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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8CX2

Cryo-EM structure of human APOBEC3G/HIV-1 Vif/CBFbeta/ELOB/ELOC dimeric complex in State 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000932cellular_componentP-body
A0002230biological_processpositive regulation of defense response to virus by host
A0002376biological_processimmune system process
A0003723molecular_functionRNA binding
A0003824molecular_functioncatalytic activity
A0004126molecular_functioncytidine deaminase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0008829molecular_functiondCTP deaminase activity
A0009972biological_processobsolete cytidine deamination
A0010526biological_processtransposable element silencing
A0016553biological_processbase conversion or substitution editing
A0016554biological_processcytidine to uridine editing
A0016787molecular_functionhydrolase activity
A0030895cellular_componentapolipoprotein B mRNA editing enzyme complex
A0042802molecular_functionidentical protein binding
A0045071biological_processnegative regulation of viral genome replication
A0045087biological_processinnate immune response
A0045869biological_processnegative regulation of single stranded viral RNA replication via double stranded DNA intermediate
A0046872molecular_functionmetal ion binding
A0048525biological_processnegative regulation of viral process
A0051607biological_processdefense response to virus
A0070383biological_processDNA cytosine deamination
A0140374biological_processantiviral innate immune response
A0140546biological_processdefense response to symbiont
A1990904cellular_componentribonucleoprotein complex
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0008289molecular_functionlipid binding
B0016020cellular_componentmembrane
B0019058biological_processviral life cycle
B0019079biological_processviral genome replication
B0020002cellular_componenthost cell plasma membrane
B0030430cellular_componenthost cell cytoplasm
B0030674molecular_functionprotein-macromolecule adaptor activity
B0039537biological_processsymbiont-mediated suppression of cytoplasmic pattern recognition receptor signaling pathway
B0042802molecular_functionidentical protein binding
B0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
B0044423cellular_componentvirion component
B0046872molecular_functionmetal ion binding
B0052170biological_processsymbiont-mediated suppression of host innate immune response
B1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
C0000122biological_processnegative regulation of transcription by RNA polymerase II
C0000209biological_processprotein polyubiquitination
C0001503biological_processossification
C0001649biological_processosteoblast differentiation
C0003677molecular_functionDNA binding
C0003713molecular_functiontranscription coactivator activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0006357biological_processregulation of transcription by RNA polymerase II
C0006366biological_processtranscription by RNA polymerase II
C0016020cellular_componentmembrane
C0016513cellular_componentcore-binding factor complex
C0030098biological_processlymphocyte differentiation
C0030099biological_processmyeloid cell differentiation
C0043371biological_processnegative regulation of CD4-positive, alpha-beta T cell differentiation
C0043378biological_processpositive regulation of CD8-positive, alpha-beta T cell differentiation
C0043565molecular_functionsequence-specific DNA binding
C0045944biological_processpositive regulation of transcription by RNA polymerase II
C0048469biological_processcell maturation
C0060216biological_processdefinitive hemopoiesis
D0000151cellular_componentubiquitin ligase complex
D0001222molecular_functiontranscription corepressor binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006367biological_processtranscription initiation at RNA polymerase II promoter
D0006368biological_processtranscription elongation by RNA polymerase II
D0016567biological_processprotein ubiquitination
D0030891cellular_componentVCB complex
D0031462cellular_componentCul2-RING ubiquitin ligase complex
D0031466cellular_componentCul5-RING ubiquitin ligase complex
D0031625molecular_functionubiquitin protein ligase binding
D0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
D0065003biological_processprotein-containing complex assembly
D0070449cellular_componentelongin complex
D0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
D0140958biological_processtarget-directed miRNA degradation
E0000151cellular_componentubiquitin ligase complex
E0001222molecular_functiontranscription corepressor binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006357biological_processregulation of transcription by RNA polymerase II
E0006367biological_processtranscription initiation at RNA polymerase II promoter
E0006511biological_processubiquitin-dependent protein catabolic process
E0016567biological_processprotein ubiquitination
E0030674molecular_functionprotein-macromolecule adaptor activity
E0031462cellular_componentCul2-RING ubiquitin ligase complex
E0031466cellular_componentCul5-RING ubiquitin ligase complex
E0070449cellular_componentelongin complex
E0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
E0140958biological_processtarget-directed miRNA degradation
F0000932cellular_componentP-body
F0002230biological_processpositive regulation of defense response to virus by host
F0002376biological_processimmune system process
F0003723molecular_functionRNA binding
F0003824molecular_functioncatalytic activity
F0004126molecular_functioncytidine deaminase activity
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0008270molecular_functionzinc ion binding
F0008829molecular_functiondCTP deaminase activity
F0009972biological_processobsolete cytidine deamination
F0010526biological_processtransposable element silencing
F0016553biological_processbase conversion or substitution editing
F0016554biological_processcytidine to uridine editing
F0016787molecular_functionhydrolase activity
F0030895cellular_componentapolipoprotein B mRNA editing enzyme complex
F0042802molecular_functionidentical protein binding
F0045071biological_processnegative regulation of viral genome replication
F0045087biological_processinnate immune response
F0045869biological_processnegative regulation of single stranded viral RNA replication via double stranded DNA intermediate
F0046872molecular_functionmetal ion binding
F0048525biological_processnegative regulation of viral process
F0051607biological_processdefense response to virus
F0070383biological_processDNA cytosine deamination
F0140374biological_processantiviral innate immune response
F0140546biological_processdefense response to symbiont
F1990904cellular_componentribonucleoprotein complex
G0003723molecular_functionRNA binding
G0005515molecular_functionprotein binding
G0005886cellular_componentplasma membrane
G0008289molecular_functionlipid binding
G0016020cellular_componentmembrane
G0019058biological_processviral life cycle
G0019079biological_processviral genome replication
G0020002cellular_componenthost cell plasma membrane
G0030430cellular_componenthost cell cytoplasm
G0030674molecular_functionprotein-macromolecule adaptor activity
G0039537biological_processsymbiont-mediated suppression of cytoplasmic pattern recognition receptor signaling pathway
G0042802molecular_functionidentical protein binding
G0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
G0044423cellular_componentvirion component
G0046872molecular_functionmetal ion binding
G0052170biological_processsymbiont-mediated suppression of host innate immune response
G1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
H0000122biological_processnegative regulation of transcription by RNA polymerase II
H0000209biological_processprotein polyubiquitination
H0001503biological_processossification
H0001649biological_processosteoblast differentiation
H0003677molecular_functionDNA binding
H0003713molecular_functiontranscription coactivator activity
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0006357biological_processregulation of transcription by RNA polymerase II
H0006366biological_processtranscription by RNA polymerase II
H0016020cellular_componentmembrane
H0016513cellular_componentcore-binding factor complex
H0030098biological_processlymphocyte differentiation
H0030099biological_processmyeloid cell differentiation
H0043371biological_processnegative regulation of CD4-positive, alpha-beta T cell differentiation
H0043378biological_processpositive regulation of CD8-positive, alpha-beta T cell differentiation
H0043565molecular_functionsequence-specific DNA binding
H0045944biological_processpositive regulation of transcription by RNA polymerase II
H0048469biological_processcell maturation
H0060216biological_processdefinitive hemopoiesis
I0000151cellular_componentubiquitin ligase complex
I0001222molecular_functiontranscription corepressor binding
I0005515molecular_functionprotein binding
I0005634cellular_componentnucleus
I0005654cellular_componentnucleoplasm
I0005737cellular_componentcytoplasm
I0005829cellular_componentcytosol
I0006367biological_processtranscription initiation at RNA polymerase II promoter
I0006368biological_processtranscription elongation by RNA polymerase II
I0016567biological_processprotein ubiquitination
I0030891cellular_componentVCB complex
I0031462cellular_componentCul2-RING ubiquitin ligase complex
I0031466cellular_componentCul5-RING ubiquitin ligase complex
I0031625molecular_functionubiquitin protein ligase binding
I0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
I0065003biological_processprotein-containing complex assembly
I0070449cellular_componentelongin complex
I0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
I0140958biological_processtarget-directed miRNA degradation
J0000151cellular_componentubiquitin ligase complex
J0001222molecular_functiontranscription corepressor binding
J0005515molecular_functionprotein binding
J0005634cellular_componentnucleus
J0005654cellular_componentnucleoplasm
J0005737cellular_componentcytoplasm
J0005829cellular_componentcytosol
J0006357biological_processregulation of transcription by RNA polymerase II
J0006367biological_processtranscription initiation at RNA polymerase II promoter
J0006511biological_processubiquitin-dependent protein catabolic process
J0016567biological_processprotein ubiquitination
J0030674molecular_functionprotein-macromolecule adaptor activity
J0031462cellular_componentCul2-RING ubiquitin ligase complex
J0031466cellular_componentCul5-RING ubiquitin ligase complex
J0070449cellular_componentelongin complex
J0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
J0140958biological_processtarget-directed miRNA degradation
Functional Information from PROSITE/UniProt
site_idPS00903
Number of Residues39
DetailsCYT_DCMP_DEAMINASES_1 Cytidine and deoxycytidylate deaminases zinc-binding region signature. HAElcFLdvipfwkldldqdyrvtcftsws..........PCfs......CaqeM
ChainResidueDetails
AHIS257-MET295
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues218
DetailsDomain: {"description":"CMP/dCMP-type deaminase 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues228
DetailsDomain: {"description":"CMP/dCMP-type deaminase 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues254
DetailsRegion: {"description":"Necessary for homooligomerization"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues18
DetailsRegion: {"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18288108","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18849968","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19153609","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25542899","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36754086","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ROV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ROW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8CX0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8CX1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01083","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"36754086","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37419875","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8CX0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8CX1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8H0I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8J62","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18288108","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18849968","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19153609","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25542899","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36754086","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"37419875","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ROV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ROW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8CX0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8CX1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8H0I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"8J62","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsSite: {"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by PKA","evidences":[{"source":"PubMed","id":"18836454","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21659520","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by PKA and CAMK2","evidences":[{"source":"PubMed","id":"21659520","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues10
DetailsCross-link: {"description":"(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"23318957","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues8
DetailsCross-link: {"description":"(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"19887642","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"23318957","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31253590","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsCross-link: {"description":"(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"23318957","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"31253590","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsCross-link: {"description":"(Microbial infection) Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"19887642","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16636053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"36754086","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8CX0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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