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

4BSN

Crystal structure of the Nuclear Export Receptor CRM1 (exportin-1) lacking the C-terminal helical extension at 4.1A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000054biological_processribosomal subunit export from nucleus
A0000055biological_processribosomal large subunit export from nucleus
A0000056biological_processribosomal small subunit export from nucleus
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000776cellular_componentkinetochore
A0003723molecular_functionRNA binding
A0005049molecular_functionnuclear export signal receptor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005642cellular_componentannulate lamellae
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006406biological_processmRNA export from nucleus
A0006611biological_processprotein export from nucleus
A0006886biological_processintracellular protein transport
A0006913biological_processnucleocytoplasmic transport
A0009410biological_processresponse to xenobiotic stimulus
A0015030cellular_componentCajal body
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0019904molecular_functionprotein domain specific binding
A0031267molecular_functionsmall GTPase binding
A0031965cellular_componentnuclear membrane
A0032434biological_processregulation of proteasomal ubiquitin-dependent protein catabolic process
A0032991cellular_componentprotein-containing complex
A0042254biological_processribosome biogenesis
A0051028biological_processmRNA transport
A0071401biological_processcellular response to triglyceride
A0140297molecular_functionDNA-binding transcription factor binding
A1902075biological_processcellular response to salt
A1990904cellular_componentribonucleoprotein complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues23
DetailsRepeat: {"description":"HEAT 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsRepeat: {"description":"HEAT 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues38
DetailsRepeat: {"description":"HEAT 4"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues37
DetailsRepeat: {"description":"HEAT 5"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues37
DetailsRepeat: {"description":"HEAT 6"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues70
DetailsRegion: {"description":"Interaction with RANBP3"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsRegion: {"description":"Necessary for HTLV-1 Rex multimerization"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q80U96","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q80U96","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q80U96","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon