Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0004072
UniProt IDP27797
Primary gene name(s)CALR
Synonym gene name(s)CRTC
Protein nameCalreticulin
Protein functionCalcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum, ER via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis, By similarity. {ECO:0000250, ECO:0000269|PubMed:11149926, ECO:0000269|PubMed:7876246}.
Subcellular locationEndoplasmic reticulum lumen {ECO:0000269|PubMed:10358038, ECO:0000269|PubMed:11149926}. Cytoplasm, cytosol {ECO:0000269|PubMed:11149926}. Secreted, extracellular space, extracellular matrix {ECO:0000305}. Cell surface {ECO:0000269|PubMed:10358038}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P28491}. Note=Also found in cell surface, T cells, cytosol and extracellular matrix, PubMed:10358038. Associated with the lytic granules in the cytolytic T-lymphocytes. {ECO:0000269|PubMed:10358038, ECO:0000269|PubMed:8418194}.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: P27797
Gene Ontology
(Biological Process)
Complete annatation
antigen processing and presentation of peptide antigen via MHC class I [GO:0002474];
ATF6-mediated unfolded protein response [GO:0036500];
cardiac muscle cell differentiation [GO:0055007];
cellular calcium ion homeostasis [GO:0006874];
cellular response to lithium ion [GO:0071285];
cellular senescence [GO:0090398];
chaperone-mediated protein folding [GO:0061077];
cortical actin cytoskeleton organization [GO:0030866];
glucocorticoid receptor signaling pathway [GO:0042921];
negative regulation of cell cycle arrest [GO:0071157];
negative regulation of intracellular steroid hormone receptor signaling pathway [GO:0033144];
negative regulation of neuron differentiation [GO:0045665];
negative regulation of retinoic acid receptor signaling pathway [GO:0048387];
negative regulation of transcription, DNA-templated [GO:0045892];
negative regulation of transcription from RNA polymerase II promoter [GO:0000122];
negative regulation of translation [GO:0017148];
peptide antigen assembly with MHC class I protein complex [GO:0002502];
positive regulation of cell cycle [GO:0045787];
positive regulation of cell proliferation [GO:0008284];
positive regulation of dendritic cell chemotaxis [GO:2000510];
positive regulation of DNA replication [GO:0045740];
positive regulation of gene expression [GO:0010628];
positive regulation of NIK/NF-kappaB signaling [GO:1901224];
positive regulation of phagocytosis [GO:0050766];
positive regulation of substrate adhesion-dependent cell spreading [GO:1900026];
protein export from nucleus [GO:0006611];
protein folding [GO:0006457];
protein folding in endoplasmic reticulum [GO:0034975];
protein localization to nucleus [GO:0034504];
protein maturation by protein folding [GO:0022417];
protein stabilization [GO:0050821];
receptor-mediated endocytosis [GO:0006898];
regulation of apoptotic process [GO:0042981];
regulation of meiotic nuclear division [GO:0040020];
regulation of transcription, DNA-templated [GO:0006355];
response to drug [GO:0042493];
response to estradiol [GO:0032355];
response to testosterone [GO:0033574];
sequestering of calcium ion [GO:0051208];
spermatogenesis [GO:0007283]
Gene Ontology
(Molecular Function)
Complete annatation
androgen receptor binding [GO:0050681];
calcium ion binding [GO:0005509];
carbohydrate binding [GO:0030246];
chaperone binding [GO:0051087];
complement component C1q binding [GO:0001849];
DNA binding [GO:0003677];
glycoprotein binding [GO:0001948];
hormone binding [GO:0042562];
integrin binding [GO:0005178];
iron ion binding [GO:0005506];
mRNA binding [GO:0003729];
peptide binding [GO:0042277];
poly(A RNA binding [GO:0044822];
protein binding involved in protein folding [GO:0044183];
ubiquitin protein ligase binding [GO:0031625];
unfolded protein binding [GO:0051082];
zinc ion binding [GO:0008270]
Gene Ontology
(Cellular Component)
Complete annatation
acrosomal vesicle [GO:0001669];
cell surface [GO:0009986];
cytoplasm [GO:0005737];
cytosol [GO:0005829];
endocytic vesicle lumen [GO:0071682];
endoplasmic reticulum [GO:0005783];
endoplasmic reticulum lumen [GO:0005788];
external side of plasma membrane [GO:0009897];
extracellular exosome [GO:0070062];
extracellular region [GO:0005576];
extracellular space [GO:0005615];
focal adhesion [GO:0005925];
Golgi apparatus [GO:0005794];
integral component of lumenal side of endoplasmic reticulum membrane [GO:0071556];
intracellular [GO:0005622];
membrane [GO:0016020];
MHC class I peptide loading complex [GO:0042824];
nucleus [GO:0005634];
perinuclear region of cytoplasm [GO:0048471];
polysome [GO:0005844];
proteinaceous extracellular matrix [GO:0005578];
sarcoplasmic reticulum lumen [GO:0033018];
smooth endoplasmic reticulum [GO:0005790]
Protein-protein interaction107262
Phylogenetic treeP27797
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. CD30.9552136721750180.003917714174161420.0118284831796797
AZA vs. DISU0.183774814228380.46834578588590.926047745875375
AZA vs. IL70.1836933520318360.337752260023310.999311006273513
AZA vs. SAHA-0.371405661548620.1275706893959750.454395220216194
DISU vs. CD3-0.7827578859783540.03144137072465810.0742980439416048
DISU vs. IL7-0.009799120238899450.9689906061311150.995379686713869
DISU vs. SAHA-0.5529693739910280.05837730685100440.304325282446035
DMSO vs. AZA-0.02608114179464930.8757507345071111
DMSO vs. CD3-0.990922244297180.00216595603921310.00667419262236559
DMSO vs. DISU-0.2113162713388470.4017977021171640.865479453669017
DMSO vs. IL70.2168871691732840.2262009885151020.733329011153799
DMSO vs. SAHA-0.3514429269989440.1355169563677230.441213231673784
HIV vs. Mock in Activation0.09496197707937280.878561618025460.999983755607037
HIV vs. Mock in Latency-0.1615789550435470.4909791557764840.999834320637052
IL7 vs. CD3-0.7654209881413670.01795638170053440.0479887484702402
SAHA vs. CD3-1.349825956611390.0001735202254310450.00077802731248017
SAHA vs. IL7-0.5573358303474690.0221707474574040.107419369490482
(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 unknown
(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) unknown
(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 0.390001 0.00261319
(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
1.007 1.016 1.09 1.141 1.167
(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
DB00025 Antihemophilic Factor (Recombinant) approved, investigational unknown chaperone
DB00031 Tenecteplase approved unknown unknown
DB01065 Melatonin approved, nutraceutical, vet_approved unknown unknown

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
2CLR X-ray 2.0Å C/F=1-10.
3DOW X-ray 2.3Å B=195-205.
3POS X-ray 1.6Å A/B/C=18-204# A/B/C=302-368.
3POW X-ray 1.5Å A=18-204# A=302-368.
5LK5 X-ray 2.3Å A/B/C/D/E/F/G/H/I/J=18-204# A/B/C/D/E/F/G/H/I/J=303-368.

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

HIV Partner Interaction Type PubMed
Rev interacts with 22174317
Envelope surface glycoprotein gp160; precursor binds 8550632
Envelope surface glycoprotein gp160; precursor interacts with 22190034
Envelope surface glycoprotein gp120 interacts with 22190034
Vpr upregulates 23874603

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa04141 Protein processing in endoplasmic reticulum - Homo sapiens (human)
hsa04145 Phagosome - Homo sapiens (human)
hsa04612 Antigen processing and presentation - Homo sapiens (human)
hsa05142 Chagas disease (American trypanosomiasis) - Homo sapiens (human)
hsa05166 HTLV-I infection - Homo sapiens (human)
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