Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0001378
UniProt IDP11142
Primary gene name(s)HSPA8
Synonym gene name(s)HSC70, HSP73, HSPA10
Protein nameHeat shock cognate 71 kDa protein
Protein functionActs as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. Binds bacterial lipopolysaccharide, LPS et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Participates in the ER-associated degradation, ERAD quality control pathway in conjunction with J domain-containing co-chaperones and the E3 ligase CHIP. {ECO:0000269|PubMed:10722728, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:23990462}.
Subcellular locationCytoplasm. Melanosome. Nucleus, nucleolus. Cell membrane. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Translocates rapidly from the cytoplasm to the nuclei, and especially to the nucleoli, upon heat shock.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: P11142
Gene Ontology
(Biological Process)
Complete annatation
ATP metabolic process [GO:0046034];
cellular response to starvation [GO:0009267];
chaperone-mediated autophagy [GO:0061684];
chaperone-mediated autophagy translocation complex disassembly [GO:1904764];
chaperone mediated protein folding requiring cofactor [GO:0051085];
chaperone-mediated protein transport involved in chaperone-mediated autophagy [GO:0061741];
clathrin coat disassembly [GO:0072318];
late endosomal microautophagy [GO:0061738];
mRNA splicing, via spliceosome [GO:0000398];
negative regulation of fibril organization [GO:1902904];
negative regulation of transcription, DNA-templated [GO:0045892];
neurotransmitter secretion [GO:0007269];
positive regulation by host of viral genome replication [GO:0044829];
positive regulation of mRNA splicing, via spliceosome [GO:0048026];
protein folding [GO:0006457];
protein refolding [GO:0042026];
protein targeting to lysosome involved in chaperone-mediated autophagy [GO:0061740];
regulation of cell cycle [GO:0051726];
regulation of cellular response to heat [GO:1900034];
regulation of mRNA stability [GO:0043488];
regulation of protein complex assembly [GO:0043254];
regulation of protein complex stability [GO:0061635];
regulation of protein import [GO:1904589];
regulation of protein stability [GO:0031647];
response to unfolded protein [GO:0006986];
transcription, DNA-templated [GO:0006351];
viral process [GO:0016032]
Gene Ontology
(Molecular Function)
Complete annatation
ATPase activity [GO:0016887];
ATPase activity, coupled [GO:0042623];
ATP binding [GO:0005524];
C3HC4-type RING finger domain binding [GO:0055131];
enzyme binding [GO:0019899];
G-protein coupled receptor binding [GO:0001664];
heat shock protein binding [GO:0031072];
MHC class II protein complex binding [GO:0023026];
phosphatidylserine binding [GO:0001786];
poly(A RNA binding [GO:0044822];
ubiquitin protein ligase binding [GO:0031625];
unfolded protein binding [GO:0051082]
Gene Ontology
(Cellular Component)
Complete annatation
blood microparticle [GO:0072562];
clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane [GO:0061202];
cytosol [GO:0005829];
extracellular exosome [GO:0070062];
extracellular space [GO:0005615];
focal adhesion [GO:0005925];
intracellular [GO:0005622];
intracellular ribonucleoprotein complex [GO:0030529];
late endosome [GO:0005770];
lumenal side of lysosomal membrane [GO:0098575];
lysosomal lumen [GO:0043202];
lysosomal membrane [GO:0005765];
melanosome [GO:0042470];
membrane [GO:0016020];
myelin sheath [GO:0043209];
nucleolus [GO:0005730];
nucleoplasm [GO:0005654];
nucleus [GO:0005634];
plasma membrane [GO:0005886];
presynapse [GO:0098793];
Prp19 complex [GO:0000974];
spliceosomal complex [GO:0005681]
Protein-protein interaction109544
Phylogenetic treeP11142
HIV replication factor status Zhou et al., Cell. Host. Microbe., 2008
      unknown
Brass et al., Science, 2008
      unknown
Smith et al., J. Immunol, 2010
      unknown
Interferon-stimulated
gene status
Lu et al., J. Virol., 2011
      Folds changes 8h: unknown; Folds changes 16h: unknown; Tested: unknown;
Schoggins JW and Rice CM, Curr. Opin. Virol., 2011
      Targeted viruses: unknown
      Viral life cycle: unknown
      Mechanism related to antiviral activity: unknown
Anti-viral restriction factor Liu et al., Retrovirology, 2011
      unknown (Triplicates)

Gene Expression Profile       top

            Up-regulated;            Down-regulated

For brief introduction to each study, please go to the help page.

Gene expression during HIV latency

(1). Mohammadi et al., PLoS Pathog., 2014

Differentially expressed transcripts (Pairwise) during latency and subsequent viral reactivation using several agents - Primary CD4+ T-cell based model


DMSO: Dimethyl suloxyde (negative control) - 0.0033% final
SAHA: Vorinostat (Histone deacetylase inhibitor) - 0.5 μM
CD3: TCR Stimulation by IL-2+ antiCD3/anti-CD28 antibodies
IL7: Interleukin-7 based stimulation
DISU: Disulfiram (alcohol dehydrogenase inhibitor) - 0.5 μM
AZA: 5-azacytidine (AZA; DNA methylation inhibitor) - 1 μM
Experimental Condition Log2 Fold Change P value Adjusted P value
AZA vs. CD31.751044356544869.70511344577929e-066.01709049176411e-05
AZA vs. DISU0.108611797738260.6967502988048660.969258184244663
AZA vs. IL70.4330596324678350.06584489444783140.733903899656133
AZA vs. SAHA-0.2158388989024070.3887200830460460.751398628882884
DISU vs. CD3-1.654313252201780.0001435152429453130.000776507096969726
DISU vs. IL70.3152939531524570.2851431794726450.672591680574263
DISU vs. SAHA-0.3233345586588170.2941312637889790.676978050788593
DMSO vs. AZA-0.07464796897686130.709371704825531
DMSO vs. CD3-1.836806142303343.01594481855183e-061.95504340324799e-05
DMSO vs. DISU-0.1852697860771630.4946128968929740.906292125753013
DMSO vs. IL70.515083189354930.02263829416685940.306623795656249
DMSO vs. SAHA-0.1481315479167360.545193528500460.836211242421171
HIV vs. Mock in Activation-0.0430764938968080.9577782926580770.999983755607037
HIV vs. Mock in Latency-0.01262485433396940.9387712688960740.999834320637052
IL7 vs. CD3-1.310005161643910.0009903466679067610.00420137780055125
SAHA vs. CD3-1.991706813712211.78210490764386e-061.36465045519273e-05
SAHA vs. IL7-0.6522061967589580.01536884121751190.0845510629608667
(2). Iglesias-Ussel et al., J. Virol., 2013

Up and Downregulated transcripts during Latency (Latently infected CD4+ T cells vs Uninfected)- Primary CD4+Tcell based model
Log2 Fold Change P Value
unknown unknown

Gene expression during HIV infection and replication

(1). Imbeault et al., PloS Pathog., 2012

Transcriptomic profiling of HIV-1 infected CD4+ T cells - Primary CD4+ T cells
Experiment type Log2 Fold Change P Value Adjusted P Value
Infected vs. Mock unknown unknown unknown
Infected vs. Bystander unknown unknown unknown
(2). Lefebvre et al., J. Virol., 2011

Transcriptome analysis of T-cell line (Sup T1)
Log2 Fold Change -1.278633514
(3). Li et al., J. Immunol., 2013

Lymphatic tissue
Acute Fold Change Acute P Value Asymt Fold Change Asypt P Value AIDS Fold Change AIDS P Value
unknown unknown unknown unknown unknown unknown
(4). Chang et al., MBio., 2011

Transcriptome analysis of T-cell line (Sup T1)

Derived from Sherrill-Mix et al., BMC Retrovirol., 2015 cross validation
Up-regulated (True) FALSE
(5). Sherrill-Mix et al., BMC Retrovirol., 2015

Deep RNA-seq analysis of primary human T cell infected with low passage HIV isolate HIV89.6 - Primary CD4+ T cell based
Test Status Log2 Fold Change P Value
OK 0.068923 0.742025
(6). Rotger et al., PLoS Pathog., 2010

Genome-wide mRNA expression of CD4+ T cells from HIV-infected patient
(Genes differentially expressed (at adjusted p<0.01) according to the empirical Bayes approach)
Log2 Fold Change P Value
unknown unknown

Proteomic/Transcriptomics studies indicating differentially expressed genes mediated by HIV

(1). Greenwood et al., Elife, 2016

Activated (CD3/CD28) Primary human CD4+ T cells infected with pNL4-3-dE-EGFP. The table shows the complete (unfiltered) TMT (tandem mass tag)-based proteomic time course dataset
6 h 24 h 48 h 72 h RTi
0.967 0.973 0.942 0.959 0.991
(2). Navare et al., Virology, 2012

SUP-T1 cell line
FC-4hpi P-value FC-8hpi P-value FC-20hpi P-value Category
unknown unknown unknown unknown unknown unknown unknown
(3). Hyrcza et al., J. Virolo., 2007

Primary human CD4+ and CD8+ T Cells
Affymetrix Prob ID Fold Change In CD8? Category
unknown unknown unknown unknown

Protein Overview       top

Drug-protein Interaction       (annotations from DrugBank)      top

Drugbank ID Drug Name Drug Status Pharmacological Action Drug Action
DB07045 (2R,3R,4S,5R)-2-[6-amino-8-[(3,4-dichlorophenyl)methylamino]purin-9-yl]-5-(hydroxymethyl)oxolane-3,4-diol experimental unknown unknown

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
3AGY X-ray 1.8Å C/D/F=639-646.
3AGZ X-ray 2.5Å C/D/E/F=639-646.
3ESK X-ray 2.0Å B=635-646.
3FZF X-ray 2.2Å A=4-381.
3FZH X-ray 2.0Å A=4-381.
3FZK X-ray 2.1Å A=4-381.
3FZL X-ray 2.2Å A=4-381.
3FZM X-ray 2.3Å A=4-381.
3LDQ X-ray 1.9Å A=4-381.
3M3Z X-ray 2.1Å A=4-381.
4H5N X-ray 1.8Å A/B=2-384.
4H5R X-ray 1.6Å A/B=2-384.
4H5T X-ray 1.9Å A=2-384.
4H5V X-ray 1.7Å A=2-384.
4H5W X-ray 1.9Å A/B=2-384.
4HWI X-ray 2.2Å A=5-381.
4KBQ X-ray 2.9Å C/D=541-646.
5AQF X-ray 1.8Å A/C=1-381.
5AQG X-ray 2.2Å A/C/E=1-381.
5AQH X-ray 2.0Å A=1-381.
5AQI X-ray 1.9Å A/C=1-381.
5AQJ X-ray 1.9Å A/C/E=1-381.
5AQK X-ray 2.0Å A=1-381.
5AQL X-ray 1.6Å A/C=1-381.
5AQM X-ray 1.6Å A/C=1-381.
5AQN X-ray 2.4Å A/C/E=1-381.
5AQO X-ray 2.1Å A/C/E=1-381.
5AQP X-ray 2.0Å A/C/E=1-381.
5AQQ X-ray 2.7Å A/C/E=1-381.
5AQR X-ray 1.9Å A/C/E=1-381.
5AQS X-ray 2.0Å A/C=1-381.
5AQT X-ray 1.9Å A=1-381.
5AQU X-ray 1.9Å A=1-381.
5AQV X-ray 1.7Å A=1-381.

HIV-1 Interaction       (annotations from NCBI HIV-1 Interaction Database)      top

HIV Partner Interaction Type PubMed
Pr55(Gag) incorporates 11932435
21738476
Gag-Pol complexes with 23125841
Nef interacts with 21763498
Nef complexes with 23125841
Tat interacts with 25496916
Vpr interacts with 21763498
Nef co-localizes with 19912576
Envelope surface glycoprotein gp120 complexes with 23125841
Envelope surface glycoprotein gp120 inhibited by 12832005
Pr55(Gag) complexes with 23125841
Vpr competes with 10964507
19275587
Tat regulated by 10617616
Envelope surface glycoprotein gp120 upregulates 7906708
matrix stimulated by 10964507

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa03040 Spliceosome - Homo sapiens (human)
hsa04010 MAPK signaling pathway - Homo sapiens (human)
hsa04141 Protein processing in endoplasmic reticulum - Homo sapiens (human)
hsa04144 Endocytosis - Homo sapiens (human)
hsa04213 Longevity regulating pathway - multiple species - Homo sapiens (human)
hsa04612 Antigen processing and presentation - Homo sapiens (human)
hsa04915 Estrogen signaling pathway - Homo sapiens (human)
hsa05134 Legionellosis - Homo sapiens (human)
hsa05145 Toxoplasmosis - Homo sapiens (human)
hsa05162 Measles - Homo sapiens (human)
hsa05164 Influenza A - Homo sapiens (human)
hsa05169 Epstein-Barr virus infection - Homo sapiens (human)
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