Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0002828
UniProt IDP12931
Primary gene name(s)SRC
Synonym gene name(s)SRC1
Protein nameProto-oncogene tyrosine-protein kinase Src
Protein functionNon-receptor protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates in signaling pathways that control a diverse spectrum of biological activities including gene transcription, immune response, cell adhesion, cell cycle progression, apoptosis, migration, and transformation. Due to functional redundancy between members of the SRC kinase family, identification of the specific role of each SRC kinase is very difficult. SRC appears to be one of the primary kinases activated following engagement of receptors and plays a role in the activation of other protein tyrosine kinase, PTK families. Receptor clustering or dimerization leads to recruitment of SRC to the receptor complexes where it phosphorylates the tyrosine residues within the receptor cytoplasmic domains. Plays an important role in the regulation of cytoskeletal organization through phosphorylation of specific substrates such as AFAP1. Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1 and to localize to actin filaments. Cytoskeletal reorganization is also controlled through the phosphorylation of cortactin, CTTN. When cells adhere via focal adhesions to the extracellular matrix, signals are transmitted by integrins into the cell resulting in tyrosine phosphorylation of a number of focal adhesion proteins, including PTK2/FAK1 and paxillin, PXN. In addition to phosphorylating focal adhesion proteins, SRC is also active at the sites of cell-cell contact adherens junctions and phosphorylates substrates such as beta-catenin, CTNNB1, delta-catenin, CTNND1, and plakoglobin, JUP. Another type of cell-cell junction, the gap junction, is also a target for SRC, which phosphorylates connexin-43, GJA1. SRC is implicated in regulation of pre-mRNA-processing and phosphorylates RNA-binding proteins such as KHDRBS1. Also plays a role in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3, leading to increased DNA binding activity of these transcription factors. Involved in the RAS pathway through phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated calcium-activated chloride channel activation. Required for epidermal growth factor receptor, EGFR internalization through phosphorylation of clathrin heavy chain, CLTC and CLTCL1 at 'Tyr-1477'. Involved in beta-arrestin, ARRB1 and ARRB2 desensitization through phosphorylation and activation of GRK2, leading to beta-arrestin phosphorylation and internalization. Has a critical role in the stimulation of the CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal growth factor. Might be involved not only in mediating the transduction of mitogenic signals at the level of the plasma membrane but also in controlling progression through the cell cycle via interaction with regulatory proteins in the nucleus. Plays an important role in osteoclastic bone resorption in conjunction with PTK2B/PYK2. Both the formation of a SRC-PTK2B/PYK2 complex and SRC kinase activity are necessary for this function. Recruited to activated integrins by PTK2B/PYK2, thereby phosphorylating CBL, which in turn induces the activation and recruitment of phosphatidylinositol 3-kinase to the cell membrane in a signaling pathway that is critical for osteoclast function. Promotes energy production in osteoclasts by activating mitochondrial cytochrome C oxidase. Phosphorylates DDR2 on tyrosine residues, thereby promoting its subsequent autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731'. Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-128'. Phosphorylates CBLC at multiple tyrosine residues, phosphorylation at 'Tyr-341' activates CBLC E3 activity. Required for podosome formation, By similarity. {ECO:0000250|UniProtKB:P05480, ECO:0000269|PubMed:11389730, ECO:0000269|PubMed:12615910, ECO:0000269|PubMed:14585963, ECO:0000269|PubMed:16186108, ECO:0000269|PubMed:18586953, ECO:0000269|PubMed:19419966, ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:20525694, ECO:0000269|PubMed:21309750, ECO:0000269|PubMed:21411625, ECO:0000269|PubMed:22710723, ECO:0000269|PubMed:2498394, ECO:0000269|PubMed:3093483, ECO:0000269|PubMed:7853507, ECO:0000269|PubMed:8755529, ECO:0000269|PubMed:8759729}.
Subcellular locationCell membrane. Mitochondrion inner membrane. Nucleus. Cytoplasm, cytoskeleton. Note=Localizes to focal adhesion sites following integrin engagement. Localization to focal adhesion sites requires myristoylation and the SH3 domain.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: P12931
Gene Ontology
(Biological Process)
Complete annatation
activation of protein kinase B activity [GO:0032148];
adherens junction organization [GO:0034332];
angiotensin-activated signaling pathway involved in heart process [GO:0086098];
bone resorption [GO:0045453];
branching involved in mammary gland duct morphogenesis [GO:0060444];
cell cycle [GO:0007049];
cell proliferation [GO:0008283];
cellular response to fatty acid [GO:0071398];
cellular response to fluid shear stress [GO:0071498];
cellular response to hypoxia [GO:0071456];
cellular response to insulin stimulus [GO:0032869];
cellular response to lipopolysaccharide [GO:0071222];
cellular response to peptide hormone stimulus [GO:0071375];
cellular response to platelet-derived growth factor stimulus [GO:0036120];
cellular response to progesterone stimulus [GO:0071393];
cellular response to reactive oxygen species [GO:0034614];
central nervous system development [GO:0007417];
ephrin receptor signaling pathway [GO:0048013];
epidermal growth factor receptor signaling pathway [GO:0007173];
ERBB2 signaling pathway [GO:0038128];
Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096];
forebrain development [GO:0030900];
innate immune response [GO:0045087];
integrin-mediated signaling pathway [GO:0007229];
intracellular estrogen receptor signaling pathway [GO:0030520];
intracellular signal transduction [GO:0035556];
leukocyte migration [GO:0050900];
negative regulation of anoikis [GO:2000811];
negative regulation of apoptotic process [GO:0043066];
negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043154];
negative regulation of extrinsic apoptotic signaling pathway [GO:2001237];
negative regulation of focal adhesion assembly [GO:0051895];
negative regulation of intrinsic apoptotic signaling pathway [GO:2001243];
negative regulation of mitochondrial depolarization [GO:0051902];
negative regulation of protein homooligomerization [GO:0032463];
negative regulation of telomerase activity [GO:0051974];
negative regulation of telomere maintenance via telomerase [GO:0032211];
negative regulation of transcription, DNA-templated [GO:0045892];
neurotrophin TRK receptor signaling pathway [GO:0048011];
oogenesis [GO:0048477];
osteoclast development [GO:0036035];
peptidyl-serine phosphorylation [GO:0018105];
peptidyl-tyrosine autophosphorylation [GO:0038083];
peptidyl-tyrosine phosphorylation [GO:0018108];
platelet activation [GO:0030168];
platelet-derived growth factor receptor signaling pathway [GO:0048008];
positive regulation of apoptotic process [GO:0043065];
positive regulation of canonical Wnt signaling pathway [GO:0090263];
positive regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045737];
positive regulation of cytokine secretion [GO:0050715];
positive regulation of DNA biosynthetic process [GO:2000573];
positive regulation of epithelial cell migration [GO:0010634];
positive regulation of ERK1 and ERK2 cascade [GO:0070374];
positive regulation of glucose metabolic process [GO:0010907];
positive regulation of insulin receptor signaling pathway [GO:0046628];
positive regulation of integrin activation [GO:0033625];
positive regulation of lamellipodium morphogenesis [GO:2000394];
positive regulation of MAP kinase activity [GO:0043406];
positive regulation of peptidyl-tyrosine phosphorylation [GO:0050731];
positive regulation of phosphatidylinositol 3-kinase activity [GO:0043552];
positive regulation of platelet-derived growth factor receptor signaling pathway [GO:0010641];
positive regulation of podosome assembly [GO:0071803];
positive regulation of protein autophosphorylation [GO:0031954];
positive regulation of protein kinase B signaling [GO:0051897];
positive regulation of protein localization to nucleus [GO:1900182];
positive regulation of protein processing [GO:0010954];
positive regulation of protein serine/threonine kinase activity [GO:0071902];
positive regulation of small GTPase mediated signal transduction [GO:0051057];
positive regulation of smooth muscle cell migration [GO:0014911];
positive regulation of transcription, DNA-templated [GO:0045893];
progesterone receptor signaling pathway [GO:0050847];
protein autophosphorylation [GO:0046777];
protein destabilization [GO:0031648];
regulation of bone resorption [GO:0045124];
regulation of caveolin-mediated endocytosis [GO:2001286];
regulation of cell-cell adhesion [GO:0022407];
regulation of cell cycle [GO:0051726];
regulation of cell projection assembly [GO:0060491];
regulation of cell proliferation [GO:0042127];
regulation of early endosome to late endosome transport [GO:2000641];
regulation of epithelial cell migration [GO:0010632];
regulation of intracellular estrogen receptor signaling pathway [GO:0033146];
regulation of podosome assembly [GO:0071801];
regulation of protein binding [GO:0043393];
regulation of vascular permeability [GO:0043114];
response to acidic pH [GO:0010447];
response to drug [GO:0042493];
response to electrical stimulus [GO:0051602];
response to hydrogen peroxide [GO:0042542];
response to interleukin-1 [GO:0070555];
response to mechanical stimulus [GO:0009612];
response to mineralocorticoid [GO:0051385];
response to nutrient levels [GO:0031667];
response to virus [GO:0009615];
signal complex assembly [GO:0007172];
signal transduction [GO:0007165];
single organismal cell-cell adhesion [GO:0016337];
stimulatory C-type lectin receptor signaling pathway [GO:0002223];
stress fiber assembly [GO:0043149];
substrate adhesion-dependent cell spreading [GO:0034446];
T cell costimulation [GO:0031295];
transcytosis [GO:0045056];
transforming growth factor beta receptor signaling pathway [GO:0007179];
uterus development [GO:0060065];
vascular endothelial growth factor receptor signaling pathway [GO:0048010]
Gene Ontology
(Molecular Function)
Complete annatation
ATP binding [GO:0005524];
enzyme binding [GO:0019899];
ephrin receptor binding [GO:0046875];
growth factor receptor binding [GO:0070851];
heme binding [GO:0020037];
hormone receptor binding [GO:0051427];
integrin binding [GO:0005178];
ion channel binding [GO:0044325];
kinase activity [GO:0016301];
kinase binding [GO:0019900];
non-membrane spanning protein tyrosine kinase activity [GO:0004715];
phosphoprotein binding [GO:0051219];
protein kinase activity [GO:0004672];
protein tyrosine kinase activity [GO:0004713];
receptor binding [GO:0005102];
scaffold protein binding [GO:0097110];
SH2 domain binding [GO:0042169];
SH3/SH2 adaptor activity [GO:0005070]
Gene Ontology
(Cellular Component)
Complete annatation
actin filament [GO:0005884];
caveola [GO:0005901];
cytoplasm [GO:0005737];
cytosol [GO:0005829];
extracellular exosome [GO:0070062];
extrinsic component of cytoplasmic side of plasma membrane [GO:0031234];
late endosome [GO:0005770];
lysosome [GO:0005764];
mitochondrial inner membrane [GO:0005743];
mitochondrion [GO:0005739];
neuron projection [GO:0043005];
nucleus [GO:0005634];
perinuclear region of cytoplasm [GO:0048471];
plasma membrane [GO:0005886];
postsynaptic density [GO:0014069];
ruffle membrane [GO:0032587]
Protein-protein interaction112592
Phylogenetic treeP12931
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. CD30.4215824515481940.2801750057173190.395912027580296
AZA vs. DISU0.3087186135101660.3497844076120090.887429206006287
AZA vs. IL7-0.2696324595477410.4308900443663560.999311006273513
AZA vs. SAHA-0.4523359732780630.4438341336026660.78829686916311
DISU vs. CD3-0.1271760372371150.7403360369509310.818409021780459
DISU vs. IL7-0.5874876143547640.06027245115763090.323891128540921
DISU vs. SAHA-0.7548544718184830.1821657653377340.547621021808296
DMSO vs. AZA0.03133489643003550.9188028713113591
DMSO vs. CD3-0.4005594196830660.256581801497960.363392388790708
DMSO vs. DISU-0.2783788726202710.3191554171261740.822006745975451
DMSO vs. IL7-0.2925145361694690.3150015152158060.796193644348194
DMSO vs. SAHA-0.4852907967435650.3855633322582350.732764814686489
HIV vs. Mock in Activation0.7922628944870730.2261265438120040.999983755607037
HIV vs. Mock in Latency0.2441962738831590.2553805218880030.999834320637052
IL7 vs. CD3-0.6916776676735320.06512492008034210.135720632157863
SAHA vs. CD3-0.8944769216526250.1503191122223020.241324067453935
SAHA vs. IL7-0.1813034248406650.7493244134773390.886950624951504
(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) TRUE
(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 0.596628 0.000305467
(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
DB01254 Dasatinib approved, investigational yes multitarget
DB01893 N6-Benzyl Adenosine-5&,39;-Diphosphate experimental unknown unknown
DB01908 RU85493 experimental unknown unknown
DB01962 Phosphonotyrosine experimental unknown unknown
DB02175 Malonic acid experimental unknown unknown
DB02336 RU83876 experimental unknown unknown
DB02432 RU90395 experimental unknown unknown
DB02908 RU78783 experimental unknown unknown
DB03104 RU82129 experimental unknown unknown
DB03268 RU82197 experimental unknown unknown
DB03298 Phenylphosphate experimental unknown unknown
DB03591 RU82209 experimental unknown unknown
DB03712 RU85053 experimental unknown unknown
DB03902 Oxalic Acid experimental unknown unknown
DB04272 Citric Acid nutraceutical, vet_approved unknown unknown
DB04495 RU81843 experimental unknown unknown
DB01678 RU84687 experimental unknown unknown
DB04739 4-[(4-METHYL-1-PIPERAZINYL)METHYL]-N-[3-[[4-(3-PYRIDINYL)-2-PYRIMIDINYL]AMINO]PHENYL]-BENZAMIDE experimental unknown unknown
DB04751 Purvalanol A experimental unknown unknown
DB05184 XL228 investigational unknown unknown
DB06882 1-[1-(3-aminophenyl)-3-tert-butyl-1H-pyrazol-5-yl]-3-naphthalen-1-ylurea experimental unknown unknown
DB06883 1-[1-(3-aminophenyl)-3-tert-butyl-1H-pyrazol-5-yl]-3-phenylurea experimental unknown unknown
DB03114 PAS219 experimental unknown unknown
DB01866 RU79256 experimental unknown unknown
DB01947 RU78262 experimental unknown unknown
DB03828 RU78299 experimental unknown unknown
DB03306 RU78300 experimental unknown unknown
DB02762 RU79072 experimental unknown unknown
DB03525 RU79073 experimental unknown unknown
DB04080 RU78191 experimental unknown unknown
DB07335 3-[4-AMINO-1-(1-METHYLETHYL)-1H-PYRAZOLO[3,4-D]PYRIMIDIN-3-YL]PHENOL experimental unknown unknown
DB07662 N-[4-(3-BROMO-PHENYLAMINO)-QUINAZOLIN-6-YL]-ACRYLAMIDE experimental unknown unknown
DB03217 DPI59 experimental unknown unknown
DB07966 [4-({4-[(5-cyclopropyl-1H-pyrazol-3-yl)amino]quinazolin-2-yl}amino)phenyl]acetonitrile experimental unknown unknown
DB03628 ISO24 experimental unknown unknown
DB08052 1-cyclopentyl-3-(1H-pyrrolo[2,3-b]pyridin-5-yl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine experimental unknown unknown
DB08053 1-cyclobutyl-3-(3,4-dimethoxyphenyl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine experimental unknown unknown
DB08054 1-(1-methylethyl)-3-quinolin-6-yl-1H-pyrazolo[3,4-d]pyrimidin-4-amine experimental unknown unknown
DB08192 2-(4-CARCOXY-5-ISOPROPYLTHIAZOLYL)BENZOPIPERIDINE experimental unknown unknown
DB03023 1-Tert-Butyl-3-(4-Chloro-Phenyl)-1h-Pyrazolo[3,4-D]Pyrimidin-4-Ylamine experimental unknown unknown
DB03078 PASBN experimental unknown unknown
DB08462 N-(4-PHENYLAMINO-QUINAZOLIN-6-YL)-ACRYLAMIDE experimental unknown unknown
DB08564 (2E)-N-{4-[(3-bromophenyl)amino]quinazolin-6-yl}-4-(dimethylamino)but-2-enamide experimental unknown unknown
DB06616 Bosutinib approved unknown inhibitor
DB08901 Ponatinib approved unknown inhibitor
DB09079 Nintedanib approved unknown Inhibitor

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
1A07 X-ray 2.2Å A/B=144-249.
1A08 X-ray 2.2Å A/B=144-249.
1A09 X-ray 2.0Å A/B=144-249.
1A1A X-ray 2.0Å A/B=144-249.
1A1B X-ray 2.2Å A/B=144-249.
1A1C X-ray 2.4Å A/B=144-249.
1A1E X-ray 2.2Å A/B=144-249.
1FMK X-ray 1.5Å A=86-536.
1HCS NMR - B=144-249.
1HCT NMR - B=144-249.
1KSW X-ray 2.8Å A=86-536.
1O41 X-ray 1.7Å A=145-252.
1O42 X-ray 1.7Å A=145-252.
1O43 X-ray 1.5Å A=145-252.
1O44 X-ray 1.7Å A=145-252.
1O45 X-ray 1.8Å A=145-252.
1O46 X-ray 2.0Å A=145-252.
1O47 X-ray 1.8Å A=145-252.
1O48 X-ray 1.5Å A=145-252.
1O49 X-ray 1.7Å A=145-252.
1O4A X-ray 1.5Å A=145-252.
1O4B X-ray 1.8Å A=145-252.
1O4C X-ray 1.8Å A=145-252.
1O4D X-ray 1.8Å A=145-252.
1O4E X-ray 2.0Å A=145-252.
1O4F X-ray 2.0Å A=145-252.
1O4G X-ray 1.5Å A=145-252.
1O4H X-ray 2.2Å A=145-252.
1O4I X-ray 1.7Å A=145-252.
1O4J X-ray 1.7Å A=145-252.
1O4K X-ray 1.5Å A=145-252.
1O4L X-ray 1.6Å A=145-252.
1O4M X-ray 1.6Å A=145-252.
1O4N X-ray 1.6Å A=145-252.
1O4O X-ray 1.7Å A=145-252.
1O4P X-ray 1.9Å A=145-252.
1O4Q X-ray 1.7Å A=145-252.
1O4R X-ray 1.5Å A=145-252.
1SHD X-ray 2.0Å A=144-249.
1Y57 X-ray 1.9Å A=86-536.
1YI6 X-ray 2.0Å A/B=261-536.
1YOJ X-ray 1.9Å A/B=254-536.
1YOL X-ray 2.3Å A/B=254-536.
1YOM X-ray 2.9Å A/B=254-536.
2BDF X-ray 2.1Å A/B=258-536.
2BDJ X-ray 2.5Å A=258-536.
2H8H X-ray 2.2Å A=2-536.
2SRC X-ray 1.5Å A=86-536.
3VRO X-ray 1.8Å B=412-424.
3ZMP X-ray 2.6Å C/D=527-536.
3ZMQ X-ray 3.3Å C=527-536.
4F59 X-ray 1.7Å A=144-252.
4F5A X-ray 1.8Å A=144-252.
4F5B X-ray 1.5Å A=144-252.
4HXJ X-ray 2.0Å A/B=87-144.
4K11 X-ray 2.3Å A=87-534.
4MXO X-ray 2.1Å A/B=254-536.
4MXX X-ray 2.6Å A/B=254-536.
4MXY X-ray 2.5Å A/B=254-536.
4MXZ X-ray 2.5Å A/B=254-536.

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

HIV Partner Interaction Type PubMed
reverse transcriptase interacts with 24413044
Nef interacts with 18042718
Nef binds 18296443
Tat activates 16105876
Tat induces phosphorylation of 20661303
Tat upregulates 22362758
Tat regulated by 24666322
Envelope surface glycoprotein gp120 activates 23119100
Nef activates 18005680
HIV-1 virus replication inhibited by expression of human gene 24413044
Envelope surface glycoprotein gp120 induces phosphorylation of 22241990

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)
hsa04012 ErbB signaling pathway - Homo sapiens (human)
hsa04015 Rap1 signaling pathway - Homo sapiens (human)
hsa04062 Chemokine signaling pathway - Homo sapiens (human)
hsa04144 Endocytosis - Homo sapiens (human)
hsa04360 Axon guidance - Homo sapiens (human)
hsa04370 VEGF signaling pathway - Homo sapiens (human)
hsa04510 Focal adhesion - Homo sapiens (human)
hsa04520 Adherens junction - Homo sapiens (human)
hsa04530 Tight junction - Homo sapiens (human)
hsa04540 Gap junction - Homo sapiens (human)
hsa04611 Platelet activation - Homo sapiens (human)
hsa04727 GABAergic synapse - Homo sapiens (human)
hsa04750 Inflammatory mediator regulation of TRP channels - 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)
hsa04917 Prolactin signaling pathway - Homo sapiens (human)
hsa04919 Thyroid hormone signaling pathway - Homo sapiens (human)
hsa04921 Oxytocin signaling pathway - Homo sapiens (human)
hsa05100 Bacterial invasion of epithelial cells - Homo sapiens (human)
hsa05120 Epithelial cell signaling in Helicobacter pylori infection - Homo sapiens (human)
hsa05131 Shigellosis - Homo sapiens (human)
hsa05152 Tuberculosis - Homo sapiens (human)
hsa05161 Hepatitis B - Homo sapiens (human)
hsa05203 Viral carcinogenesis - Homo sapiens (human)
hsa05205 Proteoglycans in cancer - Homo sapiens (human)
hsa05219 Bladder cancer - Homo sapiens (human)