HIKESHI

Protein identityUniProt · HPA

UniProt accession

Q53FT3

Gene

HIKESHI

Ensembl

ENSG00000149196

Chromosome

11

Canonical length

197 aa

Protein class

Disease related genes, Human disease related genes, Predicted intracellular proteins

Subcellular location

Nucleoplasm,Nuclear speckles,Nuclear bodies

Quaternary structure

Homodimer

OverviewNCBI Gene

This gene encodes an evolutionarily conserved nuclear transport receptor that mediates heat-shock-induced nuclear import of 70 kDa heat-shock proteins (Hsp70s) through interactions with FG-nucleoporins. The protein mediates transport of the ATP form but not the ADP form of Hsp70 proteins under conditions of heat shock stress. Structural analyses demonstrate that the protein forms an asymmetric homodimer and that the N-terminal domain consists of a jelly-roll/beta-sandwich fold structure that contains hydrophobic pockets involved in FG-nucleoporin recognition. Reduction of RNA expression levels in HeLa cells using small interfering RNAs results in inhibition of heat shock-induced nuclear accumulation of Hsp70s, indicating a role for this gene in regulation of Hsp70 nuclear import during heat shock stress. [provided by RefSeq, Apr 2016]

Canonical amino-acid sequenceUniProt

197 residues, UniProt reviewed canonical sequence.

>Q53FT3|HIKESHI
     1  MFGCLVAGRL VQTAAQQVAE DKFVFDLPDY ESINHVVVFM LGTIPFPEGM GGSVYFSYPD
    61  SNGMPVWQLL GFVTNGKPSA IFKISGLKSG EGSQHPFGAM NIVRTPSVAQ IGISVELLDS
   121  MAQQTPVGNA AVSSVDSFTQ FTQKMLDNFY NFASSFAVSQ AQMTPSPSEM FIPANVVLKW
   181  YENFQRRLAQ NPLFWKT

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against HIKESHI 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)

0.34

Highest tissue expression

52 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about HIKESHI.

Disease | AllUniProt

Conditions HIKESHI is implicated in, by any mechanism.

• Leukodystrophy, hypomyelinating, 13 (HLD13) MIM:616881

Disease | GeneticClinVar

5 pathogenic / likely-pathogenic of 68 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Hypomyelinating leukodystrophy 13
• HIKESHI-related disorder
• Inborn genetic diseases

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)

0.59

gnomAD pLI

0.52

DepMap mean gene effect

-0.18

DepMap dependency class

selective

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

• cellular response to heat
• Golgi organization
• lung development
• protein import into nucleus
• protein transport

Molecular functions

• Hsp70 protein binding
• nuclear import signal receptor activity

Cellular components

• cytosol
• nuclear body
• nuclear speck
• nucleoplasm
• nucleus

Protein domainsUniProt · Pfam · InterPro

• Hikeshi-like, N-terminal domain
• OPI10 family
• Hikeshi-like, C-terminal domain
• Hikeshi-like, N-terminal domain
• Hikeshi-like, C-terminal domain

KeywordsUniProt

• Cytoplasm
• Leukodystrophy
• Nucleus
• Protein transport
• Transport

InteractionsUniProt · HPA

Protein binding partners of HIKESHI in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• HSPA8
• NUP153
• NUP62