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4BSM

Crystal structure of the Nuclear Export Receptor CRM1 (exportin-1) lacking the C-terminal helical extension at 4.5A

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
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
A0010824biological_processregulation of centrosome duplication
A0015030cellular_componentCajal body
A0015031biological_processprotein transport
A0016020cellular_componentmembrane
A0031267molecular_functionsmall GTPase binding
A0031965cellular_componentnuclear membrane
A0032434biological_processregulation of proteasomal ubiquitin-dependent protein catabolic process
A0032991cellular_componentprotein-containing complex
A0034504biological_processprotein localization to nucleus
A0042176biological_processregulation of protein catabolic process
A0042254biological_processribosome biogenesis
A0043231cellular_componentintracellular membrane-bounded organelle
A0046825biological_processregulation of protein export from nucleus
A0051028biological_processmRNA transport
A1990904cellular_componentribonucleoprotein complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER391

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS446
ALYS693

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q80U96
ChainResidueDetails
ATHR448

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q80U96
ChainResidueDetails
ASER450

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q80U96
ChainResidueDetails
ATYR454

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER1031

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PDB entries from 2024-10-02

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