Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0012392
UniProt IDP00533
Primary gene name(s)EGFR
Synonym gene name(s)ERBB, ERBB1, HER1
Protein nameEpidermal growth factor receptor
Protein functionReceptor tyrosine kinase binding ligands of the EGF family and activating several signaling cascades to convert extracellular cues into appropriate cellular responses. Known ligands include EGF, TGFA/TGF-alpha, amphiregulin, epigen/EPGN, BTC/betacellulin, epiregulin/EREG and HBEGF/heparin-binding EGF. Ligand binding triggers receptor homo- and/or heterodimerization and autophosphorylation on key cytoplasmic residues. The phosphorylated receptor recruits adapter proteins like GRB2 which in turn activates complex downstream signaling cascades. Activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STATs modules. May also activate the NF-kappa-B signaling cascade. Also directly phosphorylates other proteins like RGS16, activating its GTPase activity and probably coupling the EGF receptor signaling to the G protein-coupled receptor signaling. Also phosphorylates MUC1 and increases its interaction with SRC and CTNNB1/beta-catenin. Plays a role in enhancing learning and memory performance, By similarity. {ECO:0000250|UniProtKB:Q01279}.; FUNCTION: Isoform 2 may act as an antagonist of EGF action.
Subcellular locationCell membrane;
Single-pass type I membrane protein. Endoplasmic reticulum membrane;
Single-pass type I membrane protein. Golgi apparatus membrane;
Single-pass type I membrane protein. Nucleus membrane;
Single-pass type I membrane protein. Endosome. Endosome membrane. Nucleus. Note=In response to EGF, translocated from the cell membrane to the nucleus via Golgi and ER. Endocytosed upon activation by ligand. Colocalized with GPER1 in the nucleus of estrogen agonist-induced cancer-associated fibroblasts, CAF.;
SUBCELLULAR LOCATION: Isoform 2: Secreted.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: P00533
Gene Ontology
(Biological Process)
Complete annatation
activation of phospholipase A2 activity by calcium-mediated signaling [GO:0043006];
activation of phospholipase C activity [GO:0007202];
astrocyte activation [GO:0048143];
cell proliferation [GO:0008283];
cell surface receptor signaling pathway [GO:0007166];
cellular response to amino acid stimulus [GO:0071230];
cellular response to dexamethasone stimulus [GO:0071549];
cellular response to drug [GO:0035690];
cellular response to epidermal growth factor stimulus [GO:0071364];
cellular response to estradiol stimulus [GO:0071392];
cellular response to mechanical stimulus [GO:0071260];
cerebral cortex cell migration [GO:0021795];
circadian rhythm [GO:0007623];
digestive tract morphogenesis [GO:0048546];
diterpenoid metabolic process [GO:0016101];
embryonic placenta development [GO:0001892];
epidermal growth factor receptor signaling pathway [GO:0007173];
ERBB2 signaling pathway [GO:0038128];
eyelid development in camera-type eye [GO:0061029];
hair follicle development [GO:0001942];
hydrogen peroxide metabolic process [GO:0042743];
learning or memory [GO:0007611];
liver regeneration [GO:0097421];
lung development [GO:0030324];
magnesium ion homeostasis [GO:0010960];
MAPK cascade [GO:0000165];
midgut development [GO:0007494];
morphogenesis of an epithelial fold [GO:0060571];
negative regulation of apoptotic process [GO:0043066];
negative regulation of cardiocyte differentiation [GO:1905208];
negative regulation of epidermal growth factor receptor signaling pathway [GO:0042059];
negative regulation of mitotic cell cycle [GO:0045930];
negative regulation of protein catabolic process [GO:0042177];
neuron projection morphogenesis [GO:0048812];
ossification [GO:0001503];
ovulation cycle [GO:0042698];
phosphatidylinositol-mediated signaling [GO:0048015];
positive regulation of bone resorption [GO:0045780];
positive regulation of catenin import into nucleus [GO:0035413];
positive regulation of cell growth [GO:0030307];
positive regulation of cell migration [GO:0030335];
positive regulation of cell proliferation [GO:0008284];
positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle [GO:0031659];
positive regulation of DNA repair [GO:0045739];
positive regulation of DNA replication [GO:0045740];
positive regulation of epithelial cell proliferation [GO:0050679];
positive regulation of ERK1 and ERK2 cascade [GO:0070374];
positive regulation of fibroblast proliferation [GO:0048146];
positive regulation of inflammatory response [GO:0050729];
positive regulation of MAP kinase activity [GO:0043406];
positive regulation of nitric oxide biosynthetic process [GO:0045429];
positive regulation of phosphorylation [GO:0042327];
positive regulation of production of miRNAs involved in gene silencing by miRNA [GO:1903800];
positive regulation of prolactin secretion [GO:1902722];
positive regulation of protein kinase B signaling [GO:0051897];
positive regulation of protein phosphorylation [GO:0001934];
positive regulation of smooth muscle cell proliferation [GO:0048661];
positive regulation of superoxide anion generation [GO:0032930];
positive regulation of synaptic transmission, glutamatergic [GO:0051968];
positive regulation of transcription from RNA polymerase II promoter [GO:0045944];
positive regulation of vasoconstriction [GO:0045907];
positive regulation of vasodilation [GO:0045909];
protein autophosphorylation [GO:0046777];
protein insertion into membrane [GO:0051205];
regulation of cell motility [GO:2000145];
regulation of nitric-oxide synthase activity [GO:0050999];
regulation of peptidyl-tyrosine phosphorylation [GO:0050730];
regulation of phosphatidylinositol 3-kinase signaling [GO:0014066];
response to calcium ion [GO:0051592];
response to cobalamin [GO:0033590];
response to hydroxyisoflavone [GO:0033594];
response to osmotic stress [GO:0006970];
response to oxidative stress [GO:0006979];
response to stress [GO:0006950];
response to UV-A [GO:0070141];
salivary gland morphogenesis [GO:0007435];
signal transduction [GO:0007165];
single organismal cell-cell adhesion [GO:0016337];
tongue development [GO:0043586];
translation [GO:0006412];
wound healing [GO:0042060]
Gene Ontology
(Molecular Function)
Complete annatation
actin filament binding [GO:0051015];
ATP binding [GO:0005524];
chromatin binding [GO:0003682];
double-stranded DNA binding [GO:0003690];
enzyme binding [GO:0019899];
epidermal growth factor-activated receptor activity [GO:0005006];
identical protein binding [GO:0042802];
MAP kinase kinase kinase activity [GO:0004709];
phosphatidylinositol-4,5-bisphosphate 3-kinase activity [GO:0046934];
protein heterodimerization activity [GO:0046982];
protein phosphatase binding [GO:0019903];
protein tyrosine kinase activity [GO:0004713];
Ras guanyl-nucleotide exchange factor activity [GO:0005088];
receptor signaling protein tyrosine kinase activity [GO:0004716];
transmembrane receptor protein tyrosine kinase activity [GO:0004714];
transmembrane signaling receptor activity [GO:0004888];
ubiquitin protein ligase binding [GO:0031625]
Gene Ontology
(Cellular Component)
Complete annatation
basolateral plasma membrane [GO:0016323];
cell surface [GO:0009986];
cytoplasm [GO:0005737];
early endosome membrane [GO:0031901];
endocytic vesicle [GO:0030139];
endoplasmic reticulum membrane [GO:0005789];
endosome [GO:0005768];
endosome membrane [GO:0010008];
extracellular space [GO:0005615];
focal adhesion [GO:0005925];
Golgi membrane [GO:0000139];
integral component of membrane [GO:0016021];
membrane [GO:0016020];
membrane raft [GO:0045121];
multivesicular body, internal vesicle lumen [GO:0097489];
nuclear membrane [GO:0031965];
nucleus [GO:0005634];
perinuclear region of cytoplasm [GO:0048471];
plasma membrane [GO:0005886];
receptor complex [GO:0043235];
Shc-EGFR complex [GO:0070435]
Protein-protein interaction108276
Phylogenetic treeP00533
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. CD3-0.3988483821927820.6210345998466480.722463220815736
AZA vs. DISU-0.1589463073903580.8358906907236710.986167923867511
AZA vs. IL7-0.3778278705662140.5474111490825310.999311006273513
AZA vs. SAHA-0.5390249338843910.4239873996725680.776949436258727
DISU vs. CD30.2264189497102350.8010461119173080.863608145547239
DISU vs. IL7-0.2286713661101490.7388764415873580.935394412047279
DISU vs. SAHA-0.3794507469706550.6003703778479590.872618571178184
DMSO vs. AZA0.02291349778288070.9721606204790931
DMSO vs. CD30.4060935121103290.562558927387280.664597729069116
DMSO vs. DISU0.1785275047353960.8010212530853710.976923151986107
DMSO vs. IL7-0.392902498502280.4679510841833230.877499426457811
DMSO vs. SAHA-0.5677230776298810.341533475310280.693886627986147
HIV vs. Mock in Activation-0.1173692868268150.9172416649498120.999983755607037
HIV vs. Mock in Latency0.03382059425954440.9547968322048410.999834320637052
IL7 vs. CD30.02589106848414390.9689089876622410.981740062586243
SAHA vs. CD3-0.1659453748697470.8198616769398620.8723913895315
SAHA vs. IL7-0.1631098999107450.7717990085544320.899393372312791
(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
NOTEST 0.28416 1
(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
unknown unknown unknown unknown unknown
(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
DB00002 Cetuximab approved yes antagonist
DB00317 Gefitinib approved, investigational yes antagonist
DB00530 Erlotinib approved, investigational yes antagonist
DB01259 Lapatinib approved, investigational yes antagonist
DB01269 Panitumumab approved, investigational yes suppressor
DB00281 Lidocaine approved, vet_approved unknown antagonist
DB03496 Flavopiridol experimental, investigational unknown unknown
DB00072 Trastuzumab approved, investigational unknown unknown
DB04988 IGN311 investigational unknown unknown
DB05294 Vandetanib approved unknown inhibitor
DB05324 HuMax-EGFr investigational unknown unknown
DB05374 CDX-110 investigational unknown unknown
DB05101 Matuzumab investigational unknown unknown
DB05424 CI-1033 investigational unknown unknown
DB05774 IMC-11F8 investigational unknown unknown
DB05900 INSM-18 investigational unknown unknown
DB07602 S-{3-[(4-ANILINOQUINAZOLIN-6-YL)AMINO]-3-OXOPROPYL}-L-CYSTEINE experimental unknown unknown
DB07662 N-[4-(3-BROMO-PHENYLAMINO)-QUINAZOLIN-6-YL]-ACRYLAMIDE experimental unknown unknown
DB08916 Afatinib approved yes inhibitor
DB09559 Necitumumab approved yes antagonist
DB09330 Osimertinib approved yes inhibitor

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
1DNQ Model - A=25-336.
1DNR Model - A=337-645.
1IVO X-ray 3.3Å A/B=25-646.
1M14 X-ray 2.6Å A=695-1022.
1M17 X-ray 2.6Å A=695-1022.
1MOX X-ray 2.5Å A/B=25-525.
1NQL X-ray 2.8Å A=25-642.
1XKK X-ray 2.4Å A=695-1022.
1YY9 X-ray 2.6Å A=25-642.
1Z9I NMR - A=669-721.
2EB2 X-ray 2.5Å A=695-1022.
2EB3 X-ray 2.8Å A=695-1022.
2EXP Model - A=311-326.
2EXQ Model - A=27-536.
2GS2 X-ray 2.8Å A=696-1022.
2GS6 X-ray 2.6Å A=696-1022.
2GS7 X-ray 2.6Å A/B=696-1022.
2ITN X-ray 2.4Å A=696-1019.
2ITO X-ray 3.2Å A=696-1022.
2ITP X-ray 2.7Å A=696-1022.
2ITQ X-ray 2.6Å A=696-1022.
2ITT X-ray 2.7Å A=696-1022.
2ITU X-ray 2.8Å A=696-1022.
2ITV X-ray 2.4Å A=696-1022.
2ITW X-ray 2.8Å A=696-1022.
2ITX X-ray 2.9Å A=696-1022.
2ITY X-ray 3.4Å A=696-1022.
2ITZ X-ray 2.7Å A=696-1022.
2J5E X-ray 3.1Å A=696-1022.
2J5F X-ray 3.0Å A=696-1022.
2J6M X-ray 3.1Å A=696-1022.
2JIT X-ray 3.1Å A/B=696-1022.
2JIU X-ray 3.0Å A/B=695-1022.
2JIV X-ray 3.5Å A/B=695-1022.
2KS1 NMR - B=634-677.
2M0B NMR - A/B=634-677.
2M20 NMR - A/B=642-697.
2N5S NMR - A=642-690.
2RF9 X-ray 3.5Å A/B=696-1022.
2RFD X-ray 3.6Å A/B=702-1022.
2RFE X-ray 2.9Å A/B/C/D=702-1022.
2RGP X-ray 2.0Å A=702-1016.
3B2U X-ray 2.5Å A/B/E/I/M/P/S/V=335-538.
3B2V X-ray 3.3Å A=25-642.
3BEL X-ray 2.3Å A=702-1016.
3BUO X-ray 2.6Å A/C=1063-1075.
3C09 X-ray 3.2Å A/D=336-538.
3G5V X-ray 2.0Å C=311-326.
3G5Y X-ray 1.5Å E=311-326.
3GOP X-ray 2.8Å A=669-1022.
3GT8 X-ray 2.9Å A/B/C/D=696-1022.
3IKA X-ray 2.9Å A/B=694-1022.
3LZB X-ray 2.7Å A/B/C/D/E/F/G/H=696-983.
3NJP X-ray 3.3Å A/B=25-638.
3OB2 X-ray 2.1Å A=1063-1074.
3OP0 X-ray 2.5Å C/D=1066-1076.
3P0Y X-ray 1.8Å A=334-538.
3PFV X-ray 2.2Å C/D=1066-1076.
3POZ X-ray 1.5Å A=696-1022.
3QWQ X-ray 2.7Å A=1-642.
3UG1 X-ray 2.7Å A=695-1022.
3UG2 X-ray 2.5Å A=695-1022.
3VJN X-ray 2.3Å A=695-1022.
3VJO X-ray 2.6Å A=695-1022.
3VRP X-ray 1.5Å B=1062-1074.
3VRR X-ray 2.0Å C=1062-1074.
3W2O X-ray 2.3Å A=698-1022.
3W2P X-ray 2.0Å A=698-1022.
3W2Q X-ray 2.2Å A=698-1022.
3W2R X-ray 2.0Å A=698-1022.
3W2S X-ray 1.9Å A=696-1022.
3W32 X-ray 1.8Å A=696-1022.
3W33 X-ray 1.7Å A=696-1022.
4G5J X-ray 2.8Å A=696-1022.
4G5P X-ray 3.1Å A/B=696-1022.
4HJO X-ray 2.7Å A=696-1022.
4I1Z X-ray 3.0Å A=695-1022.
4I20 X-ray 3.3Å A=695-1022.
4I21 X-ray 3.3Å A/B=695-1022.
4I22 X-ray 1.7Å A=695-1022.
4I23 X-ray 2.8Å A=695-1022.
4I24 X-ray 1.8Å A/B=695-1022.
4JQ7 X-ray 2.7Å A=696-1021.
4JQ8 X-ray 2.8Å A=696-1021.
4JR3 X-ray 2.7Å A=696-1021.
4JRV X-ray 2.8Å A=696-1021.
4KRL X-ray 2.8Å A=335-538.
4KRM X-ray 2.6Å A/C/E/G/I/K=335-538.
4KRO X-ray 3.0Å A=25-642.
4KRP X-ray 2.8Å A=25-642.
4LI5 X-ray 2.6Å A=696-1020.
4LL0 X-ray 4.0Å A/B=694-1022.
4LQM X-ray 2.5Å A=694-1022.
4LRM X-ray 3.5Å A/B/C/D/E=694-1022.
4R3P X-ray 2.9Å A=696-1018.
4R3R X-ray 3.2Å A=696-1018.
4R5S X-ray 3.0Å A=696-1022.
4RIW X-ray 3.1Å B/D=682-1022.
4RIX X-ray 3.1Å B/D=682-1022.
4RIY X-ray 2.9Å B/D=682-1022.
4RJ4 X-ray 2.7Å A=695-1022.
4RJ5 X-ray 3.1Å A=695-1022.
4RJ6 X-ray 2.7Å A=695-1022.
4RJ7 X-ray 2.5Å A=695-1022.
4RJ8 X-ray 2.5Å A=695-1022.
4TKS X-ray 3.2Å A=695-1022.
4UIP X-ray 2.9Å A=26-637.
4UV7 X-ray 2.1Å A=25-645.
4WD5 X-ray 3.3Å A/B=694-1022.
4WKQ X-ray 1.8Å A=696-1022.
4WRG X-ray 1.9Å A=696-1022.
4ZAU X-ray 2.8Å A=696-1022.
4ZJV X-ray 2.7Å A/B=695-1022.
4ZSE X-ray 1.9Å A/B/C/D=695-1022.
5C8K X-ray 3.0Å A=695-1022.
5C8M X-ray 2.9Å A=695-1022.
5C8N X-ray 2.4Å A=695-1022.
5CAL X-ray 2.7Å A=695-1022.
5CAN X-ray 2.8Å A=695-1022.
5CAO X-ray 2.6Å A=695-1022.
5CAP X-ray 2.4Å A=695-1022.
5CAQ X-ray 2.5Å A=695-1022.
5CAS X-ray 2.1Å A=695-1022.
5CAU X-ray 2.2Å A=695-1022.
5CAV X-ray 2.7Å A=695-1022.
5CNN X-ray 1.9Å A/B=696-1042.
5CNO X-ray 1.5Å A/B/X=696-1022.
5CZH X-ray 2.8Å A=694-1022.
5CZI X-ray 2.6Å A=694-1022.
5D41 X-ray 2.3Å A/B=695-1022.
5EDP X-ray 2.9Å A=695-1022.
5EDQ X-ray 2.8Å A=695-1022.
5EDR X-ray 2.6Å A=695-1022.
5EM5 X-ray 2.6Å A=695-1022.
5EM6 X-ray 2.7Å A=695-1022.
5EM7 X-ray 2.8Å A=695-1022.
5EM8 X-ray 2.8Å A=695-1022.
5FED X-ray 2.6Å A=696-1022.
5FEE X-ray 2.7Å A=696-1022.
5FEQ X-ray 3.4Å A=696-1022.
5HCX X-ray 2.6Å A=696-1022.
5HCY X-ray 2.4Å A=696-1022.
5HCZ X-ray 2.6Å A=696-1022.
5HG5 X-ray 1.5Å A=695-1022.
5HG7 X-ray 1.8Å A=695-1022.
5HG8 X-ray 1.4Å A=695-1022.
5HG9 X-ray 2.1Å A=695-1022.
5HIB X-ray 2.8Å A=695-1022.
5HIC X-ray 2.6Å A=695-1022.
5J9Y X-ray 2.8Å A=697-1019.
5J9Z X-ray 2.5Å A=696-1020.
5JEB X-ray 3.3Å A=696-1022.
5SX4 X-ray 2.8Å M/N=335-525.
5SX5 X-ray 2.5Å M/N=335-525.

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

HIV Partner Interaction Type PubMed
Pr55(Gag) upregulates 15507625
18187620
HIV-1 virus replication enhanced by expression of human gene 18187620

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa01521 EGFR tyrosine kinase inhibitor resistance - Homo sapiens (human)
hsa01522 Endocrine resistance - Homo sapiens (human)
hsa04010 MAPK signaling pathway - Homo sapiens (human)
hsa04012 ErbB signaling pathway - Homo sapiens (human)
hsa04014 Ras signaling pathway - Homo sapiens (human)
hsa04015 Rap1 signaling pathway - Homo sapiens (human)
hsa04020 Calcium signaling pathway - Homo sapiens (human)
hsa04060 Cytokine-cytokine receptor interaction - Homo sapiens (human)
hsa04066 HIF-1 signaling pathway - Homo sapiens (human)
hsa04068 FoxO signaling pathway - Homo sapiens (human)
hsa04072 Phospholipase D signaling pathway - Homo sapiens (human)
hsa04144 Endocytosis - Homo sapiens (human)
hsa04151 PI3K-Akt signaling pathway - Homo sapiens (human)
hsa04320 Dorso-ventral axis formation - Homo sapiens (human)
hsa04510 Focal adhesion - Homo sapiens (human)
hsa04520 Adherens junction - Homo sapiens (human)
hsa04540 Gap junction - Homo sapiens (human)
hsa04810 Regulation of actin cytoskeleton - Homo sapiens (human)
hsa04912 GnRH signaling pathway - Homo sapiens (human)
hsa04915 Estrogen signaling pathway - Homo sapiens (human)
hsa04921 Oxytocin signaling pathway - Homo sapiens (human)
hsa05120 Epithelial cell signaling in Helicobacter pylori infection - Homo sapiens (human)
hsa05160 Hepatitis C - Homo sapiens (human)
hsa05200 Pathways in cancer - Homo sapiens (human)
hsa05205 Proteoglycans in cancer - Homo sapiens (human)
hsa05206 MicroRNAs in cancer - Homo sapiens (human)
hsa05212 Pancreatic cancer - Homo sapiens (human)
hsa05213 Endometrial cancer - Homo sapiens (human)
hsa05214 Glioma - Homo sapiens (human)
hsa05215 Prostate cancer - Homo sapiens (human)
hsa05218 Melanoma - Homo sapiens (human)
hsa05219 Bladder cancer - Homo sapiens (human)
hsa05223 Non-small cell lung cancer - Homo sapiens (human)
hsa05224 Breast cancer - Homo sapiens (human)
hsa05230 Central carbon metabolism in cancer - Homo sapiens (human)
hsa05231 Choline metabolism in cancer - Homo sapiens (human)
Menu