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Protein

Protein Hikeshi

Gene

HIKESHI

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a specific nuclear import carrier for HSP70 proteins following heat-shock stress: acts by mediating the nucleoporin-dependent translocation of ATP-bound HSP70 proteins into the nucleus. HSP70 proteins import is required to protect cells from heat shock damages. Does not translocate ADP-bound HSP70 proteins into the nucleus.1 Publication

GO - Molecular functioni

  • Hsp70 protein binding Source: UniProtKB
  • protein transporter activity Source: UniProtKB

GO - Biological processi

  • cellular response to heat Source: UniProtKB
  • protein import into nucleus Source: UniProtKB
  • protein transport Source: UniProtKB
  • regulation of cellular response to heat Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-HSA-3371453. Regulation of HSF1-mediated heat shock response.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Hikeshi
Gene namesi
Name:HIKESHIImported
Synonyms:C11orf73
ORF Names:HSPC138, HSPC179, HSPC248
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:26938. HIKESHI.

Subcellular locationi

  • Cytoplasmcytosol 1 Publication
  • Nucleus 1 Publication

GO - Cellular componenti

  • cell junction Source: HPA
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • intracellular Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Leukodystrophy, hypomyelinating, 13 (HLD13)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive neurodegenerative disorder with infantile onset, affecting mainly the central white matter. Clinical features include early feeding difficulties, global developmental delay, postnatal progressive microcephaly, truncal hypotonia, spasticity, and variable neurologic deficits, such as visual impairment.
See also OMIM:616881
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07641154V → L in HLD13. 1 PublicationCorresponds to variant rs202003795dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation, Leukodystrophy

Organism-specific databases

DisGeNETi51501.
MIMi616881. phenotype.
OpenTargetsiENSG00000149196.
PharmGKBiPA144596492.

Polymorphism and mutation databases

BioMutaiC11orf73.
DMDMi110278911.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002452621 – 197Protein HikeshiAdd BLAST197

Proteomic databases

EPDiQ53FT3.
MaxQBiQ53FT3.
PaxDbiQ53FT3.
PeptideAtlasiQ53FT3.
PRIDEiQ53FT3.
TopDownProteomicsiQ53FT3.

PTM databases

iPTMnetiQ53FT3.
PhosphoSitePlusiQ53FT3.

Expressioni

Inductioni

Following heat-shock treatment.1 Publication

Gene expression databases

BgeeiENSG00000149196.
CleanExiHS_C11orf73.
ExpressionAtlasiQ53FT3. baseline and differential.
GenevisibleiQ53FT3. HS.

Organism-specific databases

HPAiHPA035063.
HPA035064.

Interactioni

Subunit structurei

Interacts with ATP-bound HSP70 proteins. Interacts with NUP62 and NUP153 (via F-X-F-G repeats).1 Publication

GO - Molecular functioni

  • Hsp70 protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119574. 8 interactors.
IntActiQ53FT3. 5 interactors.
MINTiMINT-3047121.
STRINGi9606.ENSP00000278483.

Structurei

Secondary structure

1197
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Beta strandi16 – 19Combined sources4
Beta strandi22 – 29Combined sources8
Helixi30 – 32Combined sources3
Beta strandi34 – 40Combined sources7
Beta strandi42 – 44Combined sources3
Beta strandi50 – 57Combined sources8
Beta strandi68 – 73Combined sources6
Beta strandi75 – 77Combined sources3
Beta strandi79 – 83Combined sources5
Beta strandi108 – 117Combined sources10
Helixi118 – 121Combined sources4
Helixi137 – 154Combined sources18
Helixi160 – 162Combined sources3
Beta strandi171 – 173Combined sources3
Helixi174 – 188Combined sources15
Turni192 – 195Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WVZX-ray1.88A/B1-197[»]
3WW0X-ray2.50A/B1-197[»]
ProteinModelPortaliQ53FT3.
SMRiQ53FT3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the OPI10 family.Curated

Phylogenomic databases

eggNOGiKOG4067. Eukaryota.
ENOG4111H6N. LUCA.
GeneTreeiENSGT00390000004056.
HOGENOMiHOG000175561.
HOVERGENiHBG081226.
InParanoidiQ53FT3.
OMAiQFGQRML.
OrthoDBiEOG091G0LVQ.
PhylomeDBiQ53FT3.
TreeFamiTF313222.

Family and domain databases

InterProiIPR008493. DUF775.
IPR031318. OPI10.
[Graphical view]
PANTHERiPTHR12925:SF0. PTHR12925:SF0. 1 hit.
PfamiPF05603. DUF775. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q53FT3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFGCLVAGRL VQTAAQQVAE DKFVFDLPDY ESINHVVVFM LGTIPFPEGM
60 70 80 90 100
GGSVYFSYPD SNGMPVWQLL GFVTNGKPSA IFKISGLKSG EGSQHPFGAM
110 120 130 140 150
NIVRTPSVAQ IGISVELLDS MAQQTPVGNA AVSSVDSFTQ FTQKMLDNFY
160 170 180 190
NFASSFAVSQ AQMTPSPSEM FIPANVVLKW YENFQRRLAQ NPLFWKT
Length:197
Mass (Da):21,628
Last modified:July 11, 2006 - v2
Checksum:i4FA524439B630511
GO

Sequence cautioni

The sequence AAF29102 differs from that shown. Reason: Frameshift at positions 62 and 68.Curated
The sequence AAF29142 differs from that shown. Reason: Frameshift at positions 9 and 57.Curated
The sequence AAF36168 differs from that shown. Reason: Frameshift at position 67.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti82F → L in AAF29102 (PubMed:11042152).Curated1
Sequence conflicti82F → L in BAD96918 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02696847P → A.1 PublicationCorresponds to variant rs11539213dbSNPEnsembl.1
Natural variantiVAR_07641154V → L in HLD13. 1 PublicationCorresponds to variant rs202003795dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151082 mRNA. Translation: AAF36168.1. Frameshift.
AF161487 mRNA. Translation: AAF29102.1. Frameshift.
AF161527 mRNA. Translation: AAF29142.1. Frameshift.
AK001447 mRNA. Translation: BAA91698.1.
AK223198 mRNA. Translation: BAD96918.1.
BC001677 mRNA. Translation: AAH01677.1.
BC006476 mRNA. Translation: AAH06476.1.
BC015991 mRNA. Translation: AAH15991.1.
BC018080 mRNA. Translation: AAH18080.1.
BC021621 mRNA. Translation: AAH21621.1.
CCDSiCCDS8275.1.
RefSeqiNP_057485.2. NM_016401.3.
UniGeneiHs.283322.

Genome annotation databases

EnsembliENST00000278483; ENSP00000278483; ENSG00000149196.
GeneIDi51501.
KEGGihsa:51501.
UCSCiuc001pbu.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151082 mRNA. Translation: AAF36168.1. Frameshift.
AF161487 mRNA. Translation: AAF29102.1. Frameshift.
AF161527 mRNA. Translation: AAF29142.1. Frameshift.
AK001447 mRNA. Translation: BAA91698.1.
AK223198 mRNA. Translation: BAD96918.1.
BC001677 mRNA. Translation: AAH01677.1.
BC006476 mRNA. Translation: AAH06476.1.
BC015991 mRNA. Translation: AAH15991.1.
BC018080 mRNA. Translation: AAH18080.1.
BC021621 mRNA. Translation: AAH21621.1.
CCDSiCCDS8275.1.
RefSeqiNP_057485.2. NM_016401.3.
UniGeneiHs.283322.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3WVZX-ray1.88A/B1-197[»]
3WW0X-ray2.50A/B1-197[»]
ProteinModelPortaliQ53FT3.
SMRiQ53FT3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119574. 8 interactors.
IntActiQ53FT3. 5 interactors.
MINTiMINT-3047121.
STRINGi9606.ENSP00000278483.

PTM databases

iPTMnetiQ53FT3.
PhosphoSitePlusiQ53FT3.

Polymorphism and mutation databases

BioMutaiC11orf73.
DMDMi110278911.

Proteomic databases

EPDiQ53FT3.
MaxQBiQ53FT3.
PaxDbiQ53FT3.
PeptideAtlasiQ53FT3.
PRIDEiQ53FT3.
TopDownProteomicsiQ53FT3.

Protocols and materials databases

DNASUi51501.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000278483; ENSP00000278483; ENSG00000149196.
GeneIDi51501.
KEGGihsa:51501.
UCSCiuc001pbu.4. human.

Organism-specific databases

CTDi51501.
DisGeNETi51501.
GeneCardsiC11orf73.
HGNCiHGNC:26938. HIKESHI.
HPAiHPA035063.
HPA035064.
MIMi614908. gene.
616881. phenotype.
neXtProtiNX_Q53FT3.
OpenTargetsiENSG00000149196.
PharmGKBiPA144596492.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4067. Eukaryota.
ENOG4111H6N. LUCA.
GeneTreeiENSGT00390000004056.
HOGENOMiHOG000175561.
HOVERGENiHBG081226.
InParanoidiQ53FT3.
OMAiQFGQRML.
OrthoDBiEOG091G0LVQ.
PhylomeDBiQ53FT3.
TreeFamiTF313222.

Enzyme and pathway databases

ReactomeiR-HSA-3371453. Regulation of HSF1-mediated heat shock response.

Miscellaneous databases

ChiTaRSiC11orf73. human.
GeneWikiiC11orf73.
GenomeRNAii51501.
PROiQ53FT3.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000149196.
CleanExiHS_C11orf73.
ExpressionAtlasiQ53FT3. baseline and differential.
GenevisibleiQ53FT3. HS.

Family and domain databases

InterProiIPR008493. DUF775.
IPR031318. OPI10.
[Graphical view]
PANTHERiPTHR12925:SF0. PTHR12925:SF0. 1 hit.
PfamiPF05603. DUF775. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHIKES_HUMAN
AccessioniPrimary (citable) accession number: Q53FT3
Secondary accession number(s): Q8WVE8
, Q9NVQ2, Q9NZZ1, Q9P022, Q9P0N1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: July 11, 2006
Last modified: November 2, 2016
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

'Hikeshi' is a traditional Japanese compound word used for a firefighter, smokejumper, or troubleshooter.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.