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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7UPN

Maedi visna virus Vif in complex with CypA and E3 ubiquitin ligase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000413biological_processprotein peptidyl-prolyl isomerization
A0001933biological_processnegative regulation of protein phosphorylation
A0001934biological_processpositive regulation of protein phosphorylation
A0003723molecular_functionRNA binding
A0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
A0005178molecular_functionintegrin binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005925cellular_componentfocal adhesion
A0006457biological_processprotein folding
A0006469biological_processnegative regulation of protein kinase activity
A0006915biological_processapoptotic process
A0016018molecular_functioncyclosporin A binding
A0016020cellular_componentmembrane
A0016853molecular_functionisomerase activity
A0019076biological_processviral release from host cell
A0030168biological_processplatelet activation
A0030593biological_processneutrophil chemotaxis
A0030595biological_processleukocyte chemotaxis
A0031982cellular_componentvesicle
A0032148biological_processactivation of protein kinase B activity
A0032873biological_processnegative regulation of stress-activated MAPK cascade
A0032991cellular_componentprotein-containing complex
A0034389biological_processlipid droplet organization
A0034599biological_processcellular response to oxidative stress
A0034774cellular_componentsecretory granule lumen
A0042118biological_processendothelial cell activation
A0043410biological_processpositive regulation of MAPK cascade
A0045069biological_processregulation of viral genome replication
A0045070biological_processpositive regulation of viral genome replication
A0046790molecular_functionvirion binding
A0050714biological_processpositive regulation of protein secretion
A0051082molecular_functionunfolded protein binding
A0051092biological_processobsolete positive regulation of NF-kappaB transcription factor activity
A0060352biological_processcell adhesion molecule production
A0061944biological_processnegative regulation of protein K48-linked ubiquitination
A0070062cellular_componentextracellular exosome
A0070527biological_processplatelet aggregation
A1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
A1903901biological_processnegative regulation of viral life cycle
A1904399molecular_functionheparan sulfate binding
A1904813cellular_componentficolin-1-rich granule lumen
A2001233biological_processregulation of apoptotic signaling pathway
B0000413biological_processprotein peptidyl-prolyl isomerization
B0001933biological_processnegative regulation of protein phosphorylation
B0001934biological_processpositive regulation of protein phosphorylation
B0003723molecular_functionRNA binding
B0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
B0005178molecular_functionintegrin binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005925cellular_componentfocal adhesion
B0006457biological_processprotein folding
B0006469biological_processnegative regulation of protein kinase activity
B0006915biological_processapoptotic process
B0016018molecular_functioncyclosporin A binding
B0016020cellular_componentmembrane
B0016853molecular_functionisomerase activity
B0019076biological_processviral release from host cell
B0030168biological_processplatelet activation
B0030593biological_processneutrophil chemotaxis
B0030595biological_processleukocyte chemotaxis
B0031982cellular_componentvesicle
B0032148biological_processactivation of protein kinase B activity
B0032873biological_processnegative regulation of stress-activated MAPK cascade
B0032991cellular_componentprotein-containing complex
B0034389biological_processlipid droplet organization
B0034599biological_processcellular response to oxidative stress
B0034774cellular_componentsecretory granule lumen
B0042118biological_processendothelial cell activation
B0043410biological_processpositive regulation of MAPK cascade
B0045069biological_processregulation of viral genome replication
B0045070biological_processpositive regulation of viral genome replication
B0046790molecular_functionvirion binding
B0050714biological_processpositive regulation of protein secretion
B0051082molecular_functionunfolded protein binding
B0051092biological_processobsolete positive regulation of NF-kappaB transcription factor activity
B0060352biological_processcell adhesion molecule production
B0061944biological_processnegative regulation of protein K48-linked ubiquitination
B0070062cellular_componentextracellular exosome
B0070527biological_processplatelet aggregation
B1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
B1903901biological_processnegative regulation of viral life cycle
B1904399molecular_functionheparan sulfate binding
B1904813cellular_componentficolin-1-rich granule lumen
B2001233biological_processregulation of apoptotic signaling pathway
C0030430cellular_componenthost cell cytoplasm
C0044423cellular_componentvirion component
E0006511biological_processubiquitin-dependent protein catabolic process
F0030430cellular_componenthost cell cytoplasm
F0044423cellular_componentvirion component
G0006511biological_processubiquitin-dependent protein catabolic process
H0000122biological_processnegative regulation of transcription by RNA polymerase II
H0000151cellular_componentubiquitin ligase complex
H0001222molecular_functiontranscription corepressor binding
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0005737cellular_componentcytoplasm
H0005829cellular_componentcytosol
H0006351biological_processDNA-templated transcription
H0006367biological_processtranscription initiation at RNA polymerase II promoter
H0006368biological_processtranscription elongation by RNA polymerase II
H0016567biological_processprotein ubiquitination
H0030891cellular_componentVCB complex
H0031462cellular_componentCul2-RING ubiquitin ligase complex
H0031466cellular_componentCul5-RING ubiquitin ligase complex
H0031625molecular_functionubiquitin protein ligase binding
H0032436biological_processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
H0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
H0065003biological_processprotein-containing complex assembly
H0070449cellular_componentelongin complex
H0140627biological_processubiquitin-dependent protein catabolic process via the C-end degron rule pathway
H0140958biological_processtarget-directed miRNA degradation
H1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
H2000104biological_processnegative regulation of DNA-templated DNA replication
I0000122biological_processnegative regulation of transcription by RNA polymerase II
I0000151cellular_componentubiquitin ligase complex
I0001222molecular_functiontranscription corepressor binding
I0005515molecular_functionprotein binding
I0005634cellular_componentnucleus
I0005654cellular_componentnucleoplasm
I0005737cellular_componentcytoplasm
I0005829cellular_componentcytosol
I0006351biological_processDNA-templated transcription
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
I0043161biological_processproteasome-mediated 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
I1990116biological_processribosome-associated ubiquitin-dependent protein catabolic process
I2000104biological_processnegative regulation of DNA-templated DNA replication
Functional Information from PROSITE/UniProt
site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgScFHRIIpgFMcQGG
ChainResidueDetails
ATYR48-GLY65
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues312
DetailsDomain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed","evidences":[{"source":"PubMed","id":"25489052","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Claeys D."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"20364129","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25678563","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P17742","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues130
DetailsDomain: {"description":"Ubiquitin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00214","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Waridel P.","Quadroni M."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62869","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 189
ChainResidueDetails
AARG55electrostatic stabiliser, hydrogen bond donor, steric role
APHE60polar/non-polar interaction, steric role
AGLN63electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
AASN102electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
APHE113polar/non-polar interaction, steric role
ALEU122polar/non-polar interaction, steric role
AHIS126polar/non-polar interaction, steric role
site_idMCSA2
Number of Residues7
DetailsM-CSA 189
ChainResidueDetails
ESER71electrostatic stabiliser, hydrogen bond donor, steric role
ETYR76polar/non-polar interaction, steric role
ETYR79electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor

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PDB entries from 2026-03-04

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