Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0007706
UniProt IDP63146
Primary gene name(s)UBE2B
Synonym gene name(s)RAD6B
Protein nameUbiquitin-conjugating enzyme E2 B
Protein functionAccepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In association with the E3 enzyme BRE1, RNF20 and/or RNF40, it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B at 'Lys-120' to form H2BK120ub1. H2BK120ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric silencing, and is also a prerequisite for H3K4me and H3K79me formation. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'- and 'Lys-63'-linked polyubiquitination. Required for postreplication repair of UV-damaged DNA. Associates to the E3 ligase RAD18 to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. May be involved in neurite outgrowth. {ECO:0000269|PubMed:16337599, ECO:0000269|PubMed:17108083, ECO:0000269|PubMed:17130289, ECO:0000269|PubMed:1717990, ECO:0000269|PubMed:20061386}.
Subcellular locationCell membrane {ECO:0000250|UniProtKB:P63149}. Nucleus {ECO:0000250|UniProtKB:P63149}. Note=In peripheral neurons, expressed both at the plasma membrane and in nuclei. {ECO:0000250|UniProtKB:P63149}.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: P63146
Gene Ontology
(Biological Process)
Complete annatation
canonical Wnt signaling pathway [GO:0060070];
cellular response to DNA damage stimulus [GO:0006974];
chiasma assembly [GO:0051026];
DNA damage response, detection of DNA damage [GO:0042769];
DNA repair [GO:0006281];
histone H2A ubiquitination [GO:0033522];
histone lysine demethylation [GO:0070076];
in utero embryonic development [GO:0001701];
maintenance of chromatin silencing [GO:0006344];
meiotic telomere clustering [GO:0045141];
negative regulation of apoptotic process [GO:0043066];
negative regulation of cAMP-mediated signaling [GO:0043951];
negative regulation of histone phosphorylation [GO:0033128];
positive regulation of reciprocal meiotic recombination [GO:0010845];
postreplication repair [GO:0006301];
proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161];
protein autoubiquitination [GO:0051865];
protein K11-linked ubiquitination [GO:0070979];
protein K48-linked ubiquitination [GO:0070936];
protein K63-linked ubiquitination [GO:0070534];
protein monoubiquitination [GO:0006513];
protein polyubiquitination [GO:0000209];
protein stabilization [GO:0050821];
protein ubiquitination [GO:0016567];
response to drug [GO:0042493];
response to UV [GO:0009411];
spermatogenesis [GO:0007283];
sperm axoneme assembly [GO:0007288];
synaptonemal complex organization [GO:0070193];
ubiquitin-dependent protein catabolic process [GO:0006511]
Gene Ontology
(Molecular Function)
Complete annatation
ATP binding [GO:0005524];
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
chromatin [GO:0000785];
cytoplasm [GO:0005737];
HULC complex [GO:0033503];
nuclear chromatin [GO:0000790];
nucleoplasm [GO:0005654];
nucleus [GO:0005634];
plasma membrane [GO:0005886];
replication fork [GO:0005657];
XY body [GO:0001741]
Protein-protein interaction113168
Phylogenetic treeP63146
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. CD30.6039197316624180.06591160114023040.125084317852626
AZA vs. DISU0.3456213210270680.173229939790390.75908956755824
AZA vs. IL7-0.08765817267151210.6493894731826180.999311006273513
AZA vs. SAHA0.130148219323120.5950416976497320.867158208964865
DISU vs. CD3-0.2714046294210090.4543750797544780.584606516918659
DISU vs. IL7-0.4420019129318140.08031773060119360.375643780107955
DISU vs. SAHA-0.2147151278120560.465134256645440.801281749039126
DMSO vs. AZA-0.159600617907830.342997214650751
DMSO vs. CD3-0.7747971099864320.01595336957940.0369806912930698
DMSO vs. DISU-0.5069432450200330.038809728355740.397865718585716
DMSO vs. IL70.07902592969356650.6614881376344090.930704201551623
DMSO vs. SAHA0.2824367673172720.2326014175781410.579534808640169
HIV vs. Mock in Activation-0.2787488370491520.654153135082310.999983755607037
HIV vs. Mock in Latency0.1020661207739740.5376373854357580.999834320637052
IL7 vs. CD3-0.6827808611912490.03424246389092510.0809626130553591
SAHA vs. CD3-0.4991397938773120.159727608120170.252872681413065
SAHA vs. IL70.2135062896623140.3831207679453280.633524390589699
(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 -0.120569 0.432131
(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
0.793 1.46 2.235 1.974 1.301
(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

not found

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
1JAS NMR - A=1-152.
1NXA Model - A=1-152.
2Y4W NMR - A=1-152.
2YB6 X-ray 1.5Å A=1-152.
2YBF X-ray 2.0Å A=1-152.

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

HIV Partner Interaction Type PubMed
HIV-1 virus replication enhanced by expression of human gene 18854154

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

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