HSPA1B information

HSPA1B
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1HJO, 1S3X, 1XQS, 2E88, 2E8A, 2LMG, 3A8Y, 3ATU, 3ATV, 3AY9, 3D2E, 3D2F, 3JXU, 3LOF, 4IO8, 4J8F, 4PO2, 4WV5, 4WV7, 5AR0, 5AQZ, 3Q49,%%s3D2E
Identifiers
Aliases	HSPA1B, HSP70-1B, HSP70-2, HSP70.2, heat shock protein family A (Hsp70) member 1B, HSX70, HSPA1, HSP70-1, HSP72, HSP70.1
External IDs	OMIM: 603012; MGI: 96244; HomoloGene: 74294; GeneCards: HSPA1B; OMA:HSPA1B - orthologs
Gene location (Human)
Chr.	Chromosome 6 (human)
End	31,830,254 bp
Gene location (Mouse)
Chr.	Chromosome 17 (mouse)
End	35,191,132 bp
RNA expression pattern
	Top expressed in
	ventricular zone; ; gallbladder; ; ganglionic eminence; ; mucosa of transverse colon; ; gastric mucosa; ; C1 segment; ; hypothalamus; ; right uterine tube; ; pituitary gland; ; substantia nigra;
	Top expressed in
	corneal stroma; ; conjunctival fornix; ; vestibular membrane of cochlear duct; ; ciliary body; ; plantaris muscle; ; retinal pigment epithelium; ; skin of external ear; ; Ileal epithelium; ; iris; ; esophagus;
	More reference expression data
	n/a
Gene ontology
Molecular function	nucleotide binding; heat shock protein binding; signaling receptor binding; C3HC4-type RING finger domain binding; ATPase activity; virus receptor activity; histone deacetylase binding; protein folding chaperone activity; G protein-coupled receptor binding; ATP binding; enzyme binding; ubiquitin protein ligase binding; protein binding; transcription corepressor activity; cadherin binding; RNA binding; denatured protein binding; protein N-terminus binding; unfolded protein binding; disordered domain specific binding; misfolded protein binding;
Cellular component	blood microparticle; centriole; nucleoplasm; inclusion body; focal adhesion; perinuclear region of cytoplasm; ubiquitin ligase complex; cytosol; extracellular region; ficolin-1-rich granule lumen; centrosome; microtubule organizing center; cytoskeleton; nucleus; cytoplasm; mitochondrion; endoplasmic reticulum; aggresome; nuclear speck; vesicle; extracellular exosome; COP9 signalosome; protein-containing complex; ribonucleoprotein complex;
Biological process	cellular response to oxidative stress; regulation of mRNA stability; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; positive regulation of NF-kappaB transcription factor activity; negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; cellular heat acclimation; negative regulation of inclusion body assembly; positive regulation of tumor necrosis factor-mediated signaling pathway; negative regulation of cell death; positive regulation of gene expression; viral entry into host cell; regulation of cell death; ATP metabolic process; negative regulation of protein ubiquitination; negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; positive regulation of endoribonuclease activity; positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; regulation of protein ubiquitination; positive regulation of interleukin-8 production; regulation of cellular response to heat; cellular response to heat; negative regulation of transforming growth factor beta receptor signaling pathway; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; neutrophil degranulation; negative regulation of transcription from RNA polymerase II promoter in response to stress; protein refolding; positive regulation of microtubule nucleation; regulation of mitotic spindle assembly; mRNA catabolic process; response to unfolded protein; negative regulation of cell population proliferation; negative regulation of cell growth; negative regulation of apoptotic process; protein stabilization; chaperone-mediated protein complex assembly; positive regulation of RNA splicing; Unfolded Protein Response; positive regulation of erythrocyte differentiation; chaperone cofactor-dependent protein refolding; lysosomal transport; response to heat; telomere maintenance; DNA repair;
	Sources:Amigo / QuickGO
Orthologs
	3304
	193740
ENSG00000232804; ENSG00000224501; ENSG00000212866; ENSG00000204388; ENSG00000231555;
	n/a
	ENSMUSG00000091971
	P0DMV8; P0DMV9
	Q61696
	NM_005346
	NM_010479
	NP_005337; NP_005336; NP_005336; NP_005336.3; NP_005337.2
	NP_034609
	Wikidata
View/Edit Human	View/Edit Mouse

Human gene HSPA1B is an intron-less gene which encodes for the heat shock protein HSP70-2, a member of the Hsp70 family of proteins.^[5] The gene is located in the major histocompatibility complex, on the short arm of chromosome 6, in a cluster with two paralogous genes, HSPA1A and HSPA1L.^[6]^[7]^[8] HSPA1A and HSPA1B produce nearly identical proteins because the few differences in their DNA sequences are almost exclusively synonymous substitutions or in the three prime untranslated region, heat shock 70kDa protein 1A, from HSPA1A, and heat shock 70kDa protein 1B, from HSPA1B.^[6] A third, more modified paralog to these genes exists in the same region, HSPA1L, which shares a 90% homology with the other two.^[8]

^ ^a ^b ^c ENSG00000224501, ENSG00000212866, ENSG00000204388, ENSG00000231555 GRCh38: Ensembl release 89: ENSG00000232804, ENSG00000224501, ENSG00000212866, ENSG00000204388, ENSG00000231555 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000091971 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Milner CM, Campbell RD (1990). "Structure and expression of the three MHC-linked HSP70 genes". Immunogenetics. 32 (4): 242–251. doi:10.1007/BF00187095. PMID 1700760. S2CID 9531492.
^ ^a ^b "Entrez Gene: HSPA1A heat shock 70kDa protein 1B".
^ Ito Y, Ando A, Ando H, Ando J, Saijoh Y, Inoko H, Fujimoto H (August 1998). "Genomic structure of the spermatid-specific hsp70 homolog gene located in the class III region of the major histocompatibility complex of mouse and man". Journal of Biochemistry. 124 (2): 347–353. doi:10.1093/oxfordjournals.jbchem.a022118. PMID 9685725.
^ ^a ^b Sargent CA, Dunham I, Trowsdale J, Campbell RD (March 1989). "Human major histocompatibility complex contains genes for the major heat shock protein HSP70". Proceedings of the National Academy of Sciences of the United States of America. 86 (6): 1968–1972. Bibcode:1989PNAS...86.1968S. doi:10.1073/pnas.86.6.1968. PMC 286826. PMID 2538825.

[refGRCh38Ensembl-1] ENSG00000224501, ENSG00000212866, ENSG00000204388, ENSG00000231555 GRCh38: Ensembl release 89: ENSG00000232804, ENSG00000224501, ENSG00000212866, ENSG00000204388, ENSG00000231555 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000091971 – 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.

[pmid1700760-5] Milner CM, Campbell RD (1990). "Structure and expression of the three MHC-linked HSP70 genes". Immunogenetics. 32 (4): 242–251. doi:10.1007/BF00187095. PMID 1700760. S2CID 9531492.

[entrez-6] "Entrez Gene: HSPA1A heat shock 70kDa protein 1B".

[pmid9685725-7] Ito Y, Ando A, Ando H, Ando J, Saijoh Y, Inoko H, Fujimoto H (August 1998). "Genomic structure of the spermatid-specific hsp70 homolog gene located in the class III region of the major histocompatibility complex of mouse and man". Journal of Biochemistry. 124 (2): 347–353. doi:10.1093/oxfordjournals.jbchem.a022118. PMID 9685725.

[Sargent_1989-8] Sargent CA, Dunham I, Trowsdale J, Campbell RD (March 1989). "Human major histocompatibility complex contains genes for the major heat shock protein HSP70". Proceedings of the National Academy of Sciences of the United States of America. 86 (6): 1968–1972. Bibcode:1989PNAS...86.1968S. doi:10.1073/pnas.86.6.1968. PMC 286826. PMID 2538825.

HSPA1B information

and 6 Related for: HSPA1B information

HSPA1B

Hsp70

Topoisomerase

Heat shock protein

FAM149B1

HSPA1L