Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

7F90

Crystal structure of SARS auxiliary protein in complex with human nuclear protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0000922cellular_componentspindle pole
A0000972biological_processtranscription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery
A0001650cellular_componentfibrillar center
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005643cellular_componentnuclear pore
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0006405biological_processRNA export from nucleus
A0006406biological_processmRNA export from nucleus
A0006913biological_processnucleocytoplasmic transport
A0008017molecular_functionmicrotubule binding
A0043130molecular_functionubiquitin binding
A0051301biological_processcell division
A0060236biological_processregulation of mitotic spindle organization
A0097431cellular_componentmitotic spindle pole
B0000776cellular_componentkinetochore
B0000973biological_processpost-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery
B0003713molecular_functiontranscription coactivator activity
B0003723molecular_functionRNA binding
B0003729molecular_functionmRNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005635cellular_componentnuclear envelope
B0005643cellular_componentnuclear pore
B0005654cellular_componentnucleoplasm
B0005829cellular_componentcytosol
B0006405biological_processRNA export from nucleus
B0006508biological_processproteolysis
B0006606biological_processprotein import into nucleus
B0006913biological_processnucleocytoplasmic transport
B0006999biological_processnuclear pore organization
B0008139molecular_functionnuclear localization sequence binding
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0015031biological_processprotein transport
B0016604cellular_componentnuclear body
B0016787molecular_functionhydrolase activity
B0017056molecular_functionstructural constituent of nuclear pore
B0031080cellular_componentnuclear pore outer ring
B0031965cellular_componentnuclear membrane
B0034398biological_processtelomere tethering at nuclear periphery
B0034399cellular_componentnuclear periphery
B0042277molecular_functionpeptide binding
B0042405cellular_componentnuclear inclusion body
B0044614cellular_componentnuclear pore cytoplasmic filaments
B0044615cellular_componentnuclear pore nuclear basket
B0045893biological_processpositive regulation of DNA-templated transcription
B0048026biological_processpositive regulation of mRNA splicing, via spliceosome
B0051028biological_processmRNA transport
B0051292biological_processnuclear pore complex assembly
B0140693molecular_functionmolecular condensate scaffold activity
B1990841molecular_functionpromoter-specific chromatin binding
B1990904cellular_componentribonucleoprotein complex
C0000922cellular_componentspindle pole
C0000972biological_processtranscription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery
C0001650cellular_componentfibrillar center
C0003723molecular_functionRNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005635cellular_componentnuclear envelope
C0005643cellular_componentnuclear pore
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0006405biological_processRNA export from nucleus
C0006406biological_processmRNA export from nucleus
C0006913biological_processnucleocytoplasmic transport
C0008017molecular_functionmicrotubule binding
C0043130molecular_functionubiquitin binding
C0051301biological_processcell division
C0060236biological_processregulation of mitotic spindle organization
C0097431cellular_componentmitotic spindle pole
D0000776cellular_componentkinetochore
D0000973biological_processpost-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery
D0003713molecular_functiontranscription coactivator activity
D0003723molecular_functionRNA binding
D0003729molecular_functionmRNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005635cellular_componentnuclear envelope
D0005643cellular_componentnuclear pore
D0005654cellular_componentnucleoplasm
D0005829cellular_componentcytosol
D0006405biological_processRNA export from nucleus
D0006508biological_processproteolysis
D0006606biological_processprotein import into nucleus
D0006913biological_processnucleocytoplasmic transport
D0006999biological_processnuclear pore organization
D0008139molecular_functionnuclear localization sequence binding
D0008233molecular_functionpeptidase activity
D0008236molecular_functionserine-type peptidase activity
D0015031biological_processprotein transport
D0016604cellular_componentnuclear body
D0016787molecular_functionhydrolase activity
D0017056molecular_functionstructural constituent of nuclear pore
D0031080cellular_componentnuclear pore outer ring
D0031965cellular_componentnuclear membrane
D0034398biological_processtelomere tethering at nuclear periphery
D0034399cellular_componentnuclear periphery
D0042277molecular_functionpeptide binding
D0042405cellular_componentnuclear inclusion body
D0044614cellular_componentnuclear pore cytoplasmic filaments
D0044615cellular_componentnuclear pore nuclear basket
D0045893biological_processpositive regulation of DNA-templated transcription
D0048026biological_processpositive regulation of mRNA splicing, via spliceosome
D0051028biological_processmRNA transport
D0051292biological_processnuclear pore complex assembly
D0140693molecular_functionmolecular condensate scaffold activity
D1990841molecular_functionpromoter-specific chromatin binding
D1990904cellular_componentribonucleoprotein complex
E0005515molecular_functionprotein binding
E0030430cellular_componenthost cell cytoplasm
E0039502biological_processsymbiont-mediated suppression of host type I interferon-mediated signaling pathway
E0039563biological_processsymbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity
E0044165cellular_componenthost cell endoplasmic reticulum
E0044167cellular_componenthost cell endoplasmic reticulum membrane
E0044178cellular_componenthost cell Golgi membrane
E0052170biological_processsymbiont-mediated suppression of host innate immune response
F0005515molecular_functionprotein binding
F0030430cellular_componenthost cell cytoplasm
F0039502biological_processsymbiont-mediated suppression of host type I interferon-mediated signaling pathway
F0039563biological_processsymbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity
F0044165cellular_componenthost cell endoplasmic reticulum
F0044167cellular_componenthost cell endoplasmic reticulum membrane
F0044178cellular_componenthost cell Golgi membrane
F0052170biological_processsymbiont-mediated suppression of host innate immune response
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. VFTAscDkTAKMWDL
ChainResidueDetails
AVAL101-LEU115
AVAL144-THR158

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsRegion: {"description":"Critical for disrupting nuclear import","evidences":[{"source":"PubMed","id":"17596301","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues84
DetailsRepeat: {"description":"WD 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20498086","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues60
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20498086","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues64
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20498086","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues76
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20498086","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues80
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20498086","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues60
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20498086","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues72
DetailsRepeat: {"description":"WD 7","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20498086","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

245011

PDB entries from 2025-11-19

PDB statisticsPDBj update infoContact PDBjnumon