Descriptions

HSPA8 (or hsc70) is a heat shock cognate protein involved in many cellular processes. During recovery from stress, HSPA8, initially accumulating in the nucleoplasm for folding/refolding of proteins, transiently concentrates in nucleoli for nucleolar morphology and function restoration. The inhibitory region is positioned at one of the three domains of HSPA8 protein, which is the N-terminal ATPase domain, specifically in residues 263-287 of domain IIB. Under normal growth conditions, the constitutive nucleolar targeting function that is provided by residues 225-262 is diminished by the autoinhibitory element located in residues 263-287. When cells recover from stress, the autoinhibitory element is inactivated, and the constitutive nucleolar targeting function restores.

Autoinhibitory domains (AIDs)

Target domain

225-262 (Nucleolar targeting region)

Relief mechanism

Others

Assay

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P11147

Entry ID Method Resolution Chain Position Source
AF-P11147-F1 Predicted AlphaFoldDB

No variants for P11147

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P11147

No associated diseases with P11147

3 regional properties for P11147

Type Name Position InterPro Accession
domain NB-ARC 164 - 410 IPR002182
domain Virus X resistance protein-like, coiled-coil domain 8 - 120 IPR038005
domain Rx, N-terminal 10 - 87 IPR041118

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, perinuclear region
  • Nucleus
  • Localized to a meshwork of cytoplasmic fibers around the nucleus
  • Translocates to the nucleus after thermal stress
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

8 GO annotations of cellular component

Name Definition
catalytic step 2 spliceosome A spliceosomal complex that contains three snRNPs, including U5, bound to a splicing intermediate in which the first catalytic cleavage of the 5' splice site has occurred. The precise subunit composition differs significantly from that of the catalytic step 1, or activated, spliceosome, and includes many proteins in addition to those found in the associated snRNPs.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.
perinuclear region of cytoplasm Cytoplasm situated near, or occurring around, the nucleus.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
precatalytic spliceosome A spliceosomal complex that is formed by the recruitment of a preassembled U5-containing tri-snRNP to the prespliceosome. Although all 5 snRNPs are present, the precatalytic spliceosome is catalytically inactive. The precatalytic spliceosome includes many proteins in addition to those found in the associated snRNPs.
presynapse The part of a synapse that is part of the presynaptic cell.

6 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
ATP hydrolysis activity Catalysis of the reaction
ATP-dependent protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process, driven by ATP hydrolysis.
heat shock protein binding Binding to a heat shock protein, a protein synthesized or activated in response to heat shock.
protein folding chaperone Binding to a protein or a protein-containing complex to assist the protein folding process.
protein-folding chaperone binding Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.

16 GO annotations of biological process

Name Definition
axon guidance The chemotaxis process that directs the migration of an axon growth cone to a specific target site in response to a combination of attractive and repulsive cues.
axonal fasciculation The collection of axons into a bundle of rods, known as a fascicle.
cellular response to topologically incorrect protein Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a protein that is not folded in its correct three-dimensional structure.
chaperone cofactor-dependent protein refolding The process of assisting in the correct posttranslational noncovalent assembly of proteins, which is dependent on additional protein cofactors. This process occurs over one or several cycles of nucleotide hydrolysis-dependent binding and release.
chaperone-mediated protein folding The process of inhibiting aggregation and assisting in the covalent and noncovalent assembly of single chain polypeptides or multisubunit complexes into the correct tertiary structure that is dependent on interaction with a chaperone.
follicle cell of egg chamber development The process that occurs during oogenesis involving the ovarian follicle cells, somatic cells which surround the germ cells of an ovary. An example of this is found in Drosophila melanogaster.
late endosomal microautophagy The autophagy process by which cytosolic proteins targeted for degradation are tagged with a chaperone and are directly transferred into and degraded in a late endosomal compartment.
membrane bending A membrane organization process resulting in the bending of a membrane.
mRNA splicing, via spliceosome The joining together of exons from one or more primary transcripts of messenger RNA (mRNA) and the excision of intron sequences, via a spliceosomal mechanism, so that mRNA consisting only of the joined exons is produced.
nervous system development The process whose specific outcome is the progression of nervous tissue over time, from its formation to its mature state.
neurotransmitter secretion The regulated release of neurotransmitter from the presynapse into the synaptic cleft via calcium-regulated exocytosis during synaptic transmission.
protein refolding The process carried out by a cell that restores the biological activity of an unfolded or misfolded protein, using helper proteins such as chaperones.
regulatory ncRNA-mediated post-transcriptional gene silencing A posttranscriptional gene silencing pathway in which regulatory RNAs elicit silencing of specific target genes, either by mRNA destabilization or inhibition of translation.
RISC complex assembly The process in which a single-stranded small RNA is incorporated within the RNA-initiated silencing complex (RISC). The assembly includes the maturation of the small RNA, the stabilization of the complex by accessory proteins of the RISC complex, duplex separation and the release of the second strand, forming a base-pairing completent complex that mediates gene silencing by small RNA.
SRP-dependent cotranslational protein targeting to membrane, translocation The process during cotranslational membrane targeting wherein proteins move across a membrane. SRP and its receptor initiate the transfer of the nascent chain across the endoplasmic reticulum (ER) membrane; they then dissociate from the chain, which is transferred to a set of transmembrane proteins, collectively called the translocon. Once the nascent chain translocon complex is assembled, the elongating chain passes directly from the large ribosomal subunit into the centers of the translocon, a protein-lined channel within the membrane. The growing chain is never exposed to the cytosol and does not fold until it reaches the ER lumen.
vesicle-mediated transport A cellular transport process in which transported substances are moved in membrane-bounded vesicles; transported substances are enclosed in the vesicle lumen or located in the vesicle membrane. The process begins with a step that directs a substance to the forming vesicle, and includes vesicle budding and coating. Vesicles are then targeted to, and fuse with, an acceptor membrane.

61 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P11484 SSB1 Ribosome-associated molecular chaperone SSB1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
P40150 SSB2 Ribosome-associated molecular chaperone SSB2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
P22202 SSA4 Heat shock protein SSA4 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
P09435 SSA3 Heat shock protein SSA3 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
P10592 SSA2 Heat shock protein SSA2 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
P10591 SSA1 Heat shock protein SSA1 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) SS
Q2YDD0 HSPA14 Heat shock 70 kDa protein 14 Bos taurus (Bovine) SS
P0CB32 HSPA1L Heat shock 70 kDa protein 1-like Bos taurus (Bovine) SS
P19120 HSPA8 Heat shock cognate 71 kDa protein Bos taurus (Bovine) SS
Q27975 HSPA1A Heat shock 70 kDa protein 1A Bos taurus (Bovine) SS
E1C2P3 HSPA14 Heat shock 70 kDa protein 14 Gallus gallus (Chicken) SS
P08106 Heat shock 70 kDa protein Gallus gallus (Chicken) SS
O73885 HSPA8 Heat shock cognate 71 kDa protein Gallus gallus (Chicken) SS
P77319 hscC Chaperone protein HscC Escherichia coli (strain K12) PR
P0A6Y8 dnaK Chaperone protein DnaK Escherichia coli (strain K12) SS
P02825 Hsp70Ab Major heat shock 70 kDa protein Ab Drosophila melanogaster (Fruit fly) SS
P82910 Hsp70Aa Major heat shock 70 kDa protein Aa Drosophila melanogaster (Fruit fly) SS
Q8INI8 Hsp70Ba Major heat shock 70 kDa protein Ba Drosophila melanogaster (Fruit fly) SS
Q9BIR7 Hsp70Bc Major heat shock 70 kDa protein Bc Drosophila melanogaster (Fruit fly) SS
Q9BIS2 Hsp70Bb Major heat shock 70 kDa protein Bb Drosophila melanogaster (Fruit fly) SS
O97125 Hsp68 Heat shock protein 68 Drosophila melanogaster (Fruit fly) SS
P11146 Hsc70-2 Heat shock 70 kDa protein cognate 2 Drosophila melanogaster (Fruit fly) SS
P29843 Hsc70-1 Heat shock 70 kDa protein cognate 1 Drosophila melanogaster (Fruit fly) SS
Q9VG58 Hsp70Bbb Major heat shock 70 kDa protein Bbb Drosophila melanogaster (Fruit fly) SS
A2Q0Z1 HSPA8 Heat shock cognate 71 kDa protein Equus caballus (Horse) SS
Q96MM6 HSPA12B Heat shock 70 kDa protein 12B Homo sapiens (Human) PR
P17066 HSPA6 Heat shock 70 kDa protein 6 Homo sapiens (Human) SS
O43301 HSPA12A Heat shock 70 kDa protein 12A Homo sapiens (Human) PR
Q0VDF9 HSPA14 Heat shock 70 kDa protein 14 Homo sapiens (Human) SS
P54652 HSPA2 Heat shock-related 70 kDa protein 2 Homo sapiens (Human) SS
P0DMV9 HSPA1B Heat shock 70 kDa protein 1B Homo sapiens (Human) SS
P0DMV8 HSPA1A Heat shock 70 kDa protein 1A Homo sapiens (Human) SS
P34931 HSPA1L Heat shock 70 kDa protein 1-like Homo sapiens (Human) SS
P11142 HSPA8 Heat shock cognate 71 kDa protein Homo sapiens (Human) EV
P11143 HSP70 Heat shock 70 kDa protein Zea mays (Maize) SS
Q99M31 Hspa14 Heat shock 70 kDa protein 14 Mus musculus (Mouse) SS
Q8K0U4 Hspa12a Heat shock 70 kDa protein 12A Mus musculus (Mouse) PR
P17156 Hspa2 Heat shock-related 70 kDa protein 2 Mus musculus (Mouse) SS
Q9CZJ2 Hspa12b Heat shock 70 kDa protein 12B Mus musculus (Mouse) PR
P16627 Hspa1l Heat shock 70 kDa protein 1-like Mus musculus (Mouse) SS
P17879 Hspa1b Heat shock 70 kDa protein 1B Mus musculus (Mouse) SS
P63017 Hspa8 Heat shock cognate 71 kDa protein Mus musculus (Mouse) SS
Q61696 Hspa1a Heat shock 70 kDa protein 1A Mus musculus (Mouse) SS
Q6S4N2 HSPA1B Heat shock 70 kDa protein 1B Sus scrofa (Pig) SS
P14659 Hspa2 Heat shock-related 70 kDa protein 2 Rattus norvegicus (Rat) SS
P0DMW0 Hspa1a Heat shock 70 kDa protein 1A Rattus norvegicus (Rat) SS
P0DMW1 Hspa1b Heat shock 70 kDa protein 1B Rattus norvegicus (Rat) SS
P55063 Hspa1l Heat shock 70 kDa protein 1-like Rattus norvegicus (Rat) SS
P63018 Hspa8 Heat shock cognate 71 kDa protein Rattus norvegicus (Rat) SS
P09446 hsp-1 Heat shock protein hsp-1 Caenorhabditis elegans SS
P26413 HSP70 Heat shock 70 kDa protein Glycine max (Soybean) (Glycine hispida) SS
O65719 HSP70-3 Heat shock 70 kDa protein 3 Arabidopsis thaliana (Mouse-ear cress) SS
P22954 HSP70-2 Heat shock 70 kDa protein 2 Arabidopsis thaliana (Mouse-ear cress) SS
Q9C7X7 HSP70-18 Heat shock 70 kDa protein 18 Arabidopsis thaliana (Mouse-ear cress) SS
Q9LHA8 HSP70-4 Heat shock 70 kDa protein 4 Arabidopsis thaliana (Mouse-ear cress) SS
Q9S9N1 HSP70-5 Heat shock 70 kDa protein 5 Arabidopsis thaliana (Mouse-ear cress) SS
P22953 HSP70-1 Heat shock 70 kDa protein 1 Arabidopsis thaliana (Mouse-ear cress) SS
P24629 HSC-I Heat shock cognate 70 kDa protein 1 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) SS
P27322 HSC-2 Heat shock cognate 70 kDa protein 2 Solanum lycopersicum (Tomato) (Lycopersicon esculentum) SS
Q5RGE6 hspa14 Heat shock 70 kDa protein 14 Danio rerio (Zebrafish) (Brachydanio rerio) SS
Q90473 hspa8 Heat shock cognate 71 kDa protein Danio rerio (Zebrafish) (Brachydanio rerio) SS
10 20 30 40 50 60
MSKAPAVGID LGTTYSCVGV FQHGKVEIIA NDQGNRTTPS YVAFTDTERL IGDAAKNQVA
70 80 90 100 110 120
MNPTQTIFDA KRLIGRKFDD AAVQSDMKHW PFEVVSADGK PKIEVTYKDE KKTFFPEEIS
130 140 150 160 170 180
SMVLTKMKET AEAYLGKTVT NAVITVPAYF NDSQRQATKD AGTIAGLNVL RIINEPTAAA
190 200 210 220 230 240
IAYGLDKKAV GERNVLIFDL GGGTFDVSIL SIDDGIFEVK STAGDTHLGG EDFDNRLVTH
250 260 270 280 290 300
FVQEFKRKHK KDLTTNKRAL RRLRTACERA KRTLSSSTQA SIEIDSLFEG TDFYTSITRA
310 320 330 340 350 360
RFEELNADLF RSTMDPVEKA LRDAKLDKSV IHDIVLVGGS TRIPKVQRLL QDLFNGKELN
370 380 390 400 410 420
KSINPDEAVA YGAAVQAAIL HGDKSQEVQD LLLLDVTPLS LGIETAGGVM SVLIKRNTTI
430 440 450 460 470 480
PTKQTQTFTT YSDNQPGVLI QVYEGERAMT KDNNLLGKFE LSGIPPAPRG VPQIEVTFDI
490 500 510 520 530 540
DANGILNVTA LERSTNKENK ITITNDKGRL SKEDIERMVN EAEKYRNEDE KQKETIAAKN
550 560 570 580 590 600
GLESYCFNMK ATLDEDNLKT KISDSDRTTI LDKCNETIKW LDANQLADKE EYEHRQKELE
610 620 630 640 650
GVCNPIITKL YQGAGFPPGG MPGGPGGMPG AAGAAGAAGA GGAGPTIEEV D