Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0005645
UniProt IDQ16539
Primary gene name(s)MAPK14
Synonym gene name(s)CSBP, CSBP1, CSBP2, CSPB1, MXI2, SAPK2A
Protein nameMitogen-activated protein kinase 14
Protein functionSerine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. MAPK14 is one of the four p38 MAPKs which play an important role in the cascades of cellular responses evoked by extracellular stimuli such as proinflammatory cytokines or physical stress leading to direct activation of transcription factors. Accordingly, p38 MAPKs phosphorylate a broad range of proteins and it has been estimated that they may have approximately 200 to 300 substrates each. Some of the targets are downstream kinases which are activated through phosphorylation and further phosphorylate additional targets. RPS6KA5/MSK1 and RPS6KA4/MSK2 can directly phosphorylate and activate transcription factors such as CREB1, ATF1, the NF-kappa-B isoform RELA/NFKB3, STAT1 and STAT3, but can also phosphorylate histone H3 and the nucleosomal protein HMGN1. RPS6KA5/MSK1 and RPS6KA4/MSK2 play important roles in the rapid induction of immediate-early genes in response to stress or mitogenic stimuli, either by inducing chromatin remodeling or by recruiting the transcription machinery. On the other hand, two other kinase targets, MAPKAPK2/MK2 and MAPKAPK3/MK3, participate in the control of gene expression mostly at the post-transcriptional level, by phosphorylating ZFP36, tristetraprolin and ELAVL1, and by regulating EEF2K, which is important for the elongation of mRNA during translation. MKNK1/MNK1 and MKNK2/MNK2, two other kinases activated by p38 MAPKs, regulate protein synthesis by phosphorylating the initiation factor EIF4E2. MAPK14 interacts also with casein kinase II, leading to its activation through autophosphorylation and further phosphorylation of TP53/p53. In the cytoplasm, the p38 MAPK pathway is an important regulator of protein turnover. For example, CFLAR is an inhibitor of TNF-induced apoptosis whose proteasome-mediated degradation is regulated by p38 MAPK phosphorylation. In a similar way, MAPK14 phosphorylates the ubiquitin ligase SIAH2, regulating its activity towards EGLN3. MAPK14 may also inhibit the lysosomal degradation pathway of autophagy by interfering with the intracellular trafficking of the transmembrane protein ATG9. Another function of MAPK14 is to regulate the endocytosis of membrane receptors by different mechanisms that impinge on the small GTPase RAB5A. In addition, clathrin-mediated EGFR internalization induced by inflammatory cytokines and UV irradiation depends on MAPK14-mediated phosphorylation of EGFR itself as well as of RAB5A effectors. Ectodomain shedding of transmembrane proteins is regulated by p38 MAPKs as well. In response to inflammatory stimuli, p38 MAPKs phosphorylate the membrane-associated metalloprotease ADAM17. Such phosphorylation is required for ADAM17-mediated ectodomain shedding of TGF-alpha family ligands, which results in the activation of EGFR signaling and cell proliferation. Another p38 MAPK substrate is FGFR1. FGFR1 can be translocated from the extracellular space into the cytosol and nucleus of target cells, and regulates processes such as rRNA synthesis and cell growth. FGFR1 translocation requires p38 MAPK activation. In the nucleus, many transcription factors are phosphorylated and activated by p38 MAPKs in response to different stimuli. Classical examples include ATF1, ATF2, ATF6, ELK1, PTPRH, DDIT3, TP53/p53 and MEF2C and MEF2A. The p38 MAPKs are emerging as important modulators of gene expression by regulating chromatin modifiers and remodelers. The promoters of several genes involved in the inflammatory response, such as IL6, IL8 and IL12B, display a p38 MAPK-dependent enrichment of histone H3 phosphorylation on 'Ser-10', H3S10ph in LPS-stimulated myeloid cells. This phosphorylation enhances the accessibility of the cryptic NF-kappa-B-binding sites marking promoters for increased NF-kappa-B recruitment. Phosphorylates CDC25B and CDC25C which is required for binding to 14-3-3 proteins and leads to initiation of a G2 delay after ultraviolet radiation. Phosphorylates TIAR following DNA damage, releasing TIAR from GADD45A mRNA and preventing mRNA degradation. The p38 MAPKs may also have kinase-independent roles, which are thought to be due to the binding to targets in the absence of phosphorylation. Protein O-Glc-N-acylation catalyzed by the OGT is regulated by MAPK14, and, although OGT does not seem to be phosphorylated by MAPK14, their interaction increases upon MAPK14 activation induced by glucose deprivation. This interaction may regulate OGT activity by recruiting it to specific targets such as neurofilament H, stimulating its O-Glc-N-acylation. Required in mid-fetal development for the growth of embryo-derived blood vessels in the labyrinth layer of the placenta. Also plays an essential role in developmental and stress-induced erythropoiesis, through regulation of EPO gene expression. Isoform MXI2 activation is stimulated by mitogens and oxidative stress and only poorly phosphorylates ELK1 and ATF2. Isoform EXIP may play a role in the early onset of apoptosis. Phosphorylates S100A9 at 'Thr-113'. {ECO:0000269|PubMed:10330143, ECO:0000269|PubMed:10747897, ECO:0000269|PubMed:10943842, ECO:0000269|PubMed:11154262, ECO:0000269|PubMed:11333986, ECO:0000269|PubMed:15905572, ECO:0000269|PubMed:16932740, ECO:0000269|PubMed:17003045, ECO:0000269|PubMed:17724032, ECO:0000269|PubMed:19893488, ECO:0000269|PubMed:20188673, ECO:0000269|PubMed:20932473, ECO:0000269|PubMed:9430721, ECO:0000269|PubMed:9687510, ECO:0000269|PubMed:9792677, ECO:0000269|PubMed:9858528}.; FUNCTION:, Microbial infection Activated by phosphorylation by M.tuberculosis EsxA in T-cells leading to inhibition of IFN-gamma production; phosphorylation is apparent within 15 minute and is inhibited by kinase-specific inhibitors SB203580 and siRNA, PubMed:21586573. {ECO:0000269|PubMed:21586573}.
Subcellular locationCytoplasm {ECO:0000269|PubMed:7535770}. Nucleus {ECO:0000269|PubMed:7535770}.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: Q16539
Gene Ontology
(Biological Process)
Complete annatation
3'-UTR-mediated mRNA stabilization [GO:0070935];
activation of MAPK activity [GO:0000187];
angiogenesis [GO:0001525];
apoptotic process [GO:0006915];
cartilage condensation [GO:0001502];
cell morphogenesis [GO:0000902];
cell surface receptor signaling pathway [GO:0007166];
cellular response to ionizing radiation [GO:0071479];
cellular response to lipopolysaccharide [GO:0071222];
cellular response to vascular endothelial growth factor stimulus [GO:0035924];
cellular response to virus [GO:0098586];
chemotaxis [GO:0006935];
chondrocyte differentiation [GO:0002062];
DNA damage checkpoint [GO:0000077];
fatty acid oxidation [GO:0019395];
glucose metabolic process [GO:0006006];
intracellular signal transduction [GO:0035556];
lipopolysaccharide-mediated signaling pathway [GO:0031663];
movement of cell or subcellular component [GO:0006928];
myoblast differentiation involved in skeletal muscle regeneration [GO:0014835];
negative regulation of canonical Wnt signaling pathway [GO:0090090];
osteoclast differentiation [GO:0030316];
p38MAPK cascade [GO:0038066];
peptidyl-serine phosphorylation [GO:0018105];
placenta development [GO:0001890];
positive regulation of brown fat cell differentiation [GO:0090336];
positive regulation of cardiac muscle cell proliferation [GO:0060045];
positive regulation of cyclase activity [GO:0031281];
positive regulation of erythrocyte differentiation [GO:0045648];
positive regulation of gene expression [GO:0010628];
positive regulation of glucose import [GO:0046326];
positive regulation of interleukin-12 secretion [GO:2001184];
positive regulation of muscle cell differentiation [GO:0051149];
positive regulation of myoblast differentiation [GO:0045663];
positive regulation of myoblast fusion [GO:1901741];
positive regulation of myotube differentiation [GO:0010831];
positive regulation of protein import into nucleus [GO:0042307];
positive regulation of reactive oxygen species metabolic process [GO:2000379];
positive regulation of transcription from RNA polymerase II promoter [GO:0045944];
Ras protein signal transduction [GO:0007265];
regulation of cytokine production involved in inflammatory response [GO:1900015];
regulation of ossification [GO:0030278];
regulation of sequence-specific DNA binding transcription factor activity [GO:0051090];
regulation of signal transduction by p53 class mediator [GO:1901796];
regulation of transcription from RNA polymerase II promoter [GO:0006357];
response to muramyl dipeptide [GO:0032495];
response to muscle stretch [GO:0035994];
signal transduction [GO:0007165];
signal transduction in response to DNA damage [GO:0042770];
skeletal muscle tissue development [GO:0007519];
stress-induced premature senescence [GO:0090400];
striated muscle cell differentiation [GO:0051146];
transcription, DNA-templated [GO:0006351];
transmembrane receptor protein serine/threonine kinase signaling pathway [GO:0007178];
vascular endothelial growth factor receptor signaling pathway [GO:0048010]
Gene Ontology
(Molecular Function)
Complete annatation
ATP binding [GO:0005524];
enzyme binding [GO:0019899];
MAP kinase activity [GO:0004707];
MAP kinase kinase activity [GO:0004708];
NFAT protein binding [GO:0051525];
protein phosphatase binding [GO:0019903];
protein serine/threonine kinase activity [GO:0004674]
Gene Ontology
(Cellular Component)
Complete annatation
cytoplasm [GO:0005737];
cytosol [GO:0005829];
extracellular exosome [GO:0070062];
mitochondrion [GO:0005739];
nucleoplasm [GO:0005654];
nucleus [GO:0005634];
spindle pole [GO:0000922]
Protein-protein interaction107819
Phylogenetic treeQ16539
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. CD3-0.6288378258062530.05713368375728280.111587259503663
AZA vs. DISU0.06045531561857280.8111755061545240.983626273983733
AZA vs. IL7-0.01380408903301310.9428022166554180.999311006273513
AZA vs. SAHA0.1077051695850170.6595397680151690.897607661887022
DISU vs. CD30.6769207896861320.06340280343607050.130702635346974
DISU vs. IL7-0.08342631665682830.7405015564523870.936419844268076
DISU vs. SAHA0.04873403147302570.8678029975564990.964997618852509
DMSO vs. AZA-0.06933296528068570.6794151783910891
DMSO vs. CD30.5482157066679820.08923136999836530.155713030119932
DMSO vs. DISU-0.1316292501837840.5897896055855180.934945325624988
DMSO vs. IL70.06279882821188080.7271544925333030.944866241175746
DMSO vs. SAHA0.1706661878107050.4701025166839640.795471800274973
HIV vs. Mock in Activation0.08235978823032620.8951955173187080.999983755607037
HIV vs. Mock in Latency0.02448189513024520.8822618463511930.999834320637052
IL7 vs. CD30.6223272340078280.05454611489106040.11811813316373
SAHA vs. CD30.7120414157354310.04819458528701040.0960450145828149
SAHA vs. IL70.1183249262518540.6281788851989080.815323096654361
(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 -0.139871 0.34501
(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
0.978 0.944 0.821 0.947 0.945
(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
DB01761 4-[5-[2-(1-Phenyl-Ethylamino)-Pyrimidin-4-Yl]-1-Methyl-4-(3-Trifluoromethylphenyl)-1h-Imidazol-2-Yl]-Piperidine experimental unknown unknown
DB01807 N-[(3z)-5-Tert-Butyl-2-Phenyl-1,2-Dihydro-3h-Pyrazol-3-Ylidene]-N&,39;-(4-Chlorophenyl)Urea experimental unknown unknown
DB01948 1-(2,6-Dichlorophenyl)-5-(2,4-Difluorophenyl)-7-Piperidin-4-Yl-3,4-Dihydroquinolin-2(1h)-One experimental unknown unknown
DB01953 Inhibitor of P38 Kinase experimental unknown unknown
DB01988 6((S)-3-Benzylpiperazin-1-Yl)-3-(Naphthalen-2-Yl)-4-(Pyridin-4-Yl)Pyrazine experimental unknown unknown
DB02195 3-(4-Fluorophenyl)-1-Hydroxy-2-(Pyridin-4-Yl)-1h-Pyrrolo[3,2-B]Pyridine experimental unknown unknown
DB02277 1-(5-Tert-Butyl-2-Methyl-2h-Pyrazol-3-Yl)-3-(4-Chloro-Phenyl)-Urea experimental unknown unknown
DB02352 3-(Benzyloxy)Pyridin-2-Amine experimental unknown unknown
DB02873 1-(2,6-Dichlorophenyl)-5-(2,4-Difluorophenyl)-7-Piperazin-1-Yl-3,4-Dihydroquinazolin-2(1h)-One experimental unknown unknown
DB02984 4-[3-Methylsulfanylanilino]-6,7-Dimethoxyquinazoline experimental unknown unknown
DB03044 1-(5-Tert-Butyl-2-P-Tolyl-2h-Pyrazol-3-Yl)-3-[4-(2-Morpholin-4-Yl-Ethoxy)-Naphthalen-1-Yl]-Urea experimental unknown unknown
DB03110 2-Chlorophenol experimental unknown unknown
DB04338 SB220025 experimental unknown unknown
DB04797 Triazolopyridine experimental unknown unknown
DB05412 SCIO-469 investigational unknown unknown
DB05157 KC706 investigational unknown unknown
DB05470 VX-702 investigational unknown unknown
DB06882 1-[1-(3-aminophenyl)-3-tert-butyl-1H-pyrazol-5-yl]-3-naphthalen-1-ylurea experimental unknown unknown
DB06940 N-ethyl-4-{[5-(methoxycarbamoyl)-2-methylphenyl]amino}-5-methylpyrrolo[2,1-f][1,2,4]triazine-6-carboxamide experimental unknown unknown
DB06991 N-[2-methyl-5-(methylcarbamoyl)phenyl]-2-{[(1R)-1-methylpropyl]amino}-1,3-thiazole-5-carboxamide experimental unknown unknown
DB07138 5-(2,6-dichlorophenyl)-2-[(2,4-difluorophenyl)sulfanyl]-6H-pyrimido[1,6-b]pyridazin-6-one experimental unknown unknown
DB07307 N-cyclopropyl-4-methyl-3-[1-(2-methylphenyl)phthalazin-6-yl]benzamide experimental unknown unknown
DB07459 4-PHENOXY-N-(PYRIDIN-2-YLMETHYL)BENZAMIDE experimental unknown unknown
DB07607 4-[5-(3-IODO-PHENYL)-2-(4-METHANESULFINYL-PHENYL)-1H-IMIDAZOL-4-YL]-PYRIDINE experimental unknown unknown
DB07811 N-cyclopropyl-2&,39;,6-dimethyl-4&,39;-(5-methyl-1,3,4-oxadiazol-2-yl)biphenyl-3-carboxamide experimental unknown unknown
DB07829 4-[3-(4-FLUOROPHENYL)-1H-PYRAZOL-4-YL]PYRIDINE experimental unknown unknown
DB07832 4-{4-[(5-hydroxy-2-methylphenyl)amino]quinolin-7-yl}-1,3-thiazole-2-carbaldehyde experimental unknown unknown
DB07833 N-(3-cyanophenyl)-2&,39;-methyl-5&,39;-(5-methyl-1,3,4-oxadiazol-2-yl)-4-biphenylcarboxamide experimental unknown unknown
DB07834 N-(cyclopropylmethyl)-2&,39;-methyl-5&,39;-(5-methyl-1,3,4-oxadiazol-2-yl)biphenyl-4-carboxamide experimental unknown unknown
DB07835 N~3~-cyclopropyl-N~4~&,39;-(cyclopropylmethyl)-6-methylbiphenyl-3,4&,39;-dicarboxamide experimental unknown unknown
DB07941 3-{3-bromo-4-[(2,4-difluorobenzyl)oxy]-6-methyl-2-oxopyridin-1(2H)-yl}-N,4-dimethylbenzamide experimental unknown unknown
DB07942 2-fluoro-4-[4-(4-fluorophenyl)-1H-pyrazol-3-yl]pyridine experimental unknown unknown
DB07943 2-{4-[5-(4-chlorophenyl)-4-pyrimidin-4-yl-1H-pyrazol-3-yl]piperidin-1-yl}-2-oxoethanol experimental unknown unknown
DB08064 N-(3-TERT-BUTYL-1H-PYRAZOL-5-YL)-N&,39;-{4-CHLORO-3-[(PYRIDIN-3-YLOXY)METHYL]PHENYL}UREA experimental unknown unknown
DB08068 N-[4-CHLORO-3-(PYRIDIN-3-YLOXYMETHYL)-PHENYL]-3-FLUORO- experimental unknown unknown
DB08091 3-FLUORO-5-MORPHOLIN-4-YL-N-[3-(2-PYRIDIN-4-YLETHYL)-1H-INDOL-5-YL]BENZAMIDE experimental unknown unknown
DB08092 3-fluoro-N-1H-indol-5-yl-5-morpholin-4-ylbenzamide experimental unknown unknown
DB08093 3-(1-NAPHTHYLMETHOXY)PYRIDIN-2-AMINE experimental unknown unknown
DB08095 3-(2-CHLOROPHENYL)-1-(2-{[(1S)-2-HYDROXY-1,2-DIMETHYLPROPYL]AMINO}PYRIMIDIN-4-YL)-1-(4-METHOXYPHENYL)UREA experimental unknown unknown
DB08096 8-(2-CHLOROPHENYLAMINO)-2-(2,6-DIFLUOROPHENYLAMINO)-9-ETHYL-9H-PURINE-1,7-DIIUM experimental unknown unknown
DB08097 2-(2,6-DIFLUOROPHENOXY)-N-(2-FLUOROPHENYL)-9-ISOPROPYL-9H-PURIN-8-AMINE experimental unknown unknown
DB08242 N,4-dimethyl-3-[(1-phenyl-1H-pyrazolo[3,4-d]pyrimidin-4-yl)amino]benzamide experimental unknown unknown
DB08349 N-cyclopropyl-3-{[1-(2,4-difluorophenyl)-7-methyl-6-oxo-6,7-dihydro-1H-pyrazolo[3,4-b]pyridin-4-yl]amino}-4-methylbenzamide experimental unknown unknown
DB08351 N-cyclopropyl-4-methyl-3-{2-[(2-morpholin-4-ylethyl)amino]quinazolin-6-yl}benzamide experimental unknown unknown
DB08352 6-[4-(2-fluorophenyl)-1,3-oxazol-5-yl]-N-(1-methylethyl)-1,3-benzothiazol-2-amine experimental unknown unknown
DB08395 2-(ETHOXYMETHYL)-4-(4-FLUOROPHENYL)-3-[2-(2-HYDROXYPHENOXY)PYRIMIDIN-4-YL]ISOXAZOL-5(2H)-ONE experimental unknown unknown
DB08423 [5-AMINO-1-(4-FLUOROPHENYL)-1H-PYRAZOL-4-YL][3-(PIPERIDIN-4-YLOXY)PHENYL]METHANONE experimental unknown unknown
DB08424 [5-AMINO-1-(4-FLUOROPHENYL)-1H-PYRAZOL-4-YL](3-{[(2R)-2,3-DIHYDROXYPROPYL]OXY}PHENYL)METHANONE experimental unknown unknown
DB08521 4-[5-(4-FLUORO-PHENYL)-2-(4-METHANESULFINYL-PHENYL)-3H-IMIDAZOL-4-YL]-PYRIDINE experimental unknown unknown
DB03980 4-(Fluorophenyl)-1-Cyclopropylmethyl-5-(2-Amino-4-Pyrimidinyl)Imidazole experimental unknown unknown
DB08522 4-(4-FLUOROPHENYL)-1-CYCLOROPROPYLMETHYL-5-(4-PYRIDYL)-IMIDAZOLE experimental unknown unknown
DB08730 3-FLUORO-5-MORPHOLIN-4-YL-N-[1-(2-PYRIDIN-4-YLETHYL)-1H-INDOL-6-YL]BENZAMIDE experimental unknown unknown

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
1A9U X-ray 2.5Å A=1-360.
1BL6 X-ray 2.5Å A=1-360.
1BL7 X-ray 2.5Å A=1-360.
1BMK X-ray 2.4Å A=1-360.
1DI9 X-ray 2.6Å A=1-360.
1IAN X-ray 2.0Å A=2-360.
1KV1 X-ray 2.5Å A=1-360.
1KV2 X-ray 2.8Å A=1-360.
1M7Q X-ray 2.4Å A=1-360.
1OUK X-ray 2.5Å A=1-360.
1OUY X-ray 2.5Å A=1-360.
1OVE X-ray 2.1Å A=1-360.
1OZ1 X-ray 2.1Å A=1-360.
1R39 X-ray 2.3Å A=1-360.
1R3C X-ray 2.0Å A=1-360.
1W7H X-ray 2.2Å A=2-360.
1W82 X-ray 2.2Å A=2-360.
1W83 X-ray 2.5Å A=2-360.
1W84 X-ray 2.2Å A=2-360.
1WBN X-ray 2.4Å A=2-360.
1WBO X-ray 2.1Å A=2-360.
1WBS X-ray 1.8Å A=2-360.
1WBT X-ray 2.0Å A=2-360.
1WBV X-ray 2.0Å A=2-360.
1WBW X-ray 2.4Å A=2-360.
1WFC X-ray 2.3Å A=1-360.
1YQJ X-ray 2.0Å A=2-360.
1ZYJ X-ray 2.0Å A=1-360.
1ZZ2 X-ray 2.0Å A=1-360.
1ZZL X-ray 2.0Å A=4-354.
2BAJ X-ray 2.2Å A=2-360.
2BAK X-ray 2.2Å A=2-360.
2BAL X-ray 2.1Å A=2-360.
2BAQ X-ray 2.8Å A=2-360.
2FSL X-ray 1.7Å X=2-360.
2FSM X-ray 1.8Å X=2-360.
2FSO X-ray 1.8Å X=2-360.
2FST X-ray 1.4Å X=2-360.
2GFS X-ray 1.7Å A=2-360.
2I0H X-ray 2.0Å A=1-360.
2LGC NMR - A=2-354.
2NPQ X-ray 1.8Å A=2-360.
2OKR X-ray 2.0Å A/D=2-360.
2ONL X-ray 4.0Å A/B=2-360.
2QD9 X-ray 1.7Å A=2-360.
2RG5 X-ray 2.4Å A=2-360.
2RG6 X-ray 1.7Å A=2-360.
2Y8O X-ray 1.9Å A=1-360.
2YIS X-ray 2.0Å A=2-360.
2YIW X-ray 2.0Å A=2-360.
2YIX X-ray 2.3Å A=4-354.
2ZAZ X-ray 1.8Å A=1-360.
2ZB0 X-ray 2.1Å A=1-360.
2ZB1 X-ray 2.5Å A=1-360.
3BV2 X-ray 2.4Å A=2-360.
3BV3 X-ray 2.5Å A=2-360.
3BX5 X-ray 2.4Å A=2-360.
3C5U X-ray 2.8Å A=2-360.
3CTQ X-ray 1.9Å A=5-352.
3D7Z X-ray 2.1Å A=1-360.
3D83 X-ray 1.9Å A=1-360.
3DS6 X-ray 2.9Å A/B/C/D=1-360.
3DT1 X-ray 2.8Å A=1-360.
3E92 X-ray 2.0Å A=1-360.
3E93 X-ray 2.0Å A=1-360.
3FC1 X-ray 2.4Å X=1-360.
3FI4 X-ray 2.2Å A=1-360.
3FKL X-ray 2.0Å A=1-360.
3FKN X-ray 2.0Å A=1-360.
3FKO X-ray 2.0Å A=1-360.
3FL4 X-ray 1.8Å A=1-360.
3FLN X-ray 1.9Å C=1-360.
3FLQ X-ray 1.9Å A=1-360.
3FLS X-ray 2.3Å A=1-360.
3FLW X-ray 2.1Å A=1-360.
3FLY X-ray 1.8Å A=1-360.
3FLZ X-ray 2.2Å A=1-360.
3FMH X-ray 1.9Å A=1-360.
3FMJ X-ray 2.0Å A=1-360.
3FMK X-ray 1.7Å A=1-360.
3FML X-ray 2.1Å A=1-360.
3FMM X-ray 2.0Å A=1-360.
3FMN X-ray 1.9Å A=1-360.
3FSF X-ray 2.1Å A=1-360.
3FSK X-ray 2.0Å A=1-360.
3GC7 X-ray 1.8Å A=1-360.
3GCP X-ray 2.2Å A=2-360.
3GCQ X-ray 2.0Å A=2-360.
3GCS X-ray 2.1Å A=2-360.
3GCU X-ray 2.1Å A/B=2-360.
3GCV X-ray 2.3Å A=2-360.
3GFE X-ray 2.1Å A=1-360.
3GI3 X-ray 2.4Å A=1-360.
3HA8 X-ray 2.4Å A=1-360.
3HEC X-ray 2.5Å A=5-352.
3HEG X-ray 2.2Å A=5-352.
3HL7 X-ray 1.8Å A=1-360.
3HLL X-ray 1.9Å A=1-360.
3HP2 X-ray 2.1Å A=1-360.
3HP5 X-ray 2.3Å A=1-360.
3HRB X-ray 2.2Å A=2-360.
3HUB X-ray 2.2Å A=2-360.
3HUC X-ray 1.8Å A=2-360.
3HV3 X-ray 2.0Å A=2-360.
3HV4 X-ray 2.6Å A/B=2-360.
3HV5 X-ray 2.2Å A/B=2-360.
3HV6 X-ray 1.9Å A=2-360.
3HV7 X-ray 2.4Å A=2-360.
3HVC X-ray 2.1Å A=1-360.
3IPH X-ray 2.1Å A=1-360.
3ITZ X-ray 2.2Å A=1-360.
3IW5 X-ray 2.5Å A=2-360.
3IW6 X-ray 2.1Å A=2-360.
3IW7 X-ray 2.4Å A=2-360.
3IW8 X-ray 2.0Å A=2-360.
3K3I X-ray 1.7Å A=5-352.
3K3J X-ray 2.0Å A=1-360.
3KF7 X-ray 2.0Å A=1-360.
3KQ7 X-ray 1.8Å A=1-360.
3L8S X-ray 2.3Å A=2-360.
3L8X X-ray 2.1Å A=2-360.
3LFA X-ray 2.1Å A=2-360.
3LFB X-ray 2.6Å A=2-360.
3LFC X-ray 2.8Å A=2-360.
3LFD X-ray 3.4Å A=2-360.
3LFE X-ray 2.3Å A=2-360.
3LFF X-ray 1.5Å A=2-360.
3LHJ X-ray 3.3Å A=1-360.
3MGY X-ray 2.1Å A=1-360.
3MH0 X-ray 2.0Å A=1-360.
3MH1 X-ray 2.2Å A=1-360.
3MH2 X-ray 2.3Å A=1-360.
3MH3 X-ray 2.2Å A=1-360.
3MPA X-ray 2.1Å A=1-360.
3MPT X-ray 1.8Å A=1-360.
3MVL X-ray 2.8Å A/B=2-360.
3MVM X-ray 2.0Å A/B=2-360.
3MW1 X-ray 2.8Å A=2-360.
3NEW X-ray 2.5Å A=1-360.
3NNU X-ray 2.4Å A=1-354.
3NNV X-ray 2.1Å A=1-354.
3NNW X-ray 1.8Å A=1-354.
3NNX X-ray 2.2Å A=1-354.
3NWW X-ray 2.0Å A=2-360.
3O8P X-ray 2.1Å A=1-360.
3O8T X-ray 2.0Å A=1-360.
3O8U X-ray 2.1Å A=1-360.
3OBG X-ray 2.8Å A=1-360.
3OBJ X-ray 2.4Å A=1-360.
3OC1 X-ray 2.5Å A=1-360.
3OCG X-ray 2.2Å A=2-360.
3OD6 X-ray 2.6Å X=1-360.
3ODY X-ray 2.2Å X=1-360.
3ODZ X-ray 2.3Å X=1-360.
3OEF X-ray 1.6Å X=1-360.
3PG3 X-ray 2.0Å A=2-360.
3QUD X-ray 2.0Å A=2-360.
3QUE X-ray 2.7Å A=2-360.
3RIN X-ray 2.2Å A=1-360.
3ROC X-ray 1.7Å A=1-360.
3S3I X-ray 1.8Å A=4-352.
3S4Q X-ray 2.2Å A=2-360.
3U8W X-ray 2.1Å A=1-360.
3UVP X-ray 2.4Å A=2-360.
3UVQ X-ray 2.2Å A=2-360.
3UVR X-ray 2.1Å A=2-360.
3ZS5 X-ray 1.6Å A=2-360.
3ZSG X-ray 1.8Å A=2-360.
3ZSH X-ray 2.0Å A=2-360.
3ZSI X-ray 2.4Å A=2-360.
3ZYA X-ray 1.9Å A=1-360.
4A9Y X-ray 2.2Å A=2-360.
4AA0 X-ray 1.8Å A=2-360.
4AA4 X-ray 2.3Å A=2-360.
4AA5 X-ray 2.3Å A=2-360.
4AAC X-ray 2.5Å A=2-360.
4DLI X-ray 1.9Å A=2-360.
4DLJ X-ray 2.6Å A=2-360.
4E5A X-ray 1.8Å X=1-360.
4E5B X-ray 2.0Å A=1-360.
4E6A X-ray 2.0Å A=1-360.
4E6C X-ray 2.3Å A=1-360.
4E8A X-ray 2.7Å A=1-360.
4EH2 X-ray 2.0Å A=2-360.
4EH3 X-ray 2.4Å A=2-360.
4EH4 X-ray 2.5Å A=2-360.
4EH5 X-ray 2.0Å A=2-360.
4EH6 X-ray 2.1Å A=2-360.
4EH7 X-ray 2.1Å A=2-360.
4EH8 X-ray 2.2Å A=2-360.
4EH9 X-ray 2.1Å A=2-360.
4EHV X-ray 1.6Å A=2-360.
4EWQ X-ray 2.1Å A=2-360.
4F9W X-ray 2.0Å A=2-360.
4F9Y X-ray 1.8Å A=2-360.
4FA2 X-ray 2.0Å A=2-360.
4GEO X-ray 1.6Å A=2-360.
4KIN X-ray 1.9Å A/B/C/D=2-360.
4KIP X-ray 2.2Å A/B=2-360.
4KIQ X-ray 2.5Å A/B/C/D=2-360.
4L8M X-ray 2.1Å A=2-360.
4R3C X-ray 2.0Å A=2-360.
4ZTH X-ray 2.1Å A=2-360.
5ETC X-ray 2.4Å A=1-360.
5ETI X-ray 2.8Å A=1-360.

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

HIV Partner Interaction Type PubMed
Nef induces phosphorylation of 22407921
Envelope surface glycoprotein gp120 interacts with 15642743
Nef interacts with 24658403
Tat activates 18160848
Nef inhibits 20068037
Envelope surface glycoprotein gp160; precursor activates 15603708
Envelope transmembrane glycoprotein gp41 activates 15642743
Tat interacts with 23955241
Envelope surface glycoprotein gp120 induces phosphorylation of 19023333
Vpr cooperates with 20145198
Nef regulated by 18799583
Envelope surface glycoprotein gp120 inhibited by 16111829
Tat induces phosphorylation of 24418364
Tat cooperates with 20849923
Tat regulated by 17202341
Envelope surface glycoprotein gp120 upregulates 12089333
Envelope surface glycoprotein gp120 activates 11468147
Envelope surface glycoprotein gp120 regulated by 19700666
Envelope surface glycoprotein gp120 inactivates 18371353
Nef activates 17182689

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa01522 Endocrine resistance - Homo sapiens (human)
hsa04010 MAPK signaling pathway - Homo sapiens (human)
hsa04015 Rap1 signaling pathway - Homo sapiens (human)
hsa04068 FoxO signaling pathway - Homo sapiens (human)
hsa04071 Sphingolipid signaling pathway - Homo sapiens (human)
hsa04261 Adrenergic signaling in cardiomyocytes - Homo sapiens (human)
hsa04370 VEGF signaling pathway - Homo sapiens (human)
hsa04380 Osteoclast differentiation - Homo sapiens (human)
hsa04550 Signaling pathways regulating pluripotency of stem cells - Homo sapiens (human)
hsa04611 Platelet activation - Homo sapiens (human)
hsa04620 Toll-like receptor signaling pathway - Homo sapiens (human)
hsa04621 NOD-like receptor signaling pathway - Homo sapiens (human)
hsa04622 RIG-I-like receptor signaling pathway - Homo sapiens (human)
hsa04657 IL-17 signaling pathway - Homo sapiens (human)
hsa04658 Th1 and Th2 cell differentiation - Homo sapiens (human)
hsa04659 Th17 cell differentiation - Homo sapiens (human)
hsa04660 T cell receptor signaling pathway - Homo sapiens (human)
hsa04664 Fc epsilon RI signaling pathway - Homo sapiens (human)
hsa04668 TNF signaling pathway - Homo sapiens (human)
hsa04670 Leukocyte transendothelial migration - Homo sapiens (human)
hsa04722 Neurotrophin signaling pathway - Homo sapiens (human)
hsa04723 Retrograde endocannabinoid signaling - Homo sapiens (human)
hsa04728 Dopaminergic synapse - Homo sapiens (human)
hsa04750 Inflammatory mediator regulation of TRP channels - Homo sapiens (human)
hsa04912 GnRH signaling pathway - Homo sapiens (human)
hsa04914 Progesterone-mediated oocyte maturation - Homo sapiens (human)
hsa04917 Prolactin signaling pathway - Homo sapiens (human)
hsa04933 AGE-RAGE signaling pathway in diabetic complications - Homo sapiens (human)
hsa05014 Amyotrophic lateral sclerosis (ALS) - Homo sapiens (human)
hsa05120 Epithelial cell signaling in Helicobacter pylori infection - Homo sapiens (human)
hsa05131 Shigellosis - Homo sapiens (human)
hsa05132 Salmonella infection - Homo sapiens (human)
hsa05133 Pertussis - Homo sapiens (human)
hsa05140 Leishmaniasis - Homo sapiens (human)
hsa05142 Chagas disease (American trypanosomiasis) - Homo sapiens (human)
hsa05145 Toxoplasmosis - Homo sapiens (human)
hsa05152 Tuberculosis - Homo sapiens (human)
hsa05160 Hepatitis C - Homo sapiens (human)
hsa05164 Influenza A - Homo sapiens (human)
hsa05169 Epstein-Barr virus infection - Homo sapiens (human)
hsa05205 Proteoglycans in cancer - Homo sapiens (human)