HSPA1L
Heat shock 70 kDa protein 1-like
Also known as: HS71L_HUMAN, HSP70-HOM, hum70t
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- P34931
- Gene
- HSPA1L
- Ensembl
- ENSG00000204390
- Chromosome
- 6
- Canonical length
- 641 aa
- Protein class
- Cancer-related genes, Plasma proteins, Predicted intracellular proteins
- Subcellular location
- Vesicles,Perinuclear theca,Calyx,Flagellar centriole,Annulus
OverviewNCBI Gene
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]
Canonical amino-acid sequenceUniProt
641 residues, UniProt reviewed canonical sequence.
>P34931|HSPA1L
1 MATAKGIAIG IDLGTTYSCV GVFQHGKVEI IANDQGNRTT PSYVAFTDTE RLIGDAAKNQ
61 VAMNPQNTVF DAKRLIGRKF NDPVVQADMK LWPFQVINEG GKPKVLVSYK GENKAFYPEE
121 ISSMVLTKLK ETAEAFLGHP VTNAVITVPA YFNDSQRQAT KDAGVIAGLN VLRIINEPTA
181 AAIAYGLDKG GQGERHVLIF DLGGGTFDVS ILTIDDGIFE VKATAGDTHL GGEDFDNRLV
241 SHFVEEFKRK HKKDISQNKR AVRRLRTACE RAKRTLSSST QANLEIDSLY EGIDFYTSIT
301 RARFEELCAD LFRGTLEPVE KALRDAKMDK AKIHDIVLVG GSTRIPKVQR LLQDYFNGRD
361 LNKSINPDEA VAYGAAVQAA ILMGDKSEKV QDLLLLDVAP LSLGLETAGG VMTALIKRNS
421 TIPTKQTQIF TTYSDNQPGV LIQVYEGERA MTKDNNLLGR FDLTGIPPAP RGVPQIEVTF
481 DIDANGILNV TATDKSTGKV NKITITNDKG RLSKEEIERM VLDAEKYKAE DEVQREKIAA
541 KNALESYAFN MKSVVSDEGL KGKISESDKN KILDKCNELL SWLEVNQLAE KDEFDHKRKE
601 LEQMCNPIIT KLYQGGCTGP ACGTGYVPGR PATGPTIEEV DLocalizationUniProt · AlphaFold · HPA
Whether an antibody against HSPA1L can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.26
- Highest tissue expression
- 55 nTPM
Expression across tissuesHPA
Tissue
- testis: 55 nTPM
- skeletal muscle: 3.4 nTPM
- basal ganglia: 2.9 nTPM
- cerebral cortex: 2.8 nTPM
- spinal cord: 2.5 nTPM
- amygdala: 2.4 nTPM
Single-cell type
- ependymal cells: 2.7 nCPM
- microglia: 1.7 nCPM
- astrocytes: 1.5 nCPM
- podocytes: 1.5 nCPM
- late spermatids: 1.4 nCPM
- oligodendrocytes: 1.2 nCPM
Immune cell
- basophil: 0 nTPM
- classical monocyte: 0 nTPM
- eosinophil: 0 nTPM
- gdT-cell: 0 nTPM
- intermediate monocyte: 0 nTPM
- MAIT T-cell: 0 nTPM
Brain region
- cerebellum: 3 nTPM
- white matter: 1.3 nTPM
- cerebral cortex: 1 nTPM
- pons: 1 nTPM
- thalamus: 0.9 nTPM
- medulla oblongata: 0.8 nTPM
DiseaseUniProt · ClinVar · IEDB · PubMed
Four sources answering four different questions about HSPA1L.
Disease | ImmuneIEDB
Conditions an epitope on HSPA1L was assayed in.
- multiple sclerosis B cell
- allergic disease T cell
- Timothy grass allergy T cell
- Chagas disease B cell
- type 1 diabetes mellitus T cell
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.23
- gnomAD pLI
- 0
- gnomAD missense Z
- 0.64
- DepMap mean gene effect
- 0.04
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- binding of sperm to zona pellucida
- positive regulation of protein targeting to mitochondrion
- protein refolding
- response to unfolded protein
Molecular functions
- ATP binding
- ATP hydrolysis activity
- ATP-dependent protein folding chaperone
- heat shock protein binding
- protein folding chaperone
- ubiquitin protein ligase binding
- unfolded protein binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of HSPA1L in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads HSPA1L as an antibody target. Whether an autoantibody or antibody against HSPA1L could matter depends on whether native HSPA1L is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
HSPA1L is annotated at the cell surface, where native HSPA1L is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label HSPA1L as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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