HSPE1

Protein identityUniProt · HPA

UniProt accession

P61604

Gene

HSPE1

Ensembl

ENSG00000115541

Chromosome

2

Canonical length

102 aa

Protein class

Cancer-related genes, Plasma proteins, Predicted intracellular proteins

Quaternary structure

Homoheptamer

OverviewNCBI Gene

This gene encodes a major heat shock protein which functions as a chaperonin. Its structure consists of a heptameric ring which binds to another heat shock protein in order to form a symmetric, functional heterodimer which enhances protein folding in an ATP-dependent manner. This gene and its co-chaperonin, HSPD1, are arranged in a head-to-head orientation on chromosome 2. Naturally occurring read-through transcription occurs between this locus and the neighboring locus MOBKL3.[provided by RefSeq, Feb 2011]

Canonical amino-acid sequenceUniProt

102 residues, UniProt reviewed canonical sequence.

>P61604|HSPE1
     1  MAGQAFRKFL PLFDRVLVER SAAETVTKGG IMLPEKSQGK VLQATVVAVG SGSKGKGGEI
    61  QPVSVKVGDK VLLPEYGGTK VVLDDKDYFL FRDGDILGKY VD

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against HSPE1 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

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.4

Highest tissue expression

1,081 nTPM

Expression across tissuesHPA

ReferencesPubMed · IEDB

Publications for HSPE1 from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.

Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.

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)

0.56

gnomAD pLI

0.8

gnomAD missense Z

1.45

DepMap mean gene effect

-3.37

DepMap dependency class

pan

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 6% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• intrinsic apoptotic signaling pathway
• osteoblast differentiation
• protein folding
• response to unfolded protein

Molecular functions

• ATP binding
• metal ion binding
• protein folding chaperone
• protein-folding chaperone binding
• RNA binding
• unfolded protein binding

Cellular components

• extracellular exosome
• membrane
• mitochondrial matrix
• mitochondrion

Protein domainsUniProt · Pfam · InterPro

• GroES-like superfamily
• Chaperonin GroES, conserved site
• GroES chaperonin family
• GroES chaperonin superfamily
• Chaperonin 10 Kd subunit

KeywordsUniProt

• Acetylation
• Chaperone
• Mitochondrion
• Phosphoprotein
• Stress response