Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0001371
UniProt IDP07900
Primary gene name(s)HSP90AA1
Synonym gene name(s)HSP90A, HSPC1, HSPCA
Protein nameHeat shock protein HSP 90-alpha
Protein functionMolecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Binds bacterial lipopolysaccharide, LPS et mediates LPS-induced inflammatory response, including TNF secretion by monocytes, PubMed:11274138, PubMed:11276205, PubMed:15577939, PubMed:15937123, PubMed:27353360. {ECO:0000269|PubMed:11274138, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:15577939, ECO:0000269|PubMed:15937123, ECO:0000269|PubMed:27353360}.
Subcellular locationCytoplasm. Melanosome. Cell membrane. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: P07900
Gene Ontology
(Biological Process)
Complete annatation
cardiac muscle cell apoptotic process [GO:0010659];
chaperone-mediated autophagy [GO:0061684];
chaperone-mediated protein complex assembly [GO:0051131];
ERBB2 signaling pathway [GO:0038128];
Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096];
G2/M transition of mitotic cell cycle [GO:0000086];
mitochondrial transport [GO:0006839];
neuron migration [GO:0001764];
positive regulation of cardiac muscle contraction [GO:0060452];
positive regulation of cell size [GO:0045793];
positive regulation of lamellipodium assembly [GO:0010592];
positive regulation of nitric oxide biosynthetic process [GO:0045429];
positive regulation of protein import into nucleus, translocation [GO:0033160];
protein import into mitochondrial outer membrane [GO:0045040];
protein refolding [GO:0042026];
protein stabilization [GO:0050821];
protein unfolding [GO:0043335];
receptor-mediated endocytosis [GO:0006898];
regulation of cellular response to heat [GO:1900034];
regulation of nitric-oxide synthase activity [GO:0050999];
regulation of protein complex assembly [GO:0043254];
regulation of protein ubiquitination [GO:0031396];
response to antibiotic [GO:0046677];
response to cocaine [GO:0042220];
response to cold [GO:0009409];
response to drug [GO:0042493];
response to estrogen [GO:0043627];
response to heat [GO:0009408];
response to salt stress [GO:0009651];
response to unfolded protein [GO:0006986];
signal transduction [GO:0007165];
skeletal muscle contraction [GO:0003009];
vascular endothelial growth factor receptor signaling pathway [GO:0048010]
Gene Ontology
(Molecular Function)
Complete annatation
ATPase activity [GO:0016887];
ATP binding [GO:0005524];
CTP binding [GO:0002135];
dATP binding [GO:0032564];
GTPase binding [GO:0051020];
GTP binding [GO:0005525];
histone deacetylase binding [GO:0042826];
identical protein binding [GO:0042802];
MHC class II protein complex binding [GO:0023026];
mRNA binding [GO:0003729];
nitric-oxide synthase regulator activity [GO:0030235];
nucleotide binding [GO:0000166];
poly(A RNA binding [GO:0044822];
protein homodimerization activity [GO:0042803];
protein tyrosine kinase activity [GO:0004713];
TPR domain binding [GO:0030911];
UTP binding [GO:0002134]
Gene Ontology
(Cellular Component)
Complete annatation
apical plasma membrane [GO:0016324];
basolateral plasma membrane [GO:0016323];
brush border membrane [GO:0031526];
cell surface [GO:0009986];
cytoplasm [GO:0005737];
cytosol [GO:0005829];
endocytic vesicle lumen [GO:0071682];
extracellular exosome [GO:0070062];
extracellular matrix [GO:0031012];
extracellular region [GO:0005576];
lysosomal lumen [GO:0043202];
melanosome [GO:0042470];
membrane [GO:0016020];
myelin sheath [GO:0043209];
neuronal cell body [GO:0043025];
neuron projection [GO:0043005];
nucleoplasm [GO:0005654];
nucleus [GO:0005634];
perinuclear region of cytoplasm [GO:0048471];
plasma membrane [GO:0005886];
protein complex [GO:0043234];
ruffle membrane [GO:0032587]
Protein-protein interaction109552
Phylogenetic treeP07900
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. CD31.767772060128291.60290362205551e-071.46862999341159e-06
AZA vs. DISU0.1652842227956020.5134508966122060.938109377229618
AZA vs. IL70.5370202495911790.009810291600921170.319374784666706
AZA vs. SAHA-0.4145941716544430.08899221042683030.374502674476281
DISU vs. CD3-1.615498298600481.61017032911381e-050.000113472218518287
DISU vs. IL70.3631988707828210.14881838503930.501498696298822
DISU vs. SAHA-0.5793709599239510.04704685624456590.270018522671815
DMSO vs. AZA-0.2047607284144480.219245603441251
DMSO vs. CD3-1.983909192188852.34198060944379e-092.82707835587105e-08
DMSO vs. DISU-0.3720731296275220.1271824135104540.613095944494124
DMSO vs. IL70.7491660632793253.16128435742247e-050.00501645912506776
DMSO vs. SAHA-0.2176089304394960.3547839155552480.704304586547327
HIV vs. Mock in Activation-0.1978820858776960.7505542268814320.999983755607037
HIV vs. Mock in Latency-0.07512068685963750.6480054739754350.999834320637052
IL7 vs. CD3-1.221373281891840.0001913929069106150.00102686664685209
SAHA vs. CD3-2.208340629811852.56161269973632e-093.90723718471926e-08
SAHA vs. IL7-0.9557309207887029.52542467611561e-050.00189178197058981
(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 0.419989 0.00241278
(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
1.006 1.036 1.036 1.019 0.928
(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

Drugbank ID Drug Name Drug Status Pharmacological Action Drug Action
DB00615 Rifabutin approved unknown other/unknown
DB02424 Geldanamycin experimental unknown unknown
DB02840 4-(1,3-Benzodioxol-5-Yl)-5-(5-Ethyl-2,4-Dihydroxyphenyl)-2h-Pyrazole-3-Carboxylic Acid experimental unknown unknown
DB03080 17-Dmag experimental unknown unknown
DB03749 4-(1h-Imidazol-4-Yl)-3-(5-Ethyl-2,4-Dihydroxy-Phenyl)-1h-Pyrazole experimental unknown unknown
DB05134 CNF1010 investigational unknown unknown
DB06070 SNX-5422 investigational unknown unknown
DB06956 N-(4-ACETYLPHENYL)-5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-1H-PYRAZOLE-4-CARBOXAMIDE experimental unknown unknown
DB06957 4-CHLORO-6-(4-{4-[4-(METHYLSULFONYL)BENZYL]PIPERAZIN-1-YL}-1H-PYRAZOL-5-YL)BENZENE-1,3-DIOL experimental unknown unknown
DB06958 5-(5-CHLORO-2,4-DIHYDROXYPHENYL)-N-ETHYL-4-PIPERAZIN-1-YL-1H-PYRAZOLE-3-CARBOXAMIDE experimental unknown unknown
DB06961 5-(5-chloro-2,4-dihydroxyphenyl)-N-ethyl-4-[4-(morpholin-4-ylmethyl)phenyl]isoxazole-3-carboxamide experimental unknown unknown
DB06969 2-amino-4-[2,4-dichloro-5-(2-pyrrolidin-1-ylethoxy)phenyl]-N-ethylthieno[2,3-d]pyrimidine-6-carboxamide experimental unknown unknown
DB07100 4-CHLORO-6-(4-PIPERAZIN-1-YL-1H-PYRAZOL-5-YL)BENZENE-1,3-DIOL experimental unknown unknown
DB07317 (3E)-3-[(phenylamino)methylidene]dihydrofuran-2(3H)-one experimental unknown unknown
DB07319 6-(3-BROMO-2-NAPHTHYL)-1,3,5-TRIAZINE-2,4-DIAMINE experimental unknown unknown
DB07324 3-({2-[(2-AMINO-6-METHYLPYRIMIDIN-4-YL)ETHYNYL]BENZYL}AMINO)-1,3-OXAZOL-2(3H)-ONE experimental unknown unknown
DB07502 4-bromo-6-(6-hydroxy-1,2-benzisoxazol-3-yl)benzene-1,3-diol experimental unknown unknown
DB07594 4-[4-(2,3-DIHYDRO-1,4-BENZODIOXIN-6-YL)-3-METHYL-1H-PYRAZOL-5-YL]-6-ETHYLBENZENE-1,3-DIOL experimental unknown unknown
DB07601 4-chloro-6-{5-[(2-morpholin-4-ylethyl)amino]-1,2-benzisoxazol-3-yl}benzene-1,3-diol experimental unknown unknown
DB07877 8-(6-BROMO-BENZO[1,3]DIOXOL-5-YLSULFANYL)-9-(3-ISOPROPYLAMINO-PROPYL)-ADENINE experimental unknown unknown
DB08194 4-methyl-7,8-dihydro-5H-thiopyrano[4,3-d]pyrimidin-2-amine experimental unknown unknown
DB08197 (5E,7S)-2-amino-7-(4-fluoro-2-pyridin-3-ylphenyl)-4-methyl-7,8-dihydroquinazolin-5(6H)-one oxime experimental unknown unknown
DB04054 9-Butyl-8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-Ylamine experimental unknown unknown
DB02550 8-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-2-Fluoro-9-Pent-4-Ylnyl-9h-Purin-6-Ylamine experimental unknown unknown
DB03093 8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9h-Purin-6-Ylamine experimental unknown unknown
DB02754 9-Butyl-8-(3,4,5-Trimethoxybenzyl)-9h-Purin-6-Amine experimental unknown unknown
DB03899 9-Butyl-8-(4-Methoxybenzyl)-9h-Purin-6-Amine experimental unknown unknown
DB03809 9-Butyl-8-(3-Methoxybenzyl)-9h-Purin-6-Amine experimental unknown unknown
DB08436 8-BENZO[1,3]DIOXOL-,5-YLMETHYL-9-BUTYL-9H- experimental unknown unknown
DB02359 9-Butyl-8-(2,5-Dimethoxy-Benzyl)-9h-Purin-6-Ylamine experimental unknown unknown
DB03504 9-Butyl-8-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-9h-Purin-6-Ylamine experimental unknown unknown
DB04505 8-(2-Chloro-3,4,5-Trimethoxy-Benzyl)-9-Pent-4-Ylnyl-9h-Purin-6-Ylamine experimental unknown unknown
DB04254 8-Benzo[1,3]Dioxol-,5-Ylmethyl-9-Butyl-2-Fluoro-9h-Purin-6-Ylamine experimental unknown unknown
DB03137 8-(2,5-Dimethoxy-Benzyl)-2-Fluoro-9-Pent-9h-Purin-6-Ylamine experimental unknown unknown
DB08442 4-{[(2R)-2-(2-methylphenyl)pyrrolidin-1-yl]carbonyl}benzene-1,3-diol experimental unknown unknown
DB08443 2-(1H-pyrrol-1-ylcarbonyl)benzene-1,3,5-triol experimental unknown unknown
DB08557 2-[(2-methoxyethyl)amino]-4-(4-oxo-1,2,3,4-tetrahydro-9H-carbazol-9-yl)benzamide experimental unknown unknown
DB08786 4-(2-methoxyethoxy)-6-methylpyrimidin-2-amine experimental unknown unknown
DB08787 4-(2,4-dichlorophenyl)-5-phenyldiazenyl-pyrimidin-2-amine experimental unknown unknown
DB08788 3,6-DIAMINO-5-CYANO-4-(4-ETHOXYPHENYL)THIENO[2,3-B]PYRIDINE-2-CARBOXAMIDE experimental unknown unknown
DB08789 2-AMINO-4-(2,4-DICHLOROPHENYL)-N-ETHYLTHIENO[2,3-D]PYRIMIDINE-6-CARBOXAMIDE experimental unknown unknown
DB00716 Nedocromil approved unknown unknown

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
1BYQ X-ray 1.5Å A=9-236.
1OSF X-ray 1.7Å A=9-223.
1UY6 X-ray 1.9Å A=2-236.
1UY7 X-ray 1.9Å A=2-236.
1UY8 X-ray 1.9Å A=2-236.
1UY9 X-ray 2.0Å A=2-236.
1UYC X-ray 2.0Å A=2-236.
1UYD X-ray 2.2Å A=2-236.
1UYE X-ray 2.0Å A=2-236.
1UYF X-ray 2.0Å A=2-236.
1UYG X-ray 2.0Å A=2-236.
1UYH X-ray 2.2Å A=2-236.
1UYI X-ray 2.2Å A=2-236.
1UYK X-ray 2.2Å A=2-236.
1UYL X-ray 1.4Å A=2-236.
1YC1 X-ray 1.7Å A=9-236.
1YC3 X-ray 2.1Å A=9-236.
1YC4 X-ray 1.8Å A=9-236.
1YER X-ray 1.6Å A=9-236.
1YES X-ray 2.2Å A=9-236.
1YET X-ray 1.9Å A=9-236.
2BSM X-ray 2.0Å A=2-236.
2BT0 X-ray 1.9Å A/B=2-236.
2BUG NMR - B=728-732.
2BYH X-ray 1.9Å A=11-236.
2BYI X-ray 1.6Å A=11-236.
2BZ5 X-ray 1.9Å A/B=2-236.
2C2L X-ray 3.3Å E/F/G/H=724-732.
2CCS X-ray 1.7Å A=1-236.
2CCT X-ray 2.3Å A=1-236.
2CCU X-ray 2.7Å A=1-236.
2FWY X-ray 2.1Å A=1-236.
2FWZ X-ray 2.1Å A=1-236.
2H55 X-ray 2.0Å A=1-236.
2JJC X-ray 1.9Å A=9-223.
2K5B NMR - A=14-223.
2QF6 X-ray 3.1Å A/B/C/D=17-223.
2QFO X-ray 1.6Å A/B=17-223.
2QG0 X-ray 1.8Å A/B=17-223.
2QG2 X-ray 1.8Å A=17-223.
2UWD X-ray 1.9Å A=2-236.
2VCI X-ray 2.0Å A=1-236.
2VCJ X-ray 2.5Å A=1-236.
2WI1 X-ray 2.3Å A=1-236.
2WI2 X-ray 2.0Å A/B=1-236.
2WI3 X-ray 1.9Å A=1-236.
2WI4 X-ray 2.4Å A=1-236.
2WI5 X-ray 2.1Å A=1-236.
2WI6 X-ray 2.1Å A=1-236.
2WI7 X-ray 2.5Å A=1-236.
2XAB X-ray 1.9Å A/B=9-236.
2XDK X-ray 1.9Å A=9-236.
2XDL X-ray 1.9Å A=9-236.
2XDS X-ray 1.9Å A=9-236.
2XDU X-ray 1.7Å A=14-224.
2XDX X-ray 2.4Å A=9-236.
2XHR X-ray 2.2Å A=9-236.
2XHT X-ray 2.2Å A=9-236.
2XHX X-ray 2.8Å A=9-236.
2XJG X-ray 2.2Å A=9-236.
2XJJ X-ray 1.9Å A/B=9-236.
2XJX X-ray 1.6Å A=9-236.
2XK2 X-ray 1.9Å A=9-236.
2YE2 X-ray 1.9Å A=9-236.
2YE3 X-ray 1.9Å A=9-236.
2YE4 X-ray 2.3Å A=9-236.
2YE5 X-ray 1.7Å A=9-236.
2YE6 X-ray 2.5Å A=9-236.
2YE7 X-ray 2.2Å A=9-236.
2YE8 X-ray 2.3Å A=9-236.
2YE9 X-ray 2.2Å A=9-236.
2YEA X-ray 1.7Å A=9-236.
2YEB X-ray 2.4Å A=9-236.
2YEC X-ray 2.1Å A=9-236.
2YED X-ray 2.1Å A=9-236.
2YEE X-ray 2.3Å A=9-236.
2YEF X-ray 1.5Å A=9-236.
2YEG X-ray 2.5Å A/B=9-236.
2YEH X-ray 2.1Å A=9-236.
2YEI X-ray 2.2Å A=9-236.
2YEJ X-ray 2.2Å A=9-236.
2YI0 X-ray 1.6Å A=1-229.
2YI5 X-ray 2.5Å A=1-229.
2YI6 X-ray 1.8Å A=1-229.
2YI7 X-ray 1.4Å A=1-229.
2YJW X-ray 1.6Å A=18-223.
2YJX X-ray 1.8Å A=18-223.
2YK2 X-ray 1.7Å A=18-223.
2YK9 X-ray 1.3Å A=18-223.
2YKB X-ray 1.9Å A=18-223.
2YKC X-ray 1.6Å A=18-223.
2YKE X-ray 1.4Å A=18-223.
2YKI X-ray 1.6Å A=18-223.
2YKJ X-ray 1.4Å A=18-223.
3B24 X-ray 1.7Å A/B=9-236.
3B25 X-ray 1.7Å A=9-236.
3B26 X-ray 2.1Å A/B=9-236.
3B27 X-ray 1.5Å A=9-236.
3B28 X-ray 1.3Å A/B=9-236.
3BM9 X-ray 1.6Å A=14-236.
3BMY X-ray 1.6Å A=14-236.
3D0B X-ray 1.7Å A=1-232.
3EKO X-ray 1.5Å A/B=9-225.
3EKR X-ray 2.0Å A/B=9-225.
3FT5 X-ray 1.9Å A=9-236.
3FT8 X-ray 2.0Å A=9-236.
3HEK X-ray 1.9Å A/B=9-225.
3HHU X-ray 1.5Å A/B=1-224.
3HYY X-ray 1.9Å A=9-236.
3HYZ X-ray 2.3Å A/B=9-236.
3HZ1 X-ray 2.3Å A=9-236.
3HZ5 X-ray 1.9Å A=9-236.
3INW X-ray 1.9Å A=10-236.
3INX X-ray 1.7Å A=10-236.
3K97 X-ray 1.9Å A=9-236.
3K98 X-ray 2.4Å A/B=9-225.
3K99 X-ray 2.1Å A/B/C/D=9-225.
3MNR X-ray 1.9Å P=1-232.
3O0I X-ray 1.4Å A=1-236.
3OW6 X-ray 1.8Å A=17-223.
3OWB X-ray 2.0Å A=17-223.
3OWD X-ray 1.6Å A=17-223.
3Q6M X-ray 3.0Å A/B/C=293-732.
3Q6N X-ray 3.0Å A/B/C/D/E/F=293-732.
3QDD X-ray 1.7Å A=1-236.
3QTF X-ray 1.5Å A=14-236.
3R4M X-ray 1.7Å A=9-236.
3R4N X-ray 2.0Å A/B=9-225.
3R4O X-ray 2.6Å A/B=9-225.
3R4P X-ray 1.7Å A/B=9-225.
3R91 X-ray 1.5Å A=14-236.
3R92 X-ray 1.5Å A=14-236.
3RKZ X-ray 1.5Å A=14-236.
3RLP X-ray 1.7Å A/B=9-225.
3RLQ X-ray 1.9Å A/B=9-225.
3RLR X-ray 1.7Å A/B=9-225.
3T0H X-ray 1.2Å A=9-236.
3T0Z X-ray 2.1Å A=9-236.
3T10 X-ray 1.2Å A=9-236.
3T1K X-ray 1.5Å A/B=9-236.
3T2S X-ray 1.5Å A/B=9-236.
3TUH X-ray 1.8Å A/B=16-224.
3VHA X-ray 1.3Å A=9-236.
3VHC X-ray 1.4Å A=9-236.
3VHD X-ray 1.5Å A/B=9-236.
3WHA X-ray 1.3Å A/B=9-236.
3WQ9 X-ray 1.8Å A=1-236.
4AIF X-ray 2.0Å D/E=726-732.
4AWO X-ray 1.7Å A/B=9-236.
4AWP X-ray 1.8Å A/B=9-236.
4AWQ X-ray 1.6Å A/B=9-236.
4B7P X-ray 1.7Å A=9-236.
4BQG X-ray 1.9Å A=9-236.
4BQJ X-ray 2.0Å A=9-236.
4CGQ X-ray 2.0Å Q=726-732.
4CGU X-ray 2.1Å C=726-732.
4CGV X-ray 2.5Å E/F=726-732.
4CGW X-ray 3.0Å C/D=726-732.
4CWF X-ray 2.0Å A=9-236.
4CWN X-ray 1.8Å A=9-236.
4CWO X-ray 2.3Å A=9-236.
4CWP X-ray 1.9Å A=9-236.
4CWQ X-ray 2.0Å A=9-236.
4CWR X-ray 2.0Å A=9-236.
4CWS X-ray 2.3Å A=9-236.
4CWT X-ray 1.9Å A=9-236.
4EEH X-ray 1.6Å A=9-236.
4EFT X-ray 2.1Å A=9-236.
4EFU X-ray 2.0Å A=9-236.
4EGH X-ray 1.6Å A=9-236.
4EGI X-ray 1.7Å A=9-236.
4EGK X-ray 1.6Å A=9-236.
4FCP X-ray 2.0Å A/B=1-236.
4FCQ X-ray 2.1Å A=1-236.
4FCR X-ray 1.7Å A=1-236.
4HY6 X-ray 1.6Å A=9-236.
4JQL X-ray 1.7Å A=9-236.
4L8Z X-ray 1.7Å A=9-236.
4L90 X-ray 2.0Å A=9-236.
4L91 X-ray 1.7Å A=9-236.
4L93 X-ray 1.8Å A/B=9-236.
4L94 X-ray 1.6Å A=9-236.
4LWE X-ray 1.5Å A=17-224.
4LWF X-ray 1.7Å A=17-224.
4LWG X-ray 1.6Å A=17-224.
4LWH X-ray 1.7Å A=16-224.
4LWI X-ray 1.7Å A=17-224.
4NH7 X-ray 2.0Å A/B=9-236.
4NH8 X-ray 1.6Å A=9-236.
4O04 X-ray 1.8Å A=9-236.
4O05 X-ray 1.7Å A=9-236.
4O07 X-ray 1.8Å A=9-236.
4O09 X-ray 1.9Å A=9-236.
4O0B X-ray 1.9Å A=9-236.
4R3M X-ray 1.8Å A=16-224.
4U93 X-ray 1.5Å A=1-236.
4W7T X-ray 1.8Å A=1-236.
4XIP X-ray 1.7Å A=9-236.
4XIQ X-ray 1.8Å A=9-236.
4XIR X-ray 1.7Å A=9-236.
4XIT X-ray 1.8Å A=9-236.
4YKQ X-ray 1.9Å A=2-236.
4YKR X-ray 1.6Å A=2-236.
4YKT X-ray 1.8Å A=2-236.
4YKU X-ray 1.7Å A=2-236.
4YKW X-ray 1.8Å A/B=2-236.
4YKX X-ray 1.8Å A=2-236.
4YKY X-ray 1.7Å A=2-236.
4YKZ X-ray 1.8Å A=2-236.
5CF0 X-ray 1.8Å A=9-236.

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

HIV Partner Interaction Type PubMed
Pr55(Gag) incorporates 21738476
retropepsin cleaves 22944692
Tat enhanced by 22807676
Tat upregulates 15710247
Gag-Pol incorporates 21738476
Tat regulated by 10617616
Tat downregulates 23287597
Nef cooperates with 24204260
Tat requires 15020715

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa04141 Protein processing in endoplasmic reticulum - Homo sapiens (human)
hsa04151 PI3K-Akt signaling pathway - Homo sapiens (human)
hsa04612 Antigen processing and presentation - Homo sapiens (human)
hsa04621 NOD-like receptor signaling pathway - Homo sapiens (human)
hsa04657 IL-17 signaling pathway - Homo sapiens (human)
hsa04659 Th17 cell differentiation - Homo sapiens (human)
hsa04914 Progesterone-mediated oocyte maturation - Homo sapiens (human)
hsa04915 Estrogen signaling pathway - Homo sapiens (human)
hsa05200 Pathways in cancer - Homo sapiens (human)
hsa05215 Prostate cancer - Homo sapiens (human)