to heat; response to unfolded protein; protein refolding; positive regulation of protein targeting to mitochondrion; binding of sperm to zona pellucida; cellular response to heat; Unfolded Protein Response; chaperone cofactor-dependent protein refolding;
	Sources:Amigo / QuickGO
Orthologs
	3305
	15482
ENSG00000234258; ENSG00000226704; ENSG00000236251; ENSG00000204390; ENSG00000206383;
	n/a
	ENSMUSG00000007033
	P34931
	P16627
	NM_005527
	NM_013558
	NP_005518
	NP_038586
	Wikidata
View/Edit Human	View/Edit Mouse

Heat shock 70 kDa protein 1L is a protein that in humans is encoded by the HSPA1L gene on chromosome 6.^[5]^[6]^[7] 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.^[7]^[8] Its functions contribute to biological processes including signal transduction, apoptosis, protein homeostasis, and cell growth and differentiation.^[8]^[9] It has been associated with an extensive number of cancers, neurodegenerative diseases, cell senescence and aging, and Graft-versus-host disease.^[8]^[9]^[10]

^ ^a ^b ^c ENSG00000226704, ENSG00000236251, ENSG00000204390, ENSG00000206383 GRCh38: Ensembl release 89: ENSG00000234258, ENSG00000226704, ENSG00000236251, ENSG00000204390, ENSG00000206383 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000007033 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Ito Y, Ando A, Ando H, Ando J, Saijoh Y, Inoko H, Fujimoto H (Aug 1998). "Genomic structure of the spermatid-specific hsp70 homolog gene located in the class III region of the major histocompatibility complex of mouse and man". Journal of Biochemistry. 124 (2): 347–53. doi:10.1093/oxfordjournals.jbchem.a022118. PMID 9685725.
^ Ishihara M, Ohno S (Nov 1997). "Genetic influences on sarcoidosis". Eye. 11. 11 (2): 155–61. doi:10.1038/eye.1997.44. PMID 9349405.
^ ^a ^b "Entrez Gene: HSPA1L heat shock 70kDa protein 1-like".
^ ^a ^b ^c Mayer MP, Bukau B (Mar 2005). "Hsp70 chaperones: cellular functions and molecular mechanism". Cellular and Molecular Life Sciences. 62 (6): 670–684. doi:10.1007/s00018-004-4464-6. PMC 2773841. PMID 15770419.
^ ^a ^b Wang X, Wang Q, Lin H, Li S, Sun L, Yang Y (Feb 2013). "HSP72 and gp96 in gastroenterological cancers". Clinica Chimica Acta; International Journal of Clinical Chemistry. 417: 73–9. doi:10.1016/j.cca.2012.12.017. PMID 23266770.
^ Atarod S, Turner B, Pearce KF, Ahmed SS, Norden J, Bogunia-Kubik K, Wang XN, Collin M, Dickinson AM (Feb 2015). "Elevated level of HSPA1L mRNA correlates with graft-versus-host disease". Transplant Immunology. 32 (3): 188–94. doi:10.1016/j.trim.2015.02.002. PMID 25680846.

[refGRCh38Ensembl-1] ENSG00000226704, ENSG00000236251, ENSG00000204390, ENSG00000206383 GRCh38: Ensembl release 89: ENSG00000234258, ENSG00000226704, ENSG00000236251, ENSG00000204390, ENSG00000206383 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000007033 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[Ito_1998-5] Ito Y, Ando A, Ando H, Ando J, Saijoh Y, Inoko H, Fujimoto H (Aug 1998). "Genomic structure of the spermatid-specific hsp70 homolog gene located in the class III region of the major histocompatibility complex of mouse and man". Journal of Biochemistry. 124 (2): 347–53. doi:10.1093/oxfordjournals.jbchem.a022118. PMID 9685725.

[Ishihara_1997-6] Ishihara M, Ohno S (Nov 1997). "Genetic influences on sarcoidosis". Eye. 11. 11 (2): 155–61. doi:10.1038/eye.1997.44. PMID 9349405.

[entrez-7] "Entrez Gene: HSPA1L heat shock 70kDa protein 1-like".

[Mayer_2005-8] Mayer MP, Bukau B (Mar 2005). "Hsp70 chaperones: cellular functions and molecular mechanism". Cellular and Molecular Life Sciences. 62 (6): 670–684. doi:10.1007/s00018-004-4464-6. PMC 2773841. PMID 15770419.

[Wang_2013-9] Wang X, Wang Q, Lin H, Li S, Sun L, Yang Y (Feb 2013). "HSP72 and gp96 in gastroenterological cancers". Clinica Chimica Acta; International Journal of Clinical Chemistry. 417: 73–9. doi:10.1016/j.cca.2012.12.017. PMID 23266770.

[Atarod_2015-10] Atarod S, Turner B, Pearce KF, Ahmed SS, Norden J, Bogunia-Kubik K, Wang XN, Collin M, Dickinson AM (Feb 2015). "Elevated level of HSPA1L mRNA correlates with graft-versus-host disease". Transplant Immunology. 32 (3): 188–94. doi:10.1016/j.trim.2015.02.002. PMID 25680846.

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