Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0002436
UniProt IDP62826
Primary gene name(s)RAN
Synonym gene name(s)ARA24
Protein nameGTP-binding nuclear protein Ran
Protein functionGTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensure the directionality of the transport. {ECO:0000269|PubMed:8692944, ECO:0000269|PubMed:9822603}.; FUNCTION: The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules, PubMed:18591255. Acts as a negative regulator of the kinase activity of VRK1 and VRK2, PubMed:18617507. Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases, PubMed:10400640. {ECO:0000269|PubMed:10400640, ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:18617507}.
Subcellular locationNucleus {ECO:0000269|PubMed:9822603}. Nucleus envelope {ECO:0000269|PubMed:9822603}. Cytoplasm {ECO:0000269|PubMed:9822603}. Melanosome {ECO:0000250|UniProtKB:P62827}. Note=Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000250|UniProtKB:P62827}.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: P62826
Gene Ontology
(Biological Process)
Complete annatation
actin cytoskeleton organization [GO:0030036];
androgen receptor signaling pathway [GO:0030521];
cell division [GO:0051301];
cellular protein complex localization [GO:0034629];
DNA metabolic process [GO:0006259];
gene silencing by RNA [GO:0031047];
intracellular transport of virus [GO:0075733];
mitotic nuclear division [GO:0007067];
mitotic spindle organization [GO:0007052];
positive regulation of protein binding [GO:0032092];
positive regulation of transcription, DNA-templated [GO:0045893];
pre-miRNA export from nucleus [GO:0035281];
protein export from nucleus [GO:0006611];
protein import into nucleus [GO:0006606];
protein import into nucleus, translocation [GO:0000060];
protein localization to nucleolus [GO:1902570];
protein transmembrane transport [GO:0071806];
ribosomal large subunit export from nucleus [GO:0000055];
ribosomal small subunit export from nucleus [GO:0000056];
signal transduction [GO:0007165];
small GTPase mediated signal transduction [GO:0007264];
tRNA export from nucleus [GO:0006409];
viral process [GO:0016032]
Gene Ontology
(Molecular Function)
Complete annatation
androgen receptor binding [GO:0050681];
chromatin binding [GO:0003682];
GDP binding [GO:0019003];
GTPase activity [GO:0003924];
GTP binding [GO:0005525];
poly(A RNA binding [GO:0044822];
transcription coactivator activity [GO:0003713]
Gene Ontology
(Cellular Component)
Complete annatation
centriole [GO:0005814];
cytoplasm [GO:0005737];
cytosol [GO:0005829];
extracellular exosome [GO:0070062];
male germ cell nucleus [GO:0001673];
manchette [GO:0002177];
melanosome [GO:0042470];
membrane [GO:0016020];
midbody [GO:0030496];
nuclear pore [GO:0005643];
nucleolus [GO:0005730];
nucleoplasm [GO:0005654];
nucleus [GO:0005634];
recycling endosome [GO:0055037];
RNA nuclear export complex [GO:0042565];
sperm flagellum [GO:0036126]
Protein-protein interaction111837
Phylogenetic treeP62826
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. CD32.419250486630292.10786943455332e-124.79182626207959e-11
AZA vs. DISU-0.05010856586122110.8427400014021110.987248816652333
AZA vs. IL70.5006600939965590.009178438118477520.306549179619533
AZA vs. SAHA-0.3454320389961020.156887670265560.504463468767716
DISU vs. CD3-2.481812901043138.58829674044159e-112.12229483713798e-09
DISU vs. IL70.5414614721618690.03180387938279750.231839207783207
DISU vs. SAHA-0.2933854186690850.3150543166556270.697749244131808
DMSO vs. AZA0.04316379421208340.7960489137976121
DMSO vs. CD3-2.387937570620471.15418785640031e-122.49825288170556e-11
DMSO vs. DISU0.0912099739155870.7080972904163730.960763093481455
DMSO vs. IL70.4648526059976840.009661896644976740.205434544320204
DMSO vs. SAHA-0.3945091515372550.09447173396369860.360983931819873
HIV vs. Mock in Activation-0.09198737034730680.8823090465888870.999983755607037
HIV vs. Mock in Latency-0.08867226107338970.5906287703517440.999834320637052
IL7 vs. CD3-1.911405198367098.21710743892368e-091.23980440867764e-07
SAHA vs. CD3-2.788337511401711.3855583347322e-134.87858974402201e-12
SAHA vs. IL7-0.8484784421428440.0005314148906770950.00721670996582571
(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
-0.4433 0.02159

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 -1.400282495
(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
1.8 0.000163286 1.2 0.07599545 1.2 0.289323598
(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 0.368502 0.00622456
(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
1.012 0.948 0.899 0.851 0.955
(2). Navare et al., Virology, 2012

SUP-T1 cell line
FC-4hpi P-value FC-8hpi P-value FC-20hpi P-value Category
0.73 0.0001 -0.1 0.443 -0.17 0.2036 DNA recombination; repair and maintenance (4hpi)
(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
DB04315 Guanosine-5&,39;-Diphosphate experimental unknown unknown

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
1I2M X-ray 1.7Å A/C=1-216.
1IBR X-ray 2.3Å A/C=1-216.
1K5D X-ray 2.7Å A/D/G/J=1-216.
1K5G X-ray 3.1Å A/D/G/J=1-216.
1QBK X-ray 3.0Å C=1-216.
1RRP X-ray 2.9Å A/C=8-211.
2MMC NMR - A=1-216.
2MMG NMR - A=1-216.
2N1B NMR - A=1-216.
3CH5 X-ray 2.1Å A=1-216.
3EA5 X-ray 2.5Å A/C=1-216.
3GJ0 X-ray 1.4Å A/B=2-216.
3GJ3 X-ray 1.7Å A=2-216.
3GJ4 X-ray 2.1Å A/C=2-216.
3GJ5 X-ray 1.7Å A/C=2-216.
3GJ6 X-ray 2.7Å A=2-216.
3GJ7 X-ray 1.9Å A/C=2-216.
3GJ8 X-ray 1.8Å A/C=2-216.
3GJX X-ray 2.5Å C/F=1-216.
3NBY X-ray 3.4Å C/F=5-180.
3NBZ X-ray 2.8Å C/F=5-180.
3NC0 X-ray 2.9Å C/F=5-180.
3NC1 X-ray 3.3Å C=1-180.
3ZJY X-ray 3.6Å A/D/F=1-180.
4C0Q X-ray 3.4Å C/D=2-216.
4GMX X-ray 2.1Å A=1-216.
4GPT X-ray 2.2Å A=1-216.
4HAT X-ray 1.7Å A=1-216.
4HAU X-ray 2.0Å A=1-216.
4HAV X-ray 2.0Å A=1-216.
4HAW X-ray 1.9Å A=1-216.
4HAX X-ray 2.2Å A=1-216.
4HAY X-ray 2.3Å A=1-216.
4HAZ X-ray 1.9Å A=1-216.
4HB0 X-ray 2.2Å A=1-216.
4HB2 X-ray 1.8Å A=1-216.
4HB3 X-ray 2.8Å A=1-216.
4HB4 X-ray 2.0Å A=1-216.
4OL0 X-ray 2.9Å A=1-216.
4WVF X-ray 1.8Å A=1-216.
5CIQ X-ray 1.6Å A/B=1-216.
5CIT X-ray 1.7Å A/B=1-216.
5CIW X-ray 1.7Å A/B=1-216.
5CJ2 X-ray 1.7Å A/B/C/D/E/F/G/H=1-216.
5CLL X-ray 2.4Å A/C=1-191.
5CLQ X-ray 3.2Å A/C=1-216.
5DH9 X-ray 2.5Å A=1-216.
5DHA X-ray 2.9Å A=1-216.
5DHF X-ray 2.2Å A=1-216.
5DI9 X-ray 2.2Å A=1-216.
5DIF X-ray 2.0Å A=1-216.
5DIS X-ray 2.8Å B=8-179.
5DLQ X-ray 3.2Å C/D=5-180.
5FYQ X-ray 3.0Å C/D=31-43.
5JLJ X-ray 2.5Å A=1-216.

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

HIV Partner Interaction Type PubMed
Rev interacts with 22174317
Rev enhanced by 12134013
18508616
Envelope surface glycoprotein gp120 complexes with 23125841
Rev binds 25486595
9837918
10518602
18508616
19149559
21358275
22355797
22783232
24530126
25486594
25486595
25564443
257231789837918
18508616
19149559
22783232
Gag-Pol complexes with 23125841
integrase inhibited by 23878195
matrix regulated by 9562972
Pr55(Gag) regulated by 9562972
Pr55(Gag) complexes with 23125841
capsid inhibited by 23097435
Tat interacts with 19454010
Nef complexes with 23125841

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa03008 Ribosome biogenesis in eukaryotes - Homo sapiens (human)
hsa03013 RNA transport - Homo sapiens (human)
hsa05166 HTLV-I infection - Homo sapiens (human)
hsa05169 Epstein-Barr virus infection - Homo sapiens (human)
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