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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3MI9

Crystal structure of HIV-1 Tat complexed with human P-TEFb

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000307cellular_componentcyclin-dependent protein kinase holoenzyme complex
A0000976molecular_functiontranscription cis-regulatory region binding
A0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
A0001223molecular_functiontranscription coactivator binding
A0003677molecular_functionDNA binding
A0003682molecular_functionchromatin binding
A0003711molecular_functiontranscription elongation factor activity
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0004693molecular_functioncyclin-dependent protein serine/threonine kinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0006281biological_processDNA repair
A0006282biological_processregulation of DNA repair
A0006351biological_processDNA-templated transcription
A0006366biological_processtranscription by RNA polymerase II
A0006367biological_processtranscription initiation at RNA polymerase II promoter
A0006368biological_processtranscription elongation by RNA polymerase II
A0006468biological_processprotein phosphorylation
A0006974biological_processDNA damage response
A0007346biological_processregulation of mitotic cell cycle
A0008023cellular_componenttranscription elongation factor complex
A0008024cellular_componentcyclin/CDK positive transcription elongation factor complex
A0008283biological_processcell population proliferation
A0008353molecular_functionRNA polymerase II CTD heptapeptide repeat kinase activity
A0016020cellular_componentmembrane
A0016301molecular_functionkinase activity
A0016605cellular_componentPML body
A0016740molecular_functiontransferase activity
A0017069molecular_functionsnRNA binding
A0019901molecular_functionprotein kinase binding
A0031297biological_processreplication fork processing
A0031440biological_processregulation of mRNA 3'-end processing
A0032968biological_processpositive regulation of transcription elongation by RNA polymerase II
A0043923biological_processhost-mediated activation of viral transcription
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0051147biological_processregulation of muscle cell differentiation
A0051647biological_processnucleus localization
A0051726biological_processregulation of cell cycle
A0070691cellular_componentP-TEFb complex
A0071345biological_processcellular response to cytokine stimulus
A0097322molecular_function7SK snRNA binding
A0106310molecular_functionprotein serine kinase activity
A0120186biological_processnegative regulation of protein localization to chromatin
A0120187biological_processpositive regulation of protein localization to chromatin
A0140191molecular_functionhistone H1-4S187 kinase activity
A0140673biological_processtranscription elongation-coupled chromatin remodeling
B0006357biological_processregulation of transcription by RNA polymerase II
B0016538molecular_functioncyclin-dependent protein serine/threonine kinase regulator activity
C0001070molecular_functionRNA-binding transcription regulator activity
C0001223molecular_functiontranscription coactivator binding
C0003723molecular_functionRNA binding
C0004865molecular_functionprotein serine/threonine phosphatase inhibitor activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0006351biological_processDNA-templated transcription
C0019904molecular_functionprotein domain specific binding
C0030332molecular_functioncyclin binding
C0030430cellular_componenthost cell cytoplasm
C0031491molecular_functionnucleosome binding
C0032968biological_processpositive regulation of transcription elongation by RNA polymerase II
C0035035molecular_functionhistone acetyltransferase binding
C0039502biological_processsymbiont-mediated suppression of host type I interferon-mediated signaling pathway
C0039525biological_processsymbiont-mediated perturbation of host chromatin organization
C0039588biological_processsymbiont-mediated suppression of host antigen processing and presentation
C0039606biological_processsymbiont-mediated suppression of host translation initiation
C0042025cellular_componenthost cell nucleus
C0042783biological_processsymbiont-mediated evasion of host immune response
C0042805molecular_functionactinin binding
C0043175molecular_functionRNA polymerase core enzyme binding
C0043923biological_processhost-mediated activation of viral transcription
C0044196cellular_componenthost cell nucleolus
C0046872molecular_functionmetal ion binding
C0050434biological_processpositive regulation of viral transcription
C0052031biological_processsymbiont-mediated perturbation of host defense response
C0052170biological_processsymbiont-mediated suppression of host innate immune response
C0140313molecular_functionmolecular sequestering activity
C0140537molecular_functiontranscription regulator activator activity
C1990970molecular_functiontrans-activation response element binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 87
ChainResidue
CCYS22
CHIS33
CCYS34
CCYS37
site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 88
ChainResidue
BCYS261
CCYS25
CCYS27
CCYS30
Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGQGTFGEVFkArhrktgqk..........VALK
ChainResidueDetails
AILE25-LYS48
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IlHrDMKaaNVLI
ChainResidueDetails
AILE145-ILE157
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18566585","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; by EP300/CBP, PCAF/KAT2B and GCN5/KAT2A","evidences":[{"source":"PubMed","id":"17452463","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18250157","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; by PCAF/KAT2B and GCN5/KAT2A","evidences":[{"source":"PubMed","id":"18250157","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28426094","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21533037","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CaMK1D","evidences":[{"source":"PubMed","id":"15965233","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18483222","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18566585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18829461","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20535204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20851342","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21448926","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21779453","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsSite: {"description":"Essential for interacting with HIV-1 Tat"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues47
DetailsRegion: {"description":"Transactivation","evidences":[{"source":"HAMAP-Rule","id":"MF_04079","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues23
DetailsRegion: {"description":"Interaction with human CREBBP","evidences":[{"source":"HAMAP-Rule","id":"MF_04079","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues15
DetailsRegion: {"description":"Cysteine-rich","evidences":[{"source":"HAMAP-Rule","id":"MF_04079","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues10
DetailsRegion: {"description":"Core","evidences":[{"source":"HAMAP-Rule","id":"MF_04079","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_04079","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20535204","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24727379","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsSite: {"description":"Essential for Tat translocation through the endosomal membrane","evidences":[{"source":"HAMAP-Rule","id":"MF_04079","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; by host PCAF","evidences":[{"source":"HAMAP-Rule","id":"MF_04079","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246333

PDB entries from 2025-12-17

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