Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0007713
UniProt IDP63279
Primary gene name(s)UBE2I
Synonym gene name(s)UBC9, UBCE9
Protein nameSUMO-conjugating enzyme UBC9
Protein functionAccepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3 and SUMO4 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation of FOXL2 and KAT5. Essential for nuclear architecture and chromosome segregation. Sumoylates p53/TP53 at 'Lys-386'. {ECO:0000269|PubMed:11451954, ECO:0000269|PubMed:15809060, ECO:0000269|PubMed:17466333, ECO:0000269|PubMed:19638400, ECO:0000269|PubMed:19744555, ECO:0000269|PubMed:20077568, ECO:0000269|PubMed:26524494, ECO:0000269|PubMed:8668529}.
Subcellular locationNucleus. Cytoplasm. Note=Mainly nuclear. In spermatocytes, localizes in synaptonemal complexes. Recruited by BCL11A into the nuclear body, By similarity. {ECO:0000250}.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: P63279
Gene Ontology
(Biological Process)
Complete annatation
cell division [GO:0051301];
cellular protein modification process [GO:0006464];
chromosome segregation [GO:0007059];
global genome nucleotide-excision repair [GO:0070911];
mitotic nuclear division [GO:0007067];
negative regulation of transcription, DNA-templated [GO:0045892];
negative regulation of transcription from RNA polymerase II promoter [GO:0000122];
positive regulation of I-kappaB kinase/NF-kappaB signaling [GO:0043123];
positive regulation of SUMO transferase activity [GO:1903755];
protein sumoylation [GO:0016925];
ubiquitin-dependent protein catabolic process [GO:0006511];
viral process [GO:0016032]
Gene Ontology
(Molecular Function)
Complete annatation
ATP binding [GO:0005524];
enzyme binding [GO:0019899];
ligase activity [GO:0016874];
poly(A RNA binding [GO:0044822];
RING-like zinc finger domain binding [GO:0071535];
SUMO conjugating enzyme activity [GO:0061656];
SUMO transferase activity [GO:0019789];
transcription factor binding [GO:0008134]
Gene Ontology
(Cellular Component)
Complete annatation
cytoplasm [GO:0005737];
cytosol [GO:0005829];
nuclear envelope [GO:0005635];
nucleoplasm [GO:0005654];
nucleus [GO:0005634];
PML body [GO:0016605];
sumoylated E2 ligase complex [GO:1990356];
synaptonemal complex [GO:0000795];
transferase complex [GO:1990234]
Protein-protein interaction113177
Phylogenetic treeP63279
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. CD30.4350071975720570.1844314463436110.286428162387989
AZA vs. DISU0.05446805242053620.8294276002308790.985239814541943
AZA vs. IL7-0.006846949207468370.971599046330310.999311006273513
AZA vs. SAHA0.01473812178773140.9518185987303870.989923926111013
DISU vs. CD3-0.3930288625845290.2786545082184540.408047217494169
DISU vs. IL7-0.07076822450031780.7786290216506420.948619491765825
DISU vs. SAHA-0.03744241725483660.8977290111457330.974619934229746
DMSO vs. AZA-0.04382712893121280.7937836548124661
DMSO vs. CD3-0.4896763430355560.1262900579065030.206227176153639
DMSO vs. DISU-0.09987001138366970.6821590261315840.957247128816386
DMSO vs. IL70.04410056348140550.8063205132765050.961480319778377
DMSO vs. SAHA0.05276314572843710.8229037506050870.951910990330119
HIV vs. Mock in Activation0.163231075533550.7929132634317030.999983755607037
HIV vs. Mock in Latency-0.006431515302958020.9689167115540390.999834320637052
IL7 vs. CD3-0.4356374673377820.175755659884850.292434602212645
SAHA vs. CD3-0.4435729984204930.2095375742769010.312894495080549
SAHA vs. IL70.01921535122409070.9371256556120980.976377670216807
(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 -0.0630693 0.725113
(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
1.056 0.941 0.901 0.878 0.963
(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
1A3S X-ray 2.8Å A=1-158.
1KPS X-ray 2.5Å A/C=1-158.
1Z5Q Model - A=1-158.
1Z5S X-ray 3.0Å A=1-158.
2GRN X-ray 1.8Å A=1-158.
2GRO X-ray 1.7Å A=1-158.
2GRP X-ray 2.0Å A=1-158.
2GRQ X-ray 1.7Å A=1-158.
2GRR X-ray 1.3Å A=1-158.
2O25 X-ray 2.6Å C/D=1-158.
2PE6 X-ray 2.4Å A=1-158.
2PX9 NMR - B=1-158.
2XWU X-ray 2.8Å A=1-158.
3A4S X-ray 2.7Å A/B=1-158.
3UIN X-ray 2.6Å A=1-158.
3UIO X-ray 2.6Å A=1-158.
3UIP X-ray 2.2Å A=1-158.
4W5V X-ray 2.5Å A=1-158.
4Y1L X-ray 2.7Å A/B=1-158.
5D2M X-ray 2.4Å A/D=1-158.
5F6D X-ray 1.5Å A=2-158.
5F6E X-ray 1.1Å A=2-158.
5F6U X-ray 1.5Å A=2-158.
5F6V X-ray 1.4Å A=2-158.
5F6W X-ray 1.7Å A=2-158.
5F6X X-ray 1.5Å A=2-158.
5F6Y X-ray 1.1Å A=2-158.

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

HIV Partner Interaction Type PubMed
integrase interacts with 22895527
p6 interacts with 15613319
19640976
Envelope surface glycoprotein gp120 stabilized by 19640976
2386196723861967
Pr55(Gag) co-localizes with 18684836
19640976
Envelope transmembrane glycoprotein gp41 stabilized by 19640976
Pr55(Gag) interacts with 19640976
19640976
2386196723861967

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa03013 RNA transport - Homo sapiens (human)
hsa04064 NF-kappa B signaling pathway - Homo sapiens (human)
hsa04120 Ubiquitin mediated proteolysis - Homo sapiens (human)
hsa05206 MicroRNAs in cancer - Homo sapiens (human)
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