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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
A0005856cellular_componentcytoskeleton
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
A0071407biological_processcellular response to organic cyclic compound
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
B0008236molecular_functionserine-type peptidase activity
B0015031biological_processprotein transport
B0016020cellular_componentmembrane
B0016604cellular_componentnuclear body
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
C0005856cellular_componentcytoskeleton
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
C0071407biological_processcellular response to organic cyclic compound
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
D0008236molecular_functionserine-type peptidase activity
D0015031biological_processprotein transport
D0016020cellular_componentmembrane
D0016604cellular_componentnuclear body
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
E0003674molecular_functionmolecular_function
E0005515molecular_functionprotein binding
E0005575cellular_componentcellular_component
E0008150biological_processbiological_process
E0016020cellular_componentmembrane
E0019049biological_processvirus-mediated perturbation of host defense response
E0030430cellular_componenthost cell cytoplasm
E0033644cellular_componenthost cell membrane
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
E0044177cellular_componenthost cell Golgi apparatus
E0044178cellular_componenthost cell Golgi membrane
E0052170biological_processsymbiont-mediated suppression of host innate immune response
F0003674molecular_functionmolecular_function
F0005515molecular_functionprotein binding
F0005575cellular_componentcellular_component
F0008150biological_processbiological_process
F0016020cellular_componentmembrane
F0019049biological_processvirus-mediated perturbation of host defense response
F0030430cellular_componenthost cell cytoplasm
F0033644cellular_componenthost cell membrane
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
F0044177cellular_componenthost cell Golgi apparatus
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 Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:18287282
ChainResidueDetails
BSER881
DSER881

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Breakpoint for translocation to form the NUP98-RAP1GDS1 fusion protein. Breakpoint for translocation to form the NUP98-RAP1GDS1 fusion protein => ECO:0000269|PubMed:10477737, ECO:0000269|PubMed:16419055
ChainResidueDetails
BPHE391
DPHE391

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Breakpoint for translocation to form the NUP98-HOXA9 fusion protein. Breakpoint for translocation to form the NUP98-RAP1GDS1 fusion protein => ECO:0000269|PubMed:10477737, ECO:0000269|PubMed:8563753
ChainResidueDetails
BVAL486
DVAL486

site_idSWS_FT_FI4
Number of Residues2
DetailsSITE: Breakpoint for translocation to form the NUP98-KDM5A fusion protein => ECO:0000269|PubMed:16419055
ChainResidueDetails
BGLU531
DGLU531

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Cleavage; by autolysis => ECO:0000269|PubMed:10087256, ECO:0000269|PubMed:12191480, ECO:0000269|PubMed:18287282
ChainResidueDetails
BPHE880
DPHE880

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231
ChainResidueDetails
BSER524
BSER673
DSER524
DSER673

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS603
DLYS603

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER608
DSER608

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER612
DSER612

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332
ChainResidueDetails
BSER618
BSER625
DSER618
DSER625

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER623
DSER623

site_idSWS_FT_FI12
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q6PFD9
ChainResidueDetails
BSER653
BSER1064
BSER1329
DSER653
DSER1064
DSER1329

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
BTHR670
DTHR670

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER681
DSER681

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER683
DSER683

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER839
DSER839

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER888
DSER888

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER897
DSER897

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231
ChainResidueDetails
BSER934
DSER934

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
BTHR1000
DTHR1000

site_idSWS_FT_FI21
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER1023
BSER1043
DSER1023
DSER1043

site_idSWS_FT_FI22
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:16964243, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER1028
BSER1060
DSER1028
DSER1060

site_idSWS_FT_FI23
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648
ChainResidueDetails
BTHR1070
DTHR1070

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q6PFD9
ChainResidueDetails
BTHR1772
DTHR1772

site_idSWS_FT_FI25
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS563
BLYS665
DLYS563
DLYS665

site_idSWS_FT_FI26
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
BLYS603
DLYS603

223166

PDB entries from 2024-07-31

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