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heat shock protein family A (Hsp70) member 1 like

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Immunopharmacology Ligand target has curated data in GtoImmuPdb

Target id: 2989

Nomenclature: heat shock protein family A (Hsp70) member 1 like

Systematic Nomenclature: HSPA1L

Family: Heat shock proteins

Gene and Protein Information Click here for help
Species TM AA Chromosomal Location Gene Symbol Gene Name Reference
Human - 641 6p21.33 HSPA1L heat shock protein family A (Hsp70) member 1 like
Mouse - 641 17 18.51 cM Hspa1l heat shock protein 1-like
Rat - 641 20p12 Hspa1l heat shock protein family A (Hsp70) member 1 like
Previous and Unofficial Names Click here for help
heat shock 70kDa protein 1-like | heat shock 70kD protein-like 1 | HSP70-HOM | hum70t
Database Links Click here for help
Alphafold
Ensembl Gene
Entrez Gene
Human Protein Atlas
KEGG Gene
OMIM
Pharos
RefSeq Nucleotide
RefSeq Protein
UniProtKB
Wikipedia
Immunopharmacology Comments
Mutations in HSPA1L have been identified in patients with inflammatory bowel disease (IBD) [3], suggesting a role for this protein in the pathogenesis of IBD. An elevated level of HSPA1L mRNA from human whole blood correlates with graft-versus-host disease in patients with acute and chronic stage disease [1].
Immuno Disease Associations
Disease Name:  Crohn's disease
Disease Synonyms:  no synonynms
Comment:  Genetic mutations that cause amino acid changes in the HSPA1L protein have been identified in patients with CD.
Disease X-refs:  Disease Ontology: DOID:8778
OMIM: 266600
Orphanet: ORPHA206
References:  3
Disease Name:  Ulcerative colitis
Disease Synonyms:  no synonynms
Comment:  Genetic mutations that cause amino acid changes in the HSPA1L protein have been identified in patients with UC.
Disease X-refs:  Disease Ontology: DOID:8577
OMIM: 266600
Orphanet: ORPHA771
References:  3
Biologically Significant Variants Click here for help
Type:  Naturally occurring mutation
Species:  Human
Description:  A mutation identified in a patient with Crohn's disease.
Amino acid change:  Glu558Asp
Nucleotide change:  1674A > T
References:  3
Type:  Naturally occurring mutation
Species:  Human
Description:  A mutation identified in a patient with Crohn's disease.
Amino acid change:  Ala268Thr
Nucleotide change:  802G > A
References:  3
Type:  Naturally occurring mutation
Species:  Human
Description:  A moderately conservative mutation identified in a patient with ulcerative colitis.
Amino acid change:  Ala268Thr
Nucleotide change:  802G > A
SNP accession: 
References:  3
Type:  Naturally occurring mutations
Species:  Human
Description:  A mutation identified in a patient with ulcerative colitis. Exhibits a dominant negative effect in vitro.
Amino acid change:  Ser277Leu
Nucleotide change:  830C > T
References:  3
Type:  Naturally occurring mutation
Species:  Human
Description:  An in-frame deletion identified in a patient with unclassified inflammatory bowel disease. Exhibits a dominant negative effect in vitro.
Amino acid change:  Leu172del
Nucleotide change:  515_517del
References:  3
Type:  Naturally occurring mutation
Species:  Human
Description:  A moderately conservative mutation identified in a patient with Crohn's disease.
Amino acid change:  Thr267Ile
Nucleotide change:  800C > T
SNP accession: 
References:  3
Type:  Naturally occurring mutation
Species:  Human
Description:  A moderately radical non-synonymous variant of HSPA1L identified in a patient with IBD.
Amino acid change:  Glu558Ala
Nucleotide change:  1673A > C
SNP accession: 
References:  3
Type:  Naturally occurring mutation
Species:  Human
Description:  A moderately conservative mutation identified in a patient with ulcerative colitis. Exhibits a dominant negative effect in vitro.
Amino acid change:  Gly77Ser
Nucleotide change:  c.229G > A
SNP accession: 
References:  3
General Comments
HSPA1L is a chaperone protein that is involved in ensuring the correct folding of nascent proteins, re-folding of misfolded proteins, and targeting proteins for degradation. It has a substrate (peptide) binding site that is controlled by its nucleotide binding status. When ATP is bound, substrate affinity is low. ATP hydrolysis to ADP causes a conformational change that increases affinity for substrate. Switching between these two states facilitates substrate binding and release [2].

References

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1. Atarod S, Turner B, Pearce KF, Ahmed SS, Norden J, Bogunia-Kubik K, Wang XN, Collin M, Dickinson AM. (2015) Elevated level of HSPA1L mRNA correlates with graft-versus-host disease. Transpl Immunol, 32 (3): 188-94. [PMID:25680846]

2. Radons J. (2016) The human HSP70 family of chaperones: where do we stand?. Cell Stress Chaperones, 21 (3): 379-404. [PMID:26865365]

3. Takahashi S, Andreoletti G, Chen R, Munehira Y, Batra A, Afzal NA, Beattie RM, Bernstein JA, Ennis S, Snyder M. (2017) De novo and rare mutations in the HSPA1L heat shock gene associated with inflammatory bowel disease. Genome Med, 9 (1): 8. [PMID:28126021]

How to cite this page

Heat shock proteins: heat shock protein family A (Hsp70) member 1 like. Last modified on 15/02/2018. Accessed on 26/11/2022. IUPHAR/BPS Guide to PHARMACOLOGY, http://www.guidetopharmacology.org/GRAC/ObjectDisplayForward?objectId=2989.