Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0003211
UniProt IDP61088
Primary gene name(s)UBE2N
Synonym gene name(s)BLU
Protein nameUbiquitin-conjugating enzyme E2 N
Protein functionThe UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes. {ECO:0000269|PubMed:10089880, ECO:0000269|PubMed:14562038, ECO:0000269|PubMed:19269966, ECO:0000269|PubMed:20061386, ECO:0000269|PubMed:21512573}.
Subcellular locationNucleus {ECO:0000269|PubMed:19340006}. Cytoplasm {ECO:0000269|PubMed:19340006}.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: P61088
Gene Ontology
(Biological Process)
Complete annatation
cellular protein modification process [GO:0006464];
DNA double-strand break processing [GO:0000729];
double-strand break repair via homologous recombination [GO:0000724];
double-strand break repair via nonhomologous end joining [GO:0006303];
Fc-epsilon receptor signaling pathway [GO:0038095];
global genome nucleotide-excision repair [GO:0070911];
histone ubiquitination [GO:0016574];
nucleotide-binding oligomerization domain containing signaling pathway [GO:0070423];
positive regulation of DNA repair [GO:0045739];
positive regulation of histone modification [GO:0031058];
positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123];
positive regulation of NF-kappaB transcription factor activity [GO:0051092];
positive regulation of ubiquitin-protein transferase activity [GO:0051443];
postreplication repair [GO:0006301];
protein K63-linked ubiquitination [GO:0070534];
protein ubiquitination [GO:0016567];
proteolysis [GO:0006508];
regulation of DNA repair [GO:0006282];
regulation of histone ubiquitination [GO:0033182];
stimulatory C-type lectin receptor signaling pathway [GO:0002223];
T cell receptor signaling pathway [GO:0050852];
ubiquitin-dependent protein catabolic process [GO:0006511]
Gene Ontology
(Molecular Function)
Complete annatation
ATP binding [GO:0005524];
poly(A RNA binding [GO:0044822];
ubiquitin binding [GO:0043130];
ubiquitin conjugating enzyme activity [GO:0061631];
ubiquitin protein ligase activity [GO:0061630];
ubiquitin protein ligase binding [GO:0031625];
ubiquitin-protein transferase activity [GO:0004842]
Gene Ontology
(Cellular Component)
Complete annatation
cytoplasm [GO:0005737];
cytosol [GO:0005829];
extracellular exosome [GO:0070062];
nucleolus [GO:0005730];
nucleoplasm [GO:0005654];
nucleus [GO:0005634];
protein complex [GO:0043234];
UBC13-MMS2 complex [GO:0031372];
UBC13-UEV1A complex [GO:0035370];
ubiquitin ligase complex [GO:0000151]
Protein-protein interaction113182
Phylogenetic treeP61088
HIV replication factor status Zhou et al., Cell. Host. Microbe., 2008
Brass et al., Science, 2008
Smith et al., J. Immunol, 2010
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. CD31.41312479127272.27215000987435e-050.000129571868894537
AZA vs. DISU-0.2875258668636060.2560927968587480.838123183865627
AZA vs. IL70.4340830735458380.02404641931535430.49515256603871
AZA vs. SAHA-0.07824353256458070.7490374222836590.931215822620618
DISU vs. CD3-1.713399152752184.42444021708788e-063.58955930206581e-05
DISU vs. IL70.712680406024510.004873313403232050.0743574894268453
DISU vs. SAHA0.2104820074976910.4702024539119460.804543731029398
DMSO vs. AZA-0.05964181240159060.7217586816267921
DMSO vs. CD3-1.485110226170855.43228304317189e-063.32132078106268e-05
DMSO vs. DISU0.2258510697115520.3546790253008620.845596094175604
DMSO vs. IL70.5010444386584520.005394174057092080.150678509776213
DMSO vs. SAHA-0.02486379552633920.916135681504650.980268431377818
HIV vs. Mock in Activation-0.1702707475137540.7842331576959790.999983755607037
HIV vs. Mock in Latency-0.06833867375445480.6797065611985090.999834320637052
IL7 vs. CD3-0.9708677963344680.002719226933459160.0100139036325507
SAHA vs. CD3-1.516034141353483.01743811348398e-050.000166811417352178
SAHA vs. IL7-0.5152495154675680.03534988247141560.145273753646161
(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) 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 0.214167 0.38811
(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
1.023 0.915 0.916 0.998 0.944
(2). Navare et al., Virology, 2012

SUP-T1 cell line
FC-4hpi P-value FC-8hpi P-value FC-20hpi P-value Category
0.5 0.0311 0.03 0.8237 -0.03 0.5506 Cell growth and proliferation at 4 hpi
(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

not found

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
1J7D X-ray 1.8Å B=1-152.
2C2V X-ray 2.9Å B/E/H/K=2-152.
3HCT X-ray 2.1Å B=1-152.
3HCU X-ray 2.6Å B/D=1-152.
3VON X-ray 3.1Å C/E/G/J/L/N/Q/S/U/X/Z/b/e/g/i/l/n/p=3-150.
3W31 X-ray 2.9Å B=1-152.
4DHI X-ray 1.8Å D=1-152.
4DHJ X-ray 2.3Å C/G/K/N=1-152.
4DHZ X-ray 3.1Å F=1-152.
4IP3 X-ray 2.3Å B=1-152.
4NR3 X-ray 1.8Å B=2-150.
4NRG X-ray 1.9Å B=1-152.
4NRI X-ray 2.3Å B=3-150.
4ONL X-ray 1.3Å B=1-152.
4ONM X-ray 1.3Å B=1-152.
4ONN X-ray 1.5Å B=1-152.
4ORH X-ray 4.8Å B/F/J=1-152.
4TKP X-ray 2.0Å A=2-152.
4WHV X-ray 8.3Å B/E/H/K=1-152.
5AIT X-ray 3.4Å B/E=1-152.
5AIU X-ray 2.2Å B/E=1-152.
5EYA X-ray 2.4Å A/B=1-152.

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

HIV Partner Interaction Type PubMed
capsid inhibited by 21512569

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa04120 Ubiquitin mediated proteolysis - Homo sapiens (human)