HSPA14

Protein-coding gene in the species Homo sapiens
HSPA14
Identifiers
AliasesHSPA14, HSP70-4, HSP70L1, heat shock protein family A (Hsp70) member 14
External IDsOMIM: 610369; MGI: 1354164; HomoloGene: 74307; GeneCards: HSPA14; OMA:HSPA14 - orthologs
Gene location (Human)
Chromosome 10 (human)
Chr.Chromosome 10 (human)[1]
Chromosome 10 (human)
Genomic location for HSPA14
Genomic location for HSPA14
Band10p13Start14,838,306 bp[1]
End14,871,741 bp[1]
Gene location (Mouse)
Chromosome 2 (mouse)
Chr.Chromosome 2 (mouse)[2]
Chromosome 2 (mouse)
Genomic location for HSPA14
Genomic location for HSPA14
Band2|2 A1Start3,489,887 bp[2]
End3,513,851 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • secondary oocyte

  • middle temporal gyrus

  • right testis

  • rectum

  • deltoid muscle

  • left testis

  • gastrocnemius muscle

  • mucosa of sigmoid colon

  • vastus lateralis muscle

  • Skeletal muscle tissue of biceps brachii
Top expressed in
  • primitive streak

  • epiblast

  • otic placode

  • abdominal wall

  • otic vesicle

  • yolk sac

  • dermis

  • morula

  • morula

  • embryo
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • nucleotide binding
  • protein binding
  • ATP binding
  • ATPase activity
  • heat shock protein binding
  • protein folding chaperone activity
  • unfolded protein binding
  • misfolded protein binding
Cellular component
  • cytoplasm
  • cytosol
  • ribosome
  • membrane
  • polysome
Biological process
  • 'de novo' cotranslational protein folding
  • cytoplasmic translation
  • regulation of translational fidelity
  • response to unfolded protein
  • cellular response to heat
  • Unfolded Protein Response
  • protein refolding
  • chaperone cofactor-dependent protein refolding
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

51182

50497

Ensembl

ENSG00000187522

ENSMUSG00000109865

UniProt

Q0VDF9
Q8TAQ0

Q99M31

RefSeq (mRNA)

NM_001037538
NM_001278205
NM_016299

NM_001037542
NM_015765
NM_001355397

RefSeq (protein)

NP_057383
NP_001265134.1

NP_056580
NP_001342326

Location (UCSC)Chr 10: 14.84 – 14.87 MbChr 2: 3.49 – 3.51 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Heat shock 70 kDa protein 14 also known as HSP70-like protein 1 or heat shock protein HSP60 is a protein that in humans is encoded by the HSPA14 gene.[5][6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000187522 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000109865 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Wan T, Zhou X, Chen G, An H, Chen T, Zhang W, Liu S, Jiang Y, Yang F, Wu Y, Cao X (March 2004). "Novel heat shock protein Hsp70L1 activates dendritic cells and acts as a Th1 polarizing adjuvant". Blood. 103 (5): 1747–54. doi:10.1182/blood-2003-08-2828. PMID 14592822.
  6. ^ "Entrez Gene: HSPA14 heat shock 70kDa protein 14".

Further reading

  • Furlini G, Vignoli M, Re MC, et al. (1994). "Human immunodeficiency virus type 1 interaction with the membrane of CD4+ cells induces the synthesis and nuclear translocation of 70K heat shock protein" (PDF). J. Gen. Virol. 75 (1): 193–9. doi:10.1099/0022-1317-75-1-193. PMID 7906708.
  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Scheufler C, Brinker A, Bourenkov G, et al. (2000). "Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine". Cell. 101 (2): 199–210. doi:10.1016/S0092-8674(00)80830-2. PMID 10786835. S2CID 18200460.
  • Lim MC, Brooke SM, Sapolsky RM (2003). "gp120 neurotoxicity fails to induce heat shock defenses, while the over expression of hsp70 protects against gp120". Brain Res. Bull. 61 (2): 183–8. doi:10.1016/S0361-9230(03)00113-8. PMID 12832005. S2CID 35451084.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Brandenberger R, Wei H, Zhang S, et al. (2005). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. doi:10.1038/nbt971. PMID 15146197. S2CID 27764390.

External links

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Chaperones/
protein folding
Heat shock proteins/
Chaperonins
Other
Protein targetingUbiquitin
(ubiquitylation)Ubiquitin-like proteins
(UBL)
SUMO protein
(SUMOylation)
  • E1 SUMO-activating enzyme
  • E2 SUMO-conjugating enzyme
Other
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