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9DLP

Cryo-EM structure of human TREX-2 complex bound to DDX39B(UAP56)

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A0003676molecular_functionnucleic acid binding
B0000973biological_processpost-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery
B0003690molecular_functiondouble-stranded DNA binding
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005643cellular_componentnuclear pore
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0006368biological_processtranscription elongation by RNA polymerase II
B0006406biological_processmRNA export from nucleus
B0015031biological_processprotein transport
B0016973biological_processpoly(A)+ mRNA export from nucleus
B0032991cellular_componentprotein-containing complex
B0044615cellular_componentnuclear pore nuclear basket
B0045579biological_processpositive regulation of B cell differentiation
B0045814biological_processnegative regulation of gene expression, epigenetic
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0048536biological_processspleen development
B0051028biological_processmRNA transport
B0070390cellular_componenttranscription export complex 2
B1905457biological_processnegative regulation of lymphoid progenitor cell differentiation
C0000502cellular_componentproteasome complex
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005829cellular_componentcytosol
C0006406biological_processmRNA export from nucleus
C0006979biological_processresponse to oxidative stress
C0008021cellular_componentsynaptic vesicle
C0008541cellular_componentproteasome regulatory particle, lid subcomplex
C0010498biological_processproteasomal protein catabolic process
C0032039cellular_componentintegrator complex
C0032991cellular_componentprotein-containing complex
C0043130molecular_functionubiquitin binding
C0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
C0043248biological_processproteasome assembly
C0045944biological_processpositive regulation of transcription by RNA polymerase II
C0061136biological_processregulation of proteasomal protein catabolic process
C0071357biological_processcellular response to type I interferon
D0000166molecular_functionnucleotide binding
D0000245biological_processspliceosomal complex assembly
D0000346cellular_componenttranscription export complex
D0000398biological_processmRNA splicing, via spliceosome
D0003676molecular_functionnucleic acid binding
D0003723molecular_functionRNA binding
D0003724molecular_functionRNA helicase activity
D0003729molecular_functionmRNA binding
D0004386molecular_functionhelicase activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005681cellular_componentspliceosomal complex
D0005687cellular_componentU4 snRNP
D0005688cellular_componentU6 snRNP
D0005737cellular_componentcytoplasm
D0006397biological_processmRNA processing
D0006405biological_processRNA export from nucleus
D0006406biological_processmRNA export from nucleus
D0008186molecular_functionATP-dependent activity, acting on RNA
D0008380biological_processRNA splicing
D0016607cellular_componentnuclear speck
D0016787molecular_functionhydrolase activity
D0016887molecular_functionATP hydrolysis activity
D0017070molecular_functionU6 snRNA binding
D0030621molecular_functionU4 snRNA binding
D0042802molecular_functionidentical protein binding
D0043008molecular_functionATP-dependent protein binding
D0051028biological_processmRNA transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues364
DetailsDomain: {"description":"PCI","evidences":[{"source":"PROSITE-ProRule","id":"PRU01185","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues28
DetailsMotif: {"description":"Q motif"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues3
DetailsMotif: {"description":"DECD box"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues7
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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