Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0000247
UniProt IDO15392
Primary gene name(s)BIRC5
Synonym gene name(s)API4, IAP4
Protein nameBaculoviral IAP repeat-containing protein 5
Protein functionMultitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex, CPC which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. Involved in the recruitment of CPC to centromeres during early mitosis via association with histone H3 phosphorylated at 'Thr-3', H3pT3 during mitosis. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform. {ECO:0000269|PubMed:10626797, ECO:0000269|PubMed:12773388, ECO:0000269|PubMed:16291752, ECO:0000269|PubMed:16322459, ECO:0000269|PubMed:18591255, ECO:0000269|PubMed:20826784, ECO:0000269|PubMed:20929775, ECO:0000269|PubMed:21536684, ECO:0000269|PubMed:9859993}.
Subcellular locationCytoplasm. Nucleus {ECO:0000269|PubMed:20826784}. Chromosome. Chromosome, centromere {ECO:0000269|PubMed:11084331, ECO:0000269|PubMed:14610074, ECO:0000269|PubMed:16322459}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11084331}. Chromosome, centromere, kinetochore. Midbody {ECO:0000269|PubMed:15665297}. Note=Localizes on chromosome arms and inner centromeres from prophase through metaphase. Localizes to kinetochores in metaphase, distributes to the midzone microtubules in anaphase and at telophase, localizes exclusively to the midbody. Colocalizes with AURKB at mitotic chromosomes. Acetylation at Lys-129 directs its localization to the nucleus by enhancing homodimerization and thereby inhibiting XPO1/CRM1-mediated nuclear export. {ECO:0000269|PubMed:11084331}.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: O15392
Gene Ontology
(Biological Process)
Complete annatation
apoptotic process [GO:0006915];
cell division [GO:0051301];
cytokinesis [GO:0000910];
establishment of chromosome localization [GO:0051303];
G2/M transition of mitotic cell cycle [GO:0000086];
inhibition of cysteine-type endopeptidase activity involved in apoptotic process [GO:1990001];
mitotic nuclear division [GO:0007067];
mitotic spindle assembly [GO:0090307];
negative regulation of apoptotic process [GO:0043066];
negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154];
negative regulation of transcription, DNA-templated [GO:0045892];
positive regulation of cell proliferation [GO:0008284];
positive regulation of exit from mitosis [GO:0031536];
positive regulation of mitotic cell cycle [GO:0045931];
protein complex localization [GO:0031503];
protein phosphorylation [GO:0006468];
protein sumoylation [GO:0016925];
regulation of apoptotic process [GO:0042981];
regulation of signal transduction [GO:0009966];
sister chromatid cohesion [GO:0007062];
spindle checkpoint [GO:0031577];
transcription, DNA-templated [GO:0006351]
Gene Ontology
(Molecular Function)
Complete annatation
chaperone binding [GO:0051087];
cobalt ion binding [GO:0050897];
cofactor binding [GO:0048037];
cysteine-type endopeptidase inhibitor activity [GO:0004869];
cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027];
enzyme binding [GO:0019899];
identical protein binding [GO:0042802];
metal ion binding [GO:0046872];
microtubule binding [GO:0008017];
protein heterodimerization activity [GO:0046982];
protein homodimerization activity [GO:0042803];
Ran GTPase binding [GO:0008536];
tubulin binding [GO:0015631];
ubiquitin-protein transferase activity [GO:0004842];
zinc ion binding [GO:0008270]
Gene Ontology
(Cellular Component)
Complete annatation
centriole [GO:0005814];
chromosome, centromeric region [GO:0000775];
chromosome passenger complex [GO:0032133];
condensed chromosome kinetochore [GO:0000777];
cytoplasm [GO:0005737];
cytoplasmic microtubule [GO:0005881];
cytosol [GO:0005829];
interphase microtubule organizing center [GO:0031021];
microtubule [GO:0005874];
midbody [GO:0030496];
nuclear chromosome [GO:0000228];
nucleoplasm [GO:0005654];
nucleus [GO:0005634];
spindle [GO:0005819];
spindle microtubule [GO:0005876]
Protein-protein interaction106829
Phylogenetic treeO15392
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. CD3-0.1039290170310160.9449223672741970.964470642430084
AZA vs. DISU-0.3766879591943390.536181481303070.941236712374807
AZA vs. IL70.0114145991199720.9858625069337550.999311006273513
AZA vs. SAHA-0.8947724211978840.1894948255660530.555296462010631
DISU vs. CD3-0.2836919388569750.8513811298461930.899727927040207
DISU vs. IL70.3783624206418670.5056228608523030.830044367655729
DISU vs. SAHA-0.5183206224748980.3931910811732440.756657886767226
DMSO vs. AZA0.04203285837990440.9484781973752281
DMSO vs. CD30.1268893938282150.9330393736734670.953639911064469
DMSO vs. DISU0.4137456787781290.4685995845946550.895928065625011
DMSO vs. IL7-0.02174791284983180.971615876007940.994450452088742
DMSO vs. SAHA-0.942396675011350.1466287486903290.460863789679237
HIV vs. Mock in Activation-0.06227642462161630.9796970415115370.999983755607037
HIV vs. Mock in Latency0.2165020408627420.6838522004849730.999834320637052
IL7 vs. CD30.1242400478965720.933755073397960.959209247519866
SAHA vs. CD3-0.8198905411207160.5883633210231570.687442645977592
SAHA vs. IL7-0.9100171994265670.1588190155158310.378863402418997
(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
1.9 0.000213927 1.3 0.065288151 1.4 0.200883104
(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 0.281597 0.0725046
(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
0.031 2.98E-04

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
1.207 1.14 1.852 1.735 1.027
(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
202095_s_at 2.1 Yes upregulated in CD4+ cells

Protein Overview       top

Drug-protein Interaction       (annotations from DrugBank)      top

Drugbank ID Drug Name Drug Status Pharmacological Action Drug Action
DB05141 LY2181308 investigational unknown unknown

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
1E31 X-ray 2.7Å A/B=1-142.
1F3H X-ray 2.5Å A/B=1-142.
1XOX NMR - A/B=1-117.
2QFA X-ray 1.4Å A=1-142.
2RAW X-ray 2.4Å A=1-142.
2RAX X-ray 3.3Å A/E/X=1-120.
3UEC X-ray 2.1Å A=1-142.
3UED X-ray 2.7Å A/C=1-142.
3UEE X-ray 2.6Å A/C=1-142.
3UEF X-ray 2.4Å A/C=1-142.
3UEG X-ray 2.8Å A/B=1-142.
3UEH X-ray 2.6Å A/B=1-142.
3UEI X-ray 2.7Å A/B=1-142.
3UIG X-ray 2.4Å A/B=1-142.
3UIH X-ray 2.4Å A/B=1-142.
3UII X-ray 2.6Å A/B=1-142.
3UIJ X-ray 2.7Å A/B=1-142.
3UIK X-ray 2.7Å A/B=1-142.
4A0I X-ray 2.6Å A/B=1-142.
4A0J X-ray 2.8Å A/B=1-142.
4A0N X-ray 2.7Å A=1-142.

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

HIV Partner Interaction Type PubMed
Vpr upregulates 12510154

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa01524 Platinum drug resistance - Homo sapiens (human)
hsa04210 Apoptosis - Homo sapiens (human)
hsa04215 Apoptosis - multiple species - Homo sapiens (human)
hsa04390 Hippo signaling pathway - Homo sapiens (human)
hsa05161 Hepatitis B - Homo sapiens (human)
hsa05200 Pathways in cancer - Homo sapiens (human)
hsa05210 Colorectal cancer - Homo sapiens (human)